2-O-alpha-mannosyl-D-glycerate degradation
MetaCyc:PWY0-1300
The native two-reaction pathway hydrolyzes imported MG phosphate to anomer-unspecified D-mannopyranose 6-phosphate and (R)-glycerate, then phosphorylates glycerate to 2-phosphoglycerate. MngA uptake and the PEP–PtsI–HPr relay are linked entry/energy context, not extra core members. E. coli K-12 culture and genetic evidence supports the route; the MngB purified-substrate assay, product anomer and physiological metal remain unresolved. Regulatory expression effects, constructs, source conflicts and opaque downstream interfaces retain their evidence limits. MG biosynthesis and unphosphorylated thermophile MG hydrolysis are excluded.
- Pathway type
- carbohydrate degradation
- Organism scope
Pathway network
66 nodes · 75 asserted directed edges
Arrows show recorded subject → object relationships, not necessarily metabolic flow. Select a node for details or an arrow for evidence. Scroll, zoom or find a node to explore.
- Reaction / activity
- Chemical / cofactor
- Protein / complex
- Other participant
- Cell / process context
- Pathway
- Solid arrow: mechanistic relation
- Dashed arrow: membership, location or cofactor relation
Components and activities
| Node | Kind or role | Source direction |
|---|---|---|
Escherichia coli K-12NCBITaxon:83333 | taxon | |
Escherichia coli str. K-12 substr. MG1655NCBITaxon:511145 | taxon | |
2-(alpha-D-mannosyl)-D-glycerateCHEBI:57541 | small molecule | |
2-O-(6-phospho-alpha-D-mannosyl)-D-glycerateCHEBI:60331 | small molecule | |
waterCHEBI:15377 | small molecule | |
D-mannopyranose 6-phosphate(2-)CHEBI:58735 | small molecule | |
D-glycerateCHEBI:16659 | small molecule | |
ATP(4-)CHEBI:30616 | small molecule | |
ADP(3-)CHEBI:456216 | small molecule | |
hydronCHEBI:15378 | small molecule | |
2-phosphonato-D-glycerate(3-)CHEBI:58289 | small molecule | |
phosphonatoenolpyruvateCHEBI:58702 | small molecule | |
pyruvateCHEBI:15361 | small molecule | |
alpha-D-mannose 6-phosphate(2-)CHEBI:60332 | small molecule | |
2-oxoglutarate(2-)CHEBI:16810 | small molecule | |
divalent metal cationCHEBI:60240 | cofactor | |
magnesium(2+)CHEBI:18420 | cofactor | |
iron(2+)CHEBI:29033 | cofactor | |
PTS system 2-O-alpha-mannosyl-D-glycerate-specific EIIABC componentUniProtKB:P54745 | protein | |
Mannosylglycerate hydrolaseUniProtKB:P54746 | protein | |
Glycerate 2-kinaseUniProtKB:P23524 | protein | |
Phosphoenolpyruvate-protein phosphotransferaseUniProtKB:P08839 | protein | |
Phosphocarrier protein HPrUniProtKB:P0AA04 | protein | |
Mannosyl-D-glycerate transport/metabolism system repressor MngRUniProtKB:P13669 | protein | |
Carbohydrate diacid regulatorUniProtKB:P37047 | protein | |
DNA-binding protein H-NSUniProtKB:P0ACF8 | protein | |
Fumarate and nitrate reduction regulatory proteinUniProtKB:P0A9E5 | protein | |
Ferric uptake regulation proteinUniProtKB:P0A9A9 | protein | |
Pole-localizer protein TmaRUniProtKB:P0A8M6 | protein | |
mngAEntrez:945355 | gene | |
mngBEntrez:945359 | gene | |
mngREntrez:945371 | gene | |
garKEntrez:947632 | gene | |
cdaREntrez:944860 | gene | |
cytoplasmGO:0005737 | cellular component | |
plasma membraneGO:0005886 | cellular component | |
nucleoidGO:0009295 | cellular component | |
PTS enzyme IMetaCyc:CPLX0-7938 | complex | |
DNA-binding transcriptional repressor MngREcoCyc:PC00103 | complex | |
DNA-binding transcriptional dual regulator FNREcoCyc:CPLX0-7797 | complex | |
Fur-Fe2+ DNA-binding transcriptional dual regulatorEcoCyc:CPLX0-7639 | complex | |
Gluconeogenesis from L-Malic AcidPathBank:SMP0000839 | pathway | |
D-glucarate(2-)CHEBI:30612 | small molecule | |
galactarate(2-)CHEBI:16537 | small molecule | |
dioxygenCHEBI:15379 | small molecule | |
tetra-mu3-sulfido-tetraironCHEBI:49883 | cofactor | |
MG-phosphate hydrolysis (anomer-unspecified mannose 6-phosphate)MetaCyc:RXN0-5216 | molecular activity | left to right |
(R)-glycerate + ATP => (2R)-2-phosphoglycerate + ADP + H(+)RHEA:27378 | molecular activity | left to right |
(2R)-2-O-(alpha-D-mannosyl)-glycerate(out) + N(pros)-phospho-L-histidyl-[protein] => (2R)-2-O-(6-phospho-alpha-D-mannosyl)-glycerate(in) + L-histidyl-[protein]RHEA:33308 | molecular activity | left to right |
L-histidyl-[protein] + phosphoenolpyruvate => N(pros)-phospho-L-histidyl-[protein] + pyruvateRHEA:23881 | molecular activity | left to right |
D-mannose degradation IMetaCyc:MANNCAT-PWY | pathway | |
colanic acid building blocks biosynthesisMetaCyc:COLANSYN-PWY | pathway |
Mechanistic edges
| Subject | Predicate and description | Object | Evidence |
|---|---|---|---|
PTS enzyme IMetaCyc:CPLX0-7938 | has_part The exact native assembly contains two copies of this polypeptide; stoichiometry 2 applies to this assembly, not all solution states. | Phosphoenolpyruvate-protein phosphotransferaseUniProtKB:P08839 |
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DNA-binding transcriptional repressor MngREcoCyc:PC00103 | has_part The exact native assembly contains two copies of this polypeptide; stoichiometry 2 applies to this assembly, not all solution states. | Mannosyl-D-glycerate transport/metabolism system repressor MngRUniProtKB:P13669 |
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DNA-binding transcriptional dual regulator FNREcoCyc:CPLX0-7797 | has_part The exact native assembly contains two copies of this polypeptide; stoichiometry 2 applies to this assembly, not all solution states. | Fumarate and nitrate reduction regulatory proteinUniProtKB:P0A9E5 |
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Fur-Fe2+ DNA-binding transcriptional dual regulatorEcoCyc:CPLX0-7639 | has_part The exact native assembly contains two copies of this polypeptide; stoichiometry 2 applies to this assembly, not all solution states. | Ferric uptake regulation proteinUniProtKB:P0A9A9 |
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MG-phosphate hydrolysis (anomer-unspecified mannose 6-phosphate)MetaCyc:RXN0-5216 | part_of Exact member of the two-reaction native pathway definition. | MetaCyc:PWY0-1300 |
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(R)-glycerate + ATP => (2R)-2-phosphoglycerate + ADP + H(+)RHEA:27378 | part_of Exact member of the two-reaction native pathway definition. | MetaCyc:PWY0-1300 |
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MG-phosphate hydrolysis (anomer-unspecified mannose 6-phosphate)MetaCyc:RXN0-5216 | precedes Native reaction-ordering places MG-P hydrolysis before glycerate phosphorylation. | (R)-glycerate + ATP => (2R)-2-phosphoglycerate + ADP + H(+)RHEA:27378 |
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(2R)-2-O-(alpha-D-mannosyl)-glycerate(out) + N(pros)-phospho-L-histidyl-[protein] => (2R)-2-O-(6-phospho-alpha-D-mannosyl)-glycerate(in) + L-histidyl-[protein]RHEA:33308 | provides_input_for MngA entry produces MG-P for the core hydrolase; it is an incoming interface, not a third core member. | MG-phosphate hydrolysis (anomer-unspecified mannose 6-phosphate)MetaCyc:RXN0-5216 |
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L-histidyl-[protein] + phosphoenolpyruvate => N(pros)-phospho-L-histidyl-[protein] + pyruvateRHEA:23881 | provides_input_for PEP phosphorylates HPr through PtsI; phospho-HPr then supplies MngA. PEP is consumed once in this contextual relay reaction, not again in the formal MngA equation. | (2R)-2-O-(alpha-D-mannosyl)-glycerate(out) + N(pros)-phospho-L-histidyl-[protein] => (2R)-2-O-(6-phospho-alpha-D-mannosyl)-glycerate(in) + L-histidyl-[protein]RHEA:33308 |
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2-O-(6-phospho-alpha-D-mannosyl)-D-glycerateCHEBI:60331 | consumes Coefficient 1. Native MG-P hydrolysis uses anomer-unspecified D-mannopyranose 6-phosphate; the alpha-specific Rhea27867 reaction is not asserted as an exact alias. | MG-phosphate hydrolysis (anomer-unspecified mannose 6-phosphate)MetaCyc:RXN0-5216 |
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waterCHEBI:15377 | consumes Coefficient 1. Native MG-P hydrolysis uses anomer-unspecified D-mannopyranose 6-phosphate; the alpha-specific Rhea27867 reaction is not asserted as an exact alias. | MG-phosphate hydrolysis (anomer-unspecified mannose 6-phosphate)MetaCyc:RXN0-5216 |
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MG-phosphate hydrolysis (anomer-unspecified mannose 6-phosphate)MetaCyc:RXN0-5216 | produces Coefficient 1. Native MG-P hydrolysis uses anomer-unspecified D-mannopyranose 6-phosphate; the alpha-specific Rhea27867 reaction is not asserted as an exact alias. | D-mannopyranose 6-phosphate(2-)CHEBI:58735 |
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MG-phosphate hydrolysis (anomer-unspecified mannose 6-phosphate)MetaCyc:RXN0-5216 | produces Coefficient 1. Native MG-P hydrolysis uses anomer-unspecified D-mannopyranose 6-phosphate; the alpha-specific Rhea27867 reaction is not asserted as an exact alias. | D-glycerateCHEBI:16659 |
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D-glycerateCHEBI:16659 | consumes Coefficient 1; forward glycerate 2-kinase reaction. ATP is a consumed substrate; Mg occupancy is not specified by this equation. | (R)-glycerate + ATP => (2R)-2-phosphoglycerate + ADP + H(+)RHEA:27378 |
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ATP(4-)CHEBI:30616 | consumes Coefficient 1; forward glycerate 2-kinase reaction. ATP is a consumed substrate; Mg occupancy is not specified by this equation. | (R)-glycerate + ATP => (2R)-2-phosphoglycerate + ADP + H(+)RHEA:27378 |
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(R)-glycerate + ATP => (2R)-2-phosphoglycerate + ADP + H(+)RHEA:27378 | produces Coefficient 1; forward glycerate 2-kinase reaction. ATP is a consumed substrate; Mg occupancy is not specified by this equation. | 2-phosphonato-D-glycerate(3-)CHEBI:58289 |
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(R)-glycerate + ATP => (2R)-2-phosphoglycerate + ADP + H(+)RHEA:27378 | produces Coefficient 1; forward glycerate 2-kinase reaction. ATP is a consumed substrate; Mg occupancy is not specified by this equation. | ADP(3-)CHEBI:456216 |
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(R)-glycerate + ATP => (2R)-2-phosphoglycerate + ADP + H(+)RHEA:27378 | produces Coefficient 1; forward glycerate 2-kinase reaction. ATP is a consumed substrate; Mg occupancy is not specified by this equation. | hydronCHEBI:15378 |
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2-(alpha-D-mannosyl)-D-glycerateCHEBI:57541 | consumes Coefficient 1 MG outside; native compartment CCO-OUT. MngA couples uptake to phosphorylation. | (2R)-2-O-(alpha-D-mannosyl)-glycerate(out) + N(pros)-phospho-L-histidyl-[protein] => (2R)-2-O-(6-phospho-alpha-D-mannosyl)-glycerate(in) + L-histidyl-[protein]RHEA:33308 |
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Phosphocarrier protein HPrUniProtKB:P0AA04molecular state: His15 phosphorylated HPr donor in the cytoplasm. This is the E. coli phosphocarrier protein state, not free histidine; native generic HPr Compound classes are instantiated using issuing P0AA04 identity. Qualification evidence
| consumes Coefficient 1 phosphohistidyl HPr inside; native CCO-IN. One HPr phosphate supplies the incoming MG. | (2R)-2-O-(alpha-D-mannosyl)-glycerate(out) + N(pros)-phospho-L-histidyl-[protein] => (2R)-2-O-(6-phospho-alpha-D-mannosyl)-glycerate(in) + L-histidyl-[protein]RHEA:33308 |
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(2R)-2-O-(alpha-D-mannosyl)-glycerate(out) + N(pros)-phospho-L-histidyl-[protein] => (2R)-2-O-(6-phospho-alpha-D-mannosyl)-glycerate(in) + L-histidyl-[protein]RHEA:33308 | produces Coefficient 1 MG-P inside; native CCO-IN. ATP and proton-motive force are not asserted as additional energy inputs. | 2-O-(6-phospho-alpha-D-mannosyl)-D-glycerateCHEBI:60331 |
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(2R)-2-O-(alpha-D-mannosyl)-glycerate(out) + N(pros)-phospho-L-histidyl-[protein] => (2R)-2-O-(6-phospho-alpha-D-mannosyl)-glycerate(in) + L-histidyl-[protein]RHEA:33308 | produces Coefficient 1 histidyl HPr inside; native CCO-IN. The carrier remains a protein after phosphate transfer. | Phosphocarrier protein HPrUniProtKB:P0AA04molecular state: His15 unphosphorylated HPr acceptor in the cytoplasm. This is the E. coli phosphocarrier protein state, not free histidine; native generic HPr Compound classes are instantiated using issuing P0AA04 identity. Qualification evidence
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phosphonatoenolpyruvateCHEBI:58702 | consumes Coefficient 1 PEP in the contextual PtsI-to-HPr reaction; native composite direction is physiological left-to-right. | L-histidyl-[protein] + phosphoenolpyruvate => N(pros)-phospho-L-histidyl-[protein] + pyruvateRHEA:23881 |
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Phosphocarrier protein HPrUniProtKB:P0AA04molecular state: His15 unphosphorylated HPr acceptor in the cytoplasm. This is the E. coli phosphocarrier protein state, not free histidine; native generic HPr Compound classes are instantiated using issuing P0AA04 identity. Qualification evidence
| consumes Coefficient 1 histidyl HPr accepts phosphate through PtsI. | L-histidyl-[protein] + phosphoenolpyruvate => N(pros)-phospho-L-histidyl-[protein] + pyruvateRHEA:23881 |
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L-histidyl-[protein] + phosphoenolpyruvate => N(pros)-phospho-L-histidyl-[protein] + pyruvateRHEA:23881 | produces Coefficient 1 pyruvate is formed from PEP during general PTS energy coupling. | pyruvateCHEBI:15361 |
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L-histidyl-[protein] + phosphoenolpyruvate => N(pros)-phospho-L-histidyl-[protein] + pyruvateRHEA:23881 | produces Coefficient 1 phosphohistidyl HPr supplies downstream MngA. | Phosphocarrier protein HPrUniProtKB:P0AA04molecular state: His15 phosphorylated HPr donor in the cytoplasm. This is the E. coli phosphocarrier protein state, not free histidine; native generic HPr Compound classes are instantiated using issuing P0AA04 identity. Qualification evidence
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PTS system 2-O-alpha-mannosyl-D-glycerate-specific EIIABC componentUniProtKB:P54745 | catalyzes MngA is one 658-residue EIIABC chain. MC4100 mngA deletion loses MG transport and pACS31 restores it; inverted membranes plus general PTS extracts and PEP form MG-P. This is not a purified three-protein reconstitution. Separate intact-cell uptake comparisons in MG-induced MC4100 reported weak reduction with glucose, mannose and mannitol, a smaller effect with trehalose, and no observed reduction with fructose, maltose, arabinose, gluconate, glycerate, 1-alpha-glucosylglycerol, 2-alpha-glucosylglycerate or 2-alpha-mannosylglycerol. The Discussion instead describes mannose and those three glycosyl analogues as not significantly inhibitory even at 1 mM against 0.1 micromolar radiolabeled MG; the mannose weak-effect/no-significant-effect tension remains unresolved. These are uptake comparisons, not direct binding, a proven competitive mechanism or inhibition constants. Separately, 300 mM NaCl during growth did not induce transport and reduced MG-dependent induction by about 50%; this is an induction endpoint, distinct from the KM522 500 mM salt-protection experiment and from a direct catalytic salt effect. None of these whole-cell comparisons is attributed to the pACS31 inverted-membrane assay. | (2R)-2-O-(alpha-D-mannosyl)-glycerate(out) + N(pros)-phospho-L-histidyl-[protein] => (2R)-2-O-(6-phospho-alpha-D-mannosyl)-glycerate(in) + L-histidyl-[protein]RHEA:33308 |
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PTS system 2-O-alpha-mannosyl-D-glycerate-specific EIIABC componentUniProtKB:P54745experimental construct: pACS31/pTrc99b MngA expression construct in inverted-membrane preparations; accompanying general PTS extract. This observation does not identify native oligomeric stoichiometry or directly measure His87/Cys192 phosphorylation. Qualification evidence
| enables Construct-qualified transport support: pACS31 encodes IPTG-controlled MngA in inverted membranes; general PTS-containing extract and PEP are supplied. Native MngA His87/Cys192 are putative sequence assignments, not measured occupancy. | (2R)-2-O-(alpha-D-mannosyl)-glycerate(out) + N(pros)-phospho-L-histidyl-[protein] => (2R)-2-O-(6-phospho-alpha-D-mannosyl)-glycerate(in) + L-histidyl-[protein]RHEA:33308 |
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Mannosylglycerate hydrolaseUniProtKB:P54746 | enables MngB is the native MG-P hydrolase assignment, supported by physiological genetics and p-nitrophenyl-alpha-D-mannoside surrogate activity. The inspected native record states that MngB has not been purified; MG-P turnover and product anomer were not directly measured with purified MngB. | MG-phosphate hydrolysis (anomer-unspecified mannose 6-phosphate)MetaCyc:RXN0-5216 |
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Glycerate 2-kinaseUniProtKB:P23524 | catalyzes GarK catalyzes glycerate 2-phosphorylation. Native direction and later in-vivo product selection support2PG; historical GKI/GKII naming does not justify transferring disputed pH, temperature or metal measurements between enzymes. | (R)-glycerate + ATP => (2R)-2-phosphoglycerate + ADP + H(+)RHEA:27378 |
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Glycerate 2-kinaseUniProtKB:P23524experimental construct: Plasmid-expressed E. coli GarK in ΔgpmA ΔgpmM ΔgarK ΔglxK cells; cloning primers encode an N-terminal His6 sequence. No tag cleavage or identity to native assembly is asserted. Qualification evidence
| enables GarK product specificity is supported by complementation in the engineered ΔgpmA ΔgpmM ΔgarK ΔglxK background. This growth-selection experiment is not a native oligomer assay or a purified direct product measurement. | (R)-glycerate + ATP => (2R)-2-phosphoglycerate + ADP + H(+)RHEA:27378 |
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PTS enzyme IMetaCyc:CPLX0-7938 | catalyzes The independently issued MetaCyc PtsI dimer matches the EcoCyc PTSI-MONOMER2 assembly. It transfers a PEP-derived phosphate through PtsI His189 to HPr His15; the composite native reaction has two substeps, neither a new MG core member. | L-histidyl-[protein] + phosphoenolpyruvate => N(pros)-phospho-L-histidyl-[protein] + pyruvateRHEA:23881 |
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Mannosylglycerate hydrolaseUniProtKB:P54746 | has_cofactor UniProt assigns one divalent metal cation per MngB subunit by similarity(ECO:0000250). Exact metal identity, physiological occupancy and biological assembly remain unresolved. | divalent metal cationCHEBI:60240 |
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PTS enzyme IMetaCyc:CPLX0-7938 | has_cofactor Mg2+ is required by PtsI. The Mg/oxalate-trapped phosphoenzyme structure supports the catalytic metal context; the crystallized occupancy is not a universal cellular stoichiometry. | magnesium(2+)CHEBI:18420 |
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Fur-Fe2+ DNA-binding transcriptional dual regulatorEcoCyc:CPLX0-7639 | has_part The exact native Fur-Fe2+ assembly contains two ferrous ions with two Fur polypeptides; this stoichiometry is not inferred for apo-Fur or every DNA-binding assay. | iron(2+)CHEBI:29033 |
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PTS system 2-O-alpha-mannosyl-D-glycerate-specific EIIABC componentUniProtKB:P54745 | located_in MngA is an inner-membrane multipass protein. Predicted N-terminal topology is not adopted as experimentally measured phosphorelay sidedness. | plasma membraneGO:0005886 |
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Phosphoenolpyruvate-protein phosphotransferaseUniProtKB:P08839 | located_in PtsI is cytoplasmic; its polar sequestration is a regulated state examined in general sugar studies. | cytoplasmGO:0005737 |
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Phosphocarrier protein HPrUniProtKB:P0AA04 | located_in HPr is a soluble cytoplasmic phosphocarrier, not the inner-membrane protein implied by frozen PathBank placement. | cytoplasmGO:0005737 |
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DNA-binding protein H-NSUniProtKB:P0ACF8 | located_in H-NS is a nucleoid-associated protein; it forms variable oligomers, so no fixed H-NS stoichiometry is assigned. | nucleoidGO:0009295 |
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(2R)-2-O-(alpha-D-mannosyl)-glycerate(out) + N(pros)-phospho-L-histidyl-[protein] => (2R)-2-O-(6-phospho-alpha-D-mannosyl)-glycerate(in) + L-histidyl-[protein]RHEA:33308 | occurs_in The coupled uptake/phosphorylation event crosses the cell inner membrane; individual MG and HPr sides retain their native OUT/IN assignments. | plasma membraneGO:0005886 |
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mngAEntrez:945355 | enables Issuing gene/protein cross-references identify the encoded MG1655 protein; gene-expression edges target the gene, not the enzyme catalytic state. | PTS system 2-O-alpha-mannosyl-D-glycerate-specific EIIABC componentUniProtKB:P54745 |
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mngBEntrez:945359 | enables Issuing gene/protein cross-references identify the encoded MG1655 protein; gene-expression edges target the gene, not the enzyme catalytic state. | Mannosylglycerate hydrolaseUniProtKB:P54746 |
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mngREntrez:945371 | enables Issuing gene/protein cross-references identify the encoded MG1655 protein; gene-expression edges target the gene, not the enzyme catalytic state. | Mannosyl-D-glycerate transport/metabolism system repressor MngRUniProtKB:P13669 |
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garKEntrez:947632 | enables Issuing gene/protein cross-references identify the encoded MG1655 protein; gene-expression edges target the gene, not the enzyme catalytic state. | Glycerate 2-kinaseUniProtKB:P23524 |
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cdaREntrez:944860 | enables Issuing gene/protein cross-references identify the encoded MG1655 protein; gene-expression edges target the gene, not the enzyme catalytic state. | Carbohydrate diacid regulatorUniProtKB:P37047 |
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DNA-binding transcriptional repressor MngREcoCyc:PC00103 | inhibits MngR represses mngAB expression. Gene-deletion/complementation and native operator annotation support this relation; an MG-P ligand remains proposed rather than a demonstrated direct binding interaction. | mngAEntrez:945355 |
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DNA-binding transcriptional repressor MngREcoCyc:PC00103 | inhibits MngR represses mngAB expression. Gene-deletion/complementation and native operator annotation support this relation; an MG-P ligand remains proposed rather than a demonstrated direct binding interaction. | mngBEntrez:945359 |
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DNA-binding transcriptional repressor MngREcoCyc:PC00103 | inhibits Native MngR autorepression is retained as regulatory annotation. The historical fatty-acyl-responsive interpretation is disputed; high-concentration displacement may reflect protein damage. | mngREntrez:945371 |
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Carbohydrate diacid regulatorUniProtKB:P37047experimental construct: MC4100 reporter/loss-rescue context: active wild-type or pRM1-complemented SdaR/CdaR is inferred from loss in JA176 (paper-numbered P297S) and JA177 (Tn5 20 nt before stop); these mutants are not active endpoints. The paper uses a 391-aa reference versus current P37047 (385 aa); residue numbering is not mapped to the current chain. Qualification evidence
| activates CdaR activates garPLRK expression. MC4100 reporter, regulator-mutant and complementation evidence supports activation; direct binding of small-molecule inducers is not demonstrated. | garKEntrez:947632 |
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DNA-binding protein H-NSUniProtKB:P0ACF8 | inhibits H-NS negatively controls garPLRK expression. The hns651 comparison measures garP transcript in DL1504/DL1947 at 23/37°C in M9 glycerol; it is not direct GarK inhibition or an MG-flux assay. | garKEntrez:947632 |
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DNA-binding transcriptional dual regulator FNREcoCyc:CPLX0-7797molecular state: Low-oxygen, [4Fe-4S]-containing FNR dimer. Native annotation supports this active regulatory state; exact in-vivo occupancy under MG growth is not measured. Qualification evidence
| activates Native annotation assigns positive FNR control of garPLRK-rnpB from transcriptomics. The upstream site is putative and its sequence was not shown; the cited primary article was accessible only as metadata/abstract. | garKEntrez:947632 |
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Fur-Fe2+ DNA-binding transcriptional dual regulatorEcoCyc:CPLX0-7639 | regulates Fur control is unsigned here: native negative mode conflicts with primary intragenic garP binding and discussion of prior garPLRK activation. The internal element has unknown function; established promoter repression is not asserted. | garKEntrez:947632 |
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Carbohydrate diacid regulatorUniProtKB:P37047experimental construct: MC4100 reporter/loss-rescue context: active wild-type or pRM1-complemented SdaR/CdaR is inferred from loss in JA176 (paper-numbered P297S) and JA177 (Tn5 20 nt before stop); these mutants are not active endpoints. The paper uses a 391-aa reference versus current P37047 (385 aa); residue numbering is not mapped to the current chain. Qualification evidence
| activates CdaR/sdaR positively autoregulates expression in the tested MC4100 reporter system. The three inducing carbon sources increase reporter activity only with functional regulator; this does not establish direct ligand binding. | cdaREntrez:944860 |
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2-(alpha-D-mannosyl)-D-glycerateCHEBI:57541 | activates MG exposure induces expression in the tested E. coli K-12 culture context. The effect does not establish direct MG or MG-P binding to MngR/CdaR; cdaR and garK effects belong to the linked sugar-diacid regulon. | mngAEntrez:945355 |
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2-(alpha-D-mannosyl)-D-glycerateCHEBI:57541 | activates MG exposure induces expression in the tested E. coli K-12 culture context. The effect does not establish direct MG or MG-P binding to MngR/CdaR; cdaR and garK effects belong to the linked sugar-diacid regulon. | mngBEntrez:945359 |
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2-(alpha-D-mannosyl)-D-glycerateCHEBI:57541 | activates MG exposure induces expression in the tested E. coli K-12 culture context. The effect does not establish direct MG or MG-P binding to MngR/CdaR; cdaR and garK effects belong to the linked sugar-diacid regulon. | mngREntrez:945371 |
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2-(alpha-D-mannosyl)-D-glycerateCHEBI:57541 | activates MG exposure induces expression in the tested E. coli K-12 culture context. The effect does not establish direct MG or MG-P binding to MngR/CdaR; cdaR and garK effects belong to the linked sugar-diacid regulon. | cdaREntrez:944860 |
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2-(alpha-D-mannosyl)-D-glycerateCHEBI:57541 | activates MG exposure induces expression in the tested E. coli K-12 culture context. The effect does not establish direct MG or MG-P binding to MngR/CdaR; cdaR and garK effects belong to the linked sugar-diacid regulon. | garKEntrez:947632 |
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D-mannose degradation IMetaCyc:MANNCAT-PWY | has_input The native outgoing pathway link uses alpha-D-mannose 6-phosphate. This interface granularity differs from the anomer-unspecified hydrolase product; no unobserved anomerization or exact generic-to-alpha equivalence is inserted. | alpha-D-mannose 6-phosphate(2-)CHEBI:60332 |
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colanic acid building blocks biosynthesisMetaCyc:COLANSYN-PWY | has_input The native outgoing pathway link uses alpha-D-mannose 6-phosphate. This interface granularity differs from the anomer-unspecified hydrolase product; no unobserved anomerization or exact generic-to-alpha equivalence is inserted. | alpha-D-mannose 6-phosphate(2-)CHEBI:60332 |
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MetaCyc:PWY0-1300 | has_part Frozen source context includes an opaque gluconeogenesis interface attached through an Interaction participant pair with2PG. This structural context is not an additional core reaction, proven flux direction, or biological inhibition; child chemistry remains unexpanded. | Gluconeogenesis from L-Malic AcidPathBank:SMP0000839 |
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2-oxoglutarate(2-)CHEBI:16810 | inhibits 2-Oxoglutarate inhibits full-length PtsI in the 2011 study. Its noncompetitive interpretation conflicts with the later isolated-EIC competitive model; assay scope and reagent-quality alternatives remain explicit. | Phosphoenolpyruvate-protein phosphotransferaseUniProtKB:P08839experimental construct: Full-length N-terminal His-tagged PtsI from ASKA strain b2416; the 2011 assay measures isotopic PEP/pyruvate exchange. This differs from 2013 EIC261–575 and does not measure native-cell MG uptake. Qualification evidence
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2-oxoglutarate(2-)CHEBI:16810 | inhibits The 2013 isolated EIC assay supports competition with PEP. It measures PEP hydrolysis rather than complete HPr phosphotransfer; reagent contamination is a proposed explanation for differing earlier kinetics, and mixed effects in intact EI are not excluded. | Phosphoenolpyruvate-protein phosphotransferaseUniProtKB:P08839experimental construct: Isolated PtsI EIC residues261–575; NMR comparison uses EIN1–249 and full-length1–575. The R465A mutant is a separate specificity probe. No equivalence to full native HPr phosphotransfer is asserted. Qualification evidence
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Pole-localizer protein TmaRUniProtKB:P0A8M6experimental construct: TmaR-YFP/mYFP-TmaR imaging and His-TmaR interaction experiments; Tyr72 mutants alter localization and release. These constructs do not establish a native fixed complex stoichiometry. Qualification evidence
| regulates TmaR controls PtsI localization and activity by polar sequestration/release in general sugar studies. Tagged WT and phosphosite-mutant constructs establish context; no MG-specific control, universal occupancy or fixed TmaR–EI stoichiometry is asserted. | Phosphoenolpyruvate-protein phosphotransferaseUniProtKB:P08839experimental construct: Fluorescently tagged EI and Tyr122 variants in localization experiments. Tyr122-dependent polar recruitment is distinct from catalytic His189 phosphorylation. Qualification evidence
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D-glycerateCHEBI:16659 | activates The carbon source induces garPLRK or cdaR expression in MC4100 reporter experiments. This is expression-level evidence, not direct binding to CdaR; the ionic chemical identifier normalizes structure and does not imply measured assay protonation. | garKEntrez:947632 |
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D-glycerateCHEBI:16659 | activates The carbon source induces garPLRK or cdaR expression in MC4100 reporter experiments. This is expression-level evidence, not direct binding to CdaR; the ionic chemical identifier normalizes structure and does not imply measured assay protonation. | cdaREntrez:944860 |
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D-glucarate(2-)CHEBI:30612 | activates The carbon source induces garPLRK or cdaR expression in MC4100 reporter experiments. This is expression-level evidence, not direct binding to CdaR; the ionic chemical identifier normalizes structure and does not imply measured assay protonation. | garKEntrez:947632 |
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D-glucarate(2-)CHEBI:30612 | activates The carbon source induces garPLRK or cdaR expression in MC4100 reporter experiments. This is expression-level evidence, not direct binding to CdaR; the ionic chemical identifier normalizes structure and does not imply measured assay protonation. | cdaREntrez:944860 |
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galactarate(2-)CHEBI:16537 | activates The carbon source induces garPLRK or cdaR expression in MC4100 reporter experiments. This is expression-level evidence, not direct binding to CdaR; the ionic chemical identifier normalizes structure and does not imply measured assay protonation. | garKEntrez:947632 |
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galactarate(2-)CHEBI:16537 | activates The carbon source induces garPLRK or cdaR expression in MC4100 reporter experiments. This is expression-level evidence, not direct binding to CdaR; the ionic chemical identifier normalizes structure and does not imply measured assay protonation. | cdaREntrez:944860 |
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Fumarate and nitrate reduction regulatory proteinUniProtKB:P0A9E5molecular state: Active [4Fe-4S]-containing FNR subunit; oxygen-dependent state changes prevent treating this occupancy as universal. Qualification evidence
| has_cofactor The issuing FNR annotation assigns one [4Fe-4S] cluster per subunit in the active state. This is a protein-state-specific annotation, not constitutive occupancy of every FNR molecule. | tetra-mu3-sulfido-tetraironCHEBI:49883 |
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dioxygenCHEBI:15379 | inhibits Oxygen inactivates [4Fe-4S]-FNR through cluster conversion and dimer dissociation. This is general regulator-state context, not a separately measured MG-specific flux response. | DNA-binding transcriptional dual regulator FNREcoCyc:CPLX0-7797molecular state: Low-oxygen, [4Fe-4S]-containing FNR dimer. Native annotation supports this active regulatory state; exact in-vivo occupancy under MG growth is not measured. Qualification evidence
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Fumarate and nitrate reduction regulatory proteinUniProtKB:P0A9E5 | located_in Issuing protein annotation places this regulator in the cytoplasm; the location does not independently demonstrate MG-specific action. | cytoplasmGO:0005737 |
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Ferric uptake regulation proteinUniProtKB:P0A9A9 | located_in Issuing protein annotation places this regulator in the cytoplasm; the location does not independently demonstrate MG-specific action. | cytoplasmGO:0005737 |
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Pole-localizer protein TmaRUniProtKB:P0A8M6 | located_in Issuing protein annotation places this regulator in the cytoplasm; the location does not independently demonstrate MG-specific action. | cytoplasmGO:0005737 |
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References
MetaCyc:PWY0-1300MetaCyc:PWY0-1300 native evidence (source version: META PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:PWY0-1300EcoCyc:PWY0-1300 native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)MetaCyc:RXN0-5216MetaCyc:RXN0-5216 native evidence (source version: META PGDB 27.0; complete native XML retrieved 2026-10-12)PMID:25823014An In Vivo Metabolic Approach for Deciphering the Product Specificity of Glycerate Kinase Proves that Both E. coli’s Glycerate Kinases Generate 2-Phosphoglycerate (source version: Complete retained primary article XML; figures inspected as text/captions, no image-level claim)PMID:10762278A Common Regulator for the Operons Encoding the Enzymes Involved in d-Galactarate, d-Glucarate, and d-Glycerate Utilization in Escherichia coli (source version: Complete retained primary article HTML; figures inspected as text/captions, no image-level claim)PMID:17526711Human Body Temperature (37°C) Increases the Expression of Iron, Carbohydrate, and Amino Acid Utilization Genes in Escherichia coli K-12▿ (source version: Complete retained primary article HTML; figures inspected as text/captions, no image-level claim)PMID:17921503Discovery of Fur binding site clusters in Escherichia coli by information theory models (source version: Complete retained primary article XML; figures inspected as text/captions, no image-level claim)PMID:17053069Structure of phosphorylated enzyme I, the phosphoenolpyruvate:sugar phosphotransferase system sugar translocation signal protein (source version: Complete retained primary article HTML; figures inspected as text/captions, no image-level claim)PMID:22002719α-ketoglutarate coordinates carbon and nitrogen utilization via Enzyme I inhibition (source version: Complete retained primary article HTML; figures inspected as text/captions, no image-level claim)PMID:23506042Structural basis for enzyme I inhibition by α-ketoglutarate (source version: Complete retained primary article HTML; figures inspected as text/captions, no image-level claim)PMID:33376208Tyrosine phosphorylation-dependent localization of TmaR that controls activity of a major bacterial sugar regulator by polar sequestration (source version: Complete retained primary article HTML; figures inspected as text/captions, no image-level claim)PMID:14645248Sampaio et al. 2004. Phosphotransferase-mediated transport of mannosylglycerate by MngA and regulation by MngR (source version: Full primary text inspected through retained ResearchGate web observations L86–L2902; original publisher PDF unavailable; bound projection is not original PDF)PathBank:SMP0002108Frozen PathBank 2-O-alpha-Mannosyl-D-glycerate Degradation; PW002096.owl (source version: Frozen primary BioPAX archive; hash is exact42234-byte PW002096.owl member, not wholeZIP; root SMP0002108 and opaque SMP0000839 interface)UniProtKB:P54745PTS system 2-O-alpha-mannosyl-D-glycerate-specific EIIABC component (source version: Reviewed issuing UniProt JSON retrieved 2026-10-12)UniProtKB:P54746Mannosylglycerate hydrolase (source version: Reviewed issuing UniProt JSON retrieved 2026-10-12)UniProtKB:P23524Glycerate 2-kinase (source version: Reviewed issuing UniProt JSON retrieved 2026-10-12)UniProtKB:P08839Phosphoenolpyruvate-protein phosphotransferase (source version: Reviewed issuing UniProt JSON retrieved 2026-10-12)UniProtKB:P0AA04Phosphocarrier protein HPr (source version: Reviewed issuing UniProt JSON retrieved 2026-10-12)UniProtKB:P13669Mannosyl-D-glycerate transport/metabolism system repressor MngR (source version: Reviewed issuing UniProt JSON retrieved 2026-10-12)UniProtKB:P37047Carbohydrate diacid regulator (source version: Reviewed issuing UniProt JSON retrieved 2026-10-12)UniProtKB:P0ACF8DNA-binding protein H-NS (source version: Reviewed issuing UniProt JSON retrieved 2026-10-12)UniProtKB:P0A9E5Fumarate and nitrate reduction regulatory protein (source version: Reviewed issuing UniProt JSON retrieved 2026-10-12)UniProtKB:P0A9A9Ferric uptake regulation protein (source version: Reviewed issuing UniProt JSON retrieved 2026-10-12)UniProtKB:P0A8M6Pole-localizer protein TmaR (source version: Reviewed issuing UniProt JSON retrieved 2026-10-12)Entrez:945355Entrez:945355 native evidence (source version: Exact issuing NCBI Gene XML retrieved 2026-10-12; MG1655 locus)Entrez:945359Entrez:945359 native evidence (source version: Exact issuing NCBI Gene XML retrieved 2026-10-12; MG1655 locus)Entrez:945371Entrez:945371 native evidence (source version: Exact issuing NCBI Gene XML retrieved 2026-10-12; MG1655 locus)Entrez:947632Entrez:947632 native evidence (source version: Exact issuing NCBI Gene XML retrieved 2026-10-12; MG1655 locus)Entrez:944860Entrez:944860 native evidence (source version: Exact issuing NCBI Gene XML retrieved 2026-10-12; MG1655 locus)MetaCyc:CPLX0-7938MetaCyc:CPLX0-7938 native evidence (source version: META PGDB 27.0; complete native XML retrieved 2026-10-12)MetaCyc:PTSI-MONOMERMetaCyc:PTSI-MONOMER native evidence (source version: META PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:PC00103EcoCyc:PC00103 native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:PD01103EcoCyc:PD01103 native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:CPLX0-7797EcoCyc:CPLX0-7797 native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:PD00197EcoCyc:PD00197 native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:CPLX0-7639EcoCyc:CPLX0-7639 native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:PD00260EcoCyc:PD00260 native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:RXN0-2522EcoCyc:RXN0-2522 native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:2.7.3.9-RXNEcoCyc:2.7.3.9-RXN native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:GKI-RXNEcoCyc:GKI-RXN native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:PTSH-MONOMEREcoCyc:PTSH-MONOMER native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:ENZRXN0-3541EcoCyc:ENZRXN0-3541 native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:EG13236-MONOMEREcoCyc:EG13236-MONOMER native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:ENZRXN0-6336EcoCyc:ENZRXN0-6336 native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:GKI-ENZRXNEcoCyc:GKI-ENZRXN native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:ENZRXN0-8621EcoCyc:ENZRXN0-8621 native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:FE+2EcoCyc:FE+2 native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:REG0-10703EcoCyc:REG0-10703 native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:TU0-4482EcoCyc:TU0-4482 native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:REG0-5259EcoCyc:REG0-5259 native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:TU482EcoCyc:TU482 native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:REG0-5033EcoCyc:REG0-5033 native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:REG0-9114EcoCyc:REG0-9114 native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:REG0-5032EcoCyc:REG0-5032 native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:REG0-10783EcoCyc:REG0-10783 native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)MetaCyc:MANNOSE-6PMetaCyc:MANNOSE-6P native evidence (source version: META PGDB 27.0; complete native XML retrieved 2026-10-12)MetaCyc:CPD0-1063MetaCyc:CPD0-1063 native evidence (source version: META PGDB 27.0; complete native XML retrieved 2026-10-12)EcoCyc:CPD-15979EcoCyc:CPD-15979 native evidence (source version: ECOLI PGDB 27.0; complete native XML retrieved 2026-10-12)MetaCyc:GLYCERATEMetaCyc:GLYCERATE native evidence (source version: META PGDB 27.0; complete native XML retrieved 2026-10-12)RHEA:27378Rhea142 directional reaction RHEA:27378 (source version: Rhea142 retained full issuing RDF; SHA256 binds compressed original, not extracted side projection)RHEA:33308Rhea142 directional reaction RHEA:33308 (source version: Rhea142 retained full issuing RDF; SHA256 binds compressed original, not extracted side projection)RHEA:23881Rhea142 directional reaction RHEA:23881 (source version: Rhea142 retained full issuing RDF; SHA256 binds compressed original, not extracted side projection)
Curation history
- codex
- CREATE — Curate mannosylglycerate degradation with source-backed graph and reviewed identifier authorities.
Prepared and independently assessed the exact MetaCyc:PWY0-1300 scientific successor (SHA256 b73c407b4315efc45a30ed7121cb3797945cf0a4e86ab010bf5554b276b0e0a6): two core events, 17 native chemical sides, 75 mechanistic edges, 62 references and 15 endpoint qualifiers. The independent original review identified three findings, tracked as issues 441-443. The accepted successor preserves the MC4100 uptake comparisons, Results/Discussion mannose tension and separate 300 mM growth-salt induction context; scopes both CdaR subjects to their experimental constructs and historical numbering; and corrects the PtsI His189, H-NS SUBUNIT/location and 13 Rhea chemical-side locators. The independent successor review accepted these corrections with retained source and assay limitations. Separately reviewed native authority adapters and the completed original-backed canonical build preserve all prior source and ontology objects and native source ordering; actual outputs contain 2433 source terms with 575 metadata objects and 1951 ontology terms with five metadata objects. Original findings, correction dispositions, failed build attempt, accepted completion and independent audits remain in the research dossier. The 2004 body is a retained author-uploaded text projection; unavailable historical/FNR bodies and TmaR supplements remain explicit evidence limits. This curation event records completed scientific and authority preparation. It does not assert maintained gate results, saved-review completion, page QA, issue closure or merge.
- CREATE — Curate mannosylglycerate degradation with source-backed graph and reviewed identifier authorities.