pentose phosphate pathway (non-oxidative branch) II

MetaCyc:PWY-8178

The native MetaCyc PWY-8178 boundary contains six reversible reactions: ribose-phosphate isomerase, ribulose-phosphate epimerase, two transketolase events, PPi-dependent S7P phosphorylation and sedoheptulose-bisphosphate cleavage. The displayed pentose-to-hexose layout reverses the native left/right direction of RIB5PISOM-RXN and 1TRANSKETO-RXN. RXN-21730 consumes S7P and PPi and releases SBP, phosphate and a proton; PPi is a consumed donor, not merely an activating cofactor. The source supplies twenty side occurrences but no explicit coefficient fields. Generic S7P and R5P classes, beta-D-fructofuranose6-phosphate and the source's distinct ionic identities are retained. The native PPI cross-reference to neutral diphosphoric acid conflicts with its charged native structure; no neutral-acid/anion exactMatch is asserted. Shared Rhea chemistry for the other five events does not establish a Rhea identity for the PPi-S7P event or narrow the native classes. Entamoeba histolytica 200:NIH provides historical activity-level support. The 1982 study used axenic TP-S-1 culture and partially purified native transketolase, PPi-PFK and aldolase; it did not identify a modern protein sequence, tag or oligomer. Transketolase apoenzyme requires both Mg2+ and thiamine diphosphate, with a lag when Mg is added first. Its two substrate-pair assays had apparent Km values dependent on the fixed cosubstrate: R5P0.027mM with Xu5P0.3mM, Xu5P0.23mM with R5P2mM, GAP1.60mM with F6P12mM, and E4P0.005mM with Xu5P0.1mM. The partial PFK preparation has apparent S7P Km64micromolar and PPi Km about10micromolar; the cited F6P comparator is38micromolar. Partial aldolase cleaves SBP with Km13micromolar versus FBP3micromolar and about half the FBP Vmax. Slight PFK contamination is disclosed; added triose-phosphate isomerase did not increase SBP cleavage. Reconstitution requires transketolase, PFK, aldolase and PPi with omission controls; yeast aldolase can substitute after PFK is supplied. Extract R5P consumption was8.1±1.7nmol/min/mg in four preparations, with triose0.46±0.04 and S7P0.40±0.04 per R5P, accounting for86% of substrate. These results support the route without assigning a present-day Entamoeba sequence. Reverse biosynthetic flux and retention of PPi energy were proposed, not all measured directly. Modern clostridial work separates species, strains and recombinant preparations. Thermosuccinogenes CDQ83_11320=PNT94038.1 and CDQ83_07225=PNT93300.1 are issued DSM5809 sequences; the metabolomics cultures are not silently equated to every issuing genome preparation. DSM1313 Clo1313_1876=ADU74928.1 is a separate PPi-PFK. In 2019 the pET28b constructs carried N-terminal His6 flanking a TEV site, without documented tag cleavage. Heat-treated Rosetta extracts assayed at55C gave CDQ83_11320 PPi-dependent F6P activity220±26U/mg CFE, with ATP/GTP activity not detected; CDQ83_07225 gave ATP13±1 and GTP13±5 with PPi not detected. CDQ83_10650 remained inactive in the tested heated and nonheated preparations. These are CFE measurements, not equal expression or purified kcat. CDQ83_07225 donor Km values differed: ATP0.155mM and GTP0.016mM. The 2019 Discussion mistakenly calls CDQ83_11320 PPdK; Tables2/3 identify PPdK as CDQ83_07455. The 2020 study used pET28b+/Rosetta for CDQ83 proteins and DSM1313 PCR into pD861-NT/pSH157 in E. coli T7 Express lysY/Iq for Clo1313_1876. Direct55C MS showed S7P-to-SBP conversion with PPi, alongside minus-PPi and minus-enzyme controls. The MS assay contained5mM MgCl2,5mM sodium PPi and1mM acceptor; kinetic assays used1mM PPi. Mg presence is an assay condition, not an independently measured universal metal requirement. Rabbit aldolase coupling supplies E4P/DHAP; it does not demonstrate activity of a clostridial aldolase. Unequal triose signals led to a TPI-contamination hypothesis, not a new core reaction. NADH/GPDH and other auxiliary enzymes belong to the assay, not core stoichiometry. Purified CDQ83_11320 has S7P Km0.11mM, kcat49/s and F6P0.070mM,182/s; Clo1313_1876 has S7P0.10mM,80/s and F6P0.046mM,127/s. CDQ83_07225 has no detected S7P activity through4mM and a F6P Khalf0.688mM with Hill coefficient24, not a Michaelis Km. Its ammonium requirement belongs to the ATP/F6P comparator using lyophilized rabbit aldolase/GPDH in place of ammonium-sulfate suspensions, because S7P Ba-salt precipitated BaSO4. Ultrafiltration applied to purified PFK buffer exchange, not the auxiliary enzymes; the source's NH4Cl2 formula is inconsistent. E. coli PfkA, its0.25mM ADP assay addition and delta-talAB physiology are ATP-route comparisons, not an E. coli PPi-branch assignment. The thesis-version supplemental figures reproduce the minus-enzyme control and separate Michaelis/Hill fits. Hill fits for PPi enzymes are not uniformly one; the very steep CDQ83_07225 fit and poor alternative Michaelis fit must not be confused. This thesis supplement is not asserted byte-identical to a journal supplementary PDF. Thermosuccinogenes SBP and S7P pools were about fourfold and2.5-fold higher on xylose than glucose in biological triplicates normalized to OD600. Pool accumulation does not establish six-event flux, direct xylose binding or transcriptional regulation. The 2023 study tests ATCC27405=DSM1237 Cthe_0347 Pfp=ABN51585.1 and Cthe_0349 Aldoa=ABN51587.1, distinct from DSM1313. Aldoa uses a synthetic codon-optimized pRSET-A construct with N-terminal His6/linker; Pfp uses pAHCT0347/pRSET-A with an N-terminal His6 tag. Both were expressed in E. coli T7 Shuffle. The inspected Pfp-specific passages do not establish a linker or codon optimization. Ni purification does not identify physiological nickel use. Pfp forward MS at50C used2mM PPi,2.115mM S7P and2.5mM MgCl2. Reported S7P Km3.236mM exceeds the highest measured2.12mM; Vmax is6.294±3.723micromol/min/mg. The F6P Km0.075mM and Vmax100.222±11.6 were measured separately. This preparation/strain/assay difference from the2020 values remains unresolved. Mixed S7P/F6P lowered FBP formation, consistent with competition in that assay, without a direct binding constant. Only forward S7P phosphorylation was tested. The original Taillefer thesis adds Cthe_0347 F6P-assay context. Its title page says2017, the issuing repository metadata2015-04 and the2023 citation2016; the persistent Handle identifies the retained artifact despite the date conflict. The His6 pAHCT0347/pRSET-A T7 Shuffle preparation was assayed at50C with5mM MgCl2. PPi was the sole detected donor; ATP,GTP,PEP and ADP were not detected as donors. PPi Km was0.23mM, Vmax39.7micromol/min/mg and calculated kcat30.14/s. High PPi gave substrate inhibition Ki1.38±0.5mM;1mM ATP reduced F6P-PFK activity about60%. ADP,AMP,GTP,GMP and PEP at1mM had no significant effect. These are original F6P-assay observations, not directly measured S7P inhibition or a resolved ATP-binding mechanism. The approximately50kDa SDS monomer mass is not a native oligomer measurement. The source's reference to GK protein within the PFK paragraph is retained as a wording inconsistency; effects on other thesis enzymes are outside this branch. Aldoa's direct2023 activity is FBP cleavage, Km0.145mM and Vmax27.7micromol/min/mg. The paper explicitly did not verify SBP cleavage. At55C with2mM added cations, Zn2+ increased FBP activity over twofold, Mg2+ alone was not significant, Mg2+ plus ammonium increased activity, and K+ reduced activity in the Mg/Zn comparisons. Ammonium partly attenuated the stronger Zn response, so its activation edge is restricted to the Mg-containing condition. These effects do not establish SBP-specific metal requirements. The DSM1313 Clo1313_1875=ADU74927.1 aldolase is an issuing class-II FBP annotation with promoter-binding context; neither the rabbit coupling assay nor the ATCC27405 FBP assay is transferred to an exact DSM1313 SBP catalyst. Additional RPI/RPE/TKT investigation preserves evidence levels. ATCC27405 Cthe_2597 RpiB=A3DIL8 is a149-residue unreviewed sequence with EC5.3.1.6 annotation. Issuing3HEE contains R5P and author/PISA dimer assembly;3PH3 contains unphosphorylated ribose and has a different deposited construct extent. The2011 publisher abstract reports ligand structures and mutagenesis, but its full body was unavailable. The2008 and2013 papers and2009 crystallization lead concern rare/unphosphorylated sugars; unseen body details are not converted to R5P turnover evidence. Historical ZP00503831.1 has the same149-residue sequence but older product/EC annotation, so version differences remain explicit. Crystallization salts are not a measured Mg cofactor requirement. DSM1313 Clo1313_1661=ADU74718.1 and ATCC27405 Cthe_0576=ABN51812.1 are issuing RPE annotations, without a newly acquired purified-enzyme or metal assay. A failed lexical search for DSM1313 RpiB does not establish absence. KJC335 is a DSM1313-derived delta-hpt strain carrying heterologous xylAB. The TktAB pair CLO1313_RS00385/RS00390 joins through issuing historical gene records to Clo1313_0074/0075 and ADU73172.1/ADU73173.1. Co-overexpression from the gapDH promoter on pTC131374-5 reduced doubling time on5g/L xylose from19.0±5.7h to5.8±0.6h versus pKJC84 empty vector, with no major cellobiose difference. This supports paired pathway participation, not full catalysis by each subunit or measured1:1 assembly. RNA-seq used three replicates at matched mid-exponential OD but different growth rates, which limits interpretation. Another predicted pair reported as RS01525/RS01530 changed little; the separately issued ADU73386.1/ADU73387.1 Clo1313_0295/0296 annotations are retained without silently asserting an unverified modern-locus join. Broad transport, xylitol, chemotaxis and cellulosome responses remain outside the six-event core. Rex Clo1313_2471=ADU75484.1 is issued with a generic CoA-binding-domain label; the primary study identifies Rex. DAP-seq used codon-optimized C-terminal HaloTag constructs in E. coli S30 IVTT,55C binding and a HaloTag-only control. Separate room-temperature motif EMSA used semi-purified C-terminal His6 protein from BL21(DE3); no Kd was determined. DAP-seq associates two shared sites in the divergent Clo1313_1875/1876 region, but which site acts on either gene or both is unresolved. Poor replicate correlation(Pearson0.18) and motif-versus-promoter assay scope are retained. The graph represents sequence-specific DNA binding only, without a signed expression arrow, invented live-gene endpoint or exact NADH/NAD effector dose-response. Family redox-sensing models are not direct assays of this construct. Historical Entrez12422212,12421607 and12421608 provide locus context but are not recast as currently live annotated genes. The2022 engineered LL1660 result limits necessity claims: a strain lacking PPi-PFK and introduced transaldolase could grow despite the proposed reverse biosynthetic role. A partial Clo1313_0790–1248 genome duplication includes ATP-pfk0997 and other energy genes; it does not uniquely identify the compensating mechanism. The alternate route remains unknown, with L-type PPP discussed as a possibility. This counterevidence does not negate the measured wild-type/recombinant enzyme activities. The retained publisher rendering supports these Results/Discussion claims; no supplemental reanalysis is asserted. A separate13C flux-model study is consistent with nonoxidative/SBP routing but model fits and near-equilibrium estimates are not exact enzyme assignments. Native enzyme associations are reaction-global: the16 original associations include15 excluded from transfer to the scoped organisms. The UniProtB8I4R1 cross-reference on native MetaCyc MONOMER-21313 belongs to a different species/locus, despite the native object's correct thermocellum PID ADU74928.1. B8I4R1 sequence, homodimer, cofactor and nonallosteric annotations are not transferred to DSM1313 or thermosuccinogenes. Native G-80830 has a locus/STRING cross-reference conflict. Broad Bacteria range, methylotroph substrate reports whose original bodies were not acquired, and a45-genome survey with two transaldolase-annotated R. papyrosolvens exceptions do not establish universal branch occurrence. PPi supply through glycogen cycling or proton-pumping pyrophosphatase and a metabolic relief-valve role remain proposals outside the core. Pentose assimilation, anabolic pentose supply and glycolytic F6P/GAP are interfaces; oxidative PPP/NADPH production, carbon fixation and an invented transporter are not extra core events. Unknown assemblies, locations and fine regulatory mechanisms remain unknown.

Pathway type
pentose phosphate pathway
Organism scope

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Pathway network

59 nodes · 51 asserted directed edges

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Pathway network: pentose phosphate pathway (non-oxidative branch) II 59 nodes · 51 asserted directed edges. Every arrow links to its evidence table row; nodes link to their component details. Isolated declared components are retained. MetaCyc:D-SEDOHEPTULOSE-7-P — consumes → MetaCyc:RXN-21730; Native left contains D-SEDOHEPTULOSE-7-P; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.; Evidence: MetaCyc:RXN-21730, MetaCyc:PWY-8178consumes MetaCyc:PPI — consumes → MetaCyc:RXN-21730; Native left contains PPI; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.; Evidence: MetaCyc:RXN-21730, MetaCyc:PWY-8178consumes MetaCyc:RXN-21730 — produces → MetaCyc:D-SEDOHEPTULOSE-1-7-P2; Native right contains D-SEDOHEPTULOSE-1-7-P2; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.; Evidence: MetaCyc:RXN-21730, MetaCyc:PWY-8178produces MetaCyc:RXN-21730 — produces → MetaCyc:Pi; Native right contains Pi; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.; Evidence: MetaCyc:RXN-21730, MetaCyc:PWY-8178produces MetaCyc:RXN-21730 — produces → MetaCyc:PROTON; Native right contains PROTON; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.; Evidence: MetaCyc:RXN-21730, MetaCyc:PWY-8178produces MetaCyc:D-SEDOHEPTULOSE-1-7-P2 — consumes → MetaCyc:SEDOBISALDOL-RXN; Native left contains D-SEDOHEPTULOSE-1-7-P2; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.; Evidence: MetaCyc:SEDOBISALDOL-RXN, MetaCyc:PWY-8178consumes MetaCyc:SEDOBISALDOL-RXN — produces → MetaCyc:DIHYDROXY-ACETONE-PHOSPHATE; Native right contains DIHYDROXY-ACETONE-PHOSPHATE; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.; Evidence: MetaCyc:SEDOBISALDOL-RXN, MetaCyc:PWY-8178produces MetaCyc:SEDOBISALDOL-RXN — produces → MetaCyc:ERYTHROSE-4P; Native right contains ERYTHROSE-4P; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.; Evidence: MetaCyc:SEDOBISALDOL-RXN, MetaCyc:PWY-8178produces MetaCyc:1TRANSKETO-RXN — produces → MetaCyc:D-SEDOHEPTULOSE-7-P; Native left contains D-SEDOHEPTULOSE-7-P; reaction-direction is REVERSIBLE. PWY-8178 layout uses right-to-left. No explicit coefficient is supplied; class status and species identity are retained.; Evidence: MetaCyc:1TRANSKETO-RXN, MetaCyc:PWY-8178produces MetaCyc:1TRANSKETO-RXN — produces → MetaCyc:GAP; Native left contains GAP; reaction-direction is REVERSIBLE. PWY-8178 layout uses right-to-left. No explicit coefficient is supplied; class status and species identity are retained.; Evidence: MetaCyc:1TRANSKETO-RXN, MetaCyc:PWY-8178produces MetaCyc:RIBOSE-5P — consumes → MetaCyc:1TRANSKETO-RXN; Native right contains RIBOSE-5P; reaction-direction is REVERSIBLE. PWY-8178 layout uses right-to-left. No explicit coefficient is supplied; class status and species identity are retained.; Evidence: MetaCyc:1TRANSKETO-RXN, MetaCyc:PWY-8178consumes MetaCyc:XYLULOSE-5-PHOSPHATE — consumes → MetaCyc:1TRANSKETO-RXN; Native right contains XYLULOSE-5-PHOSPHATE; reaction-direction is REVERSIBLE. PWY-8178 layout uses right-to-left. No explicit coefficient is supplied; class status and species identity are retained.; Evidence: MetaCyc:1TRANSKETO-RXN, MetaCyc:PWY-8178consumes MetaCyc:ERYTHROSE-4P — consumes → MetaCyc:2TRANSKETO-RXN; Native left contains ERYTHROSE-4P; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.; Evidence: MetaCyc:2TRANSKETO-RXN, MetaCyc:PWY-8178consumes MetaCyc:XYLULOSE-5-PHOSPHATE — consumes → MetaCyc:2TRANSKETO-RXN; Native left contains XYLULOSE-5-PHOSPHATE; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.; Evidence: MetaCyc:2TRANSKETO-RXN, MetaCyc:PWY-8178consumes MetaCyc:2TRANSKETO-RXN — produces → MetaCyc:FRUCTOSE-6P; Native right contains FRUCTOSE-6P; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.; Evidence: MetaCyc:2TRANSKETO-RXN, MetaCyc:PWY-8178produces MetaCyc:2TRANSKETO-RXN — produces → MetaCyc:GAP; Native right contains GAP; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.; Evidence: MetaCyc:2TRANSKETO-RXN, MetaCyc:PWY-8178produces MetaCyc:RIB5PISOM-RXN — produces → MetaCyc:RIBOSE-5P; Native left contains RIBOSE-5P; reaction-direction is REVERSIBLE. PWY-8178 layout uses right-to-left. No explicit coefficient is supplied; class status and species identity are retained.; Evidence: MetaCyc:RIB5PISOM-RXN, MetaCyc:PWY-8178produces MetaCyc:RIBULOSE-5P — consumes → MetaCyc:RIB5PISOM-RXN; Native right contains RIBULOSE-5P; reaction-direction is REVERSIBLE. PWY-8178 layout uses right-to-left. No explicit coefficient is supplied; class status and species identity are retained.; Evidence: MetaCyc:RIB5PISOM-RXN, MetaCyc:PWY-8178consumes MetaCyc:RIBULOSE-5P — consumes → MetaCyc:RIBULP3EPIM-RXN; Native left contains RIBULOSE-5P; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.; Evidence: MetaCyc:RIBULP3EPIM-RXN, MetaCyc:PWY-8178consumes MetaCyc:RIBULP3EPIM-RXN — produces → MetaCyc:XYLULOSE-5-PHOSPHATE; Native right contains XYLULOSE-5-PHOSPHATE; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.; Evidence: MetaCyc:RIBULP3EPIM-RXN, MetaCyc:PWY-8178produces MetaCyc:RIB5PISOM-RXN — provides_input_for → MetaCyc:1TRANSKETO-RXN; Native pathway ordering places RIB5PISOM-RXN before 1TRANSKETO-RXN; the shared metabolite transfers carbon within the six-event scope, without asserting isolated flux measurement.; Evidence: MetaCyc:PWY-8178provides input for MetaCyc:RIBULP3EPIM-RXN — provides_input_for → MetaCyc:1TRANSKETO-RXN; Native pathway ordering places RIBULP3EPIM-RXN before 1TRANSKETO-RXN; the shared metabolite transfers carbon within the six-event scope, without asserting isolated flux measurement.; Evidence: MetaCyc:PWY-8178provides input for MetaCyc:1TRANSKETO-RXN — provides_input_for → MetaCyc:RXN-21730; Native pathway ordering places 1TRANSKETO-RXN before RXN-21730; the shared metabolite transfers carbon within the six-event scope, without asserting isolated flux measurement.; Evidence: MetaCyc:PWY-8178provides input for MetaCyc:RXN-21730 — provides_input_for → MetaCyc:SEDOBISALDOL-RXN; Native pathway ordering places RXN-21730 before SEDOBISALDOL-RXN; the shared metabolite transfers carbon within the six-event scope, without asserting isolated flux measurement.; Evidence: MetaCyc:PWY-8178provides input for MetaCyc:SEDOBISALDOL-RXN — provides_input_for → MetaCyc:2TRANSKETO-RXN; Native pathway ordering places SEDOBISALDOL-RXN before 2TRANSKETO-RXN; the shared metabolite transfers carbon within the six-event scope, without asserting isolated flux measurement.; Evidence: MetaCyc:PWY-8178provides input for EC:2.7.1.90 — catalyzes → MetaCyc:RXN-21730; Partially purified Entamoeba histolytica 200:NIH PPi-PFK phosphorylates S7P. This activity endpoint does not assert a current protein sequence, oligomer or tag.; Evidence: PMID:6180735catalyzes EC:4.1.2.13 — catalyzes → MetaCyc:SEDOBISALDOL-RXN; Partial native Entamoeba 200:NIH aldolase cleaves SBP; apparent Km13 micromolar versus FBP3 and about half Vmax. Slight PFK contamination is retained; no sequenced protein assignment is made.; Evidence: PMID:6180735catalyzes EC:2.2.1.1 — catalyzes → MetaCyc:1TRANSKETO-RXN; Native partial Entamoeba 200:NIH transketolase supports both substrate pairs. The EC endpoint represents measured activity, not a sequenced clostridial subunit or fabricated complex.; Evidence: PMID:6180735catalyzes EC:2.2.1.1 — catalyzes → MetaCyc:2TRANSKETO-RXN; Native partial Entamoeba 200:NIH transketolase supports both substrate pairs. The EC endpoint represents measured activity, not a sequenced clostridial subunit or fabricated complex.; Evidence: PMID:6180735catalyzes EC:5.3.1.6 — catalyzes → MetaCyc:RIB5PISOM-RXN; The native reversible reaction assigns this isomerase/epimerase activity; this activity-level link does not identify a biochemically assayed enzyme in every pathway taxon.; Evidence: MetaCyc:RIB5PISOM-RXN, EC:5.3.1.6catalyzes EC:5.1.3.1 — catalyzes → MetaCyc:RIBULP3EPIM-RXN; The native reversible reaction assigns this isomerase/epimerase activity; this activity-level link does not identify a biochemically assayed enzyme in every pathway taxon.; Evidence: MetaCyc:RIBULP3EPIM-RXN, EC:5.1.3.1catalyzes CHEBI:18420 — activates → EC:2.2.1.1; Entamoeba 200:NIH transketolase apoenzyme add-back requires both Mg2+ and thiamine diphosphate. Adding Mg first causes a lag; this is preparation-specific reconstitution, not a new chemical reaction side.; Evidence: PMID:6180735activates CHEBI:58937 — activates → EC:2.2.1.1; Entamoeba 200:NIH transketolase apoenzyme add-back requires both Mg2+ and thiamine diphosphate. Adding Mg first causes a lag; this is preparation-specific reconstitution, not a new chemical reaction side.; Evidence: PMID:6180735activates NCBIProtein:PNT94038.1 — catalyzes → MetaCyc:RXN-21730; subject experimental construct: CDQ83_11320, DSM5809 sequence; pET28b+ N-terminal His6/TEV construct, E. coli Rosetta. 2020 MS at55C, 5mM MgCl2/5mM PPi/1mM S7P; distinct kinetic assay at1mM PPi. TEV cleavage not demonstrated.; Evidence PMID:31871051: The Methods distinguish the pET28b+ and pD861-NT preparations, expression hosts, affinity purification and MS versus kinetic assay conditions. A tag is not proof of native assembly. (XPath /article/body/sec[5]/sec[3]/p[1] | /article/body/sec[5]/sec[3]/p[2] | /article/body/sec[5]/sec[6]/sec/sec[1]/p[2] | /article/body/sec[5]/sec[6]/sec/sec[2]/p[1] | /article/body/sec[5]/sec[7]/p[1] | /article/body/sec[5]/sec[7]/p[2]); Evidence NCBIProtein:PNT94038.1: The issuing GenBank record identifies accession PNT94038.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='PNT94038.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='PNT94038.1']/GBSeq_definition); Evidence PMID:31178853: The cloned thermosuccinogenes enzymes use a pET-28b-derived construct with an N-terminal His6 tag flanking a TEV protease site and E. coli Rosetta expression. This directly supports the CDQ83_11320 construct feature; tag cleavage is not documented. (XPath /article/body/sec[2]/sec[1]/p); Purified PPi-PFK converts S7P to SBP with PPi; minus-PPi/minus-enzyme controls distinguish product formation. F6P kinetics and rabbit aldolase coupling are separate observations.; Evidence: PMID:31871051, NCBIProtein:PNT94038.1catalyzes NCBIProtein:ADU74928.1 — catalyzes → MetaCyc:RXN-21730; subject experimental construct: DSM1313 Clo1313_1876, PCR into pD861-NT/pSH157, N-terminal His construct in E. coli T7 Express lysY/Iq. 2020 MS at55C with5mM MgCl2/5mM PPi/1mM S7P; separate1mM PPi kinetic assay.; Evidence PMID:31871051: The Methods distinguish the pET28b+ and pD861-NT preparations, expression hosts, affinity purification and MS versus kinetic assay conditions. A tag is not proof of native assembly. (XPath /article/body/sec[5]/sec[3]/p[1] | /article/body/sec[5]/sec[3]/p[2] | /article/body/sec[5]/sec[6]/sec/sec[1]/p[2] | /article/body/sec[5]/sec[6]/sec/sec[2]/p[1] | /article/body/sec[5]/sec[7]/p[1] | /article/body/sec[5]/sec[7]/p[2]); Evidence NCBIProtein:ADU74928.1: The issuing GenBank record identifies accession ADU74928.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ADU74928.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ADU74928.1']/GBSeq_definition); Purified PPi-PFK converts S7P to SBP with PPi; minus-PPi/minus-enzyme controls distinguish product formation. F6P kinetics and rabbit aldolase coupling are separate observations.; Evidence: PMID:31871051, NCBIProtein:ADU74928.1catalyzes NCBIProtein:ABN51585.1 — catalyzes → MetaCyc:RXN-21730; subject experimental construct: ATCC27405/DSM1237 Cthe_0347 pAHCT0347/pRSET-A, N-terminal His6, E. coli T7 Shuffle. Pfp-specific linker and codon-optimization details remain unresolved. The 2023 S7P-MS assay at50C is distinct from F6P competition/kinetics. No native homodimer measurement is inferred from sequence annotation.; Evidence PMID:37438781: Pfp pAHCT0347 carries an N-terminal His6 tag and is expressed in E. coli T7 Shuffle. The Pfp-specific passages do not establish a linker or codon optimization. Forward MS uses50C, 2mM PPi,2.115mM S7P,2.5mM MgCl2. (XPath /article/body/sec[5]/sec[1]/p | /article/body/sec[5]/sec[2]/p | /article/body/sec[5]/sec[4]/p | /article/body/sec[5]/sec[5]/p[1] | /article/body/sec[5]/sec[5]/p[3] | /article/body/sec[5]/sec[10]/p | /article/body/sec[2]/sec[1]/p); Evidence NCBIProtein:ABN51585.1: The issuing GenBank record identifies accession ABN51585.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_definition); Evidence hdl:1993/32279: The thesis identifies synthetic pAHCT0347 with a pRSET-A backbone, T7 Shuffle expression and His6-tagged Pfp purification. Its inspected Pfp passages do not establish linker or codon-optimization details. The thesis F6P assay is distinct from the later S7P MS experiment. (Native thesis PDFpp.111–113 (printed86–88), expression, purification and PFK assays; PDFp.117 (printed92), PFK preparation); ATCC27405 Cthe_0347 Pfp forms SBP from S7P with PPi in the forward MS assay. Fitted S7P Km3.236mM exceeds the highest measured2.12mM; it is not averaged with DSM1313 kinetics.; Evidence: PMID:37438781, NCBIProtein:ABN51585.1catalyzes MetaCyc:PPI — inhibits → NCBIProtein:ABN51585.1; object experimental construct: Thesis Cthe_0347 pAHCT0347/pRSET-A His6 in E. coli T7 Shuffle; purified F6P-dependent PPi-PFK assay at50C with5mM MgCl2. Pfp-specific linker and codon-optimization details remain unresolved. This qualifier does not transfer the inhibitor sign to S7P phosphorylation.; Evidence hdl:1993/32279: The thesis used synthetic pAHCT0347/pRSET-A His6 Pfp in T7 Shuffle, Ni purification and50C F6P-coupled assay with5mM MgCl2. These inhibitor data precede the later S7P experiment. (Native thesis PDFpp.111–113 (printed86–88), expression, purification and PFK assays); Evidence NCBIProtein:ABN51585.1: The issuing GenBank record identifies accession ABN51585.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_definition); In the purified Cthe_0347 F6P assay, PPi substrate inhibition was fitted with Ki1.38±0.5mM. PPi is also the donor; this preparation-specific high-substrate effect is not direct S7P inhibition evidence.; Evidence: hdl:1993/32279, NCBIProtein:ABN51585.1inhibits CHEBI:30616 — inhibits → NCBIProtein:ABN51585.1; object experimental construct: Thesis Cthe_0347 pAHCT0347/pRSET-A His6 in E. coli T7 Shuffle; purified F6P-dependent PPi-PFK assay at50C with5mM MgCl2. Pfp-specific linker and codon-optimization details remain unresolved. This qualifier does not transfer the inhibitor sign to S7P phosphorylation.; Evidence hdl:1993/32279: The thesis used synthetic pAHCT0347/pRSET-A His6 Pfp in T7 Shuffle, Ni purification and50C F6P-coupled assay with5mM MgCl2. These inhibitor data precede the later S7P experiment. (Native thesis PDFpp.111–113 (printed86–88), expression, purification and PFK assays); Evidence NCBIProtein:ABN51585.1: The issuing GenBank record identifies accession ABN51585.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_definition); Adding1mM ATP reduced the Cthe_0347 F6P-PFK activity about60%. At1mM ADP, AMP, GTP, GMP and PEP no significant effect was reported; no direct ATP-binding site or S7P-assay sign is established.; Evidence: hdl:1993/32279, NCBIProtein:ABN51585.1inhibits MetaCyc:D-SEDOHEPTULOSE-7-P — inhibits → NCBIProtein:ABN51585.1; object experimental construct: ATCC27405/DSM1237 Cthe_0347 pAHCT0347/pRSET-A, N-terminal His6, E. coli T7 Shuffle. Pfp-specific linker and codon-optimization details remain unresolved. The 2023 S7P-MS assay at50C is distinct from F6P competition/kinetics. No native homodimer measurement is inferred from sequence annotation.; Evidence PMID:37438781: Pfp pAHCT0347 carries an N-terminal His6 tag and is expressed in E. coli T7 Shuffle. The Pfp-specific passages do not establish a linker or codon optimization. Forward MS uses50C, 2mM PPi,2.115mM S7P,2.5mM MgCl2. (XPath /article/body/sec[5]/sec[1]/p | /article/body/sec[5]/sec[2]/p | /article/body/sec[5]/sec[4]/p | /article/body/sec[5]/sec[5]/p[1] | /article/body/sec[5]/sec[5]/p[3] | /article/body/sec[5]/sec[10]/p | /article/body/sec[2]/sec[1]/p); Evidence NCBIProtein:ABN51585.1: The issuing GenBank record identifies accession ABN51585.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_definition); Evidence hdl:1993/32279: The thesis identifies synthetic pAHCT0347 with a pRSET-A backbone, T7 Shuffle expression and His6-tagged Pfp purification. Its inspected Pfp passages do not establish linker or codon-optimization details. The thesis F6P assay is distinct from the later S7P MS experiment. (Native thesis PDFpp.111–113 (printed86–88), expression, purification and PFK assays; PDFp.117 (printed92), PFK preparation); Adding S7P alongside F6P reduced FBP formation in the mixed-substrate Pfp activity assay. Competition is an interpretation of the FBP activity result, not an inhibitor-binding measurement or loss of S7P catalysis.; Evidence: PMID:37438781, NCBIProtein:ABN51585.1inhibits NCBIProtein:ABN51587.1 — enables → EC:4.1.2.13; subject experimental construct: ATCC27405 Cthe_0349 pAHCT0349/pRSET-A N-terminal His6/linker, E. coli T7 Shuffle. Purified55C FBP assay; metal additions2mM. SBP cleavage was not verified; Ni purification does not identify a physiological cofactor.; Evidence PMID:37438781: Aldoa is synthetic pAHCT0349/pRSET-A with N-terminal His6/linker, expressed in E. coli T7 Shuffle and Ni purified. FBP assays at55C are distinct from proposed SBP cleavage. (XPath /article/body/sec[5]/sec[1]/p | /article/body/sec[5]/sec[2]/p | /article/body/sec[5]/sec[4]/p | /article/body/sec[5]/sec[5]/p[4] | /article/body/sec[2]/sec[7]/p); Evidence NCBIProtein:ABN51587.1: The issuing GenBank record identifies accession ABN51587.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_definition); Purified Cthe_0349 Aldoa has measured FBP aldolase activity, Km0.145mM and Vmax27.7micromol/min/mg. The Discussion explicitly says SBP aldolase activity was not verified.; Evidence: PMID:37438781, NCBIProtein:ABN51587.1enables CHEBI:29105 — activates → NCBIProtein:ABN51587.1; object experimental construct: ATCC27405 Cthe_0349 pAHCT0349/pRSET-A N-terminal His6/linker, E. coli T7 Shuffle. Purified55C FBP assay; metal additions2mM. SBP cleavage was not verified; Ni purification does not identify a physiological cofactor.; Evidence PMID:37438781: Aldoa is synthetic pAHCT0349/pRSET-A with N-terminal His6/linker, expressed in E. coli T7 Shuffle and Ni purified. FBP assays at55C are distinct from proposed SBP cleavage. (XPath /article/body/sec[5]/sec[1]/p | /article/body/sec[5]/sec[2]/p | /article/body/sec[5]/sec[4]/p | /article/body/sec[5]/sec[5]/p[4] | /article/body/sec[2]/sec[7]/p); Evidence NCBIProtein:ABN51587.1: The issuing GenBank record identifies accession ABN51587.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_definition); In55C FBP assays,2mM Zn2+ increased recombinant Aldoa activity more than twofold over no added metal. This does not establish SBP-specific Zn dependence or an unmodified native preparation.; Evidence: PMID:37438781, NCBIProtein:ABN51587.1activates CHEBI:28938 — activates → NCBIProtein:ABN51587.1; object experimental construct: ATCC27405 Cthe_0349 pAHCT0349/pRSET-A N-terminal His6/linker, E. coli T7 Shuffle. Purified55C FBP assay; metal additions2mM. SBP cleavage was not verified; Ni purification does not identify a physiological cofactor.; Evidence PMID:37438781: Aldoa is synthetic pAHCT0349/pRSET-A with N-terminal His6/linker, expressed in E. coli T7 Shuffle and Ni purified. FBP assays at55C are distinct from proposed SBP cleavage. (XPath /article/body/sec[5]/sec[1]/p | /article/body/sec[5]/sec[2]/p | /article/body/sec[5]/sec[4]/p | /article/body/sec[5]/sec[5]/p[4] | /article/body/sec[2]/sec[7]/p); Evidence NCBIProtein:ABN51587.1: The issuing GenBank record identifies accession ABN51587.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_definition); In the tested FBP assay, added ammonium with Mg2+ increased Aldoa activity. Ammonium partly reduced the stronger Zn response; the activation sign is conditional on the Mg-containing comparison.; Evidence: PMID:37438781, NCBIProtein:ABN51587.1activates CHEBI:29103 — inhibits → NCBIProtein:ABN51587.1; object experimental construct: ATCC27405 Cthe_0349 pAHCT0349/pRSET-A N-terminal His6/linker, E. coli T7 Shuffle. Purified55C FBP assay; metal additions2mM. SBP cleavage was not verified; Ni purification does not identify a physiological cofactor.; Evidence PMID:37438781: Aldoa is synthetic pAHCT0349/pRSET-A with N-terminal His6/linker, expressed in E. coli T7 Shuffle and Ni purified. FBP assays at55C are distinct from proposed SBP cleavage. (XPath /article/body/sec[5]/sec[1]/p | /article/body/sec[5]/sec[2]/p | /article/body/sec[5]/sec[4]/p | /article/body/sec[5]/sec[5]/p[4] | /article/body/sec[2]/sec[7]/p); Evidence NCBIProtein:ABN51587.1: The issuing GenBank record identifies accession ABN51587.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_definition); Added K+ reduced Aldoa FBP activity in the Mg- or Zn-containing comparisons at2mM added ions. This is condition-specific and does not demonstrate K binding or SBP inhibition.; Evidence: PMID:37438781, NCBIProtein:ABN51587.1inhibits NCBIProtein:ADU74927.1 — enables → EC:4.1.2.13; DSM1313 Clo1313_1875 is annotated class-II FBP aldolase. DAP-seq association is not a direct SBP assay, and rabbit coupling data are not transferred to this protein.; Evidence: NCBIProtein:ADU74927.1enables NCBIProtein:ADU74718.1 — enables → EC:5.1.3.1; DSM1313 Clo1313_1661 is annotated ribulose-phosphate3-epimerase with EC5.1.3.1. This is issuing annotation support, not a newly acquired purified-enzyme assay or measured metal requirement.; Evidence: NCBIProtein:ADU74718.1enables NCBIProtein:ABN51812.1 — enables → EC:5.1.3.1; ATCC27405 Cthe_0576 is annotated ribulose-phosphate3-epimerase with EC5.1.3.1. Evidence is annotation-level; no unsupported transfer of cofactor or oligomer is made.; Evidence: NCBIProtein:ABN51812.1enables UniProtKB:A3DIL8 — enables → EC:5.3.1.6; The unreviewed ATCC27405 Cthe_2597 entry assigns EC5.3.1.6 from submitted/automatic annotation. Its R5P-bound deposited structure supports ligand context; rare-sugar kinetic papers are not substituted for a fully inspected R5P kinetic assay.; Evidence: UniProtKB:A3DIL8, DOI:10.2210/pdb3HEE/pdbenables CHEBI:28938 — activates → NCBIProtein:PNT93300.1; object experimental construct: CDQ83_07225 pET28b+/Rosetta His6/TEV construct; 55C F6P/ATP comparator. The 2020 assay used lyophilized rabbit aldolase/GPDH instead of ammonium-sulfate suspensions because S7P Ba-salt precipitated BaSO4; ammonium was added. The source NH4Cl2 formula is unresolved.; Evidence PMID:31178853: The CDQ83 proteins use pET28b N-terminal His6 constructs flanking a TEV site, Rosetta expression, heated CFE and55C donor assays; empty-vector controls are included, cleavage is not documented. (XPath /article/body/sec[2]/sec[1]/p | /article/body/sec[2]/sec[2]/p | /article/body/sec[2]/sec[4]/p[1] | /article/body/sec[2]/sec[4]/p[3]); Evidence NCBIProtein:PNT93300.1: The issuing GenBank record identifies accession PNT93300.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='PNT93300.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='PNT93300.1']/GBSeq_definition); Evidence PMID:31871051: The 55C assay used lyophilized rabbit aldolase and GPDH instead of ammonium-sulfate suspensions because S7P Ba-salt caused BaSO4 precipitation. The ATP/GTP-dependent comparator required added ammonium; the printed NH4Cl2 formula is inconsistent. PFK buffer ultrafiltration is a separate preparation step. (XPath /article/body/sec[5]/sec[7]/p[1] | /article/body/sec[5]/sec[7]/p[2]); In the 2020 F6P/ATP comparison, CDQ83_07225 required added ammonium with lyophilized auxiliary enzymes replacing ammonium-sulfate suspensions because S7P Ba-salt precipitated BaSO4. This does not apply to the PPi-S7P catalyst; the source NH4Cl2 formula is inconsistent.; Evidence: PMID:31871051, NCBIProtein:PNT93300.1activates NCBIProtein:ADU73172.1 — part_of → MetaCyc:PWY-8178; subject experimental construct: DSM1313 TktAB subunit in KJC335-derived delta-hpt/xylAB engineered strain; pTC131374-5 co-overexpresses BOTH genes from gapDH promoter. This individual endpoint does not assert solitary transketolase activity or a1:1 assembly.; Evidence PMID:32884054: KJC335 is DSM1313-derived delta-hpt with heterologous xylAB; pTC131374-5 expresses both genomic TktAB genes from gapDH promoter. The empty-vector control is pKJC84. (XPath /article/body/sec[3]/sec[1]/p[1] | /article/body/sec[3]/sec[1]/p[2]); Evidence NCBIProtein:ADU73172.1: The issuing GenBank record identifies accession ADU73172.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ADU73172.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ADU73172.1']/GBSeq_definition); KJC335-derived co-overexpression of both TktAB genes reduced xylose doubling time from19.0±5.7h to5.8±0.6h versus empty vector. This supports paired pathway participation, not isolated subunit catalysis or measured complex stoichiometry.; Evidence: PMID:32884054, NCBIProtein:ADU73172.1part of NCBIProtein:ADU73173.1 — part_of → MetaCyc:PWY-8178; subject experimental construct: DSM1313 TktAB subunit in KJC335-derived delta-hpt/xylAB engineered strain; pTC131374-5 co-overexpresses BOTH genes from gapDH promoter. This individual endpoint does not assert solitary transketolase activity or a1:1 assembly.; Evidence PMID:32884054: KJC335 is DSM1313-derived delta-hpt with heterologous xylAB; pTC131374-5 expresses both genomic TktAB genes from gapDH promoter. The empty-vector control is pKJC84. (XPath /article/body/sec[3]/sec[1]/p[1] | /article/body/sec[3]/sec[1]/p[2]); Evidence NCBIProtein:ADU73173.1: The issuing GenBank record identifies accession ADU73173.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ADU73173.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ADU73173.1']/GBSeq_definition); KJC335-derived co-overexpression of both TktAB genes reduced xylose doubling time from19.0±5.7h to5.8±0.6h versus empty vector. This supports paired pathway participation, not isolated subunit catalysis or measured complex stoichiometry.; Evidence: PMID:32884054, NCBIProtein:ADU73173.1part of NCBIProtein:ADU75484.1 — enables → GO:0043565; subject experimental construct: Two distinct Rex constructs: codon-optimized C-terminal HaloTag in E. coli S30 IVTT for55C DAP-seq, and C-terminal His6 BL21(DE3) preparation for room-temperature motif EMSA. Shared1875/1876 promoter sites do not establish signed expression.; Evidence PMID:34566906: DAP-seq uses C-terminal HaloTag Rex in E. coli S30 IVTT at55C with HaloTag-only control; separate motif EMSA uses semi-purified C-terminal His6 Rex from BL21(DE3) at room temperature. No Kd is reported. (XPath /article/body/sec[2]/sec[4]/p | /article/body/sec[2]/sec[5]/p[1] | /article/body/sec[2]/sec[8]/p[1] | /article/body/sec[2]/sec[8]/p[2] | /article/body/sec[2]/sec[8]/p[3]); Evidence NCBIProtein:ADU75484.1: The issuing GenBank record identifies accession ADU75484.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ADU75484.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ADU75484.1']/GBSeq_definition); Rex DNA-binding assays support a sequence-specific motif. DAP-seq associates two shared divergent-region sites with Clo1313_1875/1876, but site-to-gene assignment and expression sign remain unresolved; motif EMSA is not a promoter-specific regulation assay.; Evidence: PMID:34566906, NCBIProtein:ADU75484.1enables transketolase; EC:2.2.1.1; Declared type: molecular_activity molecular activity transketolase diphosphate--fructose-6-phosphate 1-phosphotransferase; EC:2.7.1.90; Declared type: molecular_activity molecular activity diphosphate-- fructose-6-phosphate 1-phosphotransferase fructose-bisphosphate aldolase; EC:4.1.2.13; Declared type: molecular_activity molecular activity fructose-bisphosphate aldolase ribulose-phosphate 3-epimerase; EC:5.1.3.1; Declared type: molecular_activity molecular activity ribulose-phosphate 3-epimerase ribose-5-phosphate isomerase; EC:5.3.1.6; Declared type: molecular_activity molecular activity ribose-5-phosphate isomerase D-sedoheptulose 1,7-bisphosphate; MetaCyc:D-SEDOHEPTULOSE-1-7-P2; Declared type: chemical_entity chemical entity D-sedoheptulose 1,7-bisphosphate D-sedoheptulose 7-phosphate; MetaCyc:D-SEDOHEPTULOSE-7-P; Declared type: chemical_entity chemical entity D-sedoheptulose 7-phosphate glycerone phosphate; MetaCyc:DIHYDROXY-ACETONE-PHOSPHATE; Declared type: chemical_entity chemical entity glycerone phosphate D-erythrose 4-phosphate; MetaCyc:ERYTHROSE-4P; Declared type: chemical_entity chemical entity D-erythrose 4-phosphate beta-D-fructofuranose 6-phosphate; MetaCyc:FRUCTOSE-6P; Declared type: chemical_entity chemical entity beta-D-fructofuranose 6-phosphate D-glyceraldehyde 3-phosphate; MetaCyc:GAP; Declared type: chemical_entity chemical entity D-glyceraldehyde 3-phosphate diphosphate; MetaCyc:PPI; Declared type: chemical_entity chemical entity diphosphate H+; MetaCyc:PROTON; Declared type: chemical_entity chemical entity H+ phosphate; MetaCyc:Pi; Declared type: chemical_entity chemical entity phosphate D-ribose 5-phosphate; MetaCyc:RIBOSE-5P; Declared type: chemical_entity chemical entity D-ribose 5-phosphate D-ribulose 5-phosphate; MetaCyc:RIBULOSE-5P; Declared type: chemical_entity chemical entity D-ribulose 5-phosphate D-xylulose 5-phosphate; MetaCyc:XYLULOSE-5-PHOSPHATE; Declared type: chemical_entity chemical entity D-xylulose 5-phosphate phosphofructokinase [Acetivibrio thermocellus ATCC 27405]; NCBIProtein:ABN51585.1; Declared type: protein protein phosphofructokinase [Acetivibrio thermocellus ATCC 27405] fructose-1,6-bisphosphate aldolase, class II [Acetivibrio thermocellus ATCC 27405]; NCBIProtein:ABN51587.1; Declared type: protein protein fructose-1,6-bisphosphate aldolase, class II [Acetivibrio thermocellus ATCC 27405] ribulose-phosphate 3-epimerase [Acetivibrio thermocellus ATCC 27405]; NCBIProtein:ABN51812.1; Declared type: protein protein ribulose-phosphate 3-epimerase [Acetivibrio thermocellus ATCC 27405] Transketolase domain-containing protein [Acetivibrio thermocellus DSM 1313]; NCBIProtein:ADU73172.1; Declared type: protein protein Transketolase domain- containing protein [Acetivibrio thermocellus DSM 1313] Transketolase domain-containing protein [Acetivibrio thermocellus DSM 1313]; NCBIProtein:ADU73173.1; Declared type: protein protein Transketolase domain- containing protein [Acetivibrio thermocellus DSM 1313] Transketolase domain-containing protein [Acetivibrio thermocellus DSM 1313]; NCBIProtein:ADU73386.1; Declared type: protein protein Transketolase domain- containing protein [Acetivibrio thermocellus DSM 1313] Transketolase central region [Acetivibrio thermocellus DSM 1313]; NCBIProtein:ADU73387.1; Declared type: protein protein Transketolase central region [Acetivibrio thermocellus DSM 1313] ribulose-phosphate 3-epimerase [Acetivibrio thermocellus DSM 1313]; NCBIProtein:ADU74718.1; Declared type: protein protein ribulose-phosphate 3-epimerase [Acetivibrio thermocellus DSM 1313] fructose-1,6-bisphosphate aldolase, class II [Acetivibrio thermocellus DSM 1313]; NCBIProtein:ADU74927.1; Declared type: protein protein fructose-1,6-bisphosphate aldolase, class II [Acetivibrio thermocellus DSM 1313] phosphofructokinase [Acetivibrio thermocellus DSM 1313]; NCBIProtein:ADU74928.1; Declared type: protein protein phosphofructokinase [Acetivibrio thermocellus DSM 1313] CoA-binding domain protein [Acetivibrio thermocellus DSM 1313]; NCBIProtein:ADU75484.1; Declared type: protein protein CoA-binding domain protein [Acetivibrio thermocellus DSM 1313] 6-phosphofructokinase [Clostridium thermosuccinogenes]; NCBIProtein:PNT93300.1; Declared type: protein protein 6-phosphofructokinase [Clostridium thermosuccinogenes] 6-phosphofructokinase [Clostridium thermosuccinogenes]; NCBIProtein:PNT94038.1; Declared type: protein protein 6-phosphofructokinase [Clostridium thermosuccinogenes] Sugar-phosphate isomerase, RpiB/LacA/LacB family; UniProtKB:A3DIL8; Declared type: protein protein Sugar-phosphate isomerase, RpiB/LacA/LacB family magnesium(2+); CHEBI:18420; Declared type: cofactor cofactor magnesium(2+) ammonium; CHEBI:28938; Declared type: chemical_entity chemical entity ammonium potassium(1+); CHEBI:29103; Declared type: chemical_entity chemical entity potassium(1+) zinc(2+); CHEBI:29105; Declared type: chemical_entity chemical entity zinc(2+) ATP(4-); CHEBI:30616; Declared type: chemical_entity chemical entity ATP(4-) thiamine(1+) diphosphate(3-); CHEBI:58937; Declared type: cofactor cofactor thiamine(1+) diphosphate(3-) sequence-specific DNA binding; GO:0043565; Declared type: molecular_activity molecular activity sequence-specific DNA binding RXN-21730; MetaCyc:RXN-21730; Declared type: molecular_activity; Source reaction direction: reversible molecular activity RXN-21730 SEDOBISALDOL-RXN; MetaCyc:SEDOBISALDOL-RXN; Declared type: molecular_activity; Source reaction direction: reversible molecular activity SEDOBISALDOL-RXN 1TRANSKETO-RXN; MetaCyc:1TRANSKETO-RXN; Declared type: molecular_activity; Source reaction direction: reversible molecular activity 1TRANSKETO-RXN 2TRANSKETO-RXN; MetaCyc:2TRANSKETO-RXN; Declared type: molecular_activity; Source reaction direction: reversible molecular activity 2TRANSKETO-RXN RIB5PISOM-RXN; MetaCyc:RIB5PISOM-RXN; Declared type: molecular_activity; Source reaction direction: reversible molecular activity RIB5PISOM-RXN RIBULP3EPIM-RXN; MetaCyc:RIBULP3EPIM-RXN; Declared type: molecular_activity; Source reaction direction: reversible molecular activity RIBULP3EPIM-RXN pentose phosphate pathway (non-oxidative branch) II; MetaCyc:PWY-8178; Declared type: pathway pathway pentose phosphate pathway (non-oxidative branch) II 6-phosphofructokinase [Clostridium thermosuccinogenes]; NCBIProtein:PNT94038.1; Declared type: protein; experimental construct: CDQ83_11320, DSM5809 sequence; pET28b+ N-terminal His6/TEV construct, E. coli Rosetta. 2020 MS at55C, 5mM MgCl2/5mM PPi/1mM S7P; distinct kinetic assay at1mM PPi. TEV cleavage not demonstrated.; Evidence PMID:31871051: The Methods distinguish the pET28b+ and pD861-NT preparations, expression hosts, affinity purification and MS versus kinetic assay conditions. A tag is not proof of native assembly. (XPath /article/body/sec[5]/sec[3]/p[1] | /article/body/sec[5]/sec[3]/p[2] | /article/body/sec[5]/sec[6]/sec/sec[1]/p[2] | /article/body/sec[5]/sec[6]/sec/sec[2]/p[1] | /article/body/sec[5]/sec[7]/p[1] | /article/body/sec[5]/sec[7]/p[2]); Evidence NCBIProtein:PNT94038.1: The issuing GenBank record identifies accession PNT94038.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='PNT94038.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='PNT94038.1']/GBSeq_definition); Evidence PMID:31178853: The cloned thermosuccinogenes enzymes use a pET-28b-derived construct with an N-terminal His6 tag flanking a TEV protease site and E. coli Rosetta expression. This directly supports the CDQ83_11320 construct feature; tag cleavage is not documented. (XPath /article/body/sec[2]/sec[1]/p) experimental construct 6-phosphofructokinase [Clostridium thermosuccinogenes] [experimental construct: CDQ83_11320, DSM5809 sequence; pET28b+ N-terminal His6/TEV construct, E. coli Rosetta. 2020 MS…] phosphofructokinase [Acetivibrio thermocellus DSM 1313]; NCBIProtein:ADU74928.1; Declared type: protein; experimental construct: DSM1313 Clo1313_1876, PCR into pD861-NT/pSH157, N-terminal His construct in E. coli T7 Express lysY/Iq. 2020 MS at55C with5mM MgCl2/5mM PPi/1mM S7P; separate1mM PPi kinetic assay.; Evidence PMID:31871051: The Methods distinguish the pET28b+ and pD861-NT preparations, expression hosts, affinity purification and MS versus kinetic assay conditions. A tag is not proof of native assembly. (XPath /article/body/sec[5]/sec[3]/p[1] | /article/body/sec[5]/sec[3]/p[2] | /article/body/sec[5]/sec[6]/sec/sec[1]/p[2] | /article/body/sec[5]/sec[6]/sec/sec[2]/p[1] | /article/body/sec[5]/sec[7]/p[1] | /article/body/sec[5]/sec[7]/p[2]); Evidence NCBIProtein:ADU74928.1: The issuing GenBank record identifies accession ADU74928.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ADU74928.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ADU74928.1']/GBSeq_definition) experimental construct phosphofructokinase [Acetivibrio thermocellus DSM 1313] [experimental construct: DSM1313 Clo1313_1876, PCR into pD861-NT/pSH157, N-terminal His construct in E. coli T7 Express…] phosphofructokinase [Acetivibrio thermocellus ATCC 27405]; NCBIProtein:ABN51585.1; Declared type: protein; experimental construct: ATCC27405/DSM1237 Cthe_0347 pAHCT0347/pRSET-A, N-terminal His6, E. coli T7 Shuffle. Pfp-specific linker and codon-optimization details remain unresolved. The 2023 S7P-MS assay at50C is distinct from F6P competition/kinetics. No native homodimer measurement is inferred from sequence annotation.; Evidence PMID:37438781: Pfp pAHCT0347 carries an N-terminal His6 tag and is expressed in E. coli T7 Shuffle. The Pfp-specific passages do not establish a linker or codon optimization. Forward MS uses50C, 2mM PPi,2.115mM S7P,2.5mM MgCl2. (XPath /article/body/sec[5]/sec[1]/p | /article/body/sec[5]/sec[2]/p | /article/body/sec[5]/sec[4]/p | /article/body/sec[5]/sec[5]/p[1] | /article/body/sec[5]/sec[5]/p[3] | /article/body/sec[5]/sec[10]/p | /article/body/sec[2]/sec[1]/p); Evidence NCBIProtein:ABN51585.1: The issuing GenBank record identifies accession ABN51585.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_definition); Evidence hdl:1993/32279: The thesis identifies synthetic pAHCT0347 with a pRSET-A backbone, T7 Shuffle expression and His6-tagged Pfp purification. Its inspected Pfp passages do not establish linker or codon-optimization details. The thesis F6P assay is distinct from the later S7P MS experiment. (Native thesis PDFpp.111–113 (printed86–88), expression, purification and PFK assays; PDFp.117 (printed92), PFK preparation) experimental construct phosphofructokinase [Acetivibrio thermocellus ATCC 27405] [experimental construct: ATCC27405/DSM1237 Cthe_0347 pAHCT0347/pRSET-A, N-terminal His6, E. coli T7 Shuffle. Pfp-specific…] phosphofructokinase [Acetivibrio thermocellus ATCC 27405]; NCBIProtein:ABN51585.1; Declared type: protein; experimental construct: Thesis Cthe_0347 pAHCT0347/pRSET-A His6 in E. coli T7 Shuffle; purified F6P-dependent PPi-PFK assay at50C with5mM MgCl2. Pfp-specific linker and codon-optimization details remain unresolved. This qualifier does not transfer the inhibitor sign to S7P phosphorylation.; Evidence hdl:1993/32279: The thesis used synthetic pAHCT0347/pRSET-A His6 Pfp in T7 Shuffle, Ni purification and50C F6P-coupled assay with5mM MgCl2. These inhibitor data precede the later S7P experiment. (Native thesis PDFpp.111–113 (printed86–88), expression, purification and PFK assays); Evidence NCBIProtein:ABN51585.1: The issuing GenBank record identifies accession ABN51585.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_definition) experimental construct phosphofructokinase [Acetivibrio thermocellus ATCC 27405] [experimental construct: Thesis Cthe_0347 pAHCT0347/pRSET-A His6 in E. coli T7 Shuffle; purified F6P-dependent PPi-PFK assay…] phosphofructokinase [Acetivibrio thermocellus ATCC 27405]; NCBIProtein:ABN51585.1; Declared type: protein; experimental construct: Thesis Cthe_0347 pAHCT0347/pRSET-A His6 in E. coli T7 Shuffle; purified F6P-dependent PPi-PFK assay at50C with5mM MgCl2. Pfp-specific linker and codon-optimization details remain unresolved. This qualifier does not transfer the inhibitor sign to S7P phosphorylation.; Evidence hdl:1993/32279: The thesis used synthetic pAHCT0347/pRSET-A His6 Pfp in T7 Shuffle, Ni purification and50C F6P-coupled assay with5mM MgCl2. These inhibitor data precede the later S7P experiment. (Native thesis PDFpp.111–113 (printed86–88), expression, purification and PFK assays); Evidence NCBIProtein:ABN51585.1: The issuing GenBank record identifies accession ABN51585.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_definition) experimental construct phosphofructokinase [Acetivibrio thermocellus ATCC 27405] [experimental construct: Thesis Cthe_0347 pAHCT0347/pRSET-A His6 in E. coli T7 Shuffle; purified F6P-dependent PPi-PFK assay…] phosphofructokinase [Acetivibrio thermocellus ATCC 27405]; NCBIProtein:ABN51585.1; Declared type: protein; experimental construct: ATCC27405/DSM1237 Cthe_0347 pAHCT0347/pRSET-A, N-terminal His6, E. coli T7 Shuffle. Pfp-specific linker and codon-optimization details remain unresolved. The 2023 S7P-MS assay at50C is distinct from F6P competition/kinetics. No native homodimer measurement is inferred from sequence annotation.; Evidence PMID:37438781: Pfp pAHCT0347 carries an N-terminal His6 tag and is expressed in E. coli T7 Shuffle. The Pfp-specific passages do not establish a linker or codon optimization. Forward MS uses50C, 2mM PPi,2.115mM S7P,2.5mM MgCl2. (XPath /article/body/sec[5]/sec[1]/p | /article/body/sec[5]/sec[2]/p | /article/body/sec[5]/sec[4]/p | /article/body/sec[5]/sec[5]/p[1] | /article/body/sec[5]/sec[5]/p[3] | /article/body/sec[5]/sec[10]/p | /article/body/sec[2]/sec[1]/p); Evidence NCBIProtein:ABN51585.1: The issuing GenBank record identifies accession ABN51585.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_definition); Evidence hdl:1993/32279: The thesis identifies synthetic pAHCT0347 with a pRSET-A backbone, T7 Shuffle expression and His6-tagged Pfp purification. Its inspected Pfp passages do not establish linker or codon-optimization details. The thesis F6P assay is distinct from the later S7P MS experiment. (Native thesis PDFpp.111–113 (printed86–88), expression, purification and PFK assays; PDFp.117 (printed92), PFK preparation) experimental construct phosphofructokinase [Acetivibrio thermocellus ATCC 27405] [experimental construct: ATCC27405/DSM1237 Cthe_0347 pAHCT0347/pRSET-A, N-terminal His6, E. coli T7 Shuffle. Pfp-specific…] fructose-1,6-bisphosphate aldolase, class II [Acetivibrio thermocellus ATCC 27405]; NCBIProtein:ABN51587.1; Declared type: protein; experimental construct: ATCC27405 Cthe_0349 pAHCT0349/pRSET-A N-terminal His6/linker, E. coli T7 Shuffle. Purified55C FBP assay; metal additions2mM. SBP cleavage was not verified; Ni purification does not identify a physiological cofactor.; Evidence PMID:37438781: Aldoa is synthetic pAHCT0349/pRSET-A with N-terminal His6/linker, expressed in E. coli T7 Shuffle and Ni purified. FBP assays at55C are distinct from proposed SBP cleavage. (XPath /article/body/sec[5]/sec[1]/p | /article/body/sec[5]/sec[2]/p | /article/body/sec[5]/sec[4]/p | /article/body/sec[5]/sec[5]/p[4] | /article/body/sec[2]/sec[7]/p); Evidence NCBIProtein:ABN51587.1: The issuing GenBank record identifies accession ABN51587.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_definition) experimental construct fructose-1,6-bisphosphate aldolase, class II [Acetivibrio thermocellus ATCC 27405] [experimental construct: ATCC27405 Cthe_0349 pAHCT0349/pRSET-A N-terminal His6/linker, E. coli T7 Shuffle. Purified55C FBP…] fructose-1,6-bisphosphate aldolase, class II [Acetivibrio thermocellus ATCC 27405]; NCBIProtein:ABN51587.1; Declared type: protein; experimental construct: ATCC27405 Cthe_0349 pAHCT0349/pRSET-A N-terminal His6/linker, E. coli T7 Shuffle. Purified55C FBP assay; metal additions2mM. SBP cleavage was not verified; Ni purification does not identify a physiological cofactor.; Evidence PMID:37438781: Aldoa is synthetic pAHCT0349/pRSET-A with N-terminal His6/linker, expressed in E. coli T7 Shuffle and Ni purified. FBP assays at55C are distinct from proposed SBP cleavage. (XPath /article/body/sec[5]/sec[1]/p | /article/body/sec[5]/sec[2]/p | /article/body/sec[5]/sec[4]/p | /article/body/sec[5]/sec[5]/p[4] | /article/body/sec[2]/sec[7]/p); Evidence NCBIProtein:ABN51587.1: The issuing GenBank record identifies accession ABN51587.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_definition) experimental construct fructose-1,6-bisphosphate aldolase, class II [Acetivibrio thermocellus ATCC 27405] [experimental construct: ATCC27405 Cthe_0349 pAHCT0349/pRSET-A N-terminal His6/linker, E. coli T7 Shuffle. Purified55C FBP…] fructose-1,6-bisphosphate aldolase, class II [Acetivibrio thermocellus ATCC 27405]; NCBIProtein:ABN51587.1; Declared type: protein; experimental construct: ATCC27405 Cthe_0349 pAHCT0349/pRSET-A N-terminal His6/linker, E. coli T7 Shuffle. Purified55C FBP assay; metal additions2mM. SBP cleavage was not verified; Ni purification does not identify a physiological cofactor.; Evidence PMID:37438781: Aldoa is synthetic pAHCT0349/pRSET-A with N-terminal His6/linker, expressed in E. coli T7 Shuffle and Ni purified. FBP assays at55C are distinct from proposed SBP cleavage. (XPath /article/body/sec[5]/sec[1]/p | /article/body/sec[5]/sec[2]/p | /article/body/sec[5]/sec[4]/p | /article/body/sec[5]/sec[5]/p[4] | /article/body/sec[2]/sec[7]/p); Evidence NCBIProtein:ABN51587.1: The issuing GenBank record identifies accession ABN51587.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_definition) experimental construct fructose-1,6-bisphosphate aldolase, class II [Acetivibrio thermocellus ATCC 27405] [experimental construct: ATCC27405 Cthe_0349 pAHCT0349/pRSET-A N-terminal His6/linker, E. coli T7 Shuffle. Purified55C FBP…] fructose-1,6-bisphosphate aldolase, class II [Acetivibrio thermocellus ATCC 27405]; NCBIProtein:ABN51587.1; Declared type: protein; experimental construct: ATCC27405 Cthe_0349 pAHCT0349/pRSET-A N-terminal His6/linker, E. coli T7 Shuffle. Purified55C FBP assay; metal additions2mM. SBP cleavage was not verified; Ni purification does not identify a physiological cofactor.; Evidence PMID:37438781: Aldoa is synthetic pAHCT0349/pRSET-A with N-terminal His6/linker, expressed in E. coli T7 Shuffle and Ni purified. FBP assays at55C are distinct from proposed SBP cleavage. (XPath /article/body/sec[5]/sec[1]/p | /article/body/sec[5]/sec[2]/p | /article/body/sec[5]/sec[4]/p | /article/body/sec[5]/sec[5]/p[4] | /article/body/sec[2]/sec[7]/p); Evidence NCBIProtein:ABN51587.1: The issuing GenBank record identifies accession ABN51587.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_definition) experimental construct fructose-1,6-bisphosphate aldolase, class II [Acetivibrio thermocellus ATCC 27405] [experimental construct: ATCC27405 Cthe_0349 pAHCT0349/pRSET-A N-terminal His6/linker, E. coli T7 Shuffle. Purified55C FBP…] 6-phosphofructokinase [Clostridium thermosuccinogenes]; NCBIProtein:PNT93300.1; Declared type: protein; experimental construct: CDQ83_07225 pET28b+/Rosetta His6/TEV construct; 55C F6P/ATP comparator. The 2020 assay used lyophilized rabbit aldolase/GPDH instead of ammonium-sulfate suspensions because S7P Ba-salt precipitated BaSO4; ammonium was added. The source NH4Cl2 formula is unresolved.; Evidence PMID:31178853: The CDQ83 proteins use pET28b N-terminal His6 constructs flanking a TEV site, Rosetta expression, heated CFE and55C donor assays; empty-vector controls are included, cleavage is not documented. (XPath /article/body/sec[2]/sec[1]/p | /article/body/sec[2]/sec[2]/p | /article/body/sec[2]/sec[4]/p[1] | /article/body/sec[2]/sec[4]/p[3]); Evidence NCBIProtein:PNT93300.1: The issuing GenBank record identifies accession PNT93300.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='PNT93300.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='PNT93300.1']/GBSeq_definition); Evidence PMID:31871051: The 55C assay used lyophilized rabbit aldolase and GPDH instead of ammonium-sulfate suspensions because S7P Ba-salt caused BaSO4 precipitation. The ATP/GTP-dependent comparator required added ammonium; the printed NH4Cl2 formula is inconsistent. PFK buffer ultrafiltration is a separate preparation step. (XPath /article/body/sec[5]/sec[7]/p[1] | /article/body/sec[5]/sec[7]/p[2]) experimental construct 6-phosphofructokinase [Clostridium thermosuccinogenes] [experimental construct: CDQ83_07225 pET28b+/Rosetta His6/TEV construct; 55C F6P/ATP comparator. The 2020 assay used…] Transketolase domain-containing protein [Acetivibrio thermocellus DSM 1313]; NCBIProtein:ADU73172.1; Declared type: protein; experimental construct: DSM1313 TktAB subunit in KJC335-derived delta-hpt/xylAB engineered strain; pTC131374-5 co-overexpresses BOTH genes from gapDH promoter. This individual endpoint does not assert solitary transketolase activity or a1:1 assembly.; Evidence PMID:32884054: KJC335 is DSM1313-derived delta-hpt with heterologous xylAB; pTC131374-5 expresses both genomic TktAB genes from gapDH promoter. The empty-vector control is pKJC84. (XPath /article/body/sec[3]/sec[1]/p[1] | /article/body/sec[3]/sec[1]/p[2]); Evidence NCBIProtein:ADU73172.1: The issuing GenBank record identifies accession ADU73172.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ADU73172.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ADU73172.1']/GBSeq_definition) experimental construct Transketolase domain- containing protein [Acetivibrio thermocellus DSM 1313] [experimental construct: DSM1313 TktAB subunit in KJC335-derived delta-hpt/xylAB engineered strain; pTC131374-5 co-…] Transketolase domain-containing protein [Acetivibrio thermocellus DSM 1313]; NCBIProtein:ADU73173.1; Declared type: protein; experimental construct: DSM1313 TktAB subunit in KJC335-derived delta-hpt/xylAB engineered strain; pTC131374-5 co-overexpresses BOTH genes from gapDH promoter. This individual endpoint does not assert solitary transketolase activity or a1:1 assembly.; Evidence PMID:32884054: KJC335 is DSM1313-derived delta-hpt with heterologous xylAB; pTC131374-5 expresses both genomic TktAB genes from gapDH promoter. The empty-vector control is pKJC84. (XPath /article/body/sec[3]/sec[1]/p[1] | /article/body/sec[3]/sec[1]/p[2]); Evidence NCBIProtein:ADU73173.1: The issuing GenBank record identifies accession ADU73173.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ADU73173.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ADU73173.1']/GBSeq_definition) experimental construct Transketolase domain- containing protein [Acetivibrio thermocellus DSM 1313] [experimental construct: DSM1313 TktAB subunit in KJC335-derived delta-hpt/xylAB engineered strain; pTC131374-5 co-…] CoA-binding domain protein [Acetivibrio thermocellus DSM 1313]; NCBIProtein:ADU75484.1; Declared type: protein; experimental construct: Two distinct Rex constructs: codon-optimized C-terminal HaloTag in E. coli S30 IVTT for55C DAP-seq, and C-terminal His6 BL21(DE3) preparation for room-temperature motif EMSA. Shared1875/1876 promoter sites do not establish signed expression.; Evidence PMID:34566906: DAP-seq uses C-terminal HaloTag Rex in E. coli S30 IVTT at55C with HaloTag-only control; separate motif EMSA uses semi-purified C-terminal His6 Rex from BL21(DE3) at room temperature. No Kd is reported. (XPath /article/body/sec[2]/sec[4]/p | /article/body/sec[2]/sec[5]/p[1] | /article/body/sec[2]/sec[8]/p[1] | /article/body/sec[2]/sec[8]/p[2] | /article/body/sec[2]/sec[8]/p[3]); Evidence NCBIProtein:ADU75484.1: The issuing GenBank record identifies accession ADU75484.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim. (XPath /GBSet/GBSeq[GBSeq_accession-version='ADU75484.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ADU75484.1']/GBSeq_definition) experimental construct CoA-binding domain protein [Acetivibrio thermocellus DSM 1313] [experimental construct: Two distinct Rex constructs: codon-optimized C-terminal HaloTag in E. coli S30 IVTT for55C DAP- seq,…]

Components and activities

Declared biological components and source reaction directions
NodeKind or roleSource direction
Entamoeba histolytica
NCBITaxon:5759		taxon
Acetivibrio thermocellus
NCBITaxon:1515		taxon
Clostridium thermosuccinogenes
NCBITaxon:84032		taxon
Acetivibrio thermocellus ATCC 27405
NCBITaxon:203119		taxon
Acetivibrio thermocellus DSM 1313
NCBITaxon:637887		taxon
transketolase
EC:2.2.1.1		molecular activity
diphosphate--fructose-6-phosphate 1-phosphotransferase
EC:2.7.1.90		molecular activity
fructose-bisphosphate aldolase
EC:4.1.2.13		molecular activity
ribulose-phosphate 3-epimerase
EC:5.1.3.1		molecular activity
ribose-5-phosphate isomerase
EC:5.3.1.6		molecular activity
D-sedoheptulose 1,7-bisphosphate
MetaCyc:D-SEDOHEPTULOSE-1-7-P2		chemical entity
D-sedoheptulose 7-phosphate
MetaCyc:D-SEDOHEPTULOSE-7-P		chemical entity
glycerone phosphate
MetaCyc:DIHYDROXY-ACETONE-PHOSPHATE		chemical entity
D-erythrose 4-phosphate
MetaCyc:ERYTHROSE-4P		chemical entity
beta-D-fructofuranose 6-phosphate
MetaCyc:FRUCTOSE-6P		chemical entity
D-glyceraldehyde 3-phosphate
MetaCyc:GAP		chemical entity
diphosphate
MetaCyc:PPI		chemical entity
H+
MetaCyc:PROTON		chemical entity
phosphate
MetaCyc:Pi		chemical entity
D-ribose 5-phosphate
MetaCyc:RIBOSE-5P		chemical entity
D-ribulose 5-phosphate
MetaCyc:RIBULOSE-5P		chemical entity
D-xylulose 5-phosphate
MetaCyc:XYLULOSE-5-PHOSPHATE		chemical entity
phosphofructokinase [Acetivibrio thermocellus ATCC 27405]
NCBIProtein:ABN51585.1		protein
fructose-1,6-bisphosphate aldolase, class II [Acetivibrio thermocellus ATCC 27405]
NCBIProtein:ABN51587.1		protein
ribulose-phosphate 3-epimerase [Acetivibrio thermocellus ATCC 27405]
NCBIProtein:ABN51812.1		protein
Transketolase domain-containing protein [Acetivibrio thermocellus DSM 1313]
NCBIProtein:ADU73172.1		protein
Transketolase domain-containing protein [Acetivibrio thermocellus DSM 1313]
NCBIProtein:ADU73173.1		protein
Transketolase domain-containing protein [Acetivibrio thermocellus DSM 1313]
NCBIProtein:ADU73386.1		protein
Transketolase central region [Acetivibrio thermocellus DSM 1313]
NCBIProtein:ADU73387.1		protein
ribulose-phosphate 3-epimerase [Acetivibrio thermocellus DSM 1313]
NCBIProtein:ADU74718.1		protein
fructose-1,6-bisphosphate aldolase, class II [Acetivibrio thermocellus DSM 1313]
NCBIProtein:ADU74927.1		protein
phosphofructokinase [Acetivibrio thermocellus DSM 1313]
NCBIProtein:ADU74928.1		protein
CoA-binding domain protein [Acetivibrio thermocellus DSM 1313]
NCBIProtein:ADU75484.1		protein
6-phosphofructokinase [Clostridium thermosuccinogenes]
NCBIProtein:PNT93300.1		protein
6-phosphofructokinase [Clostridium thermosuccinogenes]
NCBIProtein:PNT94038.1		protein
Sugar-phosphate isomerase, RpiB/LacA/LacB family
UniProtKB:A3DIL8		protein
magnesium(2+)
CHEBI:18420		cofactor
ammonium
CHEBI:28938		chemical entity
potassium(1+)
CHEBI:29103		chemical entity
zinc(2+)
CHEBI:29105		chemical entity
ATP(4-)
CHEBI:30616		chemical entity
thiamine(1+) diphosphate(3-)
CHEBI:58937		cofactor
sequence-specific DNA binding
GO:0043565		molecular activity
RXN-21730
MetaCyc:RXN-21730		molecular activityreversible
SEDOBISALDOL-RXN
MetaCyc:SEDOBISALDOL-RXN		molecular activityreversible
1TRANSKETO-RXN
MetaCyc:1TRANSKETO-RXN		molecular activityreversible
2TRANSKETO-RXN
MetaCyc:2TRANSKETO-RXN		molecular activityreversible
RIB5PISOM-RXN
MetaCyc:RIB5PISOM-RXN		molecular activityreversible
RIBULP3EPIM-RXN
MetaCyc:RIBULP3EPIM-RXN		molecular activityreversible

Mechanistic edges

Mechanistic edges and their cited evidence
SubjectPredicate and descriptionObjectEvidence
D-sedoheptulose 7-phosphate
MetaCyc:D-SEDOHEPTULOSE-7-P		consumes

Native left contains D-SEDOHEPTULOSE-7-P; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

RXN-21730
MetaCyc:RXN-21730
  • MetaCyc:RXN-21730

    Source assertion: Native left contains D-SEDOHEPTULOSE-7-P; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

    Source locationXPath /ptools-xml/Reaction[@frameid='RXN-21730']/left/Compound[@frameid='D-SEDOHEPTULOSE-7-P'] | /ptools-xml/Reaction/reaction-direction
  • MetaCyc:PWY-8178

    Source assertion: The native reaction-layout selects left-to-right for RXN-21730; this graph follows that route orientation without claiming irreversibility.

    Source locationXPath /ptools-xml/Pathway/reaction-layout[Reaction[@frameid='RXN-21730']]
diphosphate
MetaCyc:PPI		consumes

Native left contains PPI; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

RXN-21730
MetaCyc:RXN-21730
  • MetaCyc:RXN-21730

    Source assertion: Native left contains PPI; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

    Source locationXPath /ptools-xml/Reaction[@frameid='RXN-21730']/left/Compound[@frameid='PPI'] | /ptools-xml/Reaction/reaction-direction
  • MetaCyc:PWY-8178

    Source assertion: The native reaction-layout selects left-to-right for RXN-21730; this graph follows that route orientation without claiming irreversibility.

    Source locationXPath /ptools-xml/Pathway/reaction-layout[Reaction[@frameid='RXN-21730']]
RXN-21730
MetaCyc:RXN-21730		produces

Native right contains D-SEDOHEPTULOSE-1-7-P2; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

D-sedoheptulose 1,7-bisphosphate
MetaCyc:D-SEDOHEPTULOSE-1-7-P2
  • MetaCyc:RXN-21730

    Source assertion: Native right contains D-SEDOHEPTULOSE-1-7-P2; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

    Source locationXPath /ptools-xml/Reaction[@frameid='RXN-21730']/right/Compound[@frameid='D-SEDOHEPTULOSE-1-7-P2'] | /ptools-xml/Reaction/reaction-direction
  • MetaCyc:PWY-8178

    Source assertion: The native reaction-layout selects left-to-right for RXN-21730; this graph follows that route orientation without claiming irreversibility.

    Source locationXPath /ptools-xml/Pathway/reaction-layout[Reaction[@frameid='RXN-21730']]
RXN-21730
MetaCyc:RXN-21730		produces

Native right contains Pi; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

phosphate
MetaCyc:Pi
  • MetaCyc:RXN-21730

    Source assertion: Native right contains Pi; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

    Source locationXPath /ptools-xml/Reaction[@frameid='RXN-21730']/right/Compound[@frameid='Pi'] | /ptools-xml/Reaction/reaction-direction
  • MetaCyc:PWY-8178

    Source assertion: The native reaction-layout selects left-to-right for RXN-21730; this graph follows that route orientation without claiming irreversibility.

    Source locationXPath /ptools-xml/Pathway/reaction-layout[Reaction[@frameid='RXN-21730']]
RXN-21730
MetaCyc:RXN-21730		produces

Native right contains PROTON; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

H+
MetaCyc:PROTON
  • MetaCyc:RXN-21730

    Source assertion: Native right contains PROTON; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

    Source locationXPath /ptools-xml/Reaction[@frameid='RXN-21730']/right/Compound[@frameid='PROTON'] | /ptools-xml/Reaction/reaction-direction
  • MetaCyc:PWY-8178

    Source assertion: The native reaction-layout selects left-to-right for RXN-21730; this graph follows that route orientation without claiming irreversibility.

    Source locationXPath /ptools-xml/Pathway/reaction-layout[Reaction[@frameid='RXN-21730']]
D-sedoheptulose 1,7-bisphosphate
MetaCyc:D-SEDOHEPTULOSE-1-7-P2		consumes

Native left contains D-SEDOHEPTULOSE-1-7-P2; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

SEDOBISALDOL-RXN
MetaCyc:SEDOBISALDOL-RXN
  • MetaCyc:SEDOBISALDOL-RXN

    Source assertion: Native left contains D-SEDOHEPTULOSE-1-7-P2; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

    Source locationXPath /ptools-xml/Reaction[@frameid='SEDOBISALDOL-RXN']/left/Compound[@frameid='D-SEDOHEPTULOSE-1-7-P2'] | /ptools-xml/Reaction/reaction-direction
  • MetaCyc:PWY-8178

    Source assertion: The native reaction-layout selects left-to-right for SEDOBISALDOL-RXN; this graph follows that route orientation without claiming irreversibility.

    Source locationXPath /ptools-xml/Pathway/reaction-layout[Reaction[@frameid='SEDOBISALDOL-RXN']]
SEDOBISALDOL-RXN
MetaCyc:SEDOBISALDOL-RXN		produces

Native right contains DIHYDROXY-ACETONE-PHOSPHATE; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

glycerone phosphate
MetaCyc:DIHYDROXY-ACETONE-PHOSPHATE
  • MetaCyc:SEDOBISALDOL-RXN

    Source assertion: Native right contains DIHYDROXY-ACETONE-PHOSPHATE; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

    Source locationXPath /ptools-xml/Reaction[@frameid='SEDOBISALDOL-RXN']/right/Compound[@frameid='DIHYDROXY-ACETONE-PHOSPHATE'] | /ptools-xml/Reaction/reaction-direction
  • MetaCyc:PWY-8178

    Source assertion: The native reaction-layout selects left-to-right for SEDOBISALDOL-RXN; this graph follows that route orientation without claiming irreversibility.

    Source locationXPath /ptools-xml/Pathway/reaction-layout[Reaction[@frameid='SEDOBISALDOL-RXN']]
SEDOBISALDOL-RXN
MetaCyc:SEDOBISALDOL-RXN		produces

Native right contains ERYTHROSE-4P; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

D-erythrose 4-phosphate
MetaCyc:ERYTHROSE-4P
  • MetaCyc:SEDOBISALDOL-RXN

    Source assertion: Native right contains ERYTHROSE-4P; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

    Source locationXPath /ptools-xml/Reaction[@frameid='SEDOBISALDOL-RXN']/right/Compound[@frameid='ERYTHROSE-4P'] | /ptools-xml/Reaction/reaction-direction
  • MetaCyc:PWY-8178

    Source assertion: The native reaction-layout selects left-to-right for SEDOBISALDOL-RXN; this graph follows that route orientation without claiming irreversibility.

    Source locationXPath /ptools-xml/Pathway/reaction-layout[Reaction[@frameid='SEDOBISALDOL-RXN']]
1TRANSKETO-RXN
MetaCyc:1TRANSKETO-RXN		produces

Native left contains D-SEDOHEPTULOSE-7-P; reaction-direction is REVERSIBLE. PWY-8178 layout uses right-to-left. No explicit coefficient is supplied; class status and species identity are retained.

D-sedoheptulose 7-phosphate
MetaCyc:D-SEDOHEPTULOSE-7-P
  • MetaCyc:1TRANSKETO-RXN

    Source assertion: Native left contains D-SEDOHEPTULOSE-7-P; reaction-direction is REVERSIBLE. PWY-8178 layout uses right-to-left. No explicit coefficient is supplied; class status and species identity are retained.

    Source locationXPath /ptools-xml/Reaction[@frameid='1TRANSKETO-RXN']/left/Compound[@frameid='D-SEDOHEPTULOSE-7-P'] | /ptools-xml/Reaction/reaction-direction
  • MetaCyc:PWY-8178

    Source assertion: The native reaction-layout selects right-to-left for 1TRANSKETO-RXN; this graph follows that route orientation without claiming irreversibility.

    Source locationXPath /ptools-xml/Pathway/reaction-layout[Reaction[@frameid='1TRANSKETO-RXN']]
1TRANSKETO-RXN
MetaCyc:1TRANSKETO-RXN		produces

Native left contains GAP; reaction-direction is REVERSIBLE. PWY-8178 layout uses right-to-left. No explicit coefficient is supplied; class status and species identity are retained.

D-glyceraldehyde 3-phosphate
MetaCyc:GAP
  • MetaCyc:1TRANSKETO-RXN

    Source assertion: Native left contains GAP; reaction-direction is REVERSIBLE. PWY-8178 layout uses right-to-left. No explicit coefficient is supplied; class status and species identity are retained.

    Source locationXPath /ptools-xml/Reaction[@frameid='1TRANSKETO-RXN']/left/Compound[@frameid='GAP'] | /ptools-xml/Reaction/reaction-direction
  • MetaCyc:PWY-8178

    Source assertion: The native reaction-layout selects right-to-left for 1TRANSKETO-RXN; this graph follows that route orientation without claiming irreversibility.

    Source locationXPath /ptools-xml/Pathway/reaction-layout[Reaction[@frameid='1TRANSKETO-RXN']]
D-ribose 5-phosphate
MetaCyc:RIBOSE-5P		consumes

Native right contains RIBOSE-5P; reaction-direction is REVERSIBLE. PWY-8178 layout uses right-to-left. No explicit coefficient is supplied; class status and species identity are retained.

1TRANSKETO-RXN
MetaCyc:1TRANSKETO-RXN
  • MetaCyc:1TRANSKETO-RXN

    Source assertion: Native right contains RIBOSE-5P; reaction-direction is REVERSIBLE. PWY-8178 layout uses right-to-left. No explicit coefficient is supplied; class status and species identity are retained.

    Source locationXPath /ptools-xml/Reaction[@frameid='1TRANSKETO-RXN']/right/Compound[@frameid='RIBOSE-5P'] | /ptools-xml/Reaction/reaction-direction
  • MetaCyc:PWY-8178

    Source assertion: The native reaction-layout selects right-to-left for 1TRANSKETO-RXN; this graph follows that route orientation without claiming irreversibility.

    Source locationXPath /ptools-xml/Pathway/reaction-layout[Reaction[@frameid='1TRANSKETO-RXN']]
D-xylulose 5-phosphate
MetaCyc:XYLULOSE-5-PHOSPHATE		consumes

Native right contains XYLULOSE-5-PHOSPHATE; reaction-direction is REVERSIBLE. PWY-8178 layout uses right-to-left. No explicit coefficient is supplied; class status and species identity are retained.

1TRANSKETO-RXN
MetaCyc:1TRANSKETO-RXN
  • MetaCyc:1TRANSKETO-RXN

    Source assertion: Native right contains XYLULOSE-5-PHOSPHATE; reaction-direction is REVERSIBLE. PWY-8178 layout uses right-to-left. No explicit coefficient is supplied; class status and species identity are retained.

    Source locationXPath /ptools-xml/Reaction[@frameid='1TRANSKETO-RXN']/right/Compound[@frameid='XYLULOSE-5-PHOSPHATE'] | /ptools-xml/Reaction/reaction-direction
  • MetaCyc:PWY-8178

    Source assertion: The native reaction-layout selects right-to-left for 1TRANSKETO-RXN; this graph follows that route orientation without claiming irreversibility.

    Source locationXPath /ptools-xml/Pathway/reaction-layout[Reaction[@frameid='1TRANSKETO-RXN']]
D-erythrose 4-phosphate
MetaCyc:ERYTHROSE-4P		consumes

Native left contains ERYTHROSE-4P; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

2TRANSKETO-RXN
MetaCyc:2TRANSKETO-RXN
  • MetaCyc:2TRANSKETO-RXN

    Source assertion: Native left contains ERYTHROSE-4P; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

    Source locationXPath /ptools-xml/Reaction[@frameid='2TRANSKETO-RXN']/left/Compound[@frameid='ERYTHROSE-4P'] | /ptools-xml/Reaction/reaction-direction
  • MetaCyc:PWY-8178

    Source assertion: The native reaction-layout selects left-to-right for 2TRANSKETO-RXN; this graph follows that route orientation without claiming irreversibility.

    Source locationXPath /ptools-xml/Pathway/reaction-layout[Reaction[@frameid='2TRANSKETO-RXN']]
D-xylulose 5-phosphate
MetaCyc:XYLULOSE-5-PHOSPHATE		consumes

Native left contains XYLULOSE-5-PHOSPHATE; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

2TRANSKETO-RXN
MetaCyc:2TRANSKETO-RXN
  • MetaCyc:2TRANSKETO-RXN

    Source assertion: Native left contains XYLULOSE-5-PHOSPHATE; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

    Source locationXPath /ptools-xml/Reaction[@frameid='2TRANSKETO-RXN']/left/Compound[@frameid='XYLULOSE-5-PHOSPHATE'] | /ptools-xml/Reaction/reaction-direction
  • MetaCyc:PWY-8178

    Source assertion: The native reaction-layout selects left-to-right for 2TRANSKETO-RXN; this graph follows that route orientation without claiming irreversibility.

    Source locationXPath /ptools-xml/Pathway/reaction-layout[Reaction[@frameid='2TRANSKETO-RXN']]
2TRANSKETO-RXN
MetaCyc:2TRANSKETO-RXN		produces

Native right contains FRUCTOSE-6P; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

beta-D-fructofuranose 6-phosphate
MetaCyc:FRUCTOSE-6P
  • MetaCyc:2TRANSKETO-RXN

    Source assertion: Native right contains FRUCTOSE-6P; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

    Source locationXPath /ptools-xml/Reaction[@frameid='2TRANSKETO-RXN']/right/Compound[@frameid='FRUCTOSE-6P'] | /ptools-xml/Reaction/reaction-direction
  • MetaCyc:PWY-8178

    Source assertion: The native reaction-layout selects left-to-right for 2TRANSKETO-RXN; this graph follows that route orientation without claiming irreversibility.

    Source locationXPath /ptools-xml/Pathway/reaction-layout[Reaction[@frameid='2TRANSKETO-RXN']]
2TRANSKETO-RXN
MetaCyc:2TRANSKETO-RXN		produces

Native right contains GAP; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

D-glyceraldehyde 3-phosphate
MetaCyc:GAP
  • MetaCyc:2TRANSKETO-RXN

    Source assertion: Native right contains GAP; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

    Source locationXPath /ptools-xml/Reaction[@frameid='2TRANSKETO-RXN']/right/Compound[@frameid='GAP'] | /ptools-xml/Reaction/reaction-direction
  • MetaCyc:PWY-8178

    Source assertion: The native reaction-layout selects left-to-right for 2TRANSKETO-RXN; this graph follows that route orientation without claiming irreversibility.

    Source locationXPath /ptools-xml/Pathway/reaction-layout[Reaction[@frameid='2TRANSKETO-RXN']]
RIB5PISOM-RXN
MetaCyc:RIB5PISOM-RXN		produces

Native left contains RIBOSE-5P; reaction-direction is REVERSIBLE. PWY-8178 layout uses right-to-left. No explicit coefficient is supplied; class status and species identity are retained.

D-ribose 5-phosphate
MetaCyc:RIBOSE-5P
  • MetaCyc:RIB5PISOM-RXN

    Source assertion: Native left contains RIBOSE-5P; reaction-direction is REVERSIBLE. PWY-8178 layout uses right-to-left. No explicit coefficient is supplied; class status and species identity are retained.

    Source locationXPath /ptools-xml/Reaction[@frameid='RIB5PISOM-RXN']/left/Compound[@frameid='RIBOSE-5P'] | /ptools-xml/Reaction/reaction-direction
  • MetaCyc:PWY-8178

    Source assertion: The native reaction-layout selects right-to-left for RIB5PISOM-RXN; this graph follows that route orientation without claiming irreversibility.

    Source locationXPath /ptools-xml/Pathway/reaction-layout[Reaction[@frameid='RIB5PISOM-RXN']]
D-ribulose 5-phosphate
MetaCyc:RIBULOSE-5P		consumes

Native right contains RIBULOSE-5P; reaction-direction is REVERSIBLE. PWY-8178 layout uses right-to-left. No explicit coefficient is supplied; class status and species identity are retained.

RIB5PISOM-RXN
MetaCyc:RIB5PISOM-RXN
  • MetaCyc:RIB5PISOM-RXN

    Source assertion: Native right contains RIBULOSE-5P; reaction-direction is REVERSIBLE. PWY-8178 layout uses right-to-left. No explicit coefficient is supplied; class status and species identity are retained.

    Source locationXPath /ptools-xml/Reaction[@frameid='RIB5PISOM-RXN']/right/Compound[@frameid='RIBULOSE-5P'] | /ptools-xml/Reaction/reaction-direction
  • MetaCyc:PWY-8178

    Source assertion: The native reaction-layout selects right-to-left for RIB5PISOM-RXN; this graph follows that route orientation without claiming irreversibility.

    Source locationXPath /ptools-xml/Pathway/reaction-layout[Reaction[@frameid='RIB5PISOM-RXN']]
D-ribulose 5-phosphate
MetaCyc:RIBULOSE-5P		consumes

Native left contains RIBULOSE-5P; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

RIBULP3EPIM-RXN
MetaCyc:RIBULP3EPIM-RXN
  • MetaCyc:RIBULP3EPIM-RXN

    Source assertion: Native left contains RIBULOSE-5P; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

    Source locationXPath /ptools-xml/Reaction[@frameid='RIBULP3EPIM-RXN']/left/Compound[@frameid='RIBULOSE-5P'] | /ptools-xml/Reaction/reaction-direction
  • MetaCyc:PWY-8178

    Source assertion: The native reaction-layout selects left-to-right for RIBULP3EPIM-RXN; this graph follows that route orientation without claiming irreversibility.

    Source locationXPath /ptools-xml/Pathway/reaction-layout[Reaction[@frameid='RIBULP3EPIM-RXN']]
RIBULP3EPIM-RXN
MetaCyc:RIBULP3EPIM-RXN		produces

Native right contains XYLULOSE-5-PHOSPHATE; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

D-xylulose 5-phosphate
MetaCyc:XYLULOSE-5-PHOSPHATE
  • MetaCyc:RIBULP3EPIM-RXN

    Source assertion: Native right contains XYLULOSE-5-PHOSPHATE; reaction-direction is REVERSIBLE. PWY-8178 layout uses left-to-right. No explicit coefficient is supplied; class status and species identity are retained.

    Source locationXPath /ptools-xml/Reaction[@frameid='RIBULP3EPIM-RXN']/right/Compound[@frameid='XYLULOSE-5-PHOSPHATE'] | /ptools-xml/Reaction/reaction-direction
  • MetaCyc:PWY-8178

    Source assertion: The native reaction-layout selects left-to-right for RIBULP3EPIM-RXN; this graph follows that route orientation without claiming irreversibility.

    Source locationXPath /ptools-xml/Pathway/reaction-layout[Reaction[@frameid='RIBULP3EPIM-RXN']]
RIB5PISOM-RXN
MetaCyc:RIB5PISOM-RXN		provides_input_for

Native pathway ordering places RIB5PISOM-RXN before 1TRANSKETO-RXN; the shared metabolite transfers carbon within the six-event scope, without asserting isolated flux measurement.

1TRANSKETO-RXN
MetaCyc:1TRANSKETO-RXN
  • MetaCyc:PWY-8178

    Source assertion: Native pathway ordering places RIB5PISOM-RXN before 1TRANSKETO-RXN; the shared metabolite transfers carbon within the six-event scope, without asserting isolated flux measurement.

    Source locationXPath /ptools-xml/Pathway/reaction-ordering
RIBULP3EPIM-RXN
MetaCyc:RIBULP3EPIM-RXN		provides_input_for

Native pathway ordering places RIBULP3EPIM-RXN before 1TRANSKETO-RXN; the shared metabolite transfers carbon within the six-event scope, without asserting isolated flux measurement.

1TRANSKETO-RXN
MetaCyc:1TRANSKETO-RXN
  • MetaCyc:PWY-8178

    Source assertion: Native pathway ordering places RIBULP3EPIM-RXN before 1TRANSKETO-RXN; the shared metabolite transfers carbon within the six-event scope, without asserting isolated flux measurement.

    Source locationXPath /ptools-xml/Pathway/reaction-ordering
1TRANSKETO-RXN
MetaCyc:1TRANSKETO-RXN		provides_input_for

Native pathway ordering places 1TRANSKETO-RXN before RXN-21730; the shared metabolite transfers carbon within the six-event scope, without asserting isolated flux measurement.

RXN-21730
MetaCyc:RXN-21730
  • MetaCyc:PWY-8178

    Source assertion: Native pathway ordering places 1TRANSKETO-RXN before RXN-21730; the shared metabolite transfers carbon within the six-event scope, without asserting isolated flux measurement.

    Source locationXPath /ptools-xml/Pathway/reaction-ordering
RXN-21730
MetaCyc:RXN-21730		provides_input_for

Native pathway ordering places RXN-21730 before SEDOBISALDOL-RXN; the shared metabolite transfers carbon within the six-event scope, without asserting isolated flux measurement.

SEDOBISALDOL-RXN
MetaCyc:SEDOBISALDOL-RXN
  • MetaCyc:PWY-8178

    Source assertion: Native pathway ordering places RXN-21730 before SEDOBISALDOL-RXN; the shared metabolite transfers carbon within the six-event scope, without asserting isolated flux measurement.

    Source locationXPath /ptools-xml/Pathway/reaction-ordering
SEDOBISALDOL-RXN
MetaCyc:SEDOBISALDOL-RXN		provides_input_for

Native pathway ordering places SEDOBISALDOL-RXN before 2TRANSKETO-RXN; the shared metabolite transfers carbon within the six-event scope, without asserting isolated flux measurement.

2TRANSKETO-RXN
MetaCyc:2TRANSKETO-RXN
  • MetaCyc:PWY-8178

    Source assertion: Native pathway ordering places SEDOBISALDOL-RXN before 2TRANSKETO-RXN; the shared metabolite transfers carbon within the six-event scope, without asserting isolated flux measurement.

    Source locationXPath /ptools-xml/Pathway/reaction-ordering
diphosphate--fructose-6-phosphate 1-phosphotransferase
EC:2.7.1.90		catalyzes

Partially purified Entamoeba histolytica 200:NIH PPi-PFK phosphorylates S7P. This activity endpoint does not assert a current protein sequence, oligomer or tag.

RXN-21730
MetaCyc:RXN-21730
  • PMID:6180735

    Source assertion: Partially purified Entamoeba histolytica 200:NIH PPi-PFK phosphorylates S7P. This activity endpoint does not assert a current protein sequence, oligomer or tag.

    Source locationPrinted pp.192–195, PFK purification/assays, Results and Fig.2
fructose-bisphosphate aldolase
EC:4.1.2.13		catalyzes

Partial native Entamoeba 200:NIH aldolase cleaves SBP; apparent Km13 micromolar versus FBP3 and about half Vmax. Slight PFK contamination is retained; no sequenced protein assignment is made.

SEDOBISALDOL-RXN
MetaCyc:SEDOBISALDOL-RXN
  • PMID:6180735

    Source assertion: Partial native Entamoeba 200:NIH aldolase cleaves SBP; apparent Km13 micromolar versus FBP3 and about half Vmax. Slight PFK contamination is retained; no sequenced protein assignment is made.

    Source locationPrinted pp.192–195, aldolase assay and Results; Fig.2
transketolase
EC:2.2.1.1		catalyzes

Native partial Entamoeba 200:NIH transketolase supports both substrate pairs. The EC endpoint represents measured activity, not a sequenced clostridial subunit or fabricated complex.

1TRANSKETO-RXN
MetaCyc:1TRANSKETO-RXN
  • PMID:6180735

    Source assertion: Native partial Entamoeba 200:NIH transketolase supports both substrate pairs. The EC endpoint represents measured activity, not a sequenced clostridial subunit or fabricated complex.

    Source locationPrinted pp.192–194, transketolase assays, Table2 and Fig.1
transketolase
EC:2.2.1.1		catalyzes

Native partial Entamoeba 200:NIH transketolase supports both substrate pairs. The EC endpoint represents measured activity, not a sequenced clostridial subunit or fabricated complex.

2TRANSKETO-RXN
MetaCyc:2TRANSKETO-RXN
  • PMID:6180735

    Source assertion: Native partial Entamoeba 200:NIH transketolase supports both substrate pairs. The EC endpoint represents measured activity, not a sequenced clostridial subunit or fabricated complex.

    Source locationPrinted pp.192–194, transketolase assays, Table2 and Fig.1
ribose-5-phosphate isomerase
EC:5.3.1.6		catalyzes

The native reversible reaction assigns this isomerase/epimerase activity; this activity-level link does not identify a biochemically assayed enzyme in every pathway taxon.

RIB5PISOM-RXN
MetaCyc:RIB5PISOM-RXN
  • MetaCyc:RIB5PISOM-RXN

    Source assertion: The native reversible reaction assigns this isomerase/epimerase activity; this activity-level link does not identify a biochemically assayed enzyme in every pathway taxon.

    Source locationXPath /ptools-xml/Reaction/ec-number | /ptools-xml/Reaction/enzymatic-reaction
  • EC:5.3.1.6

    Source assertion: The IUBMB enzyme entry defines the corresponding phosphorylated pentose interconversion activity.

    Source locationenzyme.dat ID 5.3.1.6; DE and CA records
ribulose-phosphate 3-epimerase
EC:5.1.3.1		catalyzes

The native reversible reaction assigns this isomerase/epimerase activity; this activity-level link does not identify a biochemically assayed enzyme in every pathway taxon.

RIBULP3EPIM-RXN
MetaCyc:RIBULP3EPIM-RXN
  • MetaCyc:RIBULP3EPIM-RXN

    Source assertion: The native reversible reaction assigns this isomerase/epimerase activity; this activity-level link does not identify a biochemically assayed enzyme in every pathway taxon.

    Source locationXPath /ptools-xml/Reaction/ec-number | /ptools-xml/Reaction/enzymatic-reaction
  • EC:5.1.3.1

    Source assertion: The IUBMB enzyme entry defines the corresponding phosphorylated pentose interconversion activity.

    Source locationenzyme.dat ID 5.1.3.1; DE and CA records
magnesium(2+)
CHEBI:18420		activates

Entamoeba 200:NIH transketolase apoenzyme add-back requires both Mg2+ and thiamine diphosphate. Adding Mg first causes a lag; this is preparation-specific reconstitution, not a new chemical reaction side.

transketolase
EC:2.2.1.1
  • PMID:6180735

    Source assertion: Entamoeba 200:NIH transketolase apoenzyme add-back requires both Mg2+ and thiamine diphosphate. Adding Mg first causes a lag; this is preparation-specific reconstitution, not a new chemical reaction side.

    Source locationPrinted p.193 Fig.1 and transketolase Results
thiamine(1+) diphosphate(3-)
CHEBI:58937		activates

Entamoeba 200:NIH transketolase apoenzyme add-back requires both Mg2+ and thiamine diphosphate. Adding Mg first causes a lag; this is preparation-specific reconstitution, not a new chemical reaction side.

transketolase
EC:2.2.1.1
  • PMID:6180735

    Source assertion: Entamoeba 200:NIH transketolase apoenzyme add-back requires both Mg2+ and thiamine diphosphate. Adding Mg first causes a lag; this is preparation-specific reconstitution, not a new chemical reaction side.

    Source locationPrinted p.193 Fig.1 and transketolase Results
6-phosphofructokinase [Clostridium thermosuccinogenes]
NCBIProtein:PNT94038.1

experimental construct: CDQ83_11320, DSM5809 sequence; pET28b+ N-terminal His6/TEV construct, E. coli Rosetta. 2020 MS at55C, 5mM MgCl2/5mM PPi/1mM S7P; distinct kinetic assay at1mM PPi. TEV cleavage not demonstrated.

Qualification evidence
  • PMID:31871051

    Source assertion: The Methods distinguish the pET28b+ and pD861-NT preparations, expression hosts, affinity purification and MS versus kinetic assay conditions. A tag is not proof of native assembly.

    Source locationXPath /article/body/sec[5]/sec[3]/p[1] | /article/body/sec[5]/sec[3]/p[2] | /article/body/sec[5]/sec[6]/sec/sec[1]/p[2] | /article/body/sec[5]/sec[6]/sec/sec[2]/p[1] | /article/body/sec[5]/sec[7]/p[1] | /article/body/sec[5]/sec[7]/p[2]
  • NCBIProtein:PNT94038.1

    Source assertion: The issuing GenBank record identifies accession PNT94038.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='PNT94038.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='PNT94038.1']/GBSeq_definition
  • PMID:31178853

    Source assertion: The cloned thermosuccinogenes enzymes use a pET-28b-derived construct with an N-terminal His6 tag flanking a TEV protease site and E. coli Rosetta expression. This directly supports the CDQ83_11320 construct feature; tag cleavage is not documented.

    Source locationXPath /article/body/sec[2]/sec[1]/p
catalyzes

Purified PPi-PFK converts S7P to SBP with PPi; minus-PPi/minus-enzyme controls distinguish product formation. F6P kinetics and rabbit aldolase coupling are separate observations.

RXN-21730
MetaCyc:RXN-21730
  • PMID:31871051

    Source assertion: Purified PPi-PFK converts S7P to SBP with PPi; minus-PPi/minus-enzyme controls distinguish product formation. F6P kinetics and rabbit aldolase coupling are separate observations.

    Source locationXPath /article/body/sec[2]/sec[2]/p[2] | /article/body/sec[2]/sec[2]/fig[1] | /article/body/sec[2]/sec[2]/p[5] | /article/body/sec[2]/sec[2]/table-wrap
  • NCBIProtein:PNT94038.1

    Source assertion: The issuing GenBank record identifies accession PNT94038.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='PNT94038.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='PNT94038.1']/GBSeq_definition
phosphofructokinase [Acetivibrio thermocellus DSM 1313]
NCBIProtein:ADU74928.1

experimental construct: DSM1313 Clo1313_1876, PCR into pD861-NT/pSH157, N-terminal His construct in E. coli T7 Express lysY/Iq. 2020 MS at55C with5mM MgCl2/5mM PPi/1mM S7P; separate1mM PPi kinetic assay.

Qualification evidence
  • PMID:31871051

    Source assertion: The Methods distinguish the pET28b+ and pD861-NT preparations, expression hosts, affinity purification and MS versus kinetic assay conditions. A tag is not proof of native assembly.

    Source locationXPath /article/body/sec[5]/sec[3]/p[1] | /article/body/sec[5]/sec[3]/p[2] | /article/body/sec[5]/sec[6]/sec/sec[1]/p[2] | /article/body/sec[5]/sec[6]/sec/sec[2]/p[1] | /article/body/sec[5]/sec[7]/p[1] | /article/body/sec[5]/sec[7]/p[2]
  • NCBIProtein:ADU74928.1

    Source assertion: The issuing GenBank record identifies accession ADU74928.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ADU74928.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ADU74928.1']/GBSeq_definition
catalyzes

Purified PPi-PFK converts S7P to SBP with PPi; minus-PPi/minus-enzyme controls distinguish product formation. F6P kinetics and rabbit aldolase coupling are separate observations.

RXN-21730
MetaCyc:RXN-21730
  • PMID:31871051

    Source assertion: Purified PPi-PFK converts S7P to SBP with PPi; minus-PPi/minus-enzyme controls distinguish product formation. F6P kinetics and rabbit aldolase coupling are separate observations.

    Source locationXPath /article/body/sec[2]/sec[2]/p[2] | /article/body/sec[2]/sec[2]/fig[1] | /article/body/sec[2]/sec[2]/p[5] | /article/body/sec[2]/sec[2]/table-wrap
  • NCBIProtein:ADU74928.1

    Source assertion: The issuing GenBank record identifies accession ADU74928.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ADU74928.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ADU74928.1']/GBSeq_definition
phosphofructokinase [Acetivibrio thermocellus ATCC 27405]
NCBIProtein:ABN51585.1

experimental construct: ATCC27405/DSM1237 Cthe_0347 pAHCT0347/pRSET-A, N-terminal His6, E. coli T7 Shuffle. Pfp-specific linker and codon-optimization details remain unresolved. The 2023 S7P-MS assay at50C is distinct from F6P competition/kinetics. No native homodimer measurement is inferred from sequence annotation.

Qualification evidence
  • PMID:37438781

    Source assertion: Pfp pAHCT0347 carries an N-terminal His6 tag and is expressed in E. coli T7 Shuffle. The Pfp-specific passages do not establish a linker or codon optimization. Forward MS uses50C, 2mM PPi,2.115mM S7P,2.5mM MgCl2.

    Source locationXPath /article/body/sec[5]/sec[1]/p | /article/body/sec[5]/sec[2]/p | /article/body/sec[5]/sec[4]/p | /article/body/sec[5]/sec[5]/p[1] | /article/body/sec[5]/sec[5]/p[3] | /article/body/sec[5]/sec[10]/p | /article/body/sec[2]/sec[1]/p
  • NCBIProtein:ABN51585.1

    Source assertion: The issuing GenBank record identifies accession ABN51585.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_definition
  • hdl:1993/32279

    Source assertion: The thesis identifies synthetic pAHCT0347 with a pRSET-A backbone, T7 Shuffle expression and His6-tagged Pfp purification. Its inspected Pfp passages do not establish linker or codon-optimization details. The thesis F6P assay is distinct from the later S7P MS experiment.

    Source locationNative thesis PDFpp.111–113 (printed86–88), expression, purification and PFK assays; PDFp.117 (printed92), PFK preparation
catalyzes

ATCC27405 Cthe_0347 Pfp forms SBP from S7P with PPi in the forward MS assay. Fitted S7P Km3.236mM exceeds the highest measured2.12mM; it is not averaged with DSM1313 kinetics.

RXN-21730
MetaCyc:RXN-21730
  • PMID:37438781

    Source assertion: ATCC27405 Cthe_0347 Pfp forms SBP from S7P with PPi in the forward MS assay. Fitted S7P Km3.236mM exceeds the highest measured2.12mM; it is not averaged with DSM1313 kinetics.

    Source locationXPath /article/body/sec[2]/sec[2]/table-wrap[2] | /article/body/sec[2]/sec[3]/p | /article/body/sec[2]/sec[3]/fig | /article/body/sec[5]/sec[10]/p
  • NCBIProtein:ABN51585.1

    Source assertion: The issuing GenBank record identifies accession ABN51585.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_definition
diphosphate
MetaCyc:PPI		inhibits

In the purified Cthe_0347 F6P assay, PPi substrate inhibition was fitted with Ki1.38±0.5mM. PPi is also the donor; this preparation-specific high-substrate effect is not direct S7P inhibition evidence.

phosphofructokinase [Acetivibrio thermocellus ATCC 27405]
NCBIProtein:ABN51585.1

experimental construct: Thesis Cthe_0347 pAHCT0347/pRSET-A His6 in E. coli T7 Shuffle; purified F6P-dependent PPi-PFK assay at50C with5mM MgCl2. Pfp-specific linker and codon-optimization details remain unresolved. This qualifier does not transfer the inhibitor sign to S7P phosphorylation.

Qualification evidence
  • hdl:1993/32279

    Source assertion: The thesis used synthetic pAHCT0347/pRSET-A His6 Pfp in T7 Shuffle, Ni purification and50C F6P-coupled assay with5mM MgCl2. These inhibitor data precede the later S7P experiment.

    Source locationNative thesis PDFpp.111–113 (printed86–88), expression, purification and PFK assays
  • NCBIProtein:ABN51585.1

    Source assertion: The issuing GenBank record identifies accession ABN51585.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_definition
  • hdl:1993/32279

    Source assertion: In the purified Cthe_0347 F6P assay, PPi substrate inhibition was fitted with Ki1.38±0.5mM. PPi is also the donor; this preparation-specific high-substrate effect is not direct S7P inhibition evidence.

    Source locationNative thesis PDF p.120 (printed95), Phosphofructokinase Results; Fig.4.4 PDFp.121 (printed96)
  • NCBIProtein:ABN51585.1

    Source assertion: The issuing GenBank record identifies accession ABN51585.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_definition
ATP(4-)
CHEBI:30616		inhibits

Adding1mM ATP reduced the Cthe_0347 F6P-PFK activity about60%. At1mM ADP, AMP, GTP, GMP and PEP no significant effect was reported; no direct ATP-binding site or S7P-assay sign is established.

phosphofructokinase [Acetivibrio thermocellus ATCC 27405]
NCBIProtein:ABN51585.1

experimental construct: Thesis Cthe_0347 pAHCT0347/pRSET-A His6 in E. coli T7 Shuffle; purified F6P-dependent PPi-PFK assay at50C with5mM MgCl2. Pfp-specific linker and codon-optimization details remain unresolved. This qualifier does not transfer the inhibitor sign to S7P phosphorylation.

Qualification evidence
  • hdl:1993/32279

    Source assertion: The thesis used synthetic pAHCT0347/pRSET-A His6 Pfp in T7 Shuffle, Ni purification and50C F6P-coupled assay with5mM MgCl2. These inhibitor data precede the later S7P experiment.

    Source locationNative thesis PDFpp.111–113 (printed86–88), expression, purification and PFK assays
  • NCBIProtein:ABN51585.1

    Source assertion: The issuing GenBank record identifies accession ABN51585.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_definition
  • hdl:1993/32279

    Source assertion: Adding1mM ATP reduced the Cthe_0347 F6P-PFK activity about60%. At1mM ADP, AMP, GTP, GMP and PEP no significant effect was reported; no direct ATP-binding site or S7P-assay sign is established.

    Source locationNative thesis PDF p.120 (printed95), Phosphofructokinase Results; Fig.4.4 PDFp.121 (printed96)
  • NCBIProtein:ABN51585.1

    Source assertion: The issuing GenBank record identifies accession ABN51585.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_definition
D-sedoheptulose 7-phosphate
MetaCyc:D-SEDOHEPTULOSE-7-P		inhibits

Adding S7P alongside F6P reduced FBP formation in the mixed-substrate Pfp activity assay. Competition is an interpretation of the FBP activity result, not an inhibitor-binding measurement or loss of S7P catalysis.

phosphofructokinase [Acetivibrio thermocellus ATCC 27405]
NCBIProtein:ABN51585.1

experimental construct: ATCC27405/DSM1237 Cthe_0347 pAHCT0347/pRSET-A, N-terminal His6, E. coli T7 Shuffle. Pfp-specific linker and codon-optimization details remain unresolved. The 2023 S7P-MS assay at50C is distinct from F6P competition/kinetics. No native homodimer measurement is inferred from sequence annotation.

Qualification evidence
  • PMID:37438781

    Source assertion: Pfp pAHCT0347 carries an N-terminal His6 tag and is expressed in E. coli T7 Shuffle. The Pfp-specific passages do not establish a linker or codon optimization. Forward MS uses50C, 2mM PPi,2.115mM S7P,2.5mM MgCl2.

    Source locationXPath /article/body/sec[5]/sec[1]/p | /article/body/sec[5]/sec[2]/p | /article/body/sec[5]/sec[4]/p | /article/body/sec[5]/sec[5]/p[1] | /article/body/sec[5]/sec[5]/p[3] | /article/body/sec[5]/sec[10]/p | /article/body/sec[2]/sec[1]/p
  • NCBIProtein:ABN51585.1

    Source assertion: The issuing GenBank record identifies accession ABN51585.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_definition
  • hdl:1993/32279

    Source assertion: The thesis identifies synthetic pAHCT0347 with a pRSET-A backbone, T7 Shuffle expression and His6-tagged Pfp purification. Its inspected Pfp passages do not establish linker or codon-optimization details. The thesis F6P assay is distinct from the later S7P MS experiment.

    Source locationNative thesis PDFpp.111–113 (printed86–88), expression, purification and PFK assays; PDFp.117 (printed92), PFK preparation
  • PMID:37438781

    Source assertion: Adding S7P alongside F6P reduced FBP formation in the mixed-substrate Pfp activity assay. Competition is an interpretation of the FBP activity result, not an inhibitor-binding measurement or loss of S7P catalysis.

    Source locationXPath /article/body/sec[2]/sec[3]/p | /article/body/sec[2]/sec[3]/fig | /article/body/sec[5]/sec[5]/p[3]
  • NCBIProtein:ABN51585.1

    Source assertion: The issuing GenBank record identifies accession ABN51585.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51585.1']/GBSeq_definition
fructose-1,6-bisphosphate aldolase, class II [Acetivibrio thermocellus ATCC 27405]
NCBIProtein:ABN51587.1

experimental construct: ATCC27405 Cthe_0349 pAHCT0349/pRSET-A N-terminal His6/linker, E. coli T7 Shuffle. Purified55C FBP assay; metal additions2mM. SBP cleavage was not verified; Ni purification does not identify a physiological cofactor.

Qualification evidence
  • PMID:37438781

    Source assertion: Aldoa is synthetic pAHCT0349/pRSET-A with N-terminal His6/linker, expressed in E. coli T7 Shuffle and Ni purified. FBP assays at55C are distinct from proposed SBP cleavage.

    Source locationXPath /article/body/sec[5]/sec[1]/p | /article/body/sec[5]/sec[2]/p | /article/body/sec[5]/sec[4]/p | /article/body/sec[5]/sec[5]/p[4] | /article/body/sec[2]/sec[7]/p
  • NCBIProtein:ABN51587.1

    Source assertion: The issuing GenBank record identifies accession ABN51587.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_definition
enables

Purified Cthe_0349 Aldoa has measured FBP aldolase activity, Km0.145mM and Vmax27.7micromol/min/mg. The Discussion explicitly says SBP aldolase activity was not verified.

fructose-bisphosphate aldolase
EC:4.1.2.13
  • PMID:37438781

    Source assertion: Purified Cthe_0349 Aldoa has measured FBP aldolase activity, Km0.145mM and Vmax27.7micromol/min/mg. The Discussion explicitly says SBP aldolase activity was not verified.

    Source locationXPath /article/body/sec[2]/sec[7]/p | /article/body/sec[2]/sec[8]/p | /article/body/sec[3]/p[6]
  • NCBIProtein:ABN51587.1

    Source assertion: The issuing GenBank record identifies accession ABN51587.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_definition
zinc(2+)
CHEBI:29105		activates

In55C FBP assays,2mM Zn2+ increased recombinant Aldoa activity more than twofold over no added metal. This does not establish SBP-specific Zn dependence or an unmodified native preparation.

fructose-1,6-bisphosphate aldolase, class II [Acetivibrio thermocellus ATCC 27405]
NCBIProtein:ABN51587.1

experimental construct: ATCC27405 Cthe_0349 pAHCT0349/pRSET-A N-terminal His6/linker, E. coli T7 Shuffle. Purified55C FBP assay; metal additions2mM. SBP cleavage was not verified; Ni purification does not identify a physiological cofactor.

Qualification evidence
  • PMID:37438781

    Source assertion: Aldoa is synthetic pAHCT0349/pRSET-A with N-terminal His6/linker, expressed in E. coli T7 Shuffle and Ni purified. FBP assays at55C are distinct from proposed SBP cleavage.

    Source locationXPath /article/body/sec[5]/sec[1]/p | /article/body/sec[5]/sec[2]/p | /article/body/sec[5]/sec[4]/p | /article/body/sec[5]/sec[5]/p[4] | /article/body/sec[2]/sec[7]/p
  • NCBIProtein:ABN51587.1

    Source assertion: The issuing GenBank record identifies accession ABN51587.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_definition
  • PMID:37438781

    Source assertion: In55C FBP assays,2mM Zn2+ increased recombinant Aldoa activity more than twofold over no added metal. This does not establish SBP-specific Zn dependence or an unmodified native preparation.

    Source locationXPath /article/body/sec[2]/sec[9]/p[1] | /article/body/sec[2]/sec[9]/fig | /article/body/sec[2]/sec[9]/p[2]
  • NCBIProtein:ABN51587.1

    Source assertion: The issuing GenBank record identifies accession ABN51587.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_definition
ammonium
CHEBI:28938		activates

In the tested FBP assay, added ammonium with Mg2+ increased Aldoa activity. Ammonium partly reduced the stronger Zn response; the activation sign is conditional on the Mg-containing comparison.

fructose-1,6-bisphosphate aldolase, class II [Acetivibrio thermocellus ATCC 27405]
NCBIProtein:ABN51587.1

experimental construct: ATCC27405 Cthe_0349 pAHCT0349/pRSET-A N-terminal His6/linker, E. coli T7 Shuffle. Purified55C FBP assay; metal additions2mM. SBP cleavage was not verified; Ni purification does not identify a physiological cofactor.

Qualification evidence
  • PMID:37438781

    Source assertion: Aldoa is synthetic pAHCT0349/pRSET-A with N-terminal His6/linker, expressed in E. coli T7 Shuffle and Ni purified. FBP assays at55C are distinct from proposed SBP cleavage.

    Source locationXPath /article/body/sec[5]/sec[1]/p | /article/body/sec[5]/sec[2]/p | /article/body/sec[5]/sec[4]/p | /article/body/sec[5]/sec[5]/p[4] | /article/body/sec[2]/sec[7]/p
  • NCBIProtein:ABN51587.1

    Source assertion: The issuing GenBank record identifies accession ABN51587.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_definition
  • PMID:37438781

    Source assertion: In the tested FBP assay, added ammonium with Mg2+ increased Aldoa activity. Ammonium partly reduced the stronger Zn response; the activation sign is conditional on the Mg-containing comparison.

    Source locationXPath /article/body/sec[2]/sec[9]/p[1] | /article/body/sec[2]/sec[9]/fig | /article/body/sec[2]/sec[9]/p[2]
  • NCBIProtein:ABN51587.1

    Source assertion: The issuing GenBank record identifies accession ABN51587.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_definition
potassium(1+)
CHEBI:29103		inhibits

Added K+ reduced Aldoa FBP activity in the Mg- or Zn-containing comparisons at2mM added ions. This is condition-specific and does not demonstrate K binding or SBP inhibition.

fructose-1,6-bisphosphate aldolase, class II [Acetivibrio thermocellus ATCC 27405]
NCBIProtein:ABN51587.1

experimental construct: ATCC27405 Cthe_0349 pAHCT0349/pRSET-A N-terminal His6/linker, E. coli T7 Shuffle. Purified55C FBP assay; metal additions2mM. SBP cleavage was not verified; Ni purification does not identify a physiological cofactor.

Qualification evidence
  • PMID:37438781

    Source assertion: Aldoa is synthetic pAHCT0349/pRSET-A with N-terminal His6/linker, expressed in E. coli T7 Shuffle and Ni purified. FBP assays at55C are distinct from proposed SBP cleavage.

    Source locationXPath /article/body/sec[5]/sec[1]/p | /article/body/sec[5]/sec[2]/p | /article/body/sec[5]/sec[4]/p | /article/body/sec[5]/sec[5]/p[4] | /article/body/sec[2]/sec[7]/p
  • NCBIProtein:ABN51587.1

    Source assertion: The issuing GenBank record identifies accession ABN51587.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_definition
  • PMID:37438781

    Source assertion: Added K+ reduced Aldoa FBP activity in the Mg- or Zn-containing comparisons at2mM added ions. This is condition-specific and does not demonstrate K binding or SBP inhibition.

    Source locationXPath /article/body/sec[2]/sec[9]/p[1] | /article/body/sec[2]/sec[9]/fig | /article/body/sec[2]/sec[9]/p[2]
  • NCBIProtein:ABN51587.1

    Source assertion: The issuing GenBank record identifies accession ABN51587.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ABN51587.1']/GBSeq_definition
fructose-1,6-bisphosphate aldolase, class II [Acetivibrio thermocellus DSM 1313]
NCBIProtein:ADU74927.1		enables

DSM1313 Clo1313_1875 is annotated class-II FBP aldolase. DAP-seq association is not a direct SBP assay, and rabbit coupling data are not transferred to this protein.

fructose-bisphosphate aldolase
EC:4.1.2.13
  • NCBIProtein:ADU74927.1

    Source assertion: DSM1313 Clo1313_1875 is annotated class-II FBP aldolase. DAP-seq association is not a direct SBP assay, and rabbit coupling data are not transferred to this protein.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ADU74927.1']/GBSeq_feature-table
ribulose-phosphate 3-epimerase [Acetivibrio thermocellus DSM 1313]
NCBIProtein:ADU74718.1		enables

DSM1313 Clo1313_1661 is annotated ribulose-phosphate3-epimerase with EC5.1.3.1. This is issuing annotation support, not a newly acquired purified-enzyme assay or measured metal requirement.

ribulose-phosphate 3-epimerase
EC:5.1.3.1
  • NCBIProtein:ADU74718.1

    Source assertion: DSM1313 Clo1313_1661 is annotated ribulose-phosphate3-epimerase with EC5.1.3.1. This is issuing annotation support, not a newly acquired purified-enzyme assay or measured metal requirement.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ADU74718.1']/GBSeq_feature-table
ribulose-phosphate 3-epimerase [Acetivibrio thermocellus ATCC 27405]
NCBIProtein:ABN51812.1		enables

ATCC27405 Cthe_0576 is annotated ribulose-phosphate3-epimerase with EC5.1.3.1. Evidence is annotation-level; no unsupported transfer of cofactor or oligomer is made.

ribulose-phosphate 3-epimerase
EC:5.1.3.1
  • NCBIProtein:ABN51812.1

    Source assertion: ATCC27405 Cthe_0576 is annotated ribulose-phosphate3-epimerase with EC5.1.3.1. Evidence is annotation-level; no unsupported transfer of cofactor or oligomer is made.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ABN51812.1']/GBSeq_feature-table
Sugar-phosphate isomerase, RpiB/LacA/LacB family
UniProtKB:A3DIL8		enables

The unreviewed ATCC27405 Cthe_2597 entry assigns EC5.3.1.6 from submitted/automatic annotation. Its R5P-bound deposited structure supports ligand context; rare-sugar kinetic papers are not substituted for a fully inspected R5P kinetic assay.

ribose-5-phosphate isomerase
EC:5.3.1.6
  • UniProtKB:A3DIL8

    Source assertion: The unreviewed ATCC27405 Cthe_2597 entry assigns EC5.3.1.6 from submitted/automatic annotation. Its R5P-bound deposited structure supports ligand context; rare-sugar kinetic papers are not substituted for a fully inspected R5P kinetic assay.

    Source locationJSON /proteinDescription/submissionNames/0/ecNumbers | /genes | /organism | /uniProtKBCrossReferences
  • DOI:10.2210/pdb3HEE/pdb

    Source assertion: Deposited3HEE identifies Cthe_2597/A3DIL8 from ATCC27405, a ribose5-phosphate ligand and author/PISA dimer. These structural observations do not supply unseen full-text kinetics.

    Source locationPDBx _struct_ref; _entity_src_gen; _pdbx_entity_nonpoly; _pdbx_struct_assembly
ammonium
CHEBI:28938		activates

In the 2020 F6P/ATP comparison, CDQ83_07225 required added ammonium with lyophilized auxiliary enzymes replacing ammonium-sulfate suspensions because S7P Ba-salt precipitated BaSO4. This does not apply to the PPi-S7P catalyst; the source NH4Cl2 formula is inconsistent.

6-phosphofructokinase [Clostridium thermosuccinogenes]
NCBIProtein:PNT93300.1

experimental construct: CDQ83_07225 pET28b+/Rosetta His6/TEV construct; 55C F6P/ATP comparator. The 2020 assay used lyophilized rabbit aldolase/GPDH instead of ammonium-sulfate suspensions because S7P Ba-salt precipitated BaSO4; ammonium was added. The source NH4Cl2 formula is unresolved.

Qualification evidence
  • PMID:31178853

    Source assertion: The CDQ83 proteins use pET28b N-terminal His6 constructs flanking a TEV site, Rosetta expression, heated CFE and55C donor assays; empty-vector controls are included, cleavage is not documented.

    Source locationXPath /article/body/sec[2]/sec[1]/p | /article/body/sec[2]/sec[2]/p | /article/body/sec[2]/sec[4]/p[1] | /article/body/sec[2]/sec[4]/p[3]
  • NCBIProtein:PNT93300.1

    Source assertion: The issuing GenBank record identifies accession PNT93300.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='PNT93300.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='PNT93300.1']/GBSeq_definition
  • PMID:31871051

    Source assertion: The 55C assay used lyophilized rabbit aldolase and GPDH instead of ammonium-sulfate suspensions because S7P Ba-salt caused BaSO4 precipitation. The ATP/GTP-dependent comparator required added ammonium; the printed NH4Cl2 formula is inconsistent. PFK buffer ultrafiltration is a separate preparation step.

    Source locationXPath /article/body/sec[5]/sec[7]/p[1] | /article/body/sec[5]/sec[7]/p[2]
  • PMID:31871051

    Source assertion: In the 2020 F6P/ATP comparison, CDQ83_07225 required added ammonium with lyophilized auxiliary enzymes replacing ammonium-sulfate suspensions because S7P Ba-salt precipitated BaSO4. This does not apply to the PPi-S7P catalyst; the source NH4Cl2 formula is inconsistent.

    Source locationXPath /article/body/sec[5]/sec[7]/p[2]
  • NCBIProtein:PNT93300.1

    Source assertion: The issuing GenBank record identifies accession PNT93300.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='PNT93300.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='PNT93300.1']/GBSeq_definition
Transketolase domain-containing protein [Acetivibrio thermocellus DSM 1313]
NCBIProtein:ADU73172.1

experimental construct: DSM1313 TktAB subunit in KJC335-derived delta-hpt/xylAB engineered strain; pTC131374-5 co-overexpresses BOTH genes from gapDH promoter. This individual endpoint does not assert solitary transketolase activity or a1:1 assembly.

Qualification evidence
  • PMID:32884054

    Source assertion: KJC335 is DSM1313-derived delta-hpt with heterologous xylAB; pTC131374-5 expresses both genomic TktAB genes from gapDH promoter. The empty-vector control is pKJC84.

    Source locationXPath /article/body/sec[3]/sec[1]/p[1] | /article/body/sec[3]/sec[1]/p[2]
  • NCBIProtein:ADU73172.1

    Source assertion: The issuing GenBank record identifies accession ADU73172.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ADU73172.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ADU73172.1']/GBSeq_definition
part_of

KJC335-derived co-overexpression of both TktAB genes reduced xylose doubling time from19.0±5.7h to5.8±0.6h versus empty vector. This supports paired pathway participation, not isolated subunit catalysis or measured complex stoichiometry.

MetaCyc:PWY-8178
  • PMID:32884054

    Source assertion: KJC335-derived co-overexpression of both TktAB genes reduced xylose doubling time from19.0±5.7h to5.8±0.6h versus empty vector. This supports paired pathway participation, not isolated subunit catalysis or measured complex stoichiometry.

    Source locationXPath /article/body/sec[2]/sec[3]/p[3] | /article/body/sec[2]/sec[3]/p[4] | /article/body/sec[2]/sec[3]/fig[2] | /article/body/sec[3]/sec[1]/p[1] | /article/body/sec[3]/sec[1]/p[2]
  • NCBIProtein:ADU73172.1

    Source assertion: The issuing GenBank record identifies accession ADU73172.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ADU73172.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ADU73172.1']/GBSeq_definition
Transketolase domain-containing protein [Acetivibrio thermocellus DSM 1313]
NCBIProtein:ADU73173.1

experimental construct: DSM1313 TktAB subunit in KJC335-derived delta-hpt/xylAB engineered strain; pTC131374-5 co-overexpresses BOTH genes from gapDH promoter. This individual endpoint does not assert solitary transketolase activity or a1:1 assembly.

Qualification evidence
  • PMID:32884054

    Source assertion: KJC335 is DSM1313-derived delta-hpt with heterologous xylAB; pTC131374-5 expresses both genomic TktAB genes from gapDH promoter. The empty-vector control is pKJC84.

    Source locationXPath /article/body/sec[3]/sec[1]/p[1] | /article/body/sec[3]/sec[1]/p[2]
  • NCBIProtein:ADU73173.1

    Source assertion: The issuing GenBank record identifies accession ADU73173.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ADU73173.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ADU73173.1']/GBSeq_definition
part_of

KJC335-derived co-overexpression of both TktAB genes reduced xylose doubling time from19.0±5.7h to5.8±0.6h versus empty vector. This supports paired pathway participation, not isolated subunit catalysis or measured complex stoichiometry.

MetaCyc:PWY-8178
  • PMID:32884054

    Source assertion: KJC335-derived co-overexpression of both TktAB genes reduced xylose doubling time from19.0±5.7h to5.8±0.6h versus empty vector. This supports paired pathway participation, not isolated subunit catalysis or measured complex stoichiometry.

    Source locationXPath /article/body/sec[2]/sec[3]/p[3] | /article/body/sec[2]/sec[3]/p[4] | /article/body/sec[2]/sec[3]/fig[2] | /article/body/sec[3]/sec[1]/p[1] | /article/body/sec[3]/sec[1]/p[2]
  • NCBIProtein:ADU73173.1

    Source assertion: The issuing GenBank record identifies accession ADU73173.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ADU73173.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ADU73173.1']/GBSeq_definition
CoA-binding domain protein [Acetivibrio thermocellus DSM 1313]
NCBIProtein:ADU75484.1

experimental construct: Two distinct Rex constructs: codon-optimized C-terminal HaloTag in E. coli S30 IVTT for55C DAP-seq, and C-terminal His6 BL21(DE3) preparation for room-temperature motif EMSA. Shared1875/1876 promoter sites do not establish signed expression.

Qualification evidence
  • PMID:34566906

    Source assertion: DAP-seq uses C-terminal HaloTag Rex in E. coli S30 IVTT at55C with HaloTag-only control; separate motif EMSA uses semi-purified C-terminal His6 Rex from BL21(DE3) at room temperature. No Kd is reported.

    Source locationXPath /article/body/sec[2]/sec[4]/p | /article/body/sec[2]/sec[5]/p[1] | /article/body/sec[2]/sec[8]/p[1] | /article/body/sec[2]/sec[8]/p[2] | /article/body/sec[2]/sec[8]/p[3]
  • NCBIProtein:ADU75484.1

    Source assertion: The issuing GenBank record identifies accession ADU75484.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ADU75484.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ADU75484.1']/GBSeq_definition
enables

Rex DNA-binding assays support a sequence-specific motif. DAP-seq associates two shared divergent-region sites with Clo1313_1875/1876, but site-to-gene assignment and expression sign remain unresolved; motif EMSA is not a promoter-specific regulation assay.

sequence-specific DNA binding
GO:0043565
  • PMID:34566906

    Source assertion: Rex DNA-binding assays support a sequence-specific motif. DAP-seq associates two shared divergent-region sites with Clo1313_1875/1876, but site-to-gene assignment and expression sign remain unresolved; motif EMSA is not a promoter-specific regulation assay.

    Source locationXPath /article/body/sec[3]/sec[1]/table-wrap[1] | /article/body/sec[3]/sec[1]/table-wrap[2] | /article/body/sec[3]/sec[3]/p[1] | /article/body/sec[3]/sec[3]/fig | /article/body/sec[3]/sec[6]/sec[8]/table-wrap
  • NCBIProtein:ADU75484.1

    Source assertion: The issuing GenBank record identifies accession ADU75484.1 with its source organism, locus and annotated product. The identity supports this endpoint, not independent proof of every catalytic or regulatory claim.

    Source locationXPath /GBSet/GBSeq[GBSeq_accession-version='ADU75484.1']/GBSeq_feature-table | /GBSet/GBSeq[GBSeq_accession-version='ADU75484.1']/GBSeq_definition

References

Curation history