L-threonine degradation III (to methylglyoxal)

MetaCyc:THRDLCTCAT-PWY

The complete native L-threonine degradation-III boundary contains three elementary events: NAD-dependent threonine oxidation, spontaneous decarboxylation of the unstable (2S)-2-amino-3-oxobutanoate, and aerobic aminoacetone oxidation to methylglyoxal. All 15 formal core chemical sides are retained. The composite RXN-14249 is not an additional event. The E. coli TynA terminal assignment is explicitly HYPOTHETICAL (EV-AS-NAS): microbial washed-cell aminoacetone-to-methylglyoxal/O2-consumption evidence came from an unnamed sewage isolate described as closely related to Arthrobacter globiformis, with no identified oxidase, exact strain accession or directly measured peroxide product. Tested E. coli W1485/SBD76 preparations failed to grow on or measurably consume aminoacetone, and Serratia Sr41 work left subsequent aminoacetone metabolism unresolved. These bounded observations neither demonstrate the complete E. coli route nor prove its universal impossibility. Cytoplasmic Tdh and periplasmic TynA do not imply an established intervening aminoacetone transport mechanism. The Tdh homotetramer and His-tagged YiaY assay alternative have separate evidence. YiaY uses versioned 382-residue AAB18566.1 as reference; the assayed full construct sequence was not reported and is not equated to current 383-residue P37686. Its reported glycine-auxotrophy phenotype conflicts with the cited Keio deletion result. Metal use is preparation and condition dependent: older one-zinc measurements versus the reviewed two-zinc annotation, zinc/cobalt/cadmium alternatives, newer iron/manganese activity, contradictory cadmium activity and inferred intracellular occupancy are retained. Dps/MntH/manganese protection concerns measured Tdh activity under peroxide stress, not demonstrated pathway flux. Separate uptake context includes inward SstT Na+/threonine and TdcC H+/threonine reactions, plus ATP-dependent LIV-I activity with all five native components and no invented threonine-specific ATP stoichiometry. TdcC anaerobic induction does not assert simultaneous oxygen-requiring terminal flux. SstT expression experiments used a reported Thr301 construct distinct from current Ala301; the separate purified 2002 serine-uptake preparation carried a C-terminal eight-His tag. The current PathBank biosynthesis connection, downstream methylglyoxal degradation and parent superpathway are opaque interfaces/hierarchy; connected pathways are not expanded. Current PathBank and frozen 2019 definitions, neutral source forms and charged Rhea forms remain distinct. Lrp represses tdh in the inspected primary reporters despite positive native TU polarity; leucine induces tdh expression. LIV-I expression and transport responses depend on Lrp/leucine conditions. FeaR, FNR and NsrR edges describe conditional expression, not direct catalytic control. NsrR start-codon modification, FeaR domain-only binding assays, older anaerobic profiling versus newer reporter results, and named experimental derivative strains remain explicitly qualified. Native MG1655 reference identities do not relabel every historical assay as MG1655. This graph records a complete source-defined route with bounded uncertainty, not an experimentally reconstructed complete E. coli degradation system. The newer Nissle FeaR biosensor report is retained at abstract/native-annotation scope and is not treated as an MG1655 full-length ligand-binding or aminoacetone-induction experiment.

Pathway type
threonine catabolism with hypothetical terminal enzyme
Organism scope

Read the source YAML

Pathway network

92 nodes · 111 asserted directed edges

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Pathway network: L-threonine degradation III (to methylglyoxal) 92 nodes · 111 asserted directed edges. Every arrow links to its evidence table row; nodes link to their component details. Isolated declared components are retained. CHEBI:57926 — consumes → RHEA:13162; The directed native Rhea reaction has CHEBI:57926 on its substrates side with coefficient 1.; Evidence: RHEA:13162consumes CHEBI:57540 — consumes → RHEA:13162; The directed native Rhea reaction has CHEBI:57540 on its substrates side with coefficient 1.; Evidence: RHEA:13162consumes RHEA:13162 — produces → CHEBI:78948; The directed native Rhea reaction has CHEBI:78948 on its products side with coefficient 1.; Evidence: RHEA:13162produces RHEA:13162 — produces → CHEBI:57945; The directed native Rhea reaction has CHEBI:57945 on its products side with coefficient 1.; Evidence: RHEA:13162produces RHEA:13162 — produces → CHEBI:15378; The directed native Rhea reaction has CHEBI:15378 on its products side with coefficient 1.; Evidence: RHEA:13162produces CHEBI:78948 — consumes → RHEA:25654; The directed native Rhea reaction has CHEBI:78948 on its substrates side with coefficient 1.; Evidence: RHEA:25654consumes CHEBI:15378 — consumes → RHEA:25654; The directed native Rhea reaction has CHEBI:15378 on its substrates side with coefficient 1.; Evidence: RHEA:25654consumes RHEA:25654 — produces → CHEBI:58320; The directed native Rhea reaction has CHEBI:58320 on its products side with coefficient 1.; Evidence: RHEA:25654produces RHEA:25654 — produces → CHEBI:16526; The directed native Rhea reaction has CHEBI:16526 on its products side with coefficient 1.; Evidence: RHEA:25654produces CHEBI:58320 — consumes → RHEA:28187; The directed native Rhea reaction has CHEBI:58320 on its substrates side with coefficient 1.; Evidence: RHEA:28187consumes CHEBI:15379 — consumes → RHEA:28187; The directed native Rhea reaction has CHEBI:15379 on its substrates side with coefficient 1.; Evidence: RHEA:28187consumes CHEBI:15377 — consumes → RHEA:28187; The directed native Rhea reaction has CHEBI:15377 on its substrates side with coefficient 1.; Evidence: RHEA:28187consumes RHEA:28187 — produces → CHEBI:17158; The directed native Rhea reaction has CHEBI:17158 on its products side with coefficient 1.; Evidence: RHEA:28187produces RHEA:28187 — produces → CHEBI:16240; The directed native Rhea reaction has CHEBI:16240 on its products side with coefficient 1.; Evidence: RHEA:28187produces RHEA:28187 — produces → CHEBI:28938; The directed native Rhea reaction has CHEBI:28938 on its products side with coefficient 1.; Evidence: RHEA:28187produces CHEBI:57926 — consumes → RHEA:70001; The directed native Rhea reaction has CHEBI:57926 on its substrates side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.; Evidence: RHEA:70001consumes CHEBI:29101 — consumes → RHEA:70001; The directed native Rhea reaction has CHEBI:29101 on its substrates side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.; Evidence: RHEA:70001consumes RHEA:70001 — produces → CHEBI:57926; The directed native Rhea reaction has CHEBI:57926 on its products side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.; Evidence: RHEA:70001produces RHEA:70001 — produces → CHEBI:29101; The directed native Rhea reaction has CHEBI:29101 on its products side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.; Evidence: RHEA:70001produces CHEBI:57926 — consumes → RHEA:28885; The directed native Rhea reaction has CHEBI:57926 on its substrates side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.; Evidence: RHEA:28885consumes CHEBI:15378 — consumes → RHEA:28885; The directed native Rhea reaction has CHEBI:15378 on its substrates side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.; Evidence: RHEA:28885consumes RHEA:28885 — produces → CHEBI:57926; The directed native Rhea reaction has CHEBI:57926 on its products side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.; Evidence: RHEA:28885produces RHEA:28885 — produces → CHEBI:15378; The directed native Rhea reaction has CHEBI:15378 on its products side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.; Evidence: RHEA:28885produces RHEA:13162 — part_of → MetaCyc:THRDLCTCAT-PWY; The complete native three-event pathway includes THREODEHYD-RXN; its mapped directional Rhea event is RHEA:13162. Spontaneous decarboxylation is retained as an elementary event.; Evidence: MetaCyc:THRDLCTCAT-PWY, MetaCyc:THREODEHYD-RXNpart of RHEA:25654 — part_of → MetaCyc:THRDLCTCAT-PWY; The complete native three-event pathway includes THREOSPON-RXN; its mapped directional Rhea event is RHEA:25654. Spontaneous decarboxylation is retained as an elementary event.; Evidence: MetaCyc:THRDLCTCAT-PWY, MetaCyc:THREOSPON-RXNpart of RHEA:28187 — part_of → MetaCyc:THRDLCTCAT-PWY; The complete native three-event pathway includes AMACETOXID-RXN; its mapped directional Rhea event is RHEA:28187. Spontaneous decarboxylation is retained as an elementary event.; Evidence: MetaCyc:THRDLCTCAT-PWY, MetaCyc:AMACETOXID-RXNpart of RHEA:13162 — precedes → RHEA:25654; The native route oxidizes threonine before spontaneous decarboxylation of its unstable 2-amino-3-oxo intermediate.; Evidence: MetaCyc:THRDLCTCAT-PWYprecedes RHEA:25654 — precedes → RHEA:28187; Aminoacetone from spontaneous decarboxylation is the input to terminal oxidation; the E. coli catalyst assignment remains hypothetical.; Evidence: MetaCyc:THRDLCTCAT-PWYprecedes MetaCyc:THRDLCTCAT-PWY — part_of → MetaCyc:THREOCAT-PWY; The native record places the complete degradation-III route in the threonine-metabolism superpathway; the parent is an opaque hierarchy context.; Evidence: MetaCyc:THRDLCTCAT-PWYpart of MetaCyc:PWY-5386 — has_input → CHEBI:17158; The native pathway-link connects the methylglyoxal product to methylglyoxal degradation I; no downstream chemistry is imported here.; Evidence: MetaCyc:THRDLCTCAT-PWYhas input PathBank:SMP0000837 — has_output → CHEBI:57926; The current BioPAX includes a named threonine-biosynthesis SubPathway and its threonine-supply interface. This is a non-elementary upstream connection, not an additional degradation reaction. Neutral PathBank threonine is represented here by Rhea physiological L-threonine with the protonation distinction retained.; Evidence: PathBank:SMP0002118, PathBank:SMP0002118/PWMLhas output MetaCyc:THREODEHYD-CPLX — has_part → UniProtKB:P07913; Native component coefficient 4 and reviewed homotetramer annotation identify the Tdh assembly; the guarded functional common name does not add an unreported assembly suffix.; Evidence: MetaCyc:THREODEHYD-CPLX, UniProtKB:P07913, EcoCyc:THREODEHYD-MONOMERhas part MetaCyc:THREODEHYD-CPLX — catalyzes → RHEA:13162; Tdh supplies the NAD-dependent threonine oxidation step. Native RXN-14249 is a composite of oxidation plus spontaneous decarboxylation, not a fourth elementary reaction.; Evidence: EcoCyc:THREODEHYD-ENZRXN, UniProtKB:P07913, EcoCyc:RXN-14249catalyzes NCBIProtein:AAB18566.1 — catalyzes → RHEA:13162; subject experimental construct: N-terminal 6×His-tagged orf382 amplified from E. coli MG1655 using AAB18566.1 as reference, expressed from pET28a(+) in BL21(DE3) and purified by Ni-NTA. The complete construct sequence was not reported; this assay endpoint does not assert identity with the bare reference or current UniProtKB:P37686 sequence.; Evidence PMID:24651643: The study cloned MG1655 orf382 using AAB18566.1 as reference, reported no mutation in the sequenced insert, expressed an N-terminal 6×His fusion in BL21(DE3), and purified the recombinant preparation by Ni-NTA. (Publisher PDF pp. 749–751; Materials and Methods, Molecular Cloning, Protein Expression, Purification, and Enzymatic Activity Assays; Results and Discussion, Molecular Cloning, Protein Expression, and Purification); The purified N-terminal His-tagged YiaY/orf382 preparation showed threonine-dependent NADH formation at 340 nm. This supports an alternative oxidation activity; direct intermediate/product measurements and complete-route reconstruction were not reported.; Evidence: PMID:24651643catalyzes NCBIProtein:AAB18566.1 — has_cofactor → CHEBI:60240; subject experimental construct: N-terminal 6×His-tagged orf382 amplified from E. coli MG1655 using AAB18566.1 as reference, expressed from pET28a(+) in BL21(DE3) and purified by Ni-NTA. The complete construct sequence was not reported; this assay endpoint does not assert identity with the bare reference or current UniProtKB:P37686 sequence.; Evidence PMID:24651643: The study cloned MG1655 orf382 using AAB18566.1 as reference, reported no mutation in the sequenced insert, expressed an N-terminal 6×His fusion in BL21(DE3), and purified the recombinant preparation by Ni-NTA. (Publisher PDF pp. 749–751; Materials and Methods, Molecular Cloning, Protein Expression, Purification, and Enzymatic Activity Assays; Results and Discussion, Molecular Cloning, Protein Expression, and Purification); EDTA depleted activity and affected structure of the purified construct. Its measured preparation contained 0.424 mol Fe and 0.914 mol Zn per mol protein; these values do not fix native occupancy, iron oxidation state, or a metal stoichiometry for current P37686.; Evidence: PMID:24651643has cofactor CHEBI:4735 — inhibits → NCBIProtein:AAB18566.1; object experimental construct: N-terminal 6×His-tagged orf382 amplified from E. coli MG1655 using AAB18566.1 as reference, expressed from pET28a(+) in BL21(DE3) and purified by Ni-NTA. The complete construct sequence was not reported; this assay endpoint does not assert identity with the bare reference or current UniProtKB:P37686 sequence.; Evidence PMID:24651643: The study cloned MG1655 orf382 using AAB18566.1 as reference, reported no mutation in the sequenced insert, expressed an N-terminal 6×His fusion in BL21(DE3), and purified the recombinant preparation by Ni-NTA. (Publisher PDF pp. 749–751; Materials and Methods, Molecular Cloning, Protein Expression, Purification, and Enzymatic Activity Assays; Results and Discussion, Molecular Cloning, Protein Expression, and Purification); EDTA reduced activity and altered structural measurements in the assayed His-tagged YiaY preparation; chelation is an in-vitro treatment, not evidence of an endogenous inhibitor.; Evidence: PMID:24651643inhibits MetaCyc:AMINEOXID-CPLX — has_part → UniProtKB:P46883; The native TynA assembly has two amine-oxidase subunits; the reviewed entry independently describes a homodimer.; Evidence: MetaCyc:AMINEOXID-CPLX, UniProtKB:P46883, EcoCyc:AMINEOXID-MONOMERhas part MetaCyc:AMINEOXID-CPLX — catalyzes → RHEA:28187; HYPOTHETICAL TynA assignment: EcoCyc associates this complex with aminoacetone oxidation using EV-AS-NAS. This is not a demonstrated E. coli aminoacetone substrate assay or a reconstructed complete route.; Evidence: EcoCyc:AMACETOXID-ENZRXN, EcoCyc:THRDLCTCAT-PWYcatalyzes MetaCyc:THREODEHYD-CPLX — located_in → GO:0005737; Tdh localization is a reviewed cytoplasmic annotation with HAMAP inference, distinct from a direct localization assay.; Evidence: UniProtKB:P07913located in MetaCyc:AMINEOXID-CPLX — located_in → GO:0042597; The reviewed TynA protein is periplasmic. No aminoacetone export mechanism linking it to cytoplasmic Tdh is asserted.; Evidence: UniProtKB:P46883located in MetaCyc:AMINEOXID-CPLX — has_cofactor → CHEBI:23378; One copper ion per subunit is annotated from experimental TynA studies.; Evidence: UniProtKB:P46883has cofactor MetaCyc:AMINEOXID-CPLX — has_cofactor → CHEBI:29108; Two calcium ions per subunit are annotated from experimental TynA studies.; Evidence: UniProtKB:P46883has cofactor MetaCyc:AMINEOXID-CPLX — has_cofactor → CHEBI:79027; One topaquinone residue per subunit is annotated. Maturation and substoichiometric overexpression preparations are distinct from an assumed fully matured molecule.; Evidence: UniProtKB:P46883has cofactor MetaCyc:AMINEOXID-CPLX — has_cofactor → CHEBI:29105; Zinc cofactor use is explicitly inferred by similarity to P12807; it is not a direct E. coli substrate-specific measurement.; Evidence: UniProtKB:P46883has cofactor MetaCyc:AMINEOXID-CPLX — has_cofactor → CHEBI:29035; Manganese binding (one per subunit) is explicitly inferred by similarity to Q43077; no direct E. coli occupancy measurement is claimed.; Evidence: UniProtKB:P46883has cofactor PubChem:78645 — inhibits → MetaCyc:AMINEOXID-CPLX; 2-Hydrazinopyridine inhibits TynA in the cited structural/biochemical work. This protein-level inhibition does not validate hypothetical aminoacetone turnover.; Evidence: UniProtKB:P46883, PMID:9048544inhibits MetaCyc:THREODEHYD-CPLX — has_cofactor → CHEBI:29105; The reviewed entry reports two Zn(2+) per Tdh subunit and distinguishes a proposed structural site from a less tightly bound catalytic site.; Evidence: UniProtKB:P07913, PMID:2007567has cofactor MetaCyc:THREODEHYD-CPLX — has_cofactor → CHEBI:48828; Co(2+) substitutes for zinc in the cited in-vitro Tdh preparation; this is not evidence for routine cobalt occupancy in vivo.; Evidence: UniProtKB:P07913has cofactor MetaCyc:THREODEHYD-CPLX — has_cofactor → CHEBI:48775; The older reviewed annotation reports Cd(2+) exchange for zinc. The 2012 purified-enzyme study found no Cd-supported activity; preserve this preparation/assay conflict rather than asserting universal cadmium activation.; Evidence: UniProtKB:P07913, PMID:22411989has cofactor MetaCyc:THREODEHYD-CPLX — has_cofactor → CHEBI:29033; Fe(II)-reconstituted purified Tdh was active. Native intracellular iron use was inferred from oxidative sensitivity/reconstitution; it was not established by direct active-site occupancy measurement.; Evidence: PMID:22411989has cofactor MetaCyc:THREODEHYD-CPLX — has_cofactor → CHEBI:29035; Mn(II)-reconstituted purified Tdh retained catalytic activity but bound threonine poorly. Intracellular manganese protection does not establish active-site occupancy or continuous pathway flux.; Evidence: PMID:22411989has cofactor CHEBI:4735 — inhibits → MetaCyc:THREODEHYD-CPLX; EDTA inhibits Tdh in vitro and was used to remove exchangeable metals; apoenzyme instability and assay metal replacement limit interpretation as a simple native regulatory switch.; Evidence: UniProtKB:P07913, PMID:22411989inhibits CHEBI:16240 — inhibits → MetaCyc:THREODEHYD-CPLX; object molecular state: Tdh assayed after in-vitro Fe(II) loading or in the specified peroxide-stressed E. coli preparations. Metal state and peroxide exposure are part of this claim; a fixed native metal occupancy or complete assay-construct sequence is not asserted.; Evidence PMID:22411989: The work compared metal-reconstituted purified Tdh with extracts/cells of catalase- or peroxide-scavenging-deficient strains. (Experimental Procedures, In Vitro/In Vivo Studies of Enzyme Oxidation; Figures 1–3); Hydrogen peroxide rapidly inactivated iron-loaded Tdh and reduced measured activity in the specified stressed cells. Early damage could be rescued; prolonged stress caused increasing nonreactivatable loss.; Evidence: PMID:22411989inhibits CHEBI:18320 — activates → MetaCyc:THREODEHYD-CPLX; object molecular state: Tdh assayed after in-vitro Fe(II) loading or in the specified peroxide-stressed E. coli preparations. Metal state and peroxide exposure are part of this claim; a fixed native metal occupancy or complete assay-construct sequence is not asserted.; Evidence PMID:22411989: The work compared metal-reconstituted purified Tdh with extracts/cells of catalase- or peroxide-scavenging-deficient strains. (Experimental Procedures, In Vitro/In Vivo Studies of Enzyme Oxidation; Figures 1–3); DTT together with added metal restored activity after limited peroxide exposure in vitro. This is measured rescue of an oxidized preparation, not an endogenous activator or rescue after all prolonged damage.; Evidence: PMID:22411989activates CHEBI:63213 — activates → MetaCyc:THREODEHYD-CPLX; object molecular state: Tdh assayed after in-vitro Fe(II) loading or in the specified peroxide-stressed E. coli preparations. Metal state and peroxide exposure are part of this claim; a fixed native metal occupancy or complete assay-construct sequence is not asserted.; Evidence PMID:22411989: The work compared metal-reconstituted purified Tdh with extracts/cells of catalase- or peroxide-scavenging-deficient strains. (Experimental Procedures, In Vitro/In Vivo Studies of Enzyme Oxidation; Figures 1–3); TCEP together with added metal restored activity after limited peroxide exposure in vitro. This is measured rescue of an oxidized preparation, not an endogenous activator or rescue after all prolonged damage.; Evidence: PMID:22411989activates EcoCyc:CPLX0-1521 — has_part → UniProtKB:P0ABT2; The native EcoCyc complex lists this protein component with coefficient 12. This assembly annotation does not establish that every promoter assay used this oligomeric state.; Evidence: EcoCyc:CPLX0-1521, EcoCyc:EG11415-MONOMERhas part EcoCyc:CPLX0-7756 — has_part → UniProtKB:P0AF63; The native EcoCyc complex lists this protein component with coefficient 2. This assembly annotation does not establish that every promoter assay used this oligomeric state.; Evidence: EcoCyc:CPLX0-7756, EcoCyc:EG11212-MONOMERhas part EcoCyc:CPLX0-7797 — has_part → UniProtKB:P0A9E5; The native EcoCyc complex lists this protein component with coefficient 2. This assembly annotation does not establish that every promoter assay used this oligomeric state.; Evidence: EcoCyc:CPLX0-7797, EcoCyc:PD00197has part EcoCyc:CPLX0-7797 — has_cofactor → CHEBI:49883; The reviewed FNR entry assigns one [4Fe-4S] cluster per subunit; anaerobic cluster acquisition favors its active dimer, whereas oxygen disrupts this state.; Evidence: UniProtKB:P0A9E5, EcoCyc:CPLX0-7797has cofactor EcoCyc:CPLX0-7756 — has_cofactor → CHEBI:190135; The reviewed E. coli NsrR annotation assigns a [2Fe-2S] cluster with curator inference. Native commentary cites some physical-state work in S. coelicolor; this is not a direct E. coli tynA-promoter metal assay.; Evidence: UniProtKB:P0AF63, EcoCyc:CPLX0-7756has cofactor UniProtKB:P0A769 — regulates → MetaCyc:THREODEHYD-CPLX; MntH supported retention of measured Tdh activity under the study's chronic peroxide-stress conditions. This is indirect protection through manganese import/iron handling, not direct Tdh binding or measured complete pathway flux.; Evidence: PMID:22411989regulates EcoCyc:CPLX0-1521 — regulates → MetaCyc:THREODEHYD-CPLX; Dps supported retention of measured Tdh activity under the study's chronic peroxide-stress conditions. This is indirect protection through manganese import/iron handling, not direct Tdh binding or measured complete pathway flux.; Evidence: PMID:22411989regulates CHEBI:29035 — regulates → MetaCyc:THREODEHYD-CPLX; Supplemental manganese protected measured Tdh activity in peroxide-stressed cells, including the Dps-deficient comparison. The authors explicitly did not physically demonstrate intracellular active-site manganese.; Evidence: PMID:22411989regulates UniProtKB:P0AGE4 — catalyzes → RHEA:70001; SstT is assigned the physiological inward sodium/threonine symport direction. The purified 2002 experiment measured serine uptake and threonine competition; it did not directly measure threonine transport kinetics.; Evidence: UniProtKB:P0AGE4catalyzes UniProtKB:P0AGE4 — located_in → GO:0005886; The reviewed transporter is located in the cell inner membrane.; Evidence: UniProtKB:P0AGE4located in RHEA:70001 — provides_input_for → RHEA:13162; Threonine uptake can supply the oxidation substrate in the relevant physiological context; this connection does not assert concurrent expression or demonstrated complete-route flux.; Evidence: EcoCyc:THRDLCTCAT-PWYprovides input for UniProtKB:P0AAD8 — catalyzes → RHEA:28885; TdcC is assigned physiological inward proton/threonine symport. Its anaerobically induced uptake context does not imply simultaneous aerobic terminal aminoacetone oxidation.; Evidence: UniProtKB:P0AAD8catalyzes UniProtKB:P0AAD8 — located_in → GO:0005886; The reviewed transporter is located in the cell inner membrane.; Evidence: UniProtKB:P0AAD8located in RHEA:28885 — provides_input_for → RHEA:13162; Threonine uptake can supply the oxidation substrate in the relevant physiological context; this connection does not assert concurrent expression or demonstrated complete-route flux.; Evidence: EcoCyc:THRDLCTCAT-PWYprovides input for MetaCyc:ABC-15-CPLX — enables → GO:0015195; The LIV-I transporter is reported to take up threonine in addition to its principal branched-chain substrates. Its ATP-dependent transport context is retained without inventing a threonine-specific ATP-hydrolysis stoichiometry.; Evidence: EcoCyc:ABC-15-CPLXenables MetaCyc:ABC-15-CPLX — has_part → UniProtKB:P22731; The native LIV-I complex includes this exact LivF/LivG/LivH/LivM/LivJ component with coefficient 1. LivJ is retained; the alternative LivK binding protein is not substituted.; Evidence: EcoCyc:ABC-15-CPLX, EcoCyc:LIVF-MONOMERhas part MetaCyc:ABC-15-CPLX — has_part → UniProtKB:P0A9S7; The native LIV-I complex includes this exact LivF/LivG/LivH/LivM/LivJ component with coefficient 1. LivJ is retained; the alternative LivK binding protein is not substituted.; Evidence: EcoCyc:ABC-15-CPLX, EcoCyc:LIVG-MONOMERhas part MetaCyc:ABC-15-CPLX — has_part → UniProtKB:P0AEX7; The native LIV-I complex includes this exact LivF/LivG/LivH/LivM/LivJ component with coefficient 1. LivJ is retained; the alternative LivK binding protein is not substituted.; Evidence: EcoCyc:ABC-15-CPLX, EcoCyc:LIVH-MONOMERhas part MetaCyc:ABC-15-CPLX — has_part → UniProtKB:P22729; The native LIV-I complex includes this exact LivF/LivG/LivH/LivM/LivJ component with coefficient 1. LivJ is retained; the alternative LivK binding protein is not substituted.; Evidence: EcoCyc:ABC-15-CPLX, EcoCyc:LIVM-MONOMERhas part MetaCyc:ABC-15-CPLX — has_part → UniProtKB:P0AD96; The native LIV-I complex includes this exact LivF/LivG/LivH/LivM/LivJ component with coefficient 1. LivJ is retained; the alternative LivK binding protein is not substituted.; Evidence: EcoCyc:ABC-15-CPLX, EcoCyc:LIVJ-MONOMERhas part UniProtKB:P0AEX7 — located_in → GO:0005886; The reviewed Liv component has this membrane/periplasmic localization; binding-protein and permease roles remain distinct.; Evidence: UniProtKB:P0AEX7located in UniProtKB:P22729 — located_in → GO:0005886; The reviewed Liv component has this membrane/periplasmic localization; binding-protein and permease roles remain distinct.; Evidence: UniProtKB:P22729located in UniProtKB:P0AD96 — located_in → GO:0042597; The reviewed Liv component has this membrane/periplasmic localization; binding-protein and permease roles remain distinct.; Evidence: UniProtKB:P0AD96located in GO:0015195 — has_input → CHEBI:30616; LIV-I is an ATP-dependent uptake system containing the LivF/LivG ATP-binding subunits. This nonstoichiometric activity edge does not assert a complete threonine-specific ATP equation.; Evidence: EcoCyc:ABC-15-CPLXhas input GO:0015195 — has_input → CHEBI:57926; Threonine is a reported LIV-I uptake substrate; the shared chemical node denotes its identity, not a new extracellular chemical species.; Evidence: EcoCyc:ABC-15-CPLXhas input GO:0015195 — provides_input_for → RHEA:13162; LIV-I uptake can supply threonine to the core oxidation; its conditional expression and ATP requirement do not demonstrate complete degradation-III flux.; Evidence: EcoCyc:ABC-15-CPLXprovides input for Entrez:948139 — enables → UniProtKB:P07913; The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.; Evidence: Entrez:948139, UniProtKB:P07913enables Entrez:945939 — enables → UniProtKB:P46883; The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.; Evidence: Entrez:945939, UniProtKB:P46883enables Entrez:945941 — enables → UniProtKB:Q47129; The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.; Evidence: Entrez:945941, UniProtKB:Q47129enables Entrez:947971 — enables → UniProtKB:P0AD96; The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.; Evidence: Entrez:947971, UniProtKB:P0AD96enables Entrez:947961 — enables → UniProtKB:P22731; The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.; Evidence: Entrez:947961, UniProtKB:P22731enables Entrez:947967 — enables → UniProtKB:P0A9S7; The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.; Evidence: Entrez:947967, UniProtKB:P0A9S7enables Entrez:947965 — enables → UniProtKB:P0AEX7; The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.; Evidence: Entrez:947965, UniProtKB:P0AEX7enables Entrez:947966 — enables → UniProtKB:P22729; The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.; Evidence: Entrez:947966, UniProtKB:P22729enables UniProtKB:P0ACJ0 — inhibits → Entrez:948139; In BW3912-derived reporters, Lrp repressed tdh expression. This primary polarity takes precedence over the native TU00225 mode+ annotation, which is retained as a source conflict. Direct tdh-promoter binding was not established by the cited ilvIH binding assay.; Evidence: PMID:1917830, EcoCyc:TU00225inhibits CHEBI:15603 — activates → Entrez:948139; Leucine increased tdh reporter expression in the study's Lrp-dependent context; this is transcriptional induction, not direct allosteric activation of Tdh.; Evidence: PMID:1917830activates EcoCyc:MONOMER0-155 — has_part → UniProtKB:P0ACJ0; The native Lrp-leucine frame includes the Lrp protein; component multiplicity is not specified. No occupancy or oligomer size is inferred from this membership.; Evidence: EcoCyc:MONOMER0-155, EcoCyc:PD00353has part EcoCyc:MONOMER0-155 — has_part → CHEBI:15603; The native Lrp-leucine frame includes L-leucine without a component coefficient; no binding stoichiometry is imposed.; Evidence: EcoCyc:MONOMER0-155has part UniProtKB:P0ACJ0 — inhibits → Entrez:947971; Primary livJ/livKHMGF reporter experiments support Lrp-dependent transcriptional repression enhanced by leucine. The named CV/EG/SH derivatives are not all MG1655; direct promoter binding was unresolved. Transport behavior under Lrp overexpression was not a simple copy of reporter polarity.; Evidence: PMID:1729203inhibits UniProtKB:P0ACJ0 — inhibits → Entrez:947961; Primary livJ/livKHMGF reporter experiments support Lrp-dependent transcriptional repression enhanced by leucine. The named CV/EG/SH derivatives are not all MG1655; direct promoter binding was unresolved. Transport behavior under Lrp overexpression was not a simple copy of reporter polarity.; Evidence: PMID:1729203inhibits UniProtKB:P0ACJ0 — inhibits → Entrez:947967; Primary livJ/livKHMGF reporter experiments support Lrp-dependent transcriptional repression enhanced by leucine. The named CV/EG/SH derivatives are not all MG1655; direct promoter binding was unresolved. Transport behavior under Lrp overexpression was not a simple copy of reporter polarity.; Evidence: PMID:1729203inhibits UniProtKB:P0ACJ0 — inhibits → Entrez:947965; Primary livJ/livKHMGF reporter experiments support Lrp-dependent transcriptional repression enhanced by leucine. The named CV/EG/SH derivatives are not all MG1655; direct promoter binding was unresolved. Transport behavior under Lrp overexpression was not a simple copy of reporter polarity.; Evidence: PMID:1729203inhibits UniProtKB:P0ACJ0 — inhibits → Entrez:947966; Primary livJ/livKHMGF reporter experiments support Lrp-dependent transcriptional repression enhanced by leucine. The named CV/EG/SH derivatives are not all MG1655; direct promoter binding was unresolved. Transport behavior under Lrp overexpression was not a simple copy of reporter polarity.; Evidence: PMID:1729203inhibits UniProtKB:Q47129 — activates → Entrez:945939; MG1655 reporter and genetic experiments support FeaR-dependent tynA expression in the tested aromatic-amine carbon/nitrogen conditions. Isolated His-tagged FeaR DNA-binding-domain experiments do not establish direct ligand binding by full-length FeaR or aminoacetone induction.; Evidence: PMID:24013633activates EcoCyc:CPLX0-7797 — activates → Entrez:945939; The native complex comment reports FNR-associated tynA transcriptional activation in anaerobic profiling (PMID12754220). The inspected 2013 aromatic-amine study found no anaerobic induction under its conditions; this context conflict does not establish direct promoter binding or anaerobic oxidase flux.; Evidence: MetaCyc:AMINEOXID-CPLX, PMID:24013633activates UniProtKB:P0AF63 — inhibits → Entrez:945939; subject experimental construct: NsrR protein expressed in the cited GUG-to-AUG translation-start construct. This is a start-codon/expression-context change, not an asserted amino-acid substitution. Exact whole construct sequence and native tynA-site geometry were not established in the accessible material.; Evidence EcoCyc:TU0-42552: The native annotation specifically reports tynA repression when the nsrR start codon was changed from GUG to AUG. (Transcription-Unit/comment; PMID26239124 paragraph); The native TU reports tynA repression in the NsrR start-codon-enhanced expression context. The accessible primary abstracts do not resolve exact direct binding at tynA; the suspicious native coordinate is not reinterpreted as a validated local site.; Evidence: EcoCyc:TU0-42552inhibits CHEBI:16828 — inhibits → UniProtKB:P0AGE4; object experimental construct: W3133-2 SstT cloned into low-copy pMST3/pMST321 and assayed in WAT9, with the primary report identifying Thr301 where the current P0AGE4 reference has Ala301. Other residue identity is not assumed; this expression/uptake result is not a native MG1655 sequence assay.; Evidence PMID:9852024: The source used W3133-2 DNA and WAT9 transformants; its deduced SstT sequence had Thr301 instead of the then-reference Ala301. (main text: cloning, sequencing and Figure 1; tryptophan-expression paragraph); Growth with 5 mM tryptophan reduced measured serine transport and sstT RNA in the reported strains/constructs. The proposed effector could be tryptophan or its metabolite; this is expression control, not direct inhibition or proof that tryptophan is transported.; Evidence: PMID:9852024inhibits CHEBI:28545 — activates → UniProtKB:P0AGE4; object experimental construct: SstT carrying eight successive C-terminal histidines, overproduced from pTSTH under the trc promoter, Ni-NTA purified and reconstituted in liposomes. The reported 20-residue N terminus lacked initiating methionine; full construct identity with current P0AGE4 or the older Thr301 variant is not assumed.; Evidence PMID:12097162: The study added eight histidine codons at the sstT 3′ end, purified the fusion by Ni-NTA and reconstituted it into liposomes; only its first 20 N-terminal residues were experimentally sequenced. (issuing primary abstract); The reviewed activity-regulation annotation assigns valinomycin activation and monensin inhibition to SstT. These effects concern the cited serine-uptake assay; unspecified monensin is not assigned to monensin A.; Evidence: UniProtKB:P0AGE4, PMID:12097162activates CHEBI:3259 — inhibits → UniProtKB:P0AAD8; CCCP strongly inhibited threonine uptake in the anaerobically induced MC4100/TH16-derived TdcC assays; the result supports dependence on proton motive force. Historical TdcC was reported as 431 residues, whereas current P0AAD8 is 443; the complete assayed sequence is not established. This does not identify an engineered truncation or a distinct assayed variant.; Evidence: PMID:2115866, PMID:2115866, UniProtKB:P0AAD8inhibits CHEBI:33191 — inhibits → UniProtKB:P0AAD8; KCN partially inhibited threonine uptake in the anaerobically induced TdcC assays. Sodium/monensin effects differed from the SstT system; this is an energetic whole-cell treatment, not a purified transporter binding assay. Historical TdcC was reported as 431 residues, whereas current P0AAD8 is 443; the complete assayed sequence is not established. This does not identify an engineered truncation or a distinct assayed variant.; Evidence: PMID:2115866, PMID:2115866, UniProtKB:P0AAD8inhibits CHEBI:17115 — inhibits → UniProtKB:P0AAD8; Excess L-serine strongly reduced radiolabeled threonine uptake in the TdcC-expressing cell assay; competition does not imply an allosteric inhibitor. Historical TdcC was reported as 431 residues, whereas current P0AAD8 is 443; the complete assayed sequence is not established. This does not identify an engineered truncation or a distinct assayed variant.; Evidence: PMID:2115866, PMID:2115866, UniProtKB:P0AAD8inhibits CHEBI:15603 — inhibits → UniProtKB:P0AAD8; Excess L-leucine reduced TdcC-associated threonine uptake by about half in the cell competition assay. This differs from the transcriptional Lrp/leucine claims. Historical TdcC was reported as 431 residues, whereas current P0AAD8 is 443; the complete assayed sequence is not established. This does not identify an engineered truncation or a distinct assayed variant.; Evidence: PMID:2115866, PMID:2115866, UniProtKB:P0AAD8inhibits CHEBI:15699 — inhibits → UniProtKB:P0AAD8; Excess homoserine reduced TdcC-associated threonine uptake in the primary competition experiment; this is whole-cell substrate competition. Historical TdcC was reported as 431 residues, whereas current P0AAD8 is 443; the complete assayed sequence is not established. This does not identify an engineered truncation or a distinct assayed variant.; Evidence: PMID:2115866, PMID:2115866, UniProtKB:P0AAD8inhibits CHEBI:747879 — inhibits → MetaCyc:THREODEHYD-CPLX; Iodoacetate modification of one cysteine per Tdh subunit caused complete activity loss; the isolated peptide placed it at Cys38. The pinned ChEBI native label is misspelled iodoacetacte, while its definition/structure identify iodoacetate.; Evidence: PMID:2007567inhibits CHEBI:44975 — inhibits → MetaCyc:THREODEHYD-CPLX; Removing Tdh-associated zinc with 1,10-phenanthroline correlated with declining activity and eventually yielded an unstable protein; this is a chelation experiment, not an endogenous control.; Evidence: PMID:2007567inhibits CHEBI:15379 — inhibits → EcoCyc:CPLX0-7797; object molecular state: Active [4Fe-4S]-containing FNR dimer under anaerobic conditions; oxygen changes this molecular state. The native complex frame is retained without claiming that its identity fixes every experimental metal/redox state.; Evidence EcoCyc:CPLX0-7797: Anaerobic [4Fe-4S] acquisition promotes the active FNR dimer; oxygen oxidizes the cluster and inactivates it. (Protein/comment: second paragraph); The native FNR comment describes oxygen-mediated oxidation of the active [4Fe-4S] form to a [2Fe-2S] form and loss of the active dimer. This bounds the anaerobic regulatory context; it is not direct TynA inhibition.; Evidence: EcoCyc:CPLX0-7797inhibits L-threonine zwitterion; CHEBI:57926; Declared type: small_molecule small molecule L-threonine zwitterion NAD(1-); CHEBI:57540; Declared type: small_molecule small molecule NAD(1-) L-2-amino-3-oxobutanoic acid zwitterion; CHEBI:78948; Declared type: small_molecule small molecule L-2-amino-3-oxobutanoic acid zwitterion NADH(2-); CHEBI:57945; Declared type: small_molecule small molecule NADH(2-) hydron; CHEBI:15378; Declared type: small_molecule small molecule hydron ammonioacetone; CHEBI:58320; Declared type: small_molecule small molecule ammonioacetone carbon dioxide; CHEBI:16526; Declared type: small_molecule small molecule carbon dioxide dioxygen; CHEBI:15379; Declared type: small_molecule small molecule dioxygen water; CHEBI:15377; Declared type: small_molecule small molecule water methylglyoxal; CHEBI:17158; Declared type: small_molecule small molecule methylglyoxal hydrogen peroxide; CHEBI:16240; Declared type: small_molecule small molecule hydrogen peroxide ammonium; CHEBI:28938; Declared type: small_molecule small molecule ammonium sodium(1+); CHEBI:29101; Declared type: small_molecule small molecule sodium(1+) L-threonine 3-dehydrogenase; UniProtKB:P07913; Declared type: protein protein L-threonine 3-dehydrogenase Primary amine oxidase; UniProtKB:P46883; Declared type: protein protein Primary amine oxidase Serine/threonine transporter SstT; UniProtKB:P0AGE4; Declared type: protein protein Serine/threonine transporter SstT High-affinity branched-chain amino acid transport ATP-binding protein LivF; UniProtKB:P22731; Declared type: protein protein High-affinity branched-chain amino acid transport ATP- binding protein LivF High-affinity branched-chain amino acid transport ATP-binding protein LivG; UniProtKB:P0A9S7; Declared type: protein protein High-affinity branched-chain amino acid transport ATP- binding protein LivG High-affinity branched-chain amino acid transport system permease protein LivH; UniProtKB:P0AEX7; Declared type: protein protein High-affinity branched-chain amino acid transport system permease protein LivH High-affinity branched-chain amino acid transport system permease protein LivM; UniProtKB:P22729; Declared type: protein protein High-affinity branched-chain amino acid transport system permease protein LivM Leu/Ile/Val-binding protein; UniProtKB:P0AD96; Declared type: protein protein Leu/Ile/Val-binding protein Threonine/serine transporter TdcC; UniProtKB:P0AAD8; Declared type: protein protein Threonine/serine transporter TdcC Transcriptional activator FeaR; UniProtKB:Q47129; Declared type: protein protein Transcriptional activator FeaR Leucine-responsive regulatory protein; UniProtKB:P0ACJ0; Declared type: protein protein Leucine-responsive regulatory protein Fumarate and nitrate reduction regulatory protein; UniProtKB:P0A9E5; Declared type: protein protein Fumarate and nitrate reduction regulatory protein HTH-type transcriptional repressor NsrR; UniProtKB:P0AF63; Declared type: protein protein HTH-type transcriptional repressor NsrR Divalent metal cation transporter MntH; UniProtKB:P0A769; Declared type: protein protein Divalent metal cation transporter MntH DNA protection during starvation protein; UniProtKB:P0ABT2; Declared type: protein protein DNA protection during starvation protein hypothetical protein [Escherichia coli str. K-12 substr. MG1655]; NCBIProtein:AAB18566.1; Declared type: protein protein hypothetical protein [Escherichia coli str. K-12 substr. MG1655] threonine dehydrogenase; MetaCyc:THREODEHYD-CPLX; Declared type: complex complex threonine dehydrogenase copper-containing amine oxidase; MetaCyc:AMINEOXID-CPLX; Declared type: complex complex copper-containing amine oxidase branched chain amino acid / phenylalanine ABC transporter; MetaCyc:ABC-15-CPLX; Declared type: complex complex branched chain amino acid / phenylalanine ABC transporter stationary phase nucleoid component that sequesters iron and protects DNA from damage; EcoCyc:CPLX0-1521; Declared type: complex complex stationary phase nucleoid component that sequesters iron and protects DNA from damage DNA-binding transcriptional dual regulator NsrR; EcoCyc:CPLX0-7756; Declared type: complex complex DNA-binding transcriptional dual regulator NsrR DNA-binding transcriptional dual regulator FNR; EcoCyc:CPLX0-7797; Declared type: complex complex DNA-binding transcriptional dual regulator FNR DNA-binding transcriptional dual regulator Lrp-L-leucine; EcoCyc:MONOMER0-155; Declared type: complex complex DNA-binding transcriptional dual regulator Lrp-L-leucine periplasmic space; GO:0042597; Declared type: cellular_component cellular component periplasmic space cytoplasm; GO:0005737; Declared type: cellular_component cellular component cytoplasm plasma membrane; GO:0005886; Declared type: cellular_component cellular component plasma membrane zinc(2+); CHEBI:29105; Declared type: cofactor cofactor zinc(2+) cobalt(2+); CHEBI:48828; Declared type: cofactor cofactor cobalt(2+) cadmium(2+); CHEBI:48775; Declared type: cofactor cofactor cadmium(2+) manganese(2+); CHEBI:29035; Declared type: cofactor cofactor manganese(2+) iron(2+); CHEBI:29033; Declared type: cofactor cofactor iron(2+) copper cation; CHEBI:23378; Declared type: cofactor cofactor copper cation calcium(2+); CHEBI:29108; Declared type: cofactor cofactor calcium(2+) L-topaquinone(1-) residue; CHEBI:79027; Declared type: cofactor cofactor L-topaquinone(1-) residue divalent metal cation; CHEBI:60240; Declared type: cofactor cofactor divalent metal cation tetra-mu3-sulfido-tetrairon; CHEBI:49883; Declared type: cofactor cofactor tetra-mu3-sulfido-tetrairon di-mu-sulfido-diiron; CHEBI:190135; Declared type: cofactor cofactor di-mu-sulfido-diiron ethylenediaminetetraacetic acid; CHEBI:4735; Declared type: small_molecule small molecule ethylenediaminetetraacetic acid 2-Hydrazinopyridine; PubChem:78645; Declared type: small_molecule small molecule 2-Hydrazinopyridine 1,4-dithiothreitol; CHEBI:18320; Declared type: small_molecule small molecule 1,4-dithiothreitol TCEP; CHEBI:63213; Declared type: small_molecule small molecule TCEP ATP(4-); CHEBI:30616; Declared type: small_molecule small molecule ATP(4-) tdh; Entrez:948139; Declared type: gene gene tdh tynA; Entrez:945939; Declared type: gene gene tynA feaR; Entrez:945941; Declared type: gene gene feaR livJ; Entrez:947971; Declared type: gene gene livJ livF; Entrez:947961; Declared type: gene gene livF livG; Entrez:947967; Declared type: gene gene livG livH; Entrez:947965; Declared type: gene gene livH livM; Entrez:947966; Declared type: gene gene livM L-leucine; CHEBI:15603; Declared type: small_molecule small molecule L-leucine L-tryptophan; CHEBI:16828; Declared type: small_molecule small molecule L-tryptophan valinomycin; CHEBI:28545; Declared type: small_molecule small molecule valinomycin CCCP; CHEBI:3259; Declared type: small_molecule small molecule CCCP potassium cyanide; CHEBI:33191; Declared type: small_molecule small molecule potassium cyanide L-serine; CHEBI:17115; Declared type: small_molecule small molecule L-serine L-homoserine; CHEBI:15699; Declared type: small_molecule small molecule L-homoserine iodoacetacte; CHEBI:747879; Declared type: small_molecule small molecule iodoacetacte 1,10-phenanthroline; CHEBI:44975; Declared type: small_molecule small molecule 1,10-phenanthroline L-threonine + NAD(+) => (2S)-2-amino-3-oxobutanoate + NADH + H(+); RHEA:13162; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity L-threonine + NAD(+) => (2S)-2-amino-3-oxobutanoate + NADH + H(+) (2S)-2-amino-3-oxobutanoate + H(+) => aminoacetone + CO2; RHEA:25654; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity (2S)-2-amino-3-oxobutanoate + H(+) => aminoacetone + CO2 aminoacetone + O2 + H2O => methylglyoxal + H2O2 + NH4(+); RHEA:28187; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity aminoacetone + O2 + H2O => methylglyoxal + H2O2 + NH4(+) L-threonine(out) + Na(+)(out) => L-threonine(in) + Na(+)(in); RHEA:70001; Declared type: molecular_activity; Source reaction direction: right_to_left molecular activity L-threonine(out) + Na(+)(out) => L-threonine(in) + Na(+)(in) L-threonine(out) + H(+)(out) => L-threonine(in) + H(+)(in); RHEA:28885; Declared type: molecular_activity; Source reaction direction: right_to_left molecular activity L-threonine(out) + H(+)(out) => L-threonine(in) + H(+)(in) superpathway of L-threonine metabolism; MetaCyc:THREOCAT-PWY; Declared type: pathway pathway superpathway of L-threonine metabolism methylglyoxal degradation I; MetaCyc:PWY-5386; Declared type: pathway pathway methylglyoxal degradation I Threonine Biosynthesis; PathBank:SMP0000837; Declared type: pathway pathway Threonine Biosynthesis L-threonine transmembrane transporter activity; GO:0015195; Declared type: molecular_activity molecular activity L-threonine transmembrane transporter activity L-threonine degradation III (to methylglyoxal); MetaCyc:THRDLCTCAT-PWY; Declared type: pathway pathway L-threonine degradation III (to methylglyoxal) hypothetical protein [Escherichia coli str. K-12 substr. MG1655]; NCBIProtein:AAB18566.1; Declared type: protein; experimental construct: N-terminal 6×His-tagged orf382 amplified from E. coli MG1655 using AAB18566.1 as reference, expressed from pET28a(+) in BL21(DE3) and purified by Ni-NTA. The complete construct sequence was not reported; this assay endpoint does not assert identity with the bare reference or current UniProtKB:P37686 sequence.; Evidence PMID:24651643: The study cloned MG1655 orf382 using AAB18566.1 as reference, reported no mutation in the sequenced insert, expressed an N-terminal 6×His fusion in BL21(DE3), and purified the recombinant preparation by Ni-NTA. (Publisher PDF pp. 749–751; Materials and Methods, Molecular Cloning, Protein Expression, Purification, and Enzymatic Activity Assays; Results and Discussion, Molecular Cloning, Protein Expression, and Purification) experimental construct hypothetical protein [Escherichia coli str. K-12 substr. MG1655] [experimental construct: N-terminal 6×His-tagged orf382 amplified from E. coli MG1655 using AAB18566.1 as reference,…] hypothetical protein [Escherichia coli str. K-12 substr. MG1655]; NCBIProtein:AAB18566.1; Declared type: protein; experimental construct: N-terminal 6×His-tagged orf382 amplified from E. coli MG1655 using AAB18566.1 as reference, expressed from pET28a(+) in BL21(DE3) and purified by Ni-NTA. The complete construct sequence was not reported; this assay endpoint does not assert identity with the bare reference or current UniProtKB:P37686 sequence.; Evidence PMID:24651643: The study cloned MG1655 orf382 using AAB18566.1 as reference, reported no mutation in the sequenced insert, expressed an N-terminal 6×His fusion in BL21(DE3), and purified the recombinant preparation by Ni-NTA. (Publisher PDF pp. 749–751; Materials and Methods, Molecular Cloning, Protein Expression, Purification, and Enzymatic Activity Assays; Results and Discussion, Molecular Cloning, Protein Expression, and Purification) experimental construct hypothetical protein [Escherichia coli str. K-12 substr. MG1655] [experimental construct: N-terminal 6×His-tagged orf382 amplified from E. coli MG1655 using AAB18566.1 as reference,…] hypothetical protein [Escherichia coli str. K-12 substr. MG1655]; NCBIProtein:AAB18566.1; Declared type: protein; experimental construct: N-terminal 6×His-tagged orf382 amplified from E. coli MG1655 using AAB18566.1 as reference, expressed from pET28a(+) in BL21(DE3) and purified by Ni-NTA. The complete construct sequence was not reported; this assay endpoint does not assert identity with the bare reference or current UniProtKB:P37686 sequence.; Evidence PMID:24651643: The study cloned MG1655 orf382 using AAB18566.1 as reference, reported no mutation in the sequenced insert, expressed an N-terminal 6×His fusion in BL21(DE3), and purified the recombinant preparation by Ni-NTA. (Publisher PDF pp. 749–751; Materials and Methods, Molecular Cloning, Protein Expression, Purification, and Enzymatic Activity Assays; Results and Discussion, Molecular Cloning, Protein Expression, and Purification) experimental construct hypothetical protein [Escherichia coli str. K-12 substr. MG1655] [experimental construct: N-terminal 6×His-tagged orf382 amplified from E. coli MG1655 using AAB18566.1 as reference,…] threonine dehydrogenase; MetaCyc:THREODEHYD-CPLX; Declared type: complex; molecular state: Tdh assayed after in-vitro Fe(II) loading or in the specified peroxide-stressed E. coli preparations. Metal state and peroxide exposure are part of this claim; a fixed native metal occupancy or complete assay-construct sequence is not asserted.; Evidence PMID:22411989: The work compared metal-reconstituted purified Tdh with extracts/cells of catalase- or peroxide-scavenging-deficient strains. (Experimental Procedures, In Vitro/In Vivo Studies of Enzyme Oxidation; Figures 1–3) molecular state threonine dehydrogenase [molecular state: Tdh assayed after in-vitro Fe(II) loading or in the specified peroxide-stressed E. coli…] threonine dehydrogenase; MetaCyc:THREODEHYD-CPLX; Declared type: complex; molecular state: Tdh assayed after in-vitro Fe(II) loading or in the specified peroxide-stressed E. coli preparations. Metal state and peroxide exposure are part of this claim; a fixed native metal occupancy or complete assay-construct sequence is not asserted.; Evidence PMID:22411989: The work compared metal-reconstituted purified Tdh with extracts/cells of catalase- or peroxide-scavenging-deficient strains. (Experimental Procedures, In Vitro/In Vivo Studies of Enzyme Oxidation; Figures 1–3) molecular state threonine dehydrogenase [molecular state: Tdh assayed after in-vitro Fe(II) loading or in the specified peroxide-stressed E. coli…] threonine dehydrogenase; MetaCyc:THREODEHYD-CPLX; Declared type: complex; molecular state: Tdh assayed after in-vitro Fe(II) loading or in the specified peroxide-stressed E. coli preparations. Metal state and peroxide exposure are part of this claim; a fixed native metal occupancy or complete assay-construct sequence is not asserted.; Evidence PMID:22411989: The work compared metal-reconstituted purified Tdh with extracts/cells of catalase- or peroxide-scavenging-deficient strains. (Experimental Procedures, In Vitro/In Vivo Studies of Enzyme Oxidation; Figures 1–3) molecular state threonine dehydrogenase [molecular state: Tdh assayed after in-vitro Fe(II) loading or in the specified peroxide-stressed E. coli…] HTH-type transcriptional repressor NsrR; UniProtKB:P0AF63; Declared type: protein; experimental construct: NsrR protein expressed in the cited GUG-to-AUG translation-start construct. This is a start-codon/expression-context change, not an asserted amino-acid substitution. Exact whole construct sequence and native tynA-site geometry were not established in the accessible material.; Evidence EcoCyc:TU0-42552: The native annotation specifically reports tynA repression when the nsrR start codon was changed from GUG to AUG. (Transcription-Unit/comment; PMID26239124 paragraph) experimental construct HTH-type transcriptional repressor NsrR [experimental construct: NsrR protein expressed in the cited GUG- to-AUG translation-start construct. This is a start-…] Serine/threonine transporter SstT; UniProtKB:P0AGE4; Declared type: protein; experimental construct: W3133-2 SstT cloned into low-copy pMST3/pMST321 and assayed in WAT9, with the primary report identifying Thr301 where the current P0AGE4 reference has Ala301. Other residue identity is not assumed; this expression/uptake result is not a native MG1655 sequence assay.; Evidence PMID:9852024: The source used W3133-2 DNA and WAT9 transformants; its deduced SstT sequence had Thr301 instead of the then-reference Ala301. (main text: cloning, sequencing and Figure 1; tryptophan-expression paragraph) experimental construct Serine/threonine transporter SstT [experimental construct: W3133-2 SstT cloned into low-copy pMST3/pMST321 and assayed in WAT9, with the primary report…] Serine/threonine transporter SstT; UniProtKB:P0AGE4; Declared type: protein; experimental construct: SstT carrying eight successive C-terminal histidines, overproduced from pTSTH under the trc promoter, Ni-NTA purified and reconstituted in liposomes. The reported 20-residue N terminus lacked initiating methionine; full construct identity with current P0AGE4 or the older Thr301 variant is not assumed.; Evidence PMID:12097162: The study added eight histidine codons at the sstT 3′ end, purified the fusion by Ni-NTA and reconstituted it into liposomes; only its first 20 N-terminal residues were experimentally sequenced. (issuing primary abstract) experimental construct Serine/threonine transporter SstT [experimental construct: SstT carrying eight successive C-terminal histidines, overproduced from pTSTH under the trc…] DNA-binding transcriptional dual regulator FNR; EcoCyc:CPLX0-7797; Declared type: complex; molecular state: Active [4Fe-4S]-containing FNR dimer under anaerobic conditions; oxygen changes this molecular state. The native complex frame is retained without claiming that its identity fixes every experimental metal/redox state.; Evidence EcoCyc:CPLX0-7797: Anaerobic [4Fe-4S] acquisition promotes the active FNR dimer; oxygen oxidizes the cluster and inactivates it. (Protein/comment: second paragraph) molecular state DNA-binding transcriptional dual regulator FNR [molecular state: Active [4Fe-4S]-containing FNR dimer under anaerobic conditions; oxygen changes this molecular…]

Components and activities

Declared biological components and source reaction directions
NodeKind or roleSource direction
Escherichia coli K-12
NCBITaxon:83333		taxon
Escherichia coli str. K-12 substr. MG1655
NCBITaxon:511145		taxon
L-threonine zwitterion
CHEBI:57926		small molecule
NAD(1-)
CHEBI:57540		small molecule
L-2-amino-3-oxobutanoic acid zwitterion
CHEBI:78948		small molecule
NADH(2-)
CHEBI:57945		small molecule
hydron
CHEBI:15378		small molecule
ammonioacetone
CHEBI:58320		small molecule
carbon dioxide
CHEBI:16526		small molecule
dioxygen
CHEBI:15379		small molecule
water
CHEBI:15377		small molecule
methylglyoxal
CHEBI:17158		small molecule
hydrogen peroxide
CHEBI:16240		small molecule
ammonium
CHEBI:28938		small molecule
sodium(1+)
CHEBI:29101		small molecule
L-threonine 3-dehydrogenase
UniProtKB:P07913		protein
Primary amine oxidase
UniProtKB:P46883		protein
Serine/threonine transporter SstT
UniProtKB:P0AGE4		protein
High-affinity branched-chain amino acid transport ATP-binding protein LivF
UniProtKB:P22731		protein
High-affinity branched-chain amino acid transport ATP-binding protein LivG
UniProtKB:P0A9S7		protein
High-affinity branched-chain amino acid transport system permease protein LivH
UniProtKB:P0AEX7		protein
High-affinity branched-chain amino acid transport system permease protein LivM
UniProtKB:P22729		protein
Leu/Ile/Val-binding protein
UniProtKB:P0AD96		protein
Threonine/serine transporter TdcC
UniProtKB:P0AAD8		protein
Transcriptional activator FeaR
UniProtKB:Q47129		protein
Leucine-responsive regulatory protein
UniProtKB:P0ACJ0		protein
Fumarate and nitrate reduction regulatory protein
UniProtKB:P0A9E5		protein
HTH-type transcriptional repressor NsrR
UniProtKB:P0AF63		protein
Divalent metal cation transporter MntH
UniProtKB:P0A769		protein
DNA protection during starvation protein
UniProtKB:P0ABT2		protein
hypothetical protein [Escherichia coli str. K-12 substr. MG1655]
NCBIProtein:AAB18566.1		protein
threonine dehydrogenase
MetaCyc:THREODEHYD-CPLX		complex
copper-containing amine oxidase
MetaCyc:AMINEOXID-CPLX		complex
branched chain amino acid / phenylalanine ABC transporter
MetaCyc:ABC-15-CPLX		complex
stationary phase nucleoid component that sequesters iron and protects DNA from damage
EcoCyc:CPLX0-1521		complex
DNA-binding transcriptional dual regulator NsrR
EcoCyc:CPLX0-7756		complex
DNA-binding transcriptional dual regulator FNR
EcoCyc:CPLX0-7797		complex
DNA-binding transcriptional dual regulator Lrp-L-leucine
EcoCyc:MONOMER0-155		complex
periplasmic space
GO:0042597		cellular component
cytoplasm
GO:0005737		cellular component
plasma membrane
GO:0005886		cellular component
zinc(2+)
CHEBI:29105		cofactor
cobalt(2+)
CHEBI:48828		cofactor
cadmium(2+)
CHEBI:48775		cofactor
manganese(2+)
CHEBI:29035		cofactor
iron(2+)
CHEBI:29033		cofactor
copper cation
CHEBI:23378		cofactor
calcium(2+)
CHEBI:29108		cofactor
L-topaquinone(1-) residue
CHEBI:79027		cofactor
divalent metal cation
CHEBI:60240		cofactor
tetra-mu3-sulfido-tetrairon
CHEBI:49883		cofactor
di-mu-sulfido-diiron
CHEBI:190135		cofactor
ethylenediaminetetraacetic acid
CHEBI:4735		small molecule
2-Hydrazinopyridine
PubChem:78645		small molecule
1,4-dithiothreitol
CHEBI:18320		small molecule
TCEP
CHEBI:63213		small molecule
ATP(4-)
CHEBI:30616		small molecule
tdh
Entrez:948139		gene
tynA
Entrez:945939		gene
feaR
Entrez:945941		gene
livJ
Entrez:947971		gene
livF
Entrez:947961		gene
livG
Entrez:947967		gene
livH
Entrez:947965		gene
livM
Entrez:947966		gene
L-leucine
CHEBI:15603		small molecule
L-tryptophan
CHEBI:16828		small molecule
valinomycin
CHEBI:28545		small molecule
CCCP
CHEBI:3259		small molecule
potassium cyanide
CHEBI:33191		small molecule
L-serine
CHEBI:17115		small molecule
L-homoserine
CHEBI:15699		small molecule
iodoacetacte
CHEBI:747879		small molecule
1,10-phenanthroline
CHEBI:44975		small molecule
L-threonine + NAD(+) => (2S)-2-amino-3-oxobutanoate + NADH + H(+)
RHEA:13162		molecular activityleft to right
(2S)-2-amino-3-oxobutanoate + H(+) => aminoacetone + CO2
RHEA:25654		molecular activityleft to right
aminoacetone + O2 + H2O => methylglyoxal + H2O2 + NH4(+)
RHEA:28187		molecular activityleft to right
L-threonine(out) + Na(+)(out) => L-threonine(in) + Na(+)(in)
RHEA:70001		molecular activityright to left
L-threonine(out) + H(+)(out) => L-threonine(in) + H(+)(in)
RHEA:28885		molecular activityright to left
superpathway of L-threonine metabolism
MetaCyc:THREOCAT-PWY		pathway
methylglyoxal degradation I
MetaCyc:PWY-5386		pathway
Threonine Biosynthesis
PathBank:SMP0000837		pathway
L-threonine transmembrane transporter activity
GO:0015195		molecular activity

Mechanistic edges

Mechanistic edges and their cited evidence
SubjectPredicate and descriptionObjectEvidence
L-threonine zwitterion
CHEBI:57926		consumes

The directed native Rhea reaction has CHEBI:57926 on its substrates side with coefficient 1.

L-threonine + NAD(+) => (2S)-2-amino-3-oxobutanoate + NADH + H(+)
RHEA:13162
  • RHEA:13162

    Source assertion: The directed native Rhea reaction has CHEBI:57926 on its substrates side with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/13162/rh:substrates -> http://rdf.rhea-db.org/13161_L -> http://rdf.rhea-db.org/Participant_13161_compound_3255 -> http://rdf.rhea-db.org/Compound_3255/rh:chebi
NAD(1-)
CHEBI:57540		consumes

The directed native Rhea reaction has CHEBI:57540 on its substrates side with coefficient 1.

L-threonine + NAD(+) => (2S)-2-amino-3-oxobutanoate + NADH + H(+)
RHEA:13162
  • RHEA:13162

    Source assertion: The directed native Rhea reaction has CHEBI:57540 on its substrates side with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/13162/rh:substrates -> http://rdf.rhea-db.org/13161_L -> http://rdf.rhea-db.org/Participant_13161_compound_3484 -> http://rdf.rhea-db.org/Compound_3484/rh:chebi
L-threonine + NAD(+) => (2S)-2-amino-3-oxobutanoate + NADH + H(+)
RHEA:13162		produces

The directed native Rhea reaction has CHEBI:78948 on its products side with coefficient 1.

L-2-amino-3-oxobutanoic acid zwitterion
CHEBI:78948
  • RHEA:13162

    Source assertion: The directed native Rhea reaction has CHEBI:78948 on its products side with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/13162/rh:products -> http://rdf.rhea-db.org/13161_R -> http://rdf.rhea-db.org/Participant_13161_compound_10587 -> http://rdf.rhea-db.org/Compound_10587/rh:chebi
L-threonine + NAD(+) => (2S)-2-amino-3-oxobutanoate + NADH + H(+)
RHEA:13162		produces

The directed native Rhea reaction has CHEBI:57945 on its products side with coefficient 1.

NADH(2-)
CHEBI:57945
  • RHEA:13162

    Source assertion: The directed native Rhea reaction has CHEBI:57945 on its products side with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/13162/rh:products -> http://rdf.rhea-db.org/13161_R -> http://rdf.rhea-db.org/Participant_13161_compound_1650 -> http://rdf.rhea-db.org/Compound_1650/rh:chebi
L-threonine + NAD(+) => (2S)-2-amino-3-oxobutanoate + NADH + H(+)
RHEA:13162		produces

The directed native Rhea reaction has CHEBI:15378 on its products side with coefficient 1.

hydron
CHEBI:15378
  • RHEA:13162

    Source assertion: The directed native Rhea reaction has CHEBI:15378 on its products side with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/13162/rh:products -> http://rdf.rhea-db.org/13161_R -> http://rdf.rhea-db.org/Participant_13161_compound_3249 -> http://rdf.rhea-db.org/Compound_3249/rh:chebi
L-2-amino-3-oxobutanoic acid zwitterion
CHEBI:78948		consumes

The directed native Rhea reaction has CHEBI:78948 on its substrates side with coefficient 1.

(2S)-2-amino-3-oxobutanoate + H(+) => aminoacetone + CO2
RHEA:25654
  • RHEA:25654

    Source assertion: The directed native Rhea reaction has CHEBI:78948 on its substrates side with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/25654/rh:substrates -> http://rdf.rhea-db.org/25653_L -> http://rdf.rhea-db.org/Participant_25653_compound_10587 -> http://rdf.rhea-db.org/Compound_10587/rh:chebi
hydron
CHEBI:15378		consumes

The directed native Rhea reaction has CHEBI:15378 on its substrates side with coefficient 1.

(2S)-2-amino-3-oxobutanoate + H(+) => aminoacetone + CO2
RHEA:25654
  • RHEA:25654

    Source assertion: The directed native Rhea reaction has CHEBI:15378 on its substrates side with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/25654/rh:substrates -> http://rdf.rhea-db.org/25653_L -> http://rdf.rhea-db.org/Participant_25653_compound_3249 -> http://rdf.rhea-db.org/Compound_3249/rh:chebi
(2S)-2-amino-3-oxobutanoate + H(+) => aminoacetone + CO2
RHEA:25654		produces

The directed native Rhea reaction has CHEBI:58320 on its products side with coefficient 1.

ammonioacetone
CHEBI:58320
  • RHEA:25654

    Source assertion: The directed native Rhea reaction has CHEBI:58320 on its products side with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/25654/rh:products -> http://rdf.rhea-db.org/25653_R -> http://rdf.rhea-db.org/Participant_25653_compound_1881 -> http://rdf.rhea-db.org/Compound_1881/rh:chebi
(2S)-2-amino-3-oxobutanoate + H(+) => aminoacetone + CO2
RHEA:25654		produces

The directed native Rhea reaction has CHEBI:16526 on its products side with coefficient 1.

carbon dioxide
CHEBI:16526
  • RHEA:25654

    Source assertion: The directed native Rhea reaction has CHEBI:16526 on its products side with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/25654/rh:products -> http://rdf.rhea-db.org/25653_R -> http://rdf.rhea-db.org/Participant_25653_compound_4391 -> http://rdf.rhea-db.org/Compound_4391/rh:chebi
ammonioacetone
CHEBI:58320		consumes

The directed native Rhea reaction has CHEBI:58320 on its substrates side with coefficient 1.

aminoacetone + O2 + H2O => methylglyoxal + H2O2 + NH4(+)
RHEA:28187
  • RHEA:28187

    Source assertion: The directed native Rhea reaction has CHEBI:58320 on its substrates side with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/28187/rh:substrates -> http://rdf.rhea-db.org/28186_L -> http://rdf.rhea-db.org/Participant_28186_compound_1881 -> http://rdf.rhea-db.org/Compound_1881/rh:chebi
dioxygen
CHEBI:15379		consumes

The directed native Rhea reaction has CHEBI:15379 on its substrates side with coefficient 1.

aminoacetone + O2 + H2O => methylglyoxal + H2O2 + NH4(+)
RHEA:28187
  • RHEA:28187

    Source assertion: The directed native Rhea reaction has CHEBI:15379 on its substrates side with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/28187/rh:substrates -> http://rdf.rhea-db.org/28186_L -> http://rdf.rhea-db.org/Participant_28186_compound_1198 -> http://rdf.rhea-db.org/Compound_1198/rh:chebi
water
CHEBI:15377		consumes

The directed native Rhea reaction has CHEBI:15377 on its substrates side with coefficient 1.

aminoacetone + O2 + H2O => methylglyoxal + H2O2 + NH4(+)
RHEA:28187
  • RHEA:28187

    Source assertion: The directed native Rhea reaction has CHEBI:15377 on its substrates side with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/28187/rh:substrates -> http://rdf.rhea-db.org/28186_L -> http://rdf.rhea-db.org/Participant_28186_compound_1283 -> http://rdf.rhea-db.org/Compound_1283/rh:chebi
aminoacetone + O2 + H2O => methylglyoxal + H2O2 + NH4(+)
RHEA:28187		produces

The directed native Rhea reaction has CHEBI:17158 on its products side with coefficient 1.

methylglyoxal
CHEBI:17158
  • RHEA:28187

    Source assertion: The directed native Rhea reaction has CHEBI:17158 on its products side with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/28187/rh:products -> http://rdf.rhea-db.org/28186_R -> http://rdf.rhea-db.org/Participant_28186_compound_4547 -> http://rdf.rhea-db.org/Compound_4547/rh:chebi
aminoacetone + O2 + H2O => methylglyoxal + H2O2 + NH4(+)
RHEA:28187		produces

The directed native Rhea reaction has CHEBI:16240 on its products side with coefficient 1.

hydrogen peroxide
CHEBI:16240
  • RHEA:28187

    Source assertion: The directed native Rhea reaction has CHEBI:16240 on its products side with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/28187/rh:products -> http://rdf.rhea-db.org/28186_R -> http://rdf.rhea-db.org/Participant_28186_compound_3075 -> http://rdf.rhea-db.org/Compound_3075/rh:chebi
aminoacetone + O2 + H2O => methylglyoxal + H2O2 + NH4(+)
RHEA:28187		produces

The directed native Rhea reaction has CHEBI:28938 on its products side with coefficient 1.

ammonium
CHEBI:28938
  • RHEA:28187

    Source assertion: The directed native Rhea reaction has CHEBI:28938 on its products side with coefficient 1.

    Source locationhttp://rdf.rhea-db.org/28187/rh:products -> http://rdf.rhea-db.org/28186_R -> http://rdf.rhea-db.org/Participant_28186_compound_1012 -> http://rdf.rhea-db.org/Compound_1012/rh:chebi
L-threonine zwitterion
CHEBI:57926		consumes

The directed native Rhea reaction has CHEBI:57926 on its substrates side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.

L-threonine(out) + Na(+)(out) => L-threonine(in) + Na(+)(in)
RHEA:70001
  • RHEA:70001

    Source assertion: The directed native Rhea reaction has CHEBI:57926 on its substrates side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.

    Source locationhttp://rdf.rhea-db.org/70001/rh:substrates -> http://rdf.rhea-db.org/69999_R -> http://rdf.rhea-db.org/Participant_69999_compound_3255_out -> http://rdf.rhea-db.org/Compound_3255/rh:chebi
sodium(1+)
CHEBI:29101		consumes

The directed native Rhea reaction has CHEBI:29101 on its substrates side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.

L-threonine(out) + Na(+)(out) => L-threonine(in) + Na(+)(in)
RHEA:70001
  • RHEA:70001

    Source assertion: The directed native Rhea reaction has CHEBI:29101 on its substrates side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.

    Source locationhttp://rdf.rhea-db.org/70001/rh:substrates -> http://rdf.rhea-db.org/69999_R -> http://rdf.rhea-db.org/Participant_69999_compound_2426_out -> http://rdf.rhea-db.org/Compound_2426/rh:chebi
L-threonine(out) + Na(+)(out) => L-threonine(in) + Na(+)(in)
RHEA:70001		produces

The directed native Rhea reaction has CHEBI:57926 on its products side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.

L-threonine zwitterion
CHEBI:57926
  • RHEA:70001

    Source assertion: The directed native Rhea reaction has CHEBI:57926 on its products side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.

    Source locationhttp://rdf.rhea-db.org/70001/rh:products -> http://rdf.rhea-db.org/69999_L -> http://rdf.rhea-db.org/Participant_69999_compound_3255_in -> http://rdf.rhea-db.org/Compound_3255/rh:chebi
L-threonine(out) + Na(+)(out) => L-threonine(in) + Na(+)(in)
RHEA:70001		produces

The directed native Rhea reaction has CHEBI:29101 on its products side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.

sodium(1+)
CHEBI:29101
  • RHEA:70001

    Source assertion: The directed native Rhea reaction has CHEBI:29101 on its products side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.

    Source locationhttp://rdf.rhea-db.org/70001/rh:products -> http://rdf.rhea-db.org/69999_L -> http://rdf.rhea-db.org/Participant_69999_compound_2426_in -> http://rdf.rhea-db.org/Compound_2426/rh:chebi
L-threonine zwitterion
CHEBI:57926		consumes

The directed native Rhea reaction has CHEBI:57926 on its substrates side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.

L-threonine(out) + H(+)(out) => L-threonine(in) + H(+)(in)
RHEA:28885
  • RHEA:28885

    Source assertion: The directed native Rhea reaction has CHEBI:57926 on its substrates side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.

    Source locationhttp://rdf.rhea-db.org/28885/rh:substrates -> http://rdf.rhea-db.org/28883_R -> http://rdf.rhea-db.org/Participant_28883_compound_3255_out -> http://rdf.rhea-db.org/Compound_3255/rh:chebi
hydron
CHEBI:15378		consumes

The directed native Rhea reaction has CHEBI:15378 on its substrates side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.

L-threonine(out) + H(+)(out) => L-threonine(in) + H(+)(in)
RHEA:28885
  • RHEA:28885

    Source assertion: The directed native Rhea reaction has CHEBI:15378 on its substrates side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.

    Source locationhttp://rdf.rhea-db.org/28885/rh:substrates -> http://rdf.rhea-db.org/28883_R -> http://rdf.rhea-db.org/Participant_28883_compound_3249_out -> http://rdf.rhea-db.org/Compound_3249/rh:chebi
L-threonine(out) + H(+)(out) => L-threonine(in) + H(+)(in)
RHEA:28885		produces

The directed native Rhea reaction has CHEBI:57926 on its products side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.

L-threonine zwitterion
CHEBI:57926
  • RHEA:28885

    Source assertion: The directed native Rhea reaction has CHEBI:57926 on its products side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.

    Source locationhttp://rdf.rhea-db.org/28885/rh:products -> http://rdf.rhea-db.org/28883_L -> http://rdf.rhea-db.org/Participant_28883_compound_3255_in -> http://rdf.rhea-db.org/Compound_3255/rh:chebi
L-threonine(out) + H(+)(out) => L-threonine(in) + H(+)(in)
RHEA:28885		produces

The directed native Rhea reaction has CHEBI:15378 on its products side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.

hydron
CHEBI:15378
  • RHEA:28885

    Source assertion: The directed native Rhea reaction has CHEBI:15378 on its products side with coefficient 1. Transport compartment tags are retained in the formal equation; shared ChEBI identity does not collapse the two spatial sides.

    Source locationhttp://rdf.rhea-db.org/28885/rh:products -> http://rdf.rhea-db.org/28883_L -> http://rdf.rhea-db.org/Participant_28883_compound_3249_in -> http://rdf.rhea-db.org/Compound_3249/rh:chebi
L-threonine + NAD(+) => (2S)-2-amino-3-oxobutanoate + NADH + H(+)
RHEA:13162		part_of

The complete native three-event pathway includes THREODEHYD-RXN; its mapped directional Rhea event is RHEA:13162. Spontaneous decarboxylation is retained as an elementary event.

MetaCyc:THRDLCTCAT-PWY
  • MetaCyc:THRDLCTCAT-PWY

    Source assertion: The complete native three-event pathway includes THREODEHYD-RXN. Spontaneous decarboxylation remains an elementary event.

    Source location/ptools-xml/Pathway/reaction-list/Reaction[@frameid="THREODEHYD-RXN"]
  • MetaCyc:THREODEHYD-RXN

    Source assertion: The native reaction has a RHEA unification dblink to directional reaction 13162.

    Source location/ptools-xml/Reaction/dblink[dblink-db="RHEA" and dblink-relationship="unification"]/dblink-oid
(2S)-2-amino-3-oxobutanoate + H(+) => aminoacetone + CO2
RHEA:25654		part_of

The complete native three-event pathway includes THREOSPON-RXN; its mapped directional Rhea event is RHEA:25654. Spontaneous decarboxylation is retained as an elementary event.

MetaCyc:THRDLCTCAT-PWY
  • MetaCyc:THRDLCTCAT-PWY

    Source assertion: The complete native three-event pathway includes THREOSPON-RXN. Spontaneous decarboxylation remains an elementary event.

    Source location/ptools-xml/Pathway/reaction-list/Reaction[@frameid="THREOSPON-RXN"]
  • MetaCyc:THREOSPON-RXN

    Source assertion: The native reaction has a RHEA unification dblink to directional reaction 25654.

    Source location/ptools-xml/Reaction/dblink[dblink-db="RHEA" and dblink-relationship="unification"]/dblink-oid
aminoacetone + O2 + H2O => methylglyoxal + H2O2 + NH4(+)
RHEA:28187		part_of

The complete native three-event pathway includes AMACETOXID-RXN; its mapped directional Rhea event is RHEA:28187. Spontaneous decarboxylation is retained as an elementary event.

MetaCyc:THRDLCTCAT-PWY
  • MetaCyc:THRDLCTCAT-PWY

    Source assertion: The complete native three-event pathway includes AMACETOXID-RXN. Spontaneous decarboxylation remains an elementary event.

    Source location/ptools-xml/Pathway/reaction-list/Reaction[@frameid="AMACETOXID-RXN"]
  • MetaCyc:AMACETOXID-RXN

    Source assertion: The native reaction has a RHEA unification dblink to directional reaction 28187.

    Source location/ptools-xml/Reaction/dblink[dblink-db="RHEA" and dblink-relationship="unification"]/dblink-oid
L-threonine + NAD(+) => (2S)-2-amino-3-oxobutanoate + NADH + H(+)
RHEA:13162		precedes

The native route oxidizes threonine before spontaneous decarboxylation of its unstable 2-amino-3-oxo intermediate.

(2S)-2-amino-3-oxobutanoate + H(+) => aminoacetone + CO2
RHEA:25654
  • MetaCyc:THRDLCTCAT-PWY

    Source assertion: The native route oxidizes threonine before spontaneous decarboxylation of its unstable 2-amino-3-oxo intermediate.

    Source locationreaction-layout, reaction-ordering and comment
(2S)-2-amino-3-oxobutanoate + H(+) => aminoacetone + CO2
RHEA:25654		precedes

Aminoacetone from spontaneous decarboxylation is the input to terminal oxidation; the E. coli catalyst assignment remains hypothetical.

aminoacetone + O2 + H2O => methylglyoxal + H2O2 + NH4(+)
RHEA:28187
  • MetaCyc:THRDLCTCAT-PWY

    Source assertion: Aminoacetone from spontaneous decarboxylation is the input to terminal oxidation; the E. coli catalyst assignment remains hypothetical.

    Source locationreaction-layout and comment
MetaCyc:THRDLCTCAT-PWYpart_of

The native record places the complete degradation-III route in the threonine-metabolism superpathway; the parent is an opaque hierarchy context.

superpathway of L-threonine metabolism
MetaCyc:THREOCAT-PWY
  • MetaCyc:THRDLCTCAT-PWY

    Source assertion: The native record places the complete degradation-III route in the threonine-metabolism superpathway; the parent is an opaque hierarchy context.

    Source locationPathway/super-pathways
methylglyoxal degradation I
MetaCyc:PWY-5386		has_input

The native pathway-link connects the methylglyoxal product to methylglyoxal degradation I; no downstream chemistry is imported here.

methylglyoxal
CHEBI:17158
  • MetaCyc:THRDLCTCAT-PWY

    Source assertion: The native pathway-link connects the methylglyoxal product to methylglyoxal degradation I; no downstream chemistry is imported here.

    Source location/ptools-xml/Pathway/pathway-link[Compound/@frameid="METHYL-GLYOXAL"]/link-target/Pathway[@frameid="PWY-5386"]
Threonine Biosynthesis
PathBank:SMP0000837		has_output

The current BioPAX includes a named threonine-biosynthesis SubPathway and its threonine-supply interface. This is a non-elementary upstream connection, not an additional degradation reaction. Neutral PathBank threonine is represented here by Rhea physiological L-threonine with the protonation distinction retained.

L-threonine zwitterion
CHEBI:57926
  • PathBank:SMP0002118

    Source assertion: The current BioPAX includes a named threonine-biosynthesis SubPathway and its threonine-supply interface. This is a non-elementary upstream connection, not an additional degradation reaction. Neutral PathBank threonine is represented here by Rhea physiological L-threonine with the protonation distinction retained.

    Source locationPathway[@rdf:about="http://identifiers.org/smpdb/SMP0000837"]/displayName, xref and pathwayComponent; SubPathwayInteractions/528933 participant Compound/PW_C000109
  • PathBank:SMP0002118/PWML

    Source assertion: The intact native SubPathway fragment identifies ID528933/reference581 with Compound109 as output; its visualization places that compound on the Right. The separate BioPAX supplies the SMP0000837 identifier and biological title.

    Source locationOriginal PWML lines 24–39: sub-pathways/sub-pathway[id=528933]/reference-pathway-id=581; sub-pathway-outputs/sub-pathway-output/element-id=109 and element-type=Compound. Lines 9196–9216: sub-pathway-visualizations/sub-pathway-visualization[sub-pathway-id=528933]/sub_pathway_compound_visualizations/sub-pathway-compound-visualization/side=Right
threonine dehydrogenase
MetaCyc:THREODEHYD-CPLX		has_part

Native component coefficient 4 and reviewed homotetramer annotation identify the Tdh assembly; the guarded functional common name does not add an unreported assembly suffix.

L-threonine 3-dehydrogenase
UniProtKB:P07913
  • MetaCyc:THREODEHYD-CPLX

    Source assertion: Native component coefficient 4 and reviewed homotetramer annotation identify the Tdh assembly; the guarded functional common name does not add an unreported assembly suffix.

    Source locationProtein/component[THREODEHYD-MONOMER]/coefficient=4
  • UniProtKB:P07913

    Source assertion: The reviewed entry describes Tdh as a homotetramer.

    Source locationcomments[SUBUNIT]
  • EcoCyc:THREODEHYD-MONOMER

    Source assertion: The exact native THREODEHYD-MONOMER protein frame has a UNIPROT unification link to P07913; this establishes the named component identity separately from the complex coefficient.

    Source location/ptools-xml/Protein/dblink[dblink-db="UNIPROT" and dblink-relationship="unification"]/dblink-oid
threonine dehydrogenase
MetaCyc:THREODEHYD-CPLX		catalyzes

Tdh supplies the NAD-dependent threonine oxidation step. Native RXN-14249 is a composite of oxidation plus spontaneous decarboxylation, not a fourth elementary reaction.

L-threonine + NAD(+) => (2S)-2-amino-3-oxobutanoate + NADH + H(+)
RHEA:13162
  • EcoCyc:THREODEHYD-ENZRXN

    Source assertion: The native enzymatic-reaction object links Tdh complex THREODEHYD-CPLX to composite reaction RXN-14249.

    Source location/ptools-xml/Enzymatic-Reaction/enzyme/Protein; /ptools-xml/Enzymatic-Reaction/reaction/Reaction
  • UniProtKB:P07913

    Source assertion: The reviewed Tdh catalytic activity points to RHEA:13161, the master of the selected L-to-R oxidation.

    Source locationcomments[CATALYTIC ACTIVITY]/reactionCrossReferences
  • EcoCyc:RXN-14249

    Source assertion: RXN-14249 contains THREODEHYD-RXN and THREOSPON-RXN: oxidation plus spontaneous decarboxylation, not a fourth elementary reaction.

    Source location/ptools-xml/Reaction/reaction-list/Reaction
hypothetical protein [Escherichia coli str. K-12 substr. MG1655]
NCBIProtein:AAB18566.1

experimental construct: N-terminal 6×His-tagged orf382 amplified from E. coli MG1655 using AAB18566.1 as reference, expressed from pET28a(+) in BL21(DE3) and purified by Ni-NTA. The complete construct sequence was not reported; this assay endpoint does not assert identity with the bare reference or current UniProtKB:P37686 sequence.

Qualification evidence
  • PMID:24651643

    Source assertion: The study cloned MG1655 orf382 using AAB18566.1 as reference, reported no mutation in the sequenced insert, expressed an N-terminal 6×His fusion in BL21(DE3), and purified the recombinant preparation by Ni-NTA.

    Source locationPublisher PDF pp. 749–751; Materials and Methods, Molecular Cloning, Protein Expression, Purification, and Enzymatic Activity Assays; Results and Discussion, Molecular Cloning, Protein Expression, and Purification
catalyzes

The purified N-terminal His-tagged YiaY/orf382 preparation showed threonine-dependent NADH formation at 340 nm. This supports an alternative oxidation activity; direct intermediate/product measurements and complete-route reconstruction were not reported.

L-threonine + NAD(+) => (2S)-2-amino-3-oxobutanoate + NADH + H(+)
RHEA:13162
  • PMID:24651643

    Source assertion: The purified N-terminal His-tagged YiaY/orf382 preparation showed threonine-dependent NADH formation at 340 nm. This supports an alternative oxidation activity; direct intermediate/product measurements and complete-route reconstruction were not reported.

    Source locationPublisher PDF p. 750, Enzymatic Activity Assays and Activity with Various Hydroxyl-Group-Containing Substrates; p. 752, Exploration of Substrate Spectrum and Fig. 3; p. 753, Metal Ion Binding and Cofactor Dependence
hypothetical protein [Escherichia coli str. K-12 substr. MG1655]
NCBIProtein:AAB18566.1

experimental construct: N-terminal 6×His-tagged orf382 amplified from E. coli MG1655 using AAB18566.1 as reference, expressed from pET28a(+) in BL21(DE3) and purified by Ni-NTA. The complete construct sequence was not reported; this assay endpoint does not assert identity with the bare reference or current UniProtKB:P37686 sequence.

Qualification evidence
  • PMID:24651643

    Source assertion: The study cloned MG1655 orf382 using AAB18566.1 as reference, reported no mutation in the sequenced insert, expressed an N-terminal 6×His fusion in BL21(DE3), and purified the recombinant preparation by Ni-NTA.

    Source locationPublisher PDF pp. 749–751; Materials and Methods, Molecular Cloning, Protein Expression, Purification, and Enzymatic Activity Assays; Results and Discussion, Molecular Cloning, Protein Expression, and Purification
has_cofactor

EDTA depleted activity and affected structure of the purified construct. Its measured preparation contained 0.424 mol Fe and 0.914 mol Zn per mol protein; these values do not fix native occupancy, iron oxidation state, or a metal stoichiometry for current P37686.

divalent metal cation
CHEBI:60240
  • PMID:24651643

    Source assertion: EDTA depleted activity and affected structure of the purified construct. Its measured preparation contained 0.424 mol Fe and 0.914 mol Zn per mol protein; these values do not fix native occupancy, iron oxidation state, or a metal stoichiometry for current P37686.

    Source locationpp. 752–754; metal content, EDTA treatment and structural analysis
ethylenediaminetetraacetic acid
CHEBI:4735		inhibits

EDTA reduced activity and altered structural measurements in the assayed His-tagged YiaY preparation; chelation is an in-vitro treatment, not evidence of an endogenous inhibitor.

hypothetical protein [Escherichia coli str. K-12 substr. MG1655]
NCBIProtein:AAB18566.1

experimental construct: N-terminal 6×His-tagged orf382 amplified from E. coli MG1655 using AAB18566.1 as reference, expressed from pET28a(+) in BL21(DE3) and purified by Ni-NTA. The complete construct sequence was not reported; this assay endpoint does not assert identity with the bare reference or current UniProtKB:P37686 sequence.

Qualification evidence
  • PMID:24651643

    Source assertion: The study cloned MG1655 orf382 using AAB18566.1 as reference, reported no mutation in the sequenced insert, expressed an N-terminal 6×His fusion in BL21(DE3), and purified the recombinant preparation by Ni-NTA.

    Source locationPublisher PDF pp. 749–751; Materials and Methods, Molecular Cloning, Protein Expression, Purification, and Enzymatic Activity Assays; Results and Discussion, Molecular Cloning, Protein Expression, and Purification
  • PMID:24651643

    Source assertion: EDTA reduced activity and altered structural measurements in the assayed His-tagged YiaY preparation; chelation is an in-vitro treatment, not evidence of an endogenous inhibitor.

    Source locationpp. 752–754; EDTA treatment and activity/structure comparisons
copper-containing amine oxidase
MetaCyc:AMINEOXID-CPLX		has_part

The native TynA assembly has two amine-oxidase subunits; the reviewed entry independently describes a homodimer.

Primary amine oxidase
UniProtKB:P46883
  • MetaCyc:AMINEOXID-CPLX

    Source assertion: The native TynA assembly has two amine-oxidase subunits; the reviewed entry independently describes a homodimer.

    Source locationProtein/component[AMINEOXID-MONOMER]/coefficient=2
  • UniProtKB:P46883

    Source assertion: TynA is annotated as a homodimer.

    Source locationcomments[SUBUNIT]
  • EcoCyc:AMINEOXID-MONOMER

    Source assertion: The exact native AMINEOXID-MONOMER protein frame has a UNIPROT unification link to P46883; this establishes the named component identity separately from the complex coefficient.

    Source location/ptools-xml/Protein/dblink[dblink-db="UNIPROT" and dblink-relationship="unification"]/dblink-oid
copper-containing amine oxidase
MetaCyc:AMINEOXID-CPLX		catalyzes

HYPOTHETICAL TynA assignment: EcoCyc associates this complex with aminoacetone oxidation using EV-AS-NAS. This is not a demonstrated E. coli aminoacetone substrate assay or a reconstructed complete route.

aminoacetone + O2 + H2O => methylglyoxal + H2O2 + NH4(+)
RHEA:28187
  • EcoCyc:AMACETOXID-ENZRXN

    Source assertion: HYPOTHETICAL TynA assignment: EcoCyc associates this complex with aminoacetone oxidation using EV-AS-NAS. This is not a demonstrated E. coli aminoacetone substrate assay or a reconstructed complete route.

    Source locationEnzymatic-Reaction/enzyme, reaction and evidence/Evidence-Code[@frameid="EV-AS-NAS"]
  • EcoCyc:THRDLCTCAT-PWY

    Source assertion: The native pathway comment explicitly calls the amine-oxidase step hypothetical in E. coli.

    Source locationPathway/comment
threonine dehydrogenase
MetaCyc:THREODEHYD-CPLX		located_in

Tdh localization is a reviewed cytoplasmic annotation with HAMAP inference, distinct from a direct localization assay.

cytoplasm
GO:0005737
  • UniProtKB:P07913

    Source assertion: Tdh localization is a reviewed cytoplasmic annotation with HAMAP inference, distinct from a direct localization assay.

    Source locationcomments[SUBCELLULAR LOCATION]
copper-containing amine oxidase
MetaCyc:AMINEOXID-CPLX		located_in

The reviewed TynA protein is periplasmic. No aminoacetone export mechanism linking it to cytoplasmic Tdh is asserted.

periplasmic space
GO:0042597
  • UniProtKB:P46883

    Source assertion: The reviewed TynA protein is periplasmic. No aminoacetone export mechanism linking it to cytoplasmic Tdh is asserted.

    Source locationcomments[SUBCELLULAR LOCATION]
copper-containing amine oxidase
MetaCyc:AMINEOXID-CPLX		has_cofactor

One copper ion per subunit is annotated from experimental TynA studies.

copper cation
CHEBI:23378
  • UniProtKB:P46883

    Source assertion: One copper ion per subunit is annotated from experimental TynA studies.

    Source locationcomments[COFACTOR], cofactorCrossReference and evidence codes
copper-containing amine oxidase
MetaCyc:AMINEOXID-CPLX		has_cofactor

Two calcium ions per subunit are annotated from experimental TynA studies.

calcium(2+)
CHEBI:29108
  • UniProtKB:P46883

    Source assertion: Two calcium ions per subunit are annotated from experimental TynA studies.

    Source locationcomments[COFACTOR], cofactorCrossReference and evidence codes
copper-containing amine oxidase
MetaCyc:AMINEOXID-CPLX		has_cofactor

One topaquinone residue per subunit is annotated. Maturation and substoichiometric overexpression preparations are distinct from an assumed fully matured molecule.

L-topaquinone(1-) residue
CHEBI:79027
  • UniProtKB:P46883

    Source assertion: One topaquinone residue per subunit is annotated. Maturation and substoichiometric overexpression preparations are distinct from an assumed fully matured molecule.

    Source locationcomments[COFACTOR], cofactorCrossReference and evidence codes
copper-containing amine oxidase
MetaCyc:AMINEOXID-CPLX		has_cofactor

Zinc cofactor use is explicitly inferred by similarity to P12807; it is not a direct E. coli substrate-specific measurement.

zinc(2+)
CHEBI:29105
  • UniProtKB:P46883

    Source assertion: Zinc cofactor use is explicitly inferred by similarity to P12807; it is not a direct E. coli substrate-specific measurement.

    Source locationcomments[COFACTOR], cofactorCrossReference and evidence codes
copper-containing amine oxidase
MetaCyc:AMINEOXID-CPLX		has_cofactor

Manganese binding (one per subunit) is explicitly inferred by similarity to Q43077; no direct E. coli occupancy measurement is claimed.

manganese(2+)
CHEBI:29035
  • UniProtKB:P46883

    Source assertion: Manganese binding (one per subunit) is explicitly inferred by similarity to Q43077; no direct E. coli occupancy measurement is claimed.

    Source locationcomments[COFACTOR], cofactorCrossReference and evidence codes
2-Hydrazinopyridine
PubChem:78645		inhibits

2-Hydrazinopyridine inhibits TynA in the cited structural/biochemical work. This protein-level inhibition does not validate hypothetical aminoacetone turnover.

copper-containing amine oxidase
MetaCyc:AMINEOXID-CPLX
  • UniProtKB:P46883

    Source assertion: 2-Hydrazinopyridine inhibits TynA in the cited structural/biochemical work. This protein-level inhibition does not validate hypothetical aminoacetone turnover.

    Source locationcomments[ACTIVITY REGULATION], PMID9048544
  • PMID:9048544

    Source assertion: The accessible primary abstract concerns E. coli copper amine oxidase structures, including its inhibitor complex; full-text assay details were not inspected.

    Source locationissuing primary abstract
threonine dehydrogenase
MetaCyc:THREODEHYD-CPLX		has_cofactor

The reviewed entry reports two Zn(2+) per Tdh subunit and distinguishes a proposed structural site from a less tightly bound catalytic site.

zinc(2+)
CHEBI:29105
  • UniProtKB:P07913

    Source assertion: The reviewed entry reports two Zn(2+) per Tdh subunit and distinguishes a proposed structural site from a less tightly bound catalytic site.

    Source locationcomments[COFACTOR] note and evidence PMID2007567/9784233
  • PMID:2007567

    Source assertion: The primary abstract reports one Zn(2+) per subunit in the isolated preparation, whereas the current reviewed annotation says two. These are retained as distinct occupancy claims, not reconciled by assuming an unmeasured site.

    Source locationissuing primary abstract: neutron activation and atomic absorption analyses
threonine dehydrogenase
MetaCyc:THREODEHYD-CPLX		has_cofactor

Co(2+) substitutes for zinc in the cited in-vitro Tdh preparation; this is not evidence for routine cobalt occupancy in vivo.

cobalt(2+)
CHEBI:48828
  • UniProtKB:P07913

    Source assertion: Co(2+) substitutes for zinc in the cited in-vitro Tdh preparation; this is not evidence for routine cobalt occupancy in vivo.

    Source locationcomments[COFACTOR] note and evidence PMID2007567/9784233
threonine dehydrogenase
MetaCyc:THREODEHYD-CPLX		has_cofactor

The older reviewed annotation reports Cd(2+) exchange for zinc. The 2012 purified-enzyme study found no Cd-supported activity; preserve this preparation/assay conflict rather than asserting universal cadmium activation.

cadmium(2+)
CHEBI:48775
  • UniProtKB:P07913

    Source assertion: The reviewed cofactor note reports Cd(2+) exchange for zinc in the older studies.

    Source locationcomments[COFACTOR]/note; PMID2007567 and PMID9784233 evidence
  • PMID:22411989

    Source assertion: In the 2012 purified-enzyme metal-reconstitution comparison neither TDH nor PDF was active with Cd(II). This differs from the older Cd-exchange annotation; it does not establish universal cadmium activation.

    Source location//p[contains(., "Neither enzyme was active with Mg(II), Ca(II), or Cd(II)")]; Results, initial metal-activity comparison; Table 1 context
threonine dehydrogenase
MetaCyc:THREODEHYD-CPLX		has_cofactor

Fe(II)-reconstituted purified Tdh was active. Native intracellular iron use was inferred from oxidative sensitivity/reconstitution; it was not established by direct active-site occupancy measurement.

iron(2+)
CHEBI:29033
  • PMID:22411989

    Source assertion: Fe(II)-reconstituted purified Tdh was active. Native intracellular iron use was inferred from oxidative sensitivity/reconstitution; it was not established by direct active-site occupancy measurement.

    Source locationExperimental Procedures, metal loading; Results first section/Table 1; Discussion Protection of Mononuclear Enzymes by Imported Manganese
threonine dehydrogenase
MetaCyc:THREODEHYD-CPLX		has_cofactor

Mn(II)-reconstituted purified Tdh retained catalytic activity but bound threonine poorly. Intracellular manganese protection does not establish active-site occupancy or continuous pathway flux.

manganese(2+)
CHEBI:29035
  • PMID:22411989

    Source assertion: Mn(II)-reconstituted purified Tdh retained catalytic activity but bound threonine poorly. Intracellular manganese protection does not establish active-site occupancy or continuous pathway flux.

    Source locationExperimental Procedures, metal loading; Results first section/Table 1; Discussion Protection of Mononuclear Enzymes by Imported Manganese
ethylenediaminetetraacetic acid
CHEBI:4735		inhibits

EDTA inhibits Tdh in vitro and was used to remove exchangeable metals; apoenzyme instability and assay metal replacement limit interpretation as a simple native regulatory switch.

threonine dehydrogenase
MetaCyc:THREODEHYD-CPLX
  • UniProtKB:P07913

    Source assertion: EDTA inhibits Tdh in vitro and was used to remove exchangeable metals; apoenzyme instability and assay metal replacement limit interpretation as a simple native regulatory switch.

    Source locationcomments[ACTIVITY REGULATION]
  • PMID:22411989

    Source assertion: Purified Tdh was chelated with EDTA before metal loading; the diluted apoenzyme rapidly became nonreactivatable.

    Source locationExperimental Procedures, Protein Purification and In Vitro Studies of Enzyme Oxidation
hydrogen peroxide
CHEBI:16240		inhibits

Hydrogen peroxide rapidly inactivated iron-loaded Tdh and reduced measured activity in the specified stressed cells. Early damage could be rescued; prolonged stress caused increasing nonreactivatable loss.

threonine dehydrogenase
MetaCyc:THREODEHYD-CPLX

molecular state: Tdh assayed after in-vitro Fe(II) loading or in the specified peroxide-stressed E. coli preparations. Metal state and peroxide exposure are part of this claim; a fixed native metal occupancy or complete assay-construct sequence is not asserted.

Qualification evidence
  • PMID:22411989

    Source assertion: The work compared metal-reconstituted purified Tdh with extracts/cells of catalase- or peroxide-scavenging-deficient strains.

    Source locationExperimental Procedures, In Vitro/In Vivo Studies of Enzyme Oxidation; Figures 1–3
  • PMID:22411989

    Source assertion: Hydrogen peroxide rapidly inactivated iron-loaded Tdh and reduced measured activity in the specified stressed cells. Early damage could be rescued; prolonged stress caused increasing nonreactivatable loss.

    Source locationResults; Figures 1, 3 and 5
1,4-dithiothreitol
CHEBI:18320		activates

DTT together with added metal restored activity after limited peroxide exposure in vitro. This is measured rescue of an oxidized preparation, not an endogenous activator or rescue after all prolonged damage.

threonine dehydrogenase
MetaCyc:THREODEHYD-CPLX

molecular state: Tdh assayed after in-vitro Fe(II) loading or in the specified peroxide-stressed E. coli preparations. Metal state and peroxide exposure are part of this claim; a fixed native metal occupancy or complete assay-construct sequence is not asserted.

Qualification evidence
  • PMID:22411989

    Source assertion: The work compared metal-reconstituted purified Tdh with extracts/cells of catalase- or peroxide-scavenging-deficient strains.

    Source locationExperimental Procedures, In Vitro/In Vivo Studies of Enzyme Oxidation; Figures 1–3
  • PMID:22411989

    Source assertion: DTT together with added metal restored activity after limited peroxide exposure in vitro. This is measured rescue of an oxidized preparation, not an endogenous activator or rescue after all prolonged damage.

    Source locationExperimental Procedures, In Vitro Studies; Results/Figure 3
TCEP
CHEBI:63213		activates

TCEP together with added metal restored activity after limited peroxide exposure in vitro. This is measured rescue of an oxidized preparation, not an endogenous activator or rescue after all prolonged damage.

threonine dehydrogenase
MetaCyc:THREODEHYD-CPLX

molecular state: Tdh assayed after in-vitro Fe(II) loading or in the specified peroxide-stressed E. coli preparations. Metal state and peroxide exposure are part of this claim; a fixed native metal occupancy or complete assay-construct sequence is not asserted.

Qualification evidence
  • PMID:22411989

    Source assertion: The work compared metal-reconstituted purified Tdh with extracts/cells of catalase- or peroxide-scavenging-deficient strains.

    Source locationExperimental Procedures, In Vitro/In Vivo Studies of Enzyme Oxidation; Figures 1–3
  • PMID:22411989

    Source assertion: TCEP together with added metal restored activity after limited peroxide exposure in vitro. This is measured rescue of an oxidized preparation, not an endogenous activator or rescue after all prolonged damage.

    Source locationExperimental Procedures, In Vitro Studies; Results/Figure 3
stationary phase nucleoid component that sequesters iron and protects DNA from damage
EcoCyc:CPLX0-1521		has_part

The native EcoCyc complex lists this protein component with coefficient 12. This assembly annotation does not establish that every promoter assay used this oligomeric state.

DNA protection during starvation protein
UniProtKB:P0ABT2
  • EcoCyc:CPLX0-1521

    Source assertion: The native EcoCyc complex lists this protein component with coefficient 12. This assembly annotation does not establish that every promoter assay used this oligomeric state.

    Source locationProtein/component and coefficient
  • EcoCyc:EG11415-MONOMER

    Source assertion: The exact native EG11415-MONOMER protein frame has a UNIPROT unification link to P0ABT2; this establishes the named component identity separately from the complex coefficient.

    Source location/ptools-xml/Protein/dblink[dblink-db="UNIPROT" and dblink-relationship="unification"]/dblink-oid
DNA-binding transcriptional dual regulator NsrR
EcoCyc:CPLX0-7756		has_part

The native EcoCyc complex lists this protein component with coefficient 2. This assembly annotation does not establish that every promoter assay used this oligomeric state.

HTH-type transcriptional repressor NsrR
UniProtKB:P0AF63
  • EcoCyc:CPLX0-7756

    Source assertion: The native EcoCyc complex lists this protein component with coefficient 2. This assembly annotation does not establish that every promoter assay used this oligomeric state.

    Source locationProtein/component and coefficient
  • EcoCyc:EG11212-MONOMER

    Source assertion: The exact native EG11212-MONOMER protein frame has a UNIPROT unification link to P0AF63; this establishes the named component identity separately from the complex coefficient.

    Source location/ptools-xml/Protein/dblink[dblink-db="UNIPROT" and dblink-relationship="unification"]/dblink-oid
DNA-binding transcriptional dual regulator FNR
EcoCyc:CPLX0-7797		has_part

The native EcoCyc complex lists this protein component with coefficient 2. This assembly annotation does not establish that every promoter assay used this oligomeric state.

Fumarate and nitrate reduction regulatory protein
UniProtKB:P0A9E5
  • EcoCyc:CPLX0-7797

    Source assertion: The native EcoCyc complex lists this protein component with coefficient 2. This assembly annotation does not establish that every promoter assay used this oligomeric state.

    Source locationProtein/component and coefficient
  • EcoCyc:PD00197

    Source assertion: The exact native PD00197 protein frame has a UNIPROT unification link to P0A9E5; this establishes the named component identity separately from the complex coefficient.

    Source location/ptools-xml/Protein/dblink[dblink-db="UNIPROT" and dblink-relationship="unification"]/dblink-oid
DNA-binding transcriptional dual regulator FNR
EcoCyc:CPLX0-7797		has_cofactor

The reviewed FNR entry assigns one [4Fe-4S] cluster per subunit; anaerobic cluster acquisition favors its active dimer, whereas oxygen disrupts this state.

tetra-mu3-sulfido-tetrairon
CHEBI:49883
  • UniProtKB:P0A9E5

    Source assertion: The reviewed FNR entry assigns one [4Fe-4S] cluster per subunit.

    Source locationresults[0]/comments[COFACTOR]
  • EcoCyc:CPLX0-7797

    Source assertion: The native FNR complex comment describes anaerobic [4Fe-4S] acquisition and dimer activation; oxygen converts the cluster and promotes dimer disassembly.

    Source location/ptools-xml/Protein/comment; paragraph beginning "The cellular concentration of FNR"
DNA-binding transcriptional dual regulator NsrR
EcoCyc:CPLX0-7756		has_cofactor

The reviewed E. coli NsrR annotation assigns a [2Fe-2S] cluster with curator inference. Native commentary cites some physical-state work in S. coelicolor; this is not a direct E. coli tynA-promoter metal assay.

di-mu-sulfido-diiron
CHEBI:190135
  • UniProtKB:P0AF63

    Source assertion: The reviewed E. coli NsrR entry assigns a [2Fe-2S] cluster with curator inference ECO:0000305.

    Source locationresults[0]/comments[COFACTOR]
  • EcoCyc:CPLX0-7756

    Source assertion: Native NsrR commentary describes homodimer/DNA-binding physical-state work in S. coelicolor; it is not a direct E. coli tynA-promoter metal assay.

    Source location/ptools-xml/Protein/comment; paragraph beginning "The binding site for NsrR" and citing PMID18989365
Divalent metal cation transporter MntH
UniProtKB:P0A769		regulates

MntH supported retention of measured Tdh activity under the study's chronic peroxide-stress conditions. This is indirect protection through manganese import/iron handling, not direct Tdh binding or measured complete pathway flux.

threonine dehydrogenase
MetaCyc:THREODEHYD-CPLX
  • PMID:22411989

    Source assertion: MntH supported retention of measured Tdh activity under the study's chronic peroxide-stress conditions. This is indirect protection through manganese import/iron handling, not direct Tdh binding or measured complete pathway flux.

    Source locationResults/Figures 7 and 9; Discussion Protection of Mononuclear Enzymes by Imported Manganese
stationary phase nucleoid component that sequesters iron and protects DNA from damage
EcoCyc:CPLX0-1521		regulates

Dps supported retention of measured Tdh activity under the study's chronic peroxide-stress conditions. This is indirect protection through manganese import/iron handling, not direct Tdh binding or measured complete pathway flux.

threonine dehydrogenase
MetaCyc:THREODEHYD-CPLX
  • PMID:22411989

    Source assertion: Dps supported retention of measured Tdh activity under the study's chronic peroxide-stress conditions. This is indirect protection through manganese import/iron handling, not direct Tdh binding or measured complete pathway flux.

    Source locationResults/Figures 7 and 9; Discussion Protection of Mononuclear Enzymes by Imported Manganese
manganese(2+)
CHEBI:29035		regulates

Supplemental manganese protected measured Tdh activity in peroxide-stressed cells, including the Dps-deficient comparison. The authors explicitly did not physically demonstrate intracellular active-site manganese.

threonine dehydrogenase
MetaCyc:THREODEHYD-CPLX
  • PMID:22411989

    Source assertion: Supplemental manganese protected measured Tdh activity in peroxide-stressed cells, including the Dps-deficient comparison. The authors explicitly did not physically demonstrate intracellular active-site manganese.

    Source locationFigures 7/9B and Discussion Protection of Mononuclear Enzymes by Imported Manganese
Serine/threonine transporter SstT
UniProtKB:P0AGE4		catalyzes

SstT is assigned the physiological inward sodium/threonine symport direction. The purified 2002 experiment measured serine uptake and threonine competition; it did not directly measure threonine transport kinetics.

L-threonine(out) + Na(+)(out) => L-threonine(in) + Na(+)(in)
RHEA:70001
  • UniProtKB:P0AGE4

    Source assertion: SstT is assigned the physiological inward sodium/threonine symport direction. The purified 2002 experiment measured serine uptake and threonine competition; it did not directly measure threonine transport kinetics.

    Source locationcomments[CATALYTIC ACTIVITY]/physiologicalReactions and FUNCTION
Serine/threonine transporter SstT
UniProtKB:P0AGE4		located_in

The reviewed transporter is located in the cell inner membrane.

plasma membrane
GO:0005886
  • UniProtKB:P0AGE4

    Source assertion: The reviewed transporter is located in the cell inner membrane.

    Source locationcomments[SUBCELLULAR LOCATION]
L-threonine(out) + Na(+)(out) => L-threonine(in) + Na(+)(in)
RHEA:70001		provides_input_for

Threonine uptake can supply the oxidation substrate in the relevant physiological context; this connection does not assert concurrent expression or demonstrated complete-route flux.

L-threonine + NAD(+) => (2S)-2-amino-3-oxobutanoate + NADH + H(+)
RHEA:13162
  • EcoCyc:THRDLCTCAT-PWY

    Source assertion: Threonine uptake can supply the oxidation substrate in the relevant physiological context; this connection does not assert concurrent expression or demonstrated complete-route flux.

    Source location/ptools-xml/Pathway/comment; paragraph beginning "E. coli has three systems that can transport threonine", naming YGJU-MONOMER, ABC-15-CPLX and TDCC-MONOMER
Threonine/serine transporter TdcC
UniProtKB:P0AAD8		catalyzes

TdcC is assigned physiological inward proton/threonine symport. Its anaerobically induced uptake context does not imply simultaneous aerobic terminal aminoacetone oxidation.

L-threonine(out) + H(+)(out) => L-threonine(in) + H(+)(in)
RHEA:28885
  • UniProtKB:P0AAD8

    Source assertion: TdcC is assigned physiological inward proton/threonine symport. Its anaerobically induced uptake context does not imply simultaneous aerobic terminal aminoacetone oxidation.

    Source locationcomments[CATALYTIC ACTIVITY]/physiologicalReactions and FUNCTION
Threonine/serine transporter TdcC
UniProtKB:P0AAD8		located_in

The reviewed transporter is located in the cell inner membrane.

plasma membrane
GO:0005886
  • UniProtKB:P0AAD8

    Source assertion: The reviewed transporter is located in the cell inner membrane.

    Source locationcomments[SUBCELLULAR LOCATION]
L-threonine(out) + H(+)(out) => L-threonine(in) + H(+)(in)
RHEA:28885		provides_input_for

Threonine uptake can supply the oxidation substrate in the relevant physiological context; this connection does not assert concurrent expression or demonstrated complete-route flux.

L-threonine + NAD(+) => (2S)-2-amino-3-oxobutanoate + NADH + H(+)
RHEA:13162
  • EcoCyc:THRDLCTCAT-PWY

    Source assertion: Threonine uptake can supply the oxidation substrate in the relevant physiological context; this connection does not assert concurrent expression or demonstrated complete-route flux.

    Source location/ptools-xml/Pathway/comment; paragraph beginning "E. coli has three systems that can transport threonine", naming YGJU-MONOMER, ABC-15-CPLX and TDCC-MONOMER
branched chain amino acid / phenylalanine ABC transporter
MetaCyc:ABC-15-CPLX		enables

The LIV-I transporter is reported to take up threonine in addition to its principal branched-chain substrates. Its ATP-dependent transport context is retained without inventing a threonine-specific ATP-hydrolysis stoichiometry.

L-threonine transmembrane transporter activity
GO:0015195
  • EcoCyc:ABC-15-CPLX

    Source assertion: The LIV-I transporter is reported to take up threonine in addition to its principal branched-chain substrates. Its ATP-dependent transport context is retained without inventing a threonine-specific ATP-hydrolysis stoichiometry.

    Source locationProtein/comment; components and linked transport activities
branched chain amino acid / phenylalanine ABC transporter
MetaCyc:ABC-15-CPLX		has_part

The native LIV-I complex includes this exact LivF/LivG/LivH/LivM/LivJ component with coefficient 1. LivJ is retained; the alternative LivK binding protein is not substituted.

High-affinity branched-chain amino acid transport ATP-binding protein LivF
UniProtKB:P22731
  • EcoCyc:ABC-15-CPLX

    Source assertion: The native LIV-I complex includes this exact LivF/LivG/LivH/LivM/LivJ component with coefficient 1. LivJ is retained; the alternative LivK binding protein is not substituted.

    Source locationProtein/component/coefficient
  • EcoCyc:LIVF-MONOMER

    Source assertion: The exact native LIVF-MONOMER protein frame has a UNIPROT unification link to P22731; this establishes the named component identity separately from the complex coefficient.

    Source location/ptools-xml/Protein/dblink[dblink-db="UNIPROT" and dblink-relationship="unification"]/dblink-oid
branched chain amino acid / phenylalanine ABC transporter
MetaCyc:ABC-15-CPLX		has_part

The native LIV-I complex includes this exact LivF/LivG/LivH/LivM/LivJ component with coefficient 1. LivJ is retained; the alternative LivK binding protein is not substituted.

High-affinity branched-chain amino acid transport ATP-binding protein LivG
UniProtKB:P0A9S7
  • EcoCyc:ABC-15-CPLX

    Source assertion: The native LIV-I complex includes this exact LivF/LivG/LivH/LivM/LivJ component with coefficient 1. LivJ is retained; the alternative LivK binding protein is not substituted.

    Source locationProtein/component/coefficient
  • EcoCyc:LIVG-MONOMER

    Source assertion: The exact native LIVG-MONOMER protein frame has a UNIPROT unification link to P0A9S7; this establishes the named component identity separately from the complex coefficient.

    Source location/ptools-xml/Protein/dblink[dblink-db="UNIPROT" and dblink-relationship="unification"]/dblink-oid
branched chain amino acid / phenylalanine ABC transporter
MetaCyc:ABC-15-CPLX		has_part

The native LIV-I complex includes this exact LivF/LivG/LivH/LivM/LivJ component with coefficient 1. LivJ is retained; the alternative LivK binding protein is not substituted.

High-affinity branched-chain amino acid transport system permease protein LivH
UniProtKB:P0AEX7
  • EcoCyc:ABC-15-CPLX

    Source assertion: The native LIV-I complex includes this exact LivF/LivG/LivH/LivM/LivJ component with coefficient 1. LivJ is retained; the alternative LivK binding protein is not substituted.

    Source locationProtein/component/coefficient
  • EcoCyc:LIVH-MONOMER

    Source assertion: The exact native LIVH-MONOMER protein frame has a UNIPROT unification link to P0AEX7; this establishes the named component identity separately from the complex coefficient.

    Source location/ptools-xml/Protein/dblink[dblink-db="UNIPROT" and dblink-relationship="unification"]/dblink-oid
branched chain amino acid / phenylalanine ABC transporter
MetaCyc:ABC-15-CPLX		has_part

The native LIV-I complex includes this exact LivF/LivG/LivH/LivM/LivJ component with coefficient 1. LivJ is retained; the alternative LivK binding protein is not substituted.

High-affinity branched-chain amino acid transport system permease protein LivM
UniProtKB:P22729
  • EcoCyc:ABC-15-CPLX

    Source assertion: The native LIV-I complex includes this exact LivF/LivG/LivH/LivM/LivJ component with coefficient 1. LivJ is retained; the alternative LivK binding protein is not substituted.

    Source locationProtein/component/coefficient
  • EcoCyc:LIVM-MONOMER

    Source assertion: The exact native LIVM-MONOMER protein frame has a UNIPROT unification link to P22729; this establishes the named component identity separately from the complex coefficient.

    Source location/ptools-xml/Protein/dblink[dblink-db="UNIPROT" and dblink-relationship="unification"]/dblink-oid
branched chain amino acid / phenylalanine ABC transporter
MetaCyc:ABC-15-CPLX		has_part

The native LIV-I complex includes this exact LivF/LivG/LivH/LivM/LivJ component with coefficient 1. LivJ is retained; the alternative LivK binding protein is not substituted.

Leu/Ile/Val-binding protein
UniProtKB:P0AD96
  • EcoCyc:ABC-15-CPLX

    Source assertion: The native LIV-I complex includes this exact LivF/LivG/LivH/LivM/LivJ component with coefficient 1. LivJ is retained; the alternative LivK binding protein is not substituted.

    Source locationProtein/component/coefficient
  • EcoCyc:LIVJ-MONOMER

    Source assertion: The exact native LIVJ-MONOMER protein frame has a UNIPROT unification link to P0AD96; this establishes the named component identity separately from the complex coefficient.

    Source location/ptools-xml/Protein/dblink[dblink-db="UNIPROT" and dblink-relationship="unification"]/dblink-oid
High-affinity branched-chain amino acid transport system permease protein LivH
UniProtKB:P0AEX7		located_in

The reviewed Liv component has this membrane/periplasmic localization; binding-protein and permease roles remain distinct.

plasma membrane
GO:0005886
  • UniProtKB:P0AEX7

    Source assertion: The reviewed Liv component has this membrane/periplasmic localization; binding-protein and permease roles remain distinct.

    Source locationcomments[SUBCELLULAR LOCATION] and FUNCTION
High-affinity branched-chain amino acid transport system permease protein LivM
UniProtKB:P22729		located_in

The reviewed Liv component has this membrane/periplasmic localization; binding-protein and permease roles remain distinct.

plasma membrane
GO:0005886
  • UniProtKB:P22729

    Source assertion: The reviewed Liv component has this membrane/periplasmic localization; binding-protein and permease roles remain distinct.

    Source locationcomments[SUBCELLULAR LOCATION] and FUNCTION
Leu/Ile/Val-binding protein
UniProtKB:P0AD96		located_in

The reviewed Liv component has this membrane/periplasmic localization; binding-protein and permease roles remain distinct.

periplasmic space
GO:0042597
  • UniProtKB:P0AD96

    Source assertion: The reviewed Liv component has this membrane/periplasmic localization; binding-protein and permease roles remain distinct.

    Source locationcomments[SUBCELLULAR LOCATION] and FUNCTION
L-threonine transmembrane transporter activity
GO:0015195		has_input

LIV-I is an ATP-dependent uptake system containing the LivF/LivG ATP-binding subunits. This nonstoichiometric activity edge does not assert a complete threonine-specific ATP equation.

ATP(4-)
CHEBI:30616
  • EcoCyc:ABC-15-CPLX

    Source assertion: LIV-I is an ATP-dependent uptake system containing the LivF/LivG ATP-binding subunits. This nonstoichiometric activity edge does not assert a complete threonine-specific ATP equation.

    Source locationProtein/comment and native linked transport activities
L-threonine transmembrane transporter activity
GO:0015195		has_input

Threonine is a reported LIV-I uptake substrate; the shared chemical node denotes its identity, not a new extracellular chemical species.

L-threonine zwitterion
CHEBI:57926
  • EcoCyc:ABC-15-CPLX

    Source assertion: Threonine is a reported LIV-I uptake substrate; the shared chemical node denotes its identity, not a new extracellular chemical species.

    Source locationProtein/comment: LIV-I substrate scope
L-threonine transmembrane transporter activity
GO:0015195		provides_input_for

LIV-I uptake can supply threonine to the core oxidation; its conditional expression and ATP requirement do not demonstrate complete degradation-III flux.

L-threonine + NAD(+) => (2S)-2-amino-3-oxobutanoate + NADH + H(+)
RHEA:13162
  • EcoCyc:ABC-15-CPLX

    Source assertion: LIV-I uptake can supply threonine to the core oxidation; its conditional expression and ATP requirement do not demonstrate complete degradation-III flux.

    Source locationProtein/comment; pathway threonine input
tdh
Entrez:948139		enables

The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.

L-threonine 3-dehydrogenase
UniProtKB:P07913
  • Entrez:948139

    Source assertion: The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.

    Source location/Entrezgene-Set/Entrezgene/Entrezgene_locus/Gene-commentary/Gene-commentary_products/Gene-commentary/Gene-commentary_source/Other-source/Other-source_src/Dbtag[Dbtag_db="UniProtKB/Swiss-Prot"]/Dbtag_tag/Object-id/Object-id_str; Entrezgene_gene/Gene-ref/Gene-ref_locus
  • UniProtKB:P07913

    Source assertion: The reviewed entry includes this GeneID association.

    Source locationuniProtKBCrossReferences[GeneID]
tynA
Entrez:945939		enables

The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.

Primary amine oxidase
UniProtKB:P46883
  • Entrez:945939

    Source assertion: The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.

    Source location/Entrezgene-Set/Entrezgene/Entrezgene_locus/Gene-commentary/Gene-commentary_products/Gene-commentary/Gene-commentary_source/Other-source/Other-source_src/Dbtag[Dbtag_db="UniProtKB/Swiss-Prot"]/Dbtag_tag/Object-id/Object-id_str; Entrezgene_gene/Gene-ref/Gene-ref_locus
  • UniProtKB:P46883

    Source assertion: The reviewed entry includes this GeneID association.

    Source locationuniProtKBCrossReferences[GeneID]
feaR
Entrez:945941		enables

The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.

Transcriptional activator FeaR
UniProtKB:Q47129
  • Entrez:945941

    Source assertion: The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.

    Source location/Entrezgene-Set/Entrezgene/Entrezgene_locus/Gene-commentary/Gene-commentary_products/Gene-commentary/Gene-commentary_source/Other-source/Other-source_src/Dbtag[Dbtag_db="UniProtKB/Swiss-Prot"]/Dbtag_tag/Object-id/Object-id_str; Entrezgene_gene/Gene-ref/Gene-ref_locus
  • UniProtKB:Q47129

    Source assertion: The reviewed entry includes this GeneID association.

    Source locationuniProtKBCrossReferences[GeneID]
livJ
Entrez:947971		enables

The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.

Leu/Ile/Val-binding protein
UniProtKB:P0AD96
  • Entrez:947971

    Source assertion: The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.

    Source location/Entrezgene-Set/Entrezgene/Entrezgene_locus/Gene-commentary/Gene-commentary_products/Gene-commentary/Gene-commentary_source/Other-source/Other-source_src/Dbtag[Dbtag_db="UniProtKB/Swiss-Prot"]/Dbtag_tag/Object-id/Object-id_str; Entrezgene_gene/Gene-ref/Gene-ref_locus
  • UniProtKB:P0AD96

    Source assertion: The reviewed entry includes this GeneID association.

    Source locationuniProtKBCrossReferences[GeneID]
livF
Entrez:947961		enables

The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.

High-affinity branched-chain amino acid transport ATP-binding protein LivF
UniProtKB:P22731
  • Entrez:947961

    Source assertion: The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.

    Source location/Entrezgene-Set/Entrezgene/Entrezgene_locus/Gene-commentary/Gene-commentary_products/Gene-commentary/Gene-commentary_source/Other-source/Other-source_src/Dbtag[Dbtag_db="UniProtKB/Swiss-Prot"]/Dbtag_tag/Object-id/Object-id_str; Entrezgene_gene/Gene-ref/Gene-ref_locus
  • UniProtKB:P22731

    Source assertion: The reviewed entry includes this GeneID association.

    Source locationuniProtKBCrossReferences[GeneID]
livG
Entrez:947967		enables

The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.

High-affinity branched-chain amino acid transport ATP-binding protein LivG
UniProtKB:P0A9S7
  • Entrez:947967

    Source assertion: The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.

    Source location/Entrezgene-Set/Entrezgene/Entrezgene_locus/Gene-commentary/Gene-commentary_products/Gene-commentary/Gene-commentary_source/Other-source/Other-source_src/Dbtag[Dbtag_db="UniProtKB/Swiss-Prot"]/Dbtag_tag/Object-id/Object-id_str; Entrezgene_gene/Gene-ref/Gene-ref_locus
  • UniProtKB:P0A9S7

    Source assertion: The reviewed entry includes this GeneID association.

    Source locationuniProtKBCrossReferences[GeneID]
livH
Entrez:947965		enables

The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.

High-affinity branched-chain amino acid transport system permease protein LivH
UniProtKB:P0AEX7
  • Entrez:947965

    Source assertion: The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.

    Source location/Entrezgene-Set/Entrezgene/Entrezgene_locus/Gene-commentary/Gene-commentary_products/Gene-commentary/Gene-commentary_source/Other-source/Other-source_src/Dbtag[Dbtag_db="UniProtKB/Swiss-Prot"]/Dbtag_tag/Object-id/Object-id_str; Entrezgene_gene/Gene-ref/Gene-ref_locus
  • UniProtKB:P0AEX7

    Source assertion: The reviewed entry includes this GeneID association.

    Source locationuniProtKBCrossReferences[GeneID]
livM
Entrez:947966		enables

The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.

High-affinity branched-chain amino acid transport system permease protein LivM
UniProtKB:P22729
  • Entrez:947966

    Source assertion: The issuing gene and reviewed protein records identify this gene-product relation in the MG1655 reference. Experimental derivative strain scope is stated separately on regulatory edges.

    Source location/Entrezgene-Set/Entrezgene/Entrezgene_locus/Gene-commentary/Gene-commentary_products/Gene-commentary/Gene-commentary_source/Other-source/Other-source_src/Dbtag[Dbtag_db="UniProtKB/Swiss-Prot"]/Dbtag_tag/Object-id/Object-id_str; Entrezgene_gene/Gene-ref/Gene-ref_locus
  • UniProtKB:P22729

    Source assertion: The reviewed entry includes this GeneID association.

    Source locationuniProtKBCrossReferences[GeneID]
Leucine-responsive regulatory protein
UniProtKB:P0ACJ0		inhibits

In BW3912-derived reporters, Lrp repressed tdh expression. This primary polarity takes precedence over the native TU00225 mode+ annotation, which is retained as a source conflict. Direct tdh-promoter binding was not established by the cited ilvIH binding assay.

tdh
Entrez:948139
  • PMID:1917830

    Source assertion: In BW3912-derived reporters, Lrp repressed tdh expression. This primary polarity takes precedence over the native TU00225 mode+ annotation, which is retained as a source conflict. Direct tdh-promoter binding was not established by the cited ilvIH binding assay.

    Source locationpp. 5948–5950, Tables 2/4 and promoter analyses
  • EcoCyc:TU00225

    Source assertion: The native TU lists positive Lrp/Lrp-leucine modes; this conflicts with the inspected primary repression results and is not silently adopted.

    Source locationTranscription-Unit/component Promoter/regulates; REG0-5455 and REG0-5454 mode+
L-leucine
CHEBI:15603		activates

Leucine increased tdh reporter expression in the study's Lrp-dependent context; this is transcriptional induction, not direct allosteric activation of Tdh.

tdh
Entrez:948139
  • PMID:1917830

    Source assertion: Leucine increased tdh reporter expression in the study's Lrp-dependent context; this is transcriptional induction, not direct allosteric activation of Tdh.

    Source locationTables 2/4 and Discussion
DNA-binding transcriptional dual regulator Lrp-L-leucine
EcoCyc:MONOMER0-155		has_part

The native Lrp-leucine frame includes the Lrp protein; component multiplicity is not specified. No occupancy or oligomer size is inferred from this membership.

Leucine-responsive regulatory protein
UniProtKB:P0ACJ0
  • EcoCyc:MONOMER0-155

    Source assertion: The native Lrp-leucine frame includes the Lrp protein; component multiplicity is not specified. No occupancy or oligomer size is inferred from this membership.

    Source locationProtein/component[PD00353]
  • EcoCyc:PD00353

    Source assertion: The exact native PD00353 protein frame has a UNIPROT unification link to P0ACJ0; this establishes the named component identity separately from the complex coefficient.

    Source location/ptools-xml/Protein/dblink[dblink-db="UNIPROT" and dblink-relationship="unification"]/dblink-oid
DNA-binding transcriptional dual regulator Lrp-L-leucine
EcoCyc:MONOMER0-155		has_part

The native Lrp-leucine frame includes L-leucine without a component coefficient; no binding stoichiometry is imposed.

L-leucine
CHEBI:15603
  • EcoCyc:MONOMER0-155

    Source assertion: The native Lrp-leucine frame includes L-leucine without a component coefficient; no binding stoichiometry is imposed.

    Source locationProtein/component[Compound LEU]; no coefficient
Leucine-responsive regulatory protein
UniProtKB:P0ACJ0		inhibits

Primary livJ/livKHMGF reporter experiments support Lrp-dependent transcriptional repression enhanced by leucine. The named CV/EG/SH derivatives are not all MG1655; direct promoter binding was unresolved. Transport behavior under Lrp overexpression was not a simple copy of reporter polarity.

livJ
Entrez:947971
  • PMID:1729203

    Source assertion: Primary livJ/livKHMGF reporter experiments support Lrp-dependent transcriptional repression enhanced by leucine. The named CV/EG/SH derivatives are not all MG1655; direct promoter binding was unresolved. Transport behavior under Lrp overexpression was not a simple copy of reporter polarity.

    Source locationpp. 108–114, Table 1, Figures 4/6 and Discussion; livJ versus livKHMGF operon scope
Leucine-responsive regulatory protein
UniProtKB:P0ACJ0		inhibits

Primary livJ/livKHMGF reporter experiments support Lrp-dependent transcriptional repression enhanced by leucine. The named CV/EG/SH derivatives are not all MG1655; direct promoter binding was unresolved. Transport behavior under Lrp overexpression was not a simple copy of reporter polarity.

livF
Entrez:947961
  • PMID:1729203

    Source assertion: Primary livJ/livKHMGF reporter experiments support Lrp-dependent transcriptional repression enhanced by leucine. The named CV/EG/SH derivatives are not all MG1655; direct promoter binding was unresolved. Transport behavior under Lrp overexpression was not a simple copy of reporter polarity.

    Source locationpp. 108–114, Table 1, Figures 4/6 and Discussion; livJ versus livKHMGF operon scope
Leucine-responsive regulatory protein
UniProtKB:P0ACJ0		inhibits

Primary livJ/livKHMGF reporter experiments support Lrp-dependent transcriptional repression enhanced by leucine. The named CV/EG/SH derivatives are not all MG1655; direct promoter binding was unresolved. Transport behavior under Lrp overexpression was not a simple copy of reporter polarity.

livG
Entrez:947967
  • PMID:1729203

    Source assertion: Primary livJ/livKHMGF reporter experiments support Lrp-dependent transcriptional repression enhanced by leucine. The named CV/EG/SH derivatives are not all MG1655; direct promoter binding was unresolved. Transport behavior under Lrp overexpression was not a simple copy of reporter polarity.

    Source locationpp. 108–114, Table 1, Figures 4/6 and Discussion; livJ versus livKHMGF operon scope
Leucine-responsive regulatory protein
UniProtKB:P0ACJ0		inhibits

Primary livJ/livKHMGF reporter experiments support Lrp-dependent transcriptional repression enhanced by leucine. The named CV/EG/SH derivatives are not all MG1655; direct promoter binding was unresolved. Transport behavior under Lrp overexpression was not a simple copy of reporter polarity.

livH
Entrez:947965
  • PMID:1729203

    Source assertion: Primary livJ/livKHMGF reporter experiments support Lrp-dependent transcriptional repression enhanced by leucine. The named CV/EG/SH derivatives are not all MG1655; direct promoter binding was unresolved. Transport behavior under Lrp overexpression was not a simple copy of reporter polarity.

    Source locationpp. 108–114, Table 1, Figures 4/6 and Discussion; livJ versus livKHMGF operon scope
Leucine-responsive regulatory protein
UniProtKB:P0ACJ0		inhibits

Primary livJ/livKHMGF reporter experiments support Lrp-dependent transcriptional repression enhanced by leucine. The named CV/EG/SH derivatives are not all MG1655; direct promoter binding was unresolved. Transport behavior under Lrp overexpression was not a simple copy of reporter polarity.

livM
Entrez:947966
  • PMID:1729203

    Source assertion: Primary livJ/livKHMGF reporter experiments support Lrp-dependent transcriptional repression enhanced by leucine. The named CV/EG/SH derivatives are not all MG1655; direct promoter binding was unresolved. Transport behavior under Lrp overexpression was not a simple copy of reporter polarity.

    Source locationpp. 108–114, Table 1, Figures 4/6 and Discussion; livJ versus livKHMGF operon scope
Transcriptional activator FeaR
UniProtKB:Q47129		activates

MG1655 reporter and genetic experiments support FeaR-dependent tynA expression in the tested aromatic-amine carbon/nitrogen conditions. Isolated His-tagged FeaR DNA-binding-domain experiments do not establish direct ligand binding by full-length FeaR or aminoacetone induction.

tynA
Entrez:945939
  • PMID:24013633

    Source assertion: MG1655 reporter and genetic experiments support FeaR-dependent tynA expression in the tested aromatic-amine carbon/nitrogen conditions. Isolated His-tagged FeaR DNA-binding-domain experiments do not establish direct ligand binding by full-length FeaR or aminoacetone induction.

    Source locationMethods 2.1–2.4; Results 3.1–3.7; Discussion
DNA-binding transcriptional dual regulator FNR
EcoCyc:CPLX0-7797		activates

The native complex comment reports FNR-associated tynA transcriptional activation in anaerobic profiling (PMID12754220). The inspected 2013 aromatic-amine study found no anaerobic induction under its conditions; this context conflict does not establish direct promoter binding or anaerobic oxidase flux.

tynA
Entrez:945939
  • MetaCyc:AMINEOXID-CPLX

    Source assertion: The native complex comment reports FNR-associated tynA transcriptional activation in anaerobic profiling (PMID12754220). The inspected 2013 aromatic-amine study found no anaerobic induction under its conditions; this context conflict does not establish direct promoter binding or anaerobic oxidase flux.

    Source location/ptools-xml/Protein/comment; final paragraph beginning "Under anaerobiosis, FNR activates" and citing PMID12754220
  • PMID:24013633

    Source assertion: No anaerobic induction was observed in the tested aromatic-amine reporter conditions.

    Source locationResults/Discussion, oxygen dependence
HTH-type transcriptional repressor NsrR
UniProtKB:P0AF63

experimental construct: NsrR protein expressed in the cited GUG-to-AUG translation-start construct. This is a start-codon/expression-context change, not an asserted amino-acid substitution. Exact whole construct sequence and native tynA-site geometry were not established in the accessible material.

Qualification evidence
  • EcoCyc:TU0-42552

    Source assertion: The native annotation specifically reports tynA repression when the nsrR start codon was changed from GUG to AUG.

    Source locationTranscription-Unit/comment; PMID26239124 paragraph
inhibits

The native TU reports tynA repression in the NsrR start-codon-enhanced expression context. The accessible primary abstracts do not resolve exact direct binding at tynA; the suspicious native coordinate is not reinterpreted as a validated local site.

tynA
Entrez:945939
  • EcoCyc:TU0-42552

    Source assertion: The native TU reports tynA repression in the NsrR start-codon-enhanced expression context. The accessible primary abstracts do not resolve exact direct binding at tynA; the suspicious native coordinate is not reinterpreted as a validated local site.

    Source locationTranscription-Unit/comment; PMID26239124 and PMID19656291 paragraphs
L-tryptophan
CHEBI:16828		inhibits

Growth with 5 mM tryptophan reduced measured serine transport and sstT RNA in the reported strains/constructs. The proposed effector could be tryptophan or its metabolite; this is expression control, not direct inhibition or proof that tryptophan is transported.

Serine/threonine transporter SstT
UniProtKB:P0AGE4

experimental construct: W3133-2 SstT cloned into low-copy pMST3/pMST321 and assayed in WAT9, with the primary report identifying Thr301 where the current P0AGE4 reference has Ala301. Other residue identity is not assumed; this expression/uptake result is not a native MG1655 sequence assay.

Qualification evidence
  • PMID:9852024

    Source assertion: The source used W3133-2 DNA and WAT9 transformants; its deduced SstT sequence had Thr301 instead of the then-reference Ala301.

    Source locationmain text: cloning, sequencing and Figure 1; tryptophan-expression paragraph
  • PMID:9852024

    Source assertion: Growth with 5 mM tryptophan reduced measured serine transport and sstT RNA in the reported strains/constructs. The proposed effector could be tryptophan or its metabolite; this is expression control, not direct inhibition or proof that tryptophan is transported.

    Source locationfinal main-text paragraph; Northern blot and uptake observations
valinomycin
CHEBI:28545		activates

The reviewed activity-regulation annotation assigns valinomycin activation and monensin inhibition to SstT. These effects concern the cited serine-uptake assay; unspecified monensin is not assigned to monensin A.

Serine/threonine transporter SstT
UniProtKB:P0AGE4

experimental construct: SstT carrying eight successive C-terminal histidines, overproduced from pTSTH under the trc promoter, Ni-NTA purified and reconstituted in liposomes. The reported 20-residue N terminus lacked initiating methionine; full construct identity with current P0AGE4 or the older Thr301 variant is not assumed.

Qualification evidence
  • PMID:12097162

    Source assertion: The study added eight histidine codons at the sstT 3′ end, purified the fusion by Ni-NTA and reconstituted it into liposomes; only its first 20 N-terminal residues were experimentally sequenced.

    Source locationissuing primary abstract
  • UniProtKB:P0AGE4

    Source assertion: The reviewed activity-regulation annotation assigns valinomycin activation and monensin inhibition to SstT. These effects concern the cited serine-uptake assay; unspecified monensin is not assigned to monensin A.

    Source locationcomments[ACTIVITY REGULATION]; cited PMID12097162
  • PMID:12097162

    Source assertion: The primary abstract describes C-terminal eight-His SstT from pTSTH, Ni-NTA purification and reconstituted proteoliposomes. Serine uptake was measured; threonine competed. The first 20 residues matched the deduced sequence after excision of initiating methionine.

    Source locationissuing primary abstract: construction, purification, N-terminal sequencing and reconstitution
CCCP
CHEBI:3259		inhibits

CCCP strongly inhibited threonine uptake in the anaerobically induced MC4100/TH16-derived TdcC assays; the result supports dependence on proton motive force. Historical TdcC was reported as 431 residues, whereas current P0AAD8 is 443; the complete assayed sequence is not established. This does not identify an engineered truncation or a distinct assayed variant.

Threonine/serine transporter TdcC
UniProtKB:P0AAD8
  • PMID:2115866

    Source assertion: CCCP strongly inhibited threonine uptake in the anaerobically induced MC4100/TH16-derived TdcC assays; the result supports dependence on proton motive force.

    Source locationOriginal article p. 4291, Characterization of transport system and energetic-inhibitor experiments
  • PMID:2115866

    Source assertion: The primary Discussion describes TdcC as 431 residues; the whole-cell uptake assays are distinct from the separate PhoA/LacZ topology fusions. The complete sequence of the transport-assayed material is not established.

    Source locationOriginal article p. 4291 Fig. 5 and transport experiments; p. 4292 Discussion and separate Fig. 6 fusion experiments
  • UniProtKB:P0AAD8

    Source assertion: Current P0AAD8 is 443 residues and records historical sequence conflicts at residue 70 and residues 431–443. This does not prove that the historical transport preparation was a distinct physical variant.

    Source locationsequence/length; features[type="Sequence conflict"]/location and description
potassium cyanide
CHEBI:33191		inhibits

KCN partially inhibited threonine uptake in the anaerobically induced TdcC assays. Sodium/monensin effects differed from the SstT system; this is an energetic whole-cell treatment, not a purified transporter binding assay. Historical TdcC was reported as 431 residues, whereas current P0AAD8 is 443; the complete assayed sequence is not established. This does not identify an engineered truncation or a distinct assayed variant.

Threonine/serine transporter TdcC
UniProtKB:P0AAD8
  • PMID:2115866

    Source assertion: KCN partially inhibited threonine uptake in the anaerobically induced TdcC assays. Sodium/monensin effects differed from the SstT system; this is an energetic whole-cell treatment, not a purified transporter binding assay.

    Source locationOriginal article p. 4291, Characterization of transport system and energetic-inhibitor experiments
  • PMID:2115866

    Source assertion: The primary Discussion describes TdcC as 431 residues; the whole-cell uptake assays are distinct from the separate PhoA/LacZ topology fusions. The complete sequence of the transport-assayed material is not established.

    Source locationOriginal article p. 4291 Fig. 5 and transport experiments; p. 4292 Discussion and separate Fig. 6 fusion experiments
  • UniProtKB:P0AAD8

    Source assertion: Current P0AAD8 is 443 residues and records historical sequence conflicts at residue 70 and residues 431–443. This does not prove that the historical transport preparation was a distinct physical variant.

    Source locationsequence/length; features[type="Sequence conflict"]/location and description
L-serine
CHEBI:17115		inhibits

Excess L-serine strongly reduced radiolabeled threonine uptake in the TdcC-expressing cell assay; competition does not imply an allosteric inhibitor. Historical TdcC was reported as 431 residues, whereas current P0AAD8 is 443; the complete assayed sequence is not established. This does not identify an engineered truncation or a distinct assayed variant.

Threonine/serine transporter TdcC
UniProtKB:P0AAD8
  • PMID:2115866

    Source assertion: Excess L-serine strongly reduced radiolabeled threonine uptake in the TdcC-expressing cell assay; competition does not imply an allosteric inhibitor.

    Source locationOriginal article p. 4291, Characterization of transport system and Table 1; anaerobically induced TH16(pEC61), 0.5 mM competitor (50-fold)
  • PMID:2115866

    Source assertion: The primary Discussion describes TdcC as 431 residues; the whole-cell uptake assays are distinct from the separate PhoA/LacZ topology fusions. The complete sequence of the transport-assayed material is not established.

    Source locationOriginal article p. 4291 Fig. 5 and transport experiments; p. 4292 Discussion and separate Fig. 6 fusion experiments
  • UniProtKB:P0AAD8

    Source assertion: Current P0AAD8 is 443 residues and records historical sequence conflicts at residue 70 and residues 431–443. This does not prove that the historical transport preparation was a distinct physical variant.

    Source locationsequence/length; features[type="Sequence conflict"]/location and description
L-leucine
CHEBI:15603		inhibits

Excess L-leucine reduced TdcC-associated threonine uptake by about half in the cell competition assay. This differs from the transcriptional Lrp/leucine claims. Historical TdcC was reported as 431 residues, whereas current P0AAD8 is 443; the complete assayed sequence is not established. This does not identify an engineered truncation or a distinct assayed variant.

Threonine/serine transporter TdcC
UniProtKB:P0AAD8
  • PMID:2115866

    Source assertion: Excess L-leucine reduced TdcC-associated threonine uptake by about half in the cell competition assay. This differs from the transcriptional Lrp/leucine claims.

    Source locationOriginal article p. 4291, Characterization of transport system and Table 1; anaerobically induced TH16(pEC61), 0.5 mM competitor (50-fold)
  • PMID:2115866

    Source assertion: The primary Discussion describes TdcC as 431 residues; the whole-cell uptake assays are distinct from the separate PhoA/LacZ topology fusions. The complete sequence of the transport-assayed material is not established.

    Source locationOriginal article p. 4291 Fig. 5 and transport experiments; p. 4292 Discussion and separate Fig. 6 fusion experiments
  • UniProtKB:P0AAD8

    Source assertion: Current P0AAD8 is 443 residues and records historical sequence conflicts at residue 70 and residues 431–443. This does not prove that the historical transport preparation was a distinct physical variant.

    Source locationsequence/length; features[type="Sequence conflict"]/location and description
L-homoserine
CHEBI:15699		inhibits

Excess homoserine reduced TdcC-associated threonine uptake in the primary competition experiment; this is whole-cell substrate competition. Historical TdcC was reported as 431 residues, whereas current P0AAD8 is 443; the complete assayed sequence is not established. This does not identify an engineered truncation or a distinct assayed variant.

Threonine/serine transporter TdcC
UniProtKB:P0AAD8
  • PMID:2115866

    Source assertion: Excess homoserine reduced TdcC-associated threonine uptake in the primary competition experiment; this is whole-cell substrate competition.

    Source locationOriginal article p. 4291, Characterization of transport system and Table 1; anaerobically induced TH16(pEC61), 0.5 mM competitor (50-fold)
  • PMID:2115866

    Source assertion: The primary Discussion describes TdcC as 431 residues; the whole-cell uptake assays are distinct from the separate PhoA/LacZ topology fusions. The complete sequence of the transport-assayed material is not established.

    Source locationOriginal article p. 4291 Fig. 5 and transport experiments; p. 4292 Discussion and separate Fig. 6 fusion experiments
  • UniProtKB:P0AAD8

    Source assertion: Current P0AAD8 is 443 residues and records historical sequence conflicts at residue 70 and residues 431–443. This does not prove that the historical transport preparation was a distinct physical variant.

    Source locationsequence/length; features[type="Sequence conflict"]/location and description
iodoacetacte
CHEBI:747879		inhibits

Iodoacetate modification of one cysteine per Tdh subunit caused complete activity loss; the isolated peptide placed it at Cys38. The pinned ChEBI native label is misspelled iodoacetacte, while its definition/structure identify iodoacetate.

threonine dehydrogenase
MetaCyc:THREODEHYD-CPLX
  • PMID:2007567

    Source assertion: Iodoacetate modification of one cysteine per Tdh subunit caused complete activity loss; the isolated peptide placed it at Cys38. The pinned ChEBI native label is misspelled iodoacetacte, while its definition/structure identify iodoacetate.

    Source locationissuing primary abstract: active-site cysteine modification and metal removal
1,10-phenanthroline
CHEBI:44975		inhibits

Removing Tdh-associated zinc with 1,10-phenanthroline correlated with declining activity and eventually yielded an unstable protein; this is a chelation experiment, not an endogenous control.

threonine dehydrogenase
MetaCyc:THREODEHYD-CPLX
  • PMID:2007567

    Source assertion: Removing Tdh-associated zinc with 1,10-phenanthroline correlated with declining activity and eventually yielded an unstable protein; this is a chelation experiment, not an endogenous control.

    Source locationissuing primary abstract: active-site cysteine modification and metal removal
dioxygen
CHEBI:15379		inhibits

The native FNR comment describes oxygen-mediated oxidation of the active [4Fe-4S] form to a [2Fe-2S] form and loss of the active dimer. This bounds the anaerobic regulatory context; it is not direct TynA inhibition.

DNA-binding transcriptional dual regulator FNR
EcoCyc:CPLX0-7797

molecular state: Active [4Fe-4S]-containing FNR dimer under anaerobic conditions; oxygen changes this molecular state. The native complex frame is retained without claiming that its identity fixes every experimental metal/redox state.

Qualification evidence
  • EcoCyc:CPLX0-7797

    Source assertion: Anaerobic [4Fe-4S] acquisition promotes the active FNR dimer; oxygen oxidizes the cluster and inactivates it.

    Source locationProtein/comment: second paragraph
  • EcoCyc:CPLX0-7797

    Source assertion: The native FNR comment describes oxygen-mediated oxidation of the active [4Fe-4S] form to a [2Fe-2S] form and loss of the active dimer. This bounds the anaerobic regulatory context; it is not direct TynA inhibition.

    Source locationProtein/comment: oxygen, iron-sulfur cluster and dimerization paragraph

References

Curation history