L-ascorbate degradation I (bacterial, anaerobic)

MetaCyc:PWY0-301

The complete MetaCyc 27.0 five-event bacterial L-ascorbate degradationI route combines UlaABC PTS uptake/phosphorylation with UlaG lactonase, UlaD decarboxylase, UlaE 3-epimerase and UlaF 4-epimerase to D-xylulose 5-phosphate. E. coli K-12/MG1655 enzyme evidence and BW25113 transport genetics support anaerobic utilization at low ascorbate concentrations; strain, reporter and construct scopes are retained beside their claims. The general PTS comparison specifically uses JM101 and PB11 with a combined ptsHIcrr deletion. Native27.0 includes the PTS event, whereas 22.5 lists it as an incoming link. The PTS event is an HPr-fed aggregate; its carrier residue classes are protein-bound, not free amino acids. Obsolete Rhea 33303 and replacement 42436 are not asserted exact equivalents: the latter uses a generic immediate histidyl-protein donor, while native and UniProt relay commentary predict UlaB phosphoCys9. The complete net transport equation is retained without inventing a direct HPr-to-sugar transfer. UlaE/UlaF are distinct from SgbU/SgbE/AraD used in other contexts. The 2002 hydrolysis-before-PTS proposal lacked an assigned hydrolase; later sources support the present ordering. UlaG 2010 and UlaR 2008 primary abstracts were accessible, but their full methods/figures were not; detailed construct and kinetic claims are not inferred. UlaG retains its current UniProt Probable label despite later direct activity evidence. Ascorbate6P relieves UlaR repression; free ascorbate does not directly displace UlaR in 2004 binding tests. Anaerobic describes the selected route, not a universal inability of all mutants or other routes to use ascorbate aerobically. The separate aerobic yia route is excluded.

Pathway type
carbohydrate degradation
Organism scope

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Pathway network

47 nodes · 55 asserted directed edges

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Pathway network: L-ascorbate degradation I (bacterial, anaerobic) 47 nodes · 55 asserted directed edges. Every arrow links to its evidence table row; nodes link to their component details. Isolated declared components are retained. MetaCyc:RXN0-2461 — part_of → MetaCyc:PWY0-301; The MetaCyc 27.0 PWY0-301 reaction-list contains RXN0-2461 as a member of this pathway.; Evidence: MetaCyc:PWY0-301part of RHEA:28804 — part_of → MetaCyc:PWY0-301; The MetaCyc 27.0 PWY0-301 reaction-list contains RXN0-5214 as a member of this pathway.; Evidence: MetaCyc:PWY0-301part of RHEA:14354 — part_of → MetaCyc:PWY0-301; The MetaCyc 27.0 PWY0-301 reaction-list contains RXN0-705 as a member of this pathway.; Evidence: MetaCyc:PWY0-301part of RHEA:18499 — part_of → MetaCyc:PWY0-301; The MetaCyc 27.0 PWY0-301 reaction-list contains LXULRU5P-RXN as a member of this pathway.; Evidence: MetaCyc:PWY0-301part of RHEA:22369 — part_of → MetaCyc:PWY0-301; The MetaCyc 27.0 PWY0-301 reaction-list contains RIBULPEPIM-RXN as a member of this pathway.; Evidence: MetaCyc:PWY0-301part of MetaCyc:RXN0-2461 — precedes → RHEA:28804; The selected native pathway orders RXN0-2461 before RXN0-5214; both are members of its five-event route.; Evidence: MetaCyc:PWY0-301precedes RHEA:28804 — precedes → RHEA:14354; The selected native pathway orders RXN0-5214 before RXN0-705; both are members of its five-event route.; Evidence: MetaCyc:PWY0-301precedes RHEA:14354 — precedes → RHEA:18499; The selected native pathway orders RXN0-705 before LXULRU5P-RXN; both are members of its five-event route.; Evidence: MetaCyc:PWY0-301precedes RHEA:18499 — precedes → RHEA:22369; The selected native pathway orders LXULRU5P-RXN before RIBULPEPIM-RXN; both are members of its five-event route.; Evidence: MetaCyc:PWY0-301precedes MetaCyc:Hpr-pi-phospho-L-histidines — consumes → MetaCyc:RXN0-2461; Native RXN0-2461 left contains Hpr-pi-phospho-L-histidines. Ascorbate enters from outside and phosphorylated product is inside. HPr-linked residue classes represent the aggregate relay, not free amino acids or a direct HPr-to-sugar transfer.; Evidence: MetaCyc:RXN0-2461consumes CHEBI:38290 — consumes → MetaCyc:RXN0-2461; Native RXN0-2461 left contains ASCORBATE. Ascorbate enters from outside and phosphorylated product is inside. HPr-linked residue classes represent the aggregate relay, not free amino acids or a direct HPr-to-sugar transfer.; Evidence: MetaCyc:RXN0-2461consumes MetaCyc:RXN0-2461 — produces → CHEBI:61698; Native RXN0-2461 right contains L-ASCORBATE-6-PHOSPHATE. Ascorbate enters from outside and phosphorylated product is inside. HPr-linked residue classes represent the aggregate relay, not free amino acids or a direct HPr-to-sugar transfer.; Evidence: MetaCyc:RXN0-2461produces MetaCyc:RXN0-2461 — produces → MetaCyc:Hpr-Histidine; Native RXN0-2461 right contains Hpr-Histidine. Ascorbate enters from outside and phosphorylated product is inside. HPr-linked residue classes represent the aggregate relay, not free amino acids or a direct HPr-to-sugar transfer.; Evidence: MetaCyc:RXN0-2461produces CHEBI:61698 — consumes → RHEA:28804; The formal directional RHEA:28804 substrates side contains CHEBI:61698, coefficient 1.; Evidence: RHEA:28804consumes CHEBI:15377 — consumes → RHEA:28804; The formal directional RHEA:28804 substrates side contains CHEBI:15377, coefficient 1.; Evidence: RHEA:28804consumes RHEA:28804 — produces → CHEBI:58774; The formal directional RHEA:28804 products side contains CHEBI:58774, coefficient 1.; Evidence: RHEA:28804produces CHEBI:58774 — consumes → RHEA:14354; The formal directional RHEA:14354 substrates side contains CHEBI:58774, coefficient 1.; Evidence: RHEA:14354consumes CHEBI:15378 — consumes → RHEA:14354; The formal directional RHEA:14354 substrates side contains CHEBI:15378, coefficient 1.; Evidence: RHEA:14354consumes RHEA:14354 — produces → CHEBI:57829; The formal directional RHEA:14354 products side contains CHEBI:57829, coefficient 1.; Evidence: RHEA:14354produces RHEA:14354 — produces → CHEBI:16526; The formal directional RHEA:14354 products side contains CHEBI:16526, coefficient 1.; Evidence: RHEA:14354produces CHEBI:57829 — consumes → RHEA:18499; The formal directional RHEA:18499 substrates side contains CHEBI:57829, coefficient 1. This is the right-to-left direction of the L-ribulose/L-xylulose 5-phosphate equation.; Evidence: RHEA:18499consumes RHEA:18499 — produces → CHEBI:58226; The formal directional RHEA:18499 products side contains CHEBI:58226, coefficient 1. This is the right-to-left direction of the L-ribulose/L-xylulose 5-phosphate equation.; Evidence: RHEA:18499produces CHEBI:58226 — consumes → RHEA:22369; The formal directional RHEA:22369 substrates side contains CHEBI:58226, coefficient 1. This is the left-to-right direction from L-ribulose to D-xylulose 5-phosphate.; Evidence: RHEA:22369consumes RHEA:22369 — produces → CHEBI:57737; The formal directional RHEA:22369 products side contains CHEBI:57737, coefficient 1. This is the left-to-right direction from L-ribulose to D-xylulose 5-phosphate.; Evidence: RHEA:22369produces MetaCyc:EIISGA — catalyzes → MetaCyc:RXN0-2461; Native MetaCyc:RXN0-2461 enzymatic-reaction ENZRXN0-3481 assigns this activity to EIISGA, the L-ascorbate-specific UlaABC PTS.; Evidence: MetaCyc:RXN0-2461, PMID:12644495catalyzes MetaCyc:CPLX0-7848 — catalyzes → RHEA:28804; Native MetaCyc:RXN0-5214 enzymatic-reaction ENZRXN0-6334 assigns this activity to CPLX0-7848, the UlaG lactonase complex.; Evidence: MetaCyc:RXN0-5214, PMID:20359483catalyzes MetaCyc:CPLX0-7744 — catalyzes → RHEA:14354; subject experimental construct: The 2002 supporting assay used MG1655-derived recombinant protein expressed in BL21(DE3) with an N-terminal His10 tag, then thrombin-cleaved. Residual cleavage sequence was not reported. Native assembly is supported separately by the database source.; Evidence PMID:11741871: The genes were amplified from MG1655, expressed using modified pET15b in BL21(DE3), and affinity tags were removed by thrombin for the UlaD/E/F assays. Remaining cleavage-derived residues were not specified. (Materials and Methods, protein production and purification; Table 2); Native MetaCyc:RXN0-705 enzymatic-reaction ENZRXN0-725 assigns this activity to CPLX0-7744, the UlaD decarboxylase complex. The pathway excludes the SgbH alternative.; Evidence: MetaCyc:RXN0-705, PMID:11741871, MetaCyc:PWY0-301catalyzes UniProtKB:P39305 — catalyzes → RHEA:18499; subject experimental construct: The 2002 supporting assay used MG1655-derived recombinant protein expressed in BL21(DE3) with an N-terminal His10 tag, then thrombin-cleaved. Residual cleavage sequence was not reported. Native assembly is supported separately by the database source.; Evidence PMID:11741871: The genes were amplified from MG1655, expressed using modified pET15b in BL21(DE3), and affinity tags were removed by thrombin for the UlaD/E/F assays. Remaining cleavage-derived residues were not specified. (Materials and Methods, protein production and purification; Table 2); Native MetaCyc:LXULRU5P-RXN enzymatic-reaction ENZRXN0-726 assigns this activity to G7859-MONOMER, UlaE.; Evidence: MetaCyc:LXULRU5P-RXN, PMID:11741871, MetaCyc:G7859-MONOMERcatalyzes UniProtKB:P39306 — catalyzes → RHEA:22369; subject experimental construct: The 2002 supporting assay used MG1655-derived recombinant protein expressed in BL21(DE3) with an N-terminal His10 tag, then thrombin-cleaved. Residual cleavage sequence was not reported. Native assembly is supported separately by the database source.; Evidence PMID:11741871: The genes were amplified from MG1655, expressed using modified pET15b in BL21(DE3), and affinity tags were removed by thrombin for the UlaD/E/F assays. Remaining cleavage-derived residues were not specified. (Materials and Methods, protein production and purification; Table 2); Native MetaCyc:RIBULPEPIM-RXN enzymatic-reaction ENZRXN0-722 assigns this activity to G7860-MONOMER, UlaF. The pathway excludes AraD and SgbE alternatives.; Evidence: MetaCyc:RIBULPEPIM-RXN, PMID:11741871, MetaCyc:PWY0-301, MetaCyc:G7860-MONOMERcatalyzes UniProtKB:P39300 — part_of → MetaCyc:CPLX0-7848; Native MetaCyc:CPLX0-7848 contains 6 copies of G7855-MONOMER, resolved to UniProtKB:P39300. This defines the UlaG hexamer.; Evidence: MetaCyc:CPLX0-7848, UniProtKB:P39300part of UniProtKB:P39304 — part_of → MetaCyc:CPLX0-7744; Native MetaCyc:CPLX0-7744 contains 2 copies of G7858-MONOMER, resolved to UniProtKB:P39304. This defines the UlaD homodimer.; Evidence: MetaCyc:CPLX0-7744, UniProtKB:P39304part of UniProtKB:P39301 — part_of → MetaCyc:EIISGA; Native MetaCyc:EIISGA contains 2 copies of SGAT-MONOMER, resolved to UniProtKB:P39301. The complete native EIISGA composition is two UlaA, one UlaB and one UlaC subunit.; Evidence: MetaCyc:EIISGA, UniProtKB:P39301part of UniProtKB:P69822 — part_of → MetaCyc:EIISGA; Native MetaCyc:EIISGA contains 1 copy of YJFT-MONOMER, resolved to UniProtKB:P69822. The complete native EIISGA composition is two UlaA, one UlaB and one UlaC subunit.; Evidence: MetaCyc:EIISGA, UniProtKB:P69822part of UniProtKB:P69820 — part_of → MetaCyc:EIISGA; Native MetaCyc:EIISGA contains 1 copy of YJFU-MONOMER, resolved to UniProtKB:P69820. The complete native EIISGA composition is two UlaA, one UlaB and one UlaC subunit.; Evidence: MetaCyc:EIISGA, UniProtKB:P69820part of MetaCyc:CPLX0-7848 — has_cofactor → CHEBI:29035; The 2010 primary abstract reports that Mn2+- or Co2+-loaded UlaG hydrolyses L-ascorbate 6-phosphate. These are alternative active metal-loaded states, not a requirement that both metals bind simultaneously. Full methods/figures remain unavailable.; Evidence: PMID:20359483has cofactor MetaCyc:CPLX0-7848 — has_cofactor → CHEBI:48828; The 2010 primary abstract reports that Mn2+- or Co2+-loaded UlaG hydrolyses L-ascorbate 6-phosphate. These are alternative active metal-loaded states, not a requirement that both metals bind simultaneously. Full methods/figures remain unavailable.; Evidence: PMID:20359483has cofactor MetaCyc:CPLX0-7744 — has_cofactor → CHEBI:18420; Reviewed UlaD binds one Mg2+ per subunit; native structural commentary describes the Mg-stabilized enediolate. This assignment is not inferred merely from Mg present in a coupled assay.; Evidence: UniProtKB:P39304, MetaCyc:CPLX0-7744has cofactor UniProtKB:P39306 — has_cofactor → CHEBI:29105; UniProt annotates one Zn2+ per UlaF subunit by similarity to AraD and HAMAP, not a direct UlaF metal experiment. The 2002 Mg-containing coupled assay does not independently establish the physiological UlaF metal.; Evidence: UniProtKB:P39306has cofactor UniProtKB:P0AA04 — enables → MetaCyc:RXN0-2461; Native EIISGA requires HPr and enzyme I. The primary comparison used JM101 and its PB11 derivative carrying the combined ptsHIcrr deletion; PB11 lacked uptake and growth. This is not a BW25113 comparison or a test of individual ptsH or ptsI knockouts, and does not establish direct HPr-to-sugar transfer.; Evidence: MetaCyc:EIISGA, PMID:12644495enables UniProtKB:P08839 — enables → MetaCyc:RXN0-2461; Native EIISGA requires HPr and enzyme I. The primary comparison used JM101 and its PB11 derivative carrying the combined ptsHIcrr deletion; PB11 lacked uptake and growth. This is not a BW25113 comparison or a test of individual ptsH or ptsI knockouts, and does not establish direct HPr-to-sugar transfer.; Evidence: MetaCyc:EIISGA, PMID:12644495enables UniProtKB:P39301 — located_in → GO:0005886; Reviewed UlaA is an integral multi-pass cell inner membrane protein.; Evidence: UniProtKB:P39301located in UniProtKB:P69822 — located_in → GO:0005737; Reviewed UlaB is cytoplasmic; annotation is inferred, not direct imaging.; Evidence: UniProtKB:P69822located in UniProtKB:P69820 — located_in → GO:0005737; Reviewed UlaC is cytoplasmic; annotation is inferred, not direct imaging.; Evidence: UniProtKB:P69820located in UniProtKB:P39300 — located_in → GO:0005737; Reviewed UlaG cytoplasmic location is inferred; the 2003 lack of an N-terminal export signal is supporting context.; Evidence: UniProtKB:P39300located in UniProtKB:P0A9W0 — inhibits → Entrez:948705; subject experimental construct: Supporting DNA-binding assays used NusA/His6-UlaR after thrombin tag removal. The separate promoter reporter experiments used JA134-derived cells; no engineered tag is attributed to their chromosomal UlaR.; Evidence PMID:14996803: Purified recombinant UlaR was produced from pET43c+ in BL21(DE3), its tag removed with thrombin, and tested by gel retardation. Promoter reporter strains derive from JA134. (Materials and Methods, overexpression and purification of UlaR; Table 1); UlaR represses this promoter-bearing gene. The ulaA promoter controls the six-gene ulaABCDEF operon. Reporter and binding experiments used JA134 derivatives and tag-cleaved recombinant UlaR; DNA-looping was proposed rather than directly visualized.; Evidence: PMID:14996803inhibits UniProtKB:P0A9W0 — inhibits → Entrez:948717; subject experimental construct: Supporting DNA-binding assays used NusA/His6-UlaR after thrombin tag removal. The separate promoter reporter experiments used JA134-derived cells; no engineered tag is attributed to their chromosomal UlaR.; Evidence PMID:14996803: Purified recombinant UlaR was produced from pET43c+ in BL21(DE3), its tag removed with thrombin, and tested by gel retardation. Promoter reporter strains derive from JA134. (Materials and Methods, overexpression and purification of UlaR; Table 1); UlaR represses this promoter-bearing gene. The ulaA promoter controls the six-gene ulaABCDEF operon. Reporter and binding experiments used JA134 derivatives and tag-cleaved recombinant UlaR; DNA-looping was proposed rather than directly visualized.; Evidence: PMID:14996803inhibits EcoCyc:CPLX0-226 — activates → Entrez:948717; cAMP-CRP directly binds and activates the ulaA promoter controlling ulaABCDEF. ulaG expression was not CRP-dependent in the same reporter conditions; no CRP→ulaG activation is asserted.; Evidence: PMID:14996803activates EcoCyc:PC00027 — inhibits → Entrez:948705; IHF contributes to repression of basal expression at this divergent ula promoter in JA134 derivatives, especially ulaA. The effect is regulatory context for UlaR-dependent promoter organization; no direct inhibition of catalytic protein is implied.; Evidence: PMID:14996803inhibits EcoCyc:PC00027 — inhibits → Entrez:948717; IHF contributes to repression of basal expression at this divergent ula promoter in JA134 derivatives, especially ulaA. The effect is regulatory context for UlaR-dependent promoter organization; no direct inhibition of catalytic protein is implied.; Evidence: PMID:14996803inhibits CHEBI:17634 — inhibits → Entrez:948705; Glucose strongly represses the ula promoter reporter under tested JA134 conditions. Added cAMP did not fully relieve repression, so a second mechanism was proposed; glucose binding to UlaR or a particular inducer-exclusion step was not demonstrated.; Evidence: PMID:14996803inhibits CHEBI:17634 — inhibits → Entrez:948717; Glucose strongly represses the ula promoter reporter under tested JA134 conditions. Added cAMP did not fully relieve repression, so a second mechanism was proposed; glucose binding to UlaR or a particular inducer-exclusion step was not demonstrated.; Evidence: PMID:14996803inhibits CHEBI:61698 — inhibits → UniProtKB:P0A9W0; The 2008 primary abstract identifies L-ascorbate 6-phosphate as direct UlaR effector, shifting the DNA-bound tetramer toward a DNA-free dimer and relieving repression. Fullbody/construct details were unavailable. Free L-ascorbate is not substituted for its 6-phosphate.; Evidence: PMID:18844374inhibits Entrez:948705 — enables → RHEA:28804; Expression of this ula gene supplies its encoded Ula protein. Gene deletion impairs L-ascorbate utilization; this edge connects the promoter regulation context to the corresponding pathway component.; Evidence: UniProtKB:P39300, PMID:12644495enables Entrez:948717 — enables → MetaCyc:RXN0-2461; Expression of this ula gene supplies its encoded Ula protein. Gene deletion impairs L-ascorbate utilization; this edge connects the promoter regulation context to the corresponding pathway component.; Evidence: UniProtKB:P39301, PMID:12644495enables RHEA:22369 — provides_input_for → MetaCyc:NONOXIPENT-PWY; The native pathway-link routes the D-xylulose5P product into the non-oxidative pentose phosphate pathway. This is an interface; downstream pentose-phosphate reactions are outside the selected five-event core.; Evidence: MetaCyc:PWY0-301provides input for 3-keto-L-gulonate-6-phosphate decarboxylase UlaD; UniProtKB:P39304; Declared type: protein protein 3-keto-L- gulonate-6-phosphate decarboxylase UlaD Ascorbate-specific PTS system EIIC component; UniProtKB:P39301; Declared type: protein protein Ascorbate-specific PTS system EIIC component HTH-type transcriptional regulator UlaR; UniProtKB:P0A9W0; Declared type: protein protein HTH-type transcriptional regulator UlaR Ascorbate-specific PTS system EIIA component; UniProtKB:P69820; Declared type: protein protein Ascorbate-specific PTS system EIIA component L-ribulose-5-phosphate 4-epimerase UlaF; UniProtKB:P39306; Declared type: protein protein L-ribulose-5-phosphate 4-epimerase UlaF Probable L-ascorbate-6-phosphate lactonase UlaG; UniProtKB:P39300; Declared type: protein protein Probable L-ascorbate-6-phosphate lactonase UlaG Ascorbate-specific PTS system EIIB component; UniProtKB:P69822; Declared type: protein protein Ascorbate-specific PTS system EIIB component L-ribulose-5-phosphate 3-epimerase UlaE; UniProtKB:P39305; Declared type: protein protein L-ribulose-5-phosphate 3-epimerase UlaE Phosphocarrier protein HPr; UniProtKB:P0AA04; Declared type: protein protein Phosphocarrier protein HPr Phosphoenolpyruvate-protein phosphotransferase; UniProtKB:P08839; Declared type: protein protein Phosphoenolpyruvate-protein phosphotransferase L-ascorbate; CHEBI:38290; Declared type: small_molecule small molecule L-ascorbate L-ascorbate 6-phosphate(3-); CHEBI:61698; Declared type: small_molecule small molecule L-ascorbate 6-phosphate(3-) 3-dehydro-L-gulonate 6-phosphate; CHEBI:58774; Declared type: small_molecule small molecule 3-dehydro-L-gulonate 6-phosphate L-xylulose 5-phosphate(2-); CHEBI:57829; Declared type: small_molecule small molecule L-xylulose 5-phosphate(2-) L-ribulose 5-phosphate(2-); CHEBI:58226; Declared type: small_molecule small molecule L-ribulose 5-phosphate(2-) D-xylulose 5-phosphate(2-); CHEBI:57737; Declared type: small_molecule small molecule D-xylulose 5-phosphate(2-) water; CHEBI:15377; Declared type: small_molecule small molecule water hydron; CHEBI:15378; Declared type: small_molecule small molecule hydron carbon dioxide; CHEBI:16526; Declared type: small_molecule small molecule carbon dioxide D-glucose; CHEBI:17634; Declared type: small_molecule small molecule D-glucose manganese(2+); CHEBI:29035; Declared type: cofactor cofactor manganese(2+) cobalt(2+); CHEBI:48828; Declared type: cofactor cofactor cobalt(2+) magnesium(2+); CHEBI:18420; Declared type: cofactor cofactor magnesium(2+) zinc(2+); CHEBI:29105; Declared type: cofactor cofactor zinc(2+) an [HPr]-L-histidine; MetaCyc:Hpr-Histidine; Declared type: chemical_entity chemical entity an [HPr]-L-histidine an [HPr protein]-Npi-phospho-L-histidine; MetaCyc:Hpr-pi-phospho-L-histidines; Declared type: chemical_entity chemical entity an [HPr protein]-Npi- phospho-L-histidine L-ascorbate-6-phosphate lactonase; MetaCyc:CPLX0-7848; Declared type: complex complex L-ascorbate-6-phosphate lactonase 3-keto-L-gulonate-6-phosphate decarboxylase UlaD; MetaCyc:CPLX0-7744; Declared type: complex complex 3-keto-L- gulonate-6-phosphate decarboxylase UlaD L-ascorbate specific PTS enzyme II; MetaCyc:EIISGA; Declared type: complex complex L-ascorbate specific PTS enzyme II cytoplasm; GO:0005737; Declared type: cellular_component cellular component cytoplasm plasma membrane; GO:0005886; Declared type: cellular_component cellular component plasma membrane ulaG; Entrez:948705; Declared type: gene gene ulaG ulaA; Entrez:948717; Declared type: gene gene ulaA CRP-cyclic-AMP DNA-binding transcriptional dual regulator; EcoCyc:CPLX0-226; Declared type: complex complex CRP-cyclic-AMP DNA-binding transcriptional dual regulator DNA-binding transcriptional dual regulator IHF; EcoCyc:PC00027; Declared type: complex complex DNA-binding transcriptional dual regulator IHF EC 2.7.1.194; MetaCyc:RXN0-2461; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity EC 2.7.1.194 L-ascorbate 6-phosphate + H2O => 3-dehydro-L-gulonate 6-phosphate; RHEA:28804; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity L-ascorbate 6-phosphate + H2O => 3-dehydro-L-gulonate 6-phosphate 3-dehydro-L-gulonate 6-phosphate + H(+) => L-xylulose 5-phosphate + CO2; RHEA:14354; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity 3-dehydro-L-gulonate 6-phosphate + H(+) => L-xylulose 5-phosphate + CO2 L-xylulose 5-phosphate => L-ribulose 5-phosphate; RHEA:18499; Declared type: molecular_activity; Source reaction direction: right_to_left molecular activity L-xylulose 5-phosphate => L-ribulose 5-phosphate L-ribulose 5-phosphate => D-xylulose 5-phosphate; RHEA:22369; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity L-ribulose 5-phosphate => D-xylulose 5-phosphate pentose phosphate pathway (non-oxidative branch); MetaCyc:NONOXIPENT-PWY; Declared type: pathway pathway pentose phosphate pathway (non-oxidative branch) L-ascorbate degradation I (bacterial, anaerobic); MetaCyc:PWY0-301; Declared type: pathway pathway L-ascorbate degradation I (bacterial, anaerobic) 3-keto-L-gulonate-6-phosphate decarboxylase UlaD; MetaCyc:CPLX0-7744; Declared type: complex; experimental construct: The 2002 supporting assay used MG1655-derived recombinant protein expressed in BL21(DE3) with an N-terminal His10 tag, then thrombin-cleaved. Residual cleavage sequence was not reported. Native assembly is supported separately by the database source.; Evidence PMID:11741871: The genes were amplified from MG1655, expressed using modified pET15b in BL21(DE3), and affinity tags were removed by thrombin for the UlaD/E/F assays. Remaining cleavage-derived residues were not specified. (Materials and Methods, protein production and purification; Table 2) experimental construct 3-keto-L- gulonate-6-phosphate decarboxylase UlaD [experimental construct: The 2002 supporting assay used MG1655-derived recombinant protein expressed in BL21(DE3) with an…] L-ribulose-5-phosphate 3-epimerase UlaE; UniProtKB:P39305; Declared type: protein; experimental construct: The 2002 supporting assay used MG1655-derived recombinant protein expressed in BL21(DE3) with an N-terminal His10 tag, then thrombin-cleaved. Residual cleavage sequence was not reported. Native assembly is supported separately by the database source.; Evidence PMID:11741871: The genes were amplified from MG1655, expressed using modified pET15b in BL21(DE3), and affinity tags were removed by thrombin for the UlaD/E/F assays. Remaining cleavage-derived residues were not specified. (Materials and Methods, protein production and purification; Table 2) experimental construct L-ribulose-5-phosphate 3-epimerase UlaE [experimental construct: The 2002 supporting assay used MG1655-derived recombinant protein expressed in BL21(DE3) with an…] L-ribulose-5-phosphate 4-epimerase UlaF; UniProtKB:P39306; Declared type: protein; experimental construct: The 2002 supporting assay used MG1655-derived recombinant protein expressed in BL21(DE3) with an N-terminal His10 tag, then thrombin-cleaved. Residual cleavage sequence was not reported. Native assembly is supported separately by the database source.; Evidence PMID:11741871: The genes were amplified from MG1655, expressed using modified pET15b in BL21(DE3), and affinity tags were removed by thrombin for the UlaD/E/F assays. Remaining cleavage-derived residues were not specified. (Materials and Methods, protein production and purification; Table 2) experimental construct L-ribulose-5-phosphate 4-epimerase UlaF [experimental construct: The 2002 supporting assay used MG1655-derived recombinant protein expressed in BL21(DE3) with an…] HTH-type transcriptional regulator UlaR; UniProtKB:P0A9W0; Declared type: protein; experimental construct: Supporting DNA-binding assays used NusA/His6-UlaR after thrombin tag removal. The separate promoter reporter experiments used JA134-derived cells; no engineered tag is attributed to their chromosomal UlaR.; Evidence PMID:14996803: Purified recombinant UlaR was produced from pET43c+ in BL21(DE3), its tag removed with thrombin, and tested by gel retardation. Promoter reporter strains derive from JA134. (Materials and Methods, overexpression and purification of UlaR; Table 1) experimental construct HTH-type transcriptional regulator UlaR [experimental construct: Supporting DNA- binding assays used NusA/His6-UlaR after thrombin tag removal. The separate promoter…] HTH-type transcriptional regulator UlaR; UniProtKB:P0A9W0; Declared type: protein; experimental construct: Supporting DNA-binding assays used NusA/His6-UlaR after thrombin tag removal. The separate promoter reporter experiments used JA134-derived cells; no engineered tag is attributed to their chromosomal UlaR.; Evidence PMID:14996803: Purified recombinant UlaR was produced from pET43c+ in BL21(DE3), its tag removed with thrombin, and tested by gel retardation. Promoter reporter strains derive from JA134. (Materials and Methods, overexpression and purification of UlaR; Table 1) experimental construct HTH-type transcriptional regulator UlaR [experimental construct: Supporting DNA- binding assays used NusA/His6-UlaR after thrombin tag removal. The separate promoter…]

Components and activities

Declared biological components and source reaction directions
NodeKind or roleSource direction
Escherichia coli K-12
NCBITaxon:83333		taxon
Escherichia coli str. K-12 substr. MG1655
NCBITaxon:511145		taxon
3-keto-L-gulonate-6-phosphate decarboxylase UlaD
UniProtKB:P39304		protein
Ascorbate-specific PTS system EIIC component
UniProtKB:P39301		protein
HTH-type transcriptional regulator UlaR
UniProtKB:P0A9W0		protein
Ascorbate-specific PTS system EIIA component
UniProtKB:P69820		protein
L-ribulose-5-phosphate 4-epimerase UlaF
UniProtKB:P39306		protein
Probable L-ascorbate-6-phosphate lactonase UlaG
UniProtKB:P39300		protein
Ascorbate-specific PTS system EIIB component
UniProtKB:P69822		protein
L-ribulose-5-phosphate 3-epimerase UlaE
UniProtKB:P39305		protein
Phosphocarrier protein HPr
UniProtKB:P0AA04		protein
Phosphoenolpyruvate-protein phosphotransferase
UniProtKB:P08839		protein
L-ascorbate
CHEBI:38290		small molecule
L-ascorbate 6-phosphate(3-)
CHEBI:61698		small molecule
3-dehydro-L-gulonate 6-phosphate
CHEBI:58774		small molecule
L-xylulose 5-phosphate(2-)
CHEBI:57829		small molecule
L-ribulose 5-phosphate(2-)
CHEBI:58226		small molecule
D-xylulose 5-phosphate(2-)
CHEBI:57737		small molecule
water
CHEBI:15377		small molecule
hydron
CHEBI:15378		small molecule
carbon dioxide
CHEBI:16526		small molecule
D-glucose
CHEBI:17634		small molecule
manganese(2+)
CHEBI:29035		cofactor
cobalt(2+)
CHEBI:48828		cofactor
magnesium(2+)
CHEBI:18420		cofactor
zinc(2+)
CHEBI:29105		cofactor
an [HPr]-L-histidine
MetaCyc:Hpr-Histidine		chemical entity
an [HPr protein]-Npi-phospho-L-histidine
MetaCyc:Hpr-pi-phospho-L-histidines		chemical entity
L-ascorbate-6-phosphate lactonase
MetaCyc:CPLX0-7848		complex
3-keto-L-gulonate-6-phosphate decarboxylase UlaD
MetaCyc:CPLX0-7744		complex
L-ascorbate specific PTS enzyme II
MetaCyc:EIISGA		complex
cytoplasm
GO:0005737		cellular component
plasma membrane
GO:0005886		cellular component
ulaG
Entrez:948705		gene
ulaA
Entrez:948717		gene
CRP-cyclic-AMP DNA-binding transcriptional dual regulator
EcoCyc:CPLX0-226		complex
DNA-binding transcriptional dual regulator IHF
EcoCyc:PC00027		complex
EC 2.7.1.194
MetaCyc:RXN0-2461		molecular activityleft to right
L-ascorbate 6-phosphate + H2O => 3-dehydro-L-gulonate 6-phosphate
RHEA:28804		molecular activityleft to right
3-dehydro-L-gulonate 6-phosphate + H(+) => L-xylulose 5-phosphate + CO2
RHEA:14354		molecular activityleft to right
L-xylulose 5-phosphate => L-ribulose 5-phosphate
RHEA:18499		molecular activityright to left
L-ribulose 5-phosphate => D-xylulose 5-phosphate
RHEA:22369		molecular activityleft to right
pentose phosphate pathway (non-oxidative branch)
MetaCyc:NONOXIPENT-PWY		pathway

Mechanistic edges

Mechanistic edges and their cited evidence
SubjectPredicate and descriptionObjectEvidence
EC 2.7.1.194
MetaCyc:RXN0-2461		part_of

The MetaCyc 27.0 PWY0-301 reaction-list contains RXN0-2461 as a member of this pathway.

MetaCyc:PWY0-301
  • MetaCyc:PWY0-301

    Source assertion: The MetaCyc 27.0 PWY0-301 reaction-list contains RXN0-2461 as a member of this pathway.

    Source locationXPath /ptools-xml/Pathway/reaction-list/Reaction[@frameid="RXN0-2461"]
L-ascorbate 6-phosphate + H2O => 3-dehydro-L-gulonate 6-phosphate
RHEA:28804		part_of

The MetaCyc 27.0 PWY0-301 reaction-list contains RXN0-5214 as a member of this pathway.

MetaCyc:PWY0-301
  • MetaCyc:PWY0-301

    Source assertion: The MetaCyc 27.0 PWY0-301 reaction-list contains RXN0-5214 as a member of this pathway.

    Source locationXPath /ptools-xml/Pathway/reaction-list/Reaction[@frameid="RXN0-5214"]
3-dehydro-L-gulonate 6-phosphate + H(+) => L-xylulose 5-phosphate + CO2
RHEA:14354		part_of

The MetaCyc 27.0 PWY0-301 reaction-list contains RXN0-705 as a member of this pathway.

MetaCyc:PWY0-301
  • MetaCyc:PWY0-301

    Source assertion: The MetaCyc 27.0 PWY0-301 reaction-list contains RXN0-705 as a member of this pathway.

    Source locationXPath /ptools-xml/Pathway/reaction-list/Reaction[@frameid="RXN0-705"]
L-xylulose 5-phosphate => L-ribulose 5-phosphate
RHEA:18499		part_of

The MetaCyc 27.0 PWY0-301 reaction-list contains LXULRU5P-RXN as a member of this pathway.

MetaCyc:PWY0-301
  • MetaCyc:PWY0-301

    Source assertion: The MetaCyc 27.0 PWY0-301 reaction-list contains LXULRU5P-RXN as a member of this pathway.

    Source locationXPath /ptools-xml/Pathway/reaction-list/Reaction[@frameid="LXULRU5P-RXN"]
L-ribulose 5-phosphate => D-xylulose 5-phosphate
RHEA:22369		part_of

The MetaCyc 27.0 PWY0-301 reaction-list contains RIBULPEPIM-RXN as a member of this pathway.

MetaCyc:PWY0-301
  • MetaCyc:PWY0-301

    Source assertion: The MetaCyc 27.0 PWY0-301 reaction-list contains RIBULPEPIM-RXN as a member of this pathway.

    Source locationXPath /ptools-xml/Pathway/reaction-list/Reaction[@frameid="RIBULPEPIM-RXN"]
EC 2.7.1.194
MetaCyc:RXN0-2461		precedes

The selected native pathway orders RXN0-2461 before RXN0-5214; both are members of its five-event route.

L-ascorbate 6-phosphate + H2O => 3-dehydro-L-gulonate 6-phosphate
RHEA:28804
  • MetaCyc:PWY0-301

    Source assertion: The selected native pathway orders RXN0-2461 before RXN0-5214; both are members of its five-event route.

    Source locationXPath /ptools-xml/Pathway/reaction-ordering containing RXN0-2461 and RXN0-5214
L-ascorbate 6-phosphate + H2O => 3-dehydro-L-gulonate 6-phosphate
RHEA:28804		precedes

The selected native pathway orders RXN0-5214 before RXN0-705; both are members of its five-event route.

3-dehydro-L-gulonate 6-phosphate + H(+) => L-xylulose 5-phosphate + CO2
RHEA:14354
  • MetaCyc:PWY0-301

    Source assertion: The selected native pathway orders RXN0-5214 before RXN0-705; both are members of its five-event route.

    Source locationXPath /ptools-xml/Pathway/reaction-ordering containing RXN0-5214 and RXN0-705
3-dehydro-L-gulonate 6-phosphate + H(+) => L-xylulose 5-phosphate + CO2
RHEA:14354		precedes

The selected native pathway orders RXN0-705 before LXULRU5P-RXN; both are members of its five-event route.

L-xylulose 5-phosphate => L-ribulose 5-phosphate
RHEA:18499
  • MetaCyc:PWY0-301

    Source assertion: The selected native pathway orders RXN0-705 before LXULRU5P-RXN; both are members of its five-event route.

    Source locationXPath /ptools-xml/Pathway/reaction-ordering containing RXN0-705 and LXULRU5P-RXN
L-xylulose 5-phosphate => L-ribulose 5-phosphate
RHEA:18499		precedes

The selected native pathway orders LXULRU5P-RXN before RIBULPEPIM-RXN; both are members of its five-event route.

L-ribulose 5-phosphate => D-xylulose 5-phosphate
RHEA:22369
  • MetaCyc:PWY0-301

    Source assertion: The selected native pathway orders LXULRU5P-RXN before RIBULPEPIM-RXN; both are members of its five-event route.

    Source locationXPath /ptools-xml/Pathway/reaction-ordering containing LXULRU5P-RXN and RIBULPEPIM-RXN
an [HPr protein]-Npi-phospho-L-histidine
MetaCyc:Hpr-pi-phospho-L-histidines		consumes

Native RXN0-2461 left contains Hpr-pi-phospho-L-histidines. Ascorbate enters from outside and phosphorylated product is inside. HPr-linked residue classes represent the aggregate relay, not free amino acids or a direct HPr-to-sugar transfer.

EC 2.7.1.194
MetaCyc:RXN0-2461
  • MetaCyc:RXN0-2461

    Source assertion: Native RXN0-2461 left contains Hpr-pi-phospho-L-histidines. Ascorbate enters from outside and phosphorylated product is inside. HPr-linked residue classes represent the aggregate relay, not free amino acids or a direct HPr-to-sugar transfer.

    Source locationXPath /ptools-xml/Reaction/left/Compound[@frameid="Hpr-pi-phospho-L-histidines"]; compartment
L-ascorbate
CHEBI:38290		consumes

Native RXN0-2461 left contains ASCORBATE. Ascorbate enters from outside and phosphorylated product is inside. HPr-linked residue classes represent the aggregate relay, not free amino acids or a direct HPr-to-sugar transfer.

EC 2.7.1.194
MetaCyc:RXN0-2461
  • MetaCyc:RXN0-2461

    Source assertion: Native RXN0-2461 left contains ASCORBATE. Ascorbate enters from outside and phosphorylated product is inside. HPr-linked residue classes represent the aggregate relay, not free amino acids or a direct HPr-to-sugar transfer.

    Source locationXPath /ptools-xml/Reaction/left/Compound[@frameid="ASCORBATE"]; compartment
EC 2.7.1.194
MetaCyc:RXN0-2461		produces

Native RXN0-2461 right contains L-ASCORBATE-6-PHOSPHATE. Ascorbate enters from outside and phosphorylated product is inside. HPr-linked residue classes represent the aggregate relay, not free amino acids or a direct HPr-to-sugar transfer.

L-ascorbate 6-phosphate(3-)
CHEBI:61698
  • MetaCyc:RXN0-2461

    Source assertion: Native RXN0-2461 right contains L-ASCORBATE-6-PHOSPHATE. Ascorbate enters from outside and phosphorylated product is inside. HPr-linked residue classes represent the aggregate relay, not free amino acids or a direct HPr-to-sugar transfer.

    Source locationXPath /ptools-xml/Reaction/right/Compound[@frameid="L-ASCORBATE-6-PHOSPHATE"]; compartment
EC 2.7.1.194
MetaCyc:RXN0-2461		produces

Native RXN0-2461 right contains Hpr-Histidine. Ascorbate enters from outside and phosphorylated product is inside. HPr-linked residue classes represent the aggregate relay, not free amino acids or a direct HPr-to-sugar transfer.

an [HPr]-L-histidine
MetaCyc:Hpr-Histidine
  • MetaCyc:RXN0-2461

    Source assertion: Native RXN0-2461 right contains Hpr-Histidine. Ascorbate enters from outside and phosphorylated product is inside. HPr-linked residue classes represent the aggregate relay, not free amino acids or a direct HPr-to-sugar transfer.

    Source locationXPath /ptools-xml/Reaction/right/Compound[@frameid="Hpr-Histidine"]; compartment
L-ascorbate 6-phosphate(3-)
CHEBI:61698		consumes

The formal directional RHEA:28804 substrates side contains CHEBI:61698, coefficient 1.

L-ascorbate 6-phosphate + H2O => 3-dehydro-L-gulonate 6-phosphate
RHEA:28804
  • RHEA:28804

    Source assertion: The formal directional RHEA:28804 substrates side contains CHEBI:61698, coefficient 1.

    Source locationRDF subject http://rdf.rhea-db.org/28804; substrates/contains/compound/chebi closure
water
CHEBI:15377		consumes

The formal directional RHEA:28804 substrates side contains CHEBI:15377, coefficient 1.

L-ascorbate 6-phosphate + H2O => 3-dehydro-L-gulonate 6-phosphate
RHEA:28804
  • RHEA:28804

    Source assertion: The formal directional RHEA:28804 substrates side contains CHEBI:15377, coefficient 1.

    Source locationRDF subject http://rdf.rhea-db.org/28804; substrates/contains/compound/chebi closure
L-ascorbate 6-phosphate + H2O => 3-dehydro-L-gulonate 6-phosphate
RHEA:28804		produces

The formal directional RHEA:28804 products side contains CHEBI:58774, coefficient 1.

3-dehydro-L-gulonate 6-phosphate
CHEBI:58774
  • RHEA:28804

    Source assertion: The formal directional RHEA:28804 products side contains CHEBI:58774, coefficient 1.

    Source locationRDF subject http://rdf.rhea-db.org/28804; products/contains/compound/chebi closure
3-dehydro-L-gulonate 6-phosphate
CHEBI:58774		consumes

The formal directional RHEA:14354 substrates side contains CHEBI:58774, coefficient 1.

3-dehydro-L-gulonate 6-phosphate + H(+) => L-xylulose 5-phosphate + CO2
RHEA:14354
  • RHEA:14354

    Source assertion: The formal directional RHEA:14354 substrates side contains CHEBI:58774, coefficient 1.

    Source locationRDF subject http://rdf.rhea-db.org/14354; substrates/contains/compound/chebi closure
hydron
CHEBI:15378		consumes

The formal directional RHEA:14354 substrates side contains CHEBI:15378, coefficient 1.

3-dehydro-L-gulonate 6-phosphate + H(+) => L-xylulose 5-phosphate + CO2
RHEA:14354
  • RHEA:14354

    Source assertion: The formal directional RHEA:14354 substrates side contains CHEBI:15378, coefficient 1.

    Source locationRDF subject http://rdf.rhea-db.org/14354; substrates/contains/compound/chebi closure
3-dehydro-L-gulonate 6-phosphate + H(+) => L-xylulose 5-phosphate + CO2
RHEA:14354		produces

The formal directional RHEA:14354 products side contains CHEBI:57829, coefficient 1.

L-xylulose 5-phosphate(2-)
CHEBI:57829
  • RHEA:14354

    Source assertion: The formal directional RHEA:14354 products side contains CHEBI:57829, coefficient 1.

    Source locationRDF subject http://rdf.rhea-db.org/14354; products/contains/compound/chebi closure
3-dehydro-L-gulonate 6-phosphate + H(+) => L-xylulose 5-phosphate + CO2
RHEA:14354		produces

The formal directional RHEA:14354 products side contains CHEBI:16526, coefficient 1.

carbon dioxide
CHEBI:16526
  • RHEA:14354

    Source assertion: The formal directional RHEA:14354 products side contains CHEBI:16526, coefficient 1.

    Source locationRDF subject http://rdf.rhea-db.org/14354; products/contains/compound/chebi closure
L-xylulose 5-phosphate(2-)
CHEBI:57829		consumes

The formal directional RHEA:18499 substrates side contains CHEBI:57829, coefficient 1. This is the right-to-left direction of the L-ribulose/L-xylulose 5-phosphate equation.

L-xylulose 5-phosphate => L-ribulose 5-phosphate
RHEA:18499
  • RHEA:18499

    Source assertion: The formal directional RHEA:18499 substrates side contains CHEBI:57829, coefficient 1. This is the right-to-left direction of the L-ribulose/L-xylulose 5-phosphate equation.

    Source locationRDF subject http://rdf.rhea-db.org/18499; substrates/contains/compound/chebi closure
L-xylulose 5-phosphate => L-ribulose 5-phosphate
RHEA:18499		produces

The formal directional RHEA:18499 products side contains CHEBI:58226, coefficient 1. This is the right-to-left direction of the L-ribulose/L-xylulose 5-phosphate equation.

L-ribulose 5-phosphate(2-)
CHEBI:58226
  • RHEA:18499

    Source assertion: The formal directional RHEA:18499 products side contains CHEBI:58226, coefficient 1. This is the right-to-left direction of the L-ribulose/L-xylulose 5-phosphate equation.

    Source locationRDF subject http://rdf.rhea-db.org/18499; products/contains/compound/chebi closure
L-ribulose 5-phosphate(2-)
CHEBI:58226		consumes

The formal directional RHEA:22369 substrates side contains CHEBI:58226, coefficient 1. This is the left-to-right direction from L-ribulose to D-xylulose 5-phosphate.

L-ribulose 5-phosphate => D-xylulose 5-phosphate
RHEA:22369
  • RHEA:22369

    Source assertion: The formal directional RHEA:22369 substrates side contains CHEBI:58226, coefficient 1. This is the left-to-right direction from L-ribulose to D-xylulose 5-phosphate.

    Source locationRDF subject http://rdf.rhea-db.org/22369; substrates/contains/compound/chebi closure
L-ribulose 5-phosphate => D-xylulose 5-phosphate
RHEA:22369		produces

The formal directional RHEA:22369 products side contains CHEBI:57737, coefficient 1. This is the left-to-right direction from L-ribulose to D-xylulose 5-phosphate.

D-xylulose 5-phosphate(2-)
CHEBI:57737
  • RHEA:22369

    Source assertion: The formal directional RHEA:22369 products side contains CHEBI:57737, coefficient 1. This is the left-to-right direction from L-ribulose to D-xylulose 5-phosphate.

    Source locationRDF subject http://rdf.rhea-db.org/22369; products/contains/compound/chebi closure
L-ascorbate specific PTS enzyme II
MetaCyc:EIISGA		catalyzes

Native MetaCyc:RXN0-2461 enzymatic-reaction ENZRXN0-3481 assigns this activity to EIISGA, the L-ascorbate-specific UlaABC PTS.

EC 2.7.1.194
MetaCyc:RXN0-2461
  • MetaCyc:RXN0-2461

    Source assertion: Native MetaCyc:RXN0-2461 enzymatic-reaction ENZRXN0-3481 assigns this activity to EIISGA, the L-ascorbate-specific UlaABC PTS.

    Source locationXPath /ptools-xml/Reaction/enzymatic-reaction/Enzymatic-Reaction[@frameid="ENZRXN0-3481"]/enzyme
  • PMID:12644495

    Source assertion: In-frame deletion and complementation tests establish that UlaA, UlaB and UlaC are all required for uptake and PEP-dependent phosphorylation in BW25113. Crude extracts contain soluble PTS components.

    Source locationResults; Figures 2–4; Materials and Methods, PEP-dependent phosphorylation assay
L-ascorbate-6-phosphate lactonase
MetaCyc:CPLX0-7848		catalyzes

Native MetaCyc:RXN0-5214 enzymatic-reaction ENZRXN0-6334 assigns this activity to CPLX0-7848, the UlaG lactonase complex.

L-ascorbate 6-phosphate + H2O => 3-dehydro-L-gulonate 6-phosphate
RHEA:28804
  • MetaCyc:RXN0-5214

    Source assertion: Native MetaCyc:RXN0-5214 enzymatic-reaction ENZRXN0-6334 assigns this activity to CPLX0-7848, the UlaG lactonase complex.

    Source locationXPath /ptools-xml/Reaction/enzymatic-reaction/Enzymatic-Reaction[@frameid="ENZRXN0-6334"]/enzyme
  • PMID:20359483

    Source assertion: The primary abstract reports L-ascorbate 6-phosphate lactonase activity for Mn2+- or Co2+-loaded UlaG. Full methods and figures were unavailable; exact construct details are not inferred.

    Source locationEuropePMC result PMID20359483/abstractText
3-keto-L-gulonate-6-phosphate decarboxylase UlaD
MetaCyc:CPLX0-7744

experimental construct: The 2002 supporting assay used MG1655-derived recombinant protein expressed in BL21(DE3) with an N-terminal His10 tag, then thrombin-cleaved. Residual cleavage sequence was not reported. Native assembly is supported separately by the database source.

Qualification evidence
  • PMID:11741871

    Source assertion: The genes were amplified from MG1655, expressed using modified pET15b in BL21(DE3), and affinity tags were removed by thrombin for the UlaD/E/F assays. Remaining cleavage-derived residues were not specified.

    Source locationMaterials and Methods, protein production and purification; Table 2
catalyzes

Native MetaCyc:RXN0-705 enzymatic-reaction ENZRXN0-725 assigns this activity to CPLX0-7744, the UlaD decarboxylase complex. The pathway excludes the SgbH alternative.

3-dehydro-L-gulonate 6-phosphate + H(+) => L-xylulose 5-phosphate + CO2
RHEA:14354
  • MetaCyc:RXN0-705

    Source assertion: Native MetaCyc:RXN0-705 enzymatic-reaction ENZRXN0-725 assigns this activity to CPLX0-7744, the UlaD decarboxylase complex.

    Source locationXPath /ptools-xml/Reaction/enzymatic-reaction/Enzymatic-Reaction[@frameid="ENZRXN0-725"]/enzyme
  • PMID:11741871

    Source assertion: Purified, tag-cleaved SgaH (UlaD) catalyzed decarboxylation of 3-keto-L-gulonate 6-phosphate to L-xylulose 5-phosphate. MG1655-derived genes were expressed in BL21(DE3), with His10 tags removed before assay.

    Source locationProtein purification; Identification of biochemical functions; Table 2; Figure 3
  • MetaCyc:PWY0-301

    Source assertion: PWY0-301 excludes EG12285-MONOMER (SgbH), the alternative catalyst present in the general RXN0-705 reaction. The pathway therefore uses UlaD here.

    Source locationXPath /ptools-xml/Pathway/enzymes-not-used/Protein[@frameid="EG12285-MONOMER"]
L-ribulose-5-phosphate 3-epimerase UlaE
UniProtKB:P39305

experimental construct: The 2002 supporting assay used MG1655-derived recombinant protein expressed in BL21(DE3) with an N-terminal His10 tag, then thrombin-cleaved. Residual cleavage sequence was not reported. Native assembly is supported separately by the database source.

Qualification evidence
  • PMID:11741871

    Source assertion: The genes were amplified from MG1655, expressed using modified pET15b in BL21(DE3), and affinity tags were removed by thrombin for the UlaD/E/F assays. Remaining cleavage-derived residues were not specified.

    Source locationMaterials and Methods, protein production and purification; Table 2
catalyzes

Native MetaCyc:LXULRU5P-RXN enzymatic-reaction ENZRXN0-726 assigns this activity to G7859-MONOMER, UlaE.

L-xylulose 5-phosphate => L-ribulose 5-phosphate
RHEA:18499
  • MetaCyc:LXULRU5P-RXN

    Source assertion: Native MetaCyc:LXULRU5P-RXN enzymatic-reaction ENZRXN0-726 assigns this activity to G7859-MONOMER, UlaE.

    Source locationXPath /ptools-xml/Reaction/enzymatic-reaction/Enzymatic-Reaction[@frameid="ENZRXN0-726"]/enzyme
  • PMID:11741871

    Source assertion: Purified, tag-cleaved SgaU (UlaE) catalyzed conversion of L-xylulose 5-phosphate to L-ribulose 5-phosphate. MG1655-derived genes were expressed in BL21(DE3), with His10 tags removed before assay.

    Source locationProtein purification; Identification of biochemical functions; Table 2; Figure 3
  • MetaCyc:G7859-MONOMER

    Source assertion: Native G7859-MONOMER identifies UlaE and directly cross-references UniProt P39305; this supplies the protein identity join used for the catalytic edge.

    Source locationXPath /ptools-xml/Protein/common-name and dblink[dblink-db="UNIPROT"]/dblink-oid
L-ribulose-5-phosphate 4-epimerase UlaF
UniProtKB:P39306

experimental construct: The 2002 supporting assay used MG1655-derived recombinant protein expressed in BL21(DE3) with an N-terminal His10 tag, then thrombin-cleaved. Residual cleavage sequence was not reported. Native assembly is supported separately by the database source.

Qualification evidence
  • PMID:11741871

    Source assertion: The genes were amplified from MG1655, expressed using modified pET15b in BL21(DE3), and affinity tags were removed by thrombin for the UlaD/E/F assays. Remaining cleavage-derived residues were not specified.

    Source locationMaterials and Methods, protein production and purification; Table 2
catalyzes

Native MetaCyc:RIBULPEPIM-RXN enzymatic-reaction ENZRXN0-722 assigns this activity to G7860-MONOMER, UlaF. The pathway excludes AraD and SgbE alternatives.

L-ribulose 5-phosphate => D-xylulose 5-phosphate
RHEA:22369
  • MetaCyc:RIBULPEPIM-RXN

    Source assertion: Native MetaCyc:RIBULPEPIM-RXN enzymatic-reaction ENZRXN0-722 assigns this activity to G7860-MONOMER, UlaF.

    Source locationXPath /ptools-xml/Reaction/enzymatic-reaction/Enzymatic-Reaction[@frameid="ENZRXN0-722"]/enzyme
  • PMID:11741871

    Source assertion: Purified, tag-cleaved SgaE (UlaF) catalyzed conversion of L-ribulose 5-phosphate to D-xylulose 5-phosphate. MG1655-derived genes were expressed in BL21(DE3), with His10 tags removed before assay.

    Source locationProtein purification; Identification of biochemical functions; Table 2; Figure 3
  • MetaCyc:PWY0-301

    Source assertion: PWY0-301 excludes RIBULPEPIM-CPLX (AraD) and EG12287-MONOMER (SgbE), alternatives present in the general RIBULPEPIM-RXN reaction. This route uses UlaF.

    Source locationXPath /ptools-xml/Pathway/enzymes-not-used/Protein[@frameid="RIBULPEPIM-CPLX" or @frameid="EG12287-MONOMER"]
  • MetaCyc:G7860-MONOMER

    Source assertion: Native G7860-MONOMER identifies UlaF and directly cross-references UniProt P39306; this supplies the protein identity join used for the catalytic edge.

    Source locationXPath /ptools-xml/Protein/common-name and dblink[dblink-db="UNIPROT"]/dblink-oid
Probable L-ascorbate-6-phosphate lactonase UlaG
UniProtKB:P39300		part_of

Native MetaCyc:CPLX0-7848 contains 6 copies of G7855-MONOMER, resolved to UniProtKB:P39300. This defines the UlaG hexamer.

L-ascorbate-6-phosphate lactonase
MetaCyc:CPLX0-7848
  • MetaCyc:CPLX0-7848

    Source assertion: Native MetaCyc:CPLX0-7848 contains 6 copies of G7855-MONOMER, resolved to UniProtKB:P39300. This defines the UlaG hexamer.

    Source locationXPath /ptools-xml/Protein/component/Protein[@frameid="G7855-MONOMER"]; sibling coefficient
  • UniProtKB:P39300

    Source assertion: Exact reviewed entry UniProtKB:P39300 identifies the corresponding Ula gene product.

    Source locationJSON results[primaryAccession]; genes; BioCyc cross-reference
3-keto-L-gulonate-6-phosphate decarboxylase UlaD
UniProtKB:P39304		part_of

Native MetaCyc:CPLX0-7744 contains 2 copies of G7858-MONOMER, resolved to UniProtKB:P39304. This defines the UlaD homodimer.

3-keto-L-gulonate-6-phosphate decarboxylase UlaD
MetaCyc:CPLX0-7744
  • MetaCyc:CPLX0-7744

    Source assertion: Native MetaCyc:CPLX0-7744 contains 2 copies of G7858-MONOMER, resolved to UniProtKB:P39304. This defines the UlaD homodimer.

    Source locationXPath /ptools-xml/Protein/component/Protein[@frameid="G7858-MONOMER"]; sibling coefficient
  • UniProtKB:P39304

    Source assertion: Exact reviewed entry UniProtKB:P39304 identifies the corresponding Ula gene product.

    Source locationJSON results[primaryAccession]; genes; BioCyc cross-reference
Ascorbate-specific PTS system EIIC component
UniProtKB:P39301		part_of

Native MetaCyc:EIISGA contains 2 copies of SGAT-MONOMER, resolved to UniProtKB:P39301. The complete native EIISGA composition is two UlaA, one UlaB and one UlaC subunit.

L-ascorbate specific PTS enzyme II
MetaCyc:EIISGA
  • MetaCyc:EIISGA

    Source assertion: Native MetaCyc:EIISGA contains 2 copies of SGAT-MONOMER, resolved to UniProtKB:P39301. The complete native EIISGA composition is two UlaA, one UlaB and one UlaC subunit.

    Source locationXPath /ptools-xml/Protein/component/Protein[@frameid="SGAT-MONOMER"]; sibling coefficient
  • UniProtKB:P39301

    Source assertion: Exact reviewed entry UniProtKB:P39301 identifies the corresponding Ula gene product.

    Source locationJSON results[primaryAccession]; genes; BioCyc cross-reference
Ascorbate-specific PTS system EIIB component
UniProtKB:P69822		part_of

Native MetaCyc:EIISGA contains 1 copy of YJFT-MONOMER, resolved to UniProtKB:P69822. The complete native EIISGA composition is two UlaA, one UlaB and one UlaC subunit.

L-ascorbate specific PTS enzyme II
MetaCyc:EIISGA
  • MetaCyc:EIISGA

    Source assertion: Native MetaCyc:EIISGA contains 1 copy of YJFT-MONOMER, resolved to UniProtKB:P69822. The complete native EIISGA composition is two UlaA, one UlaB and one UlaC subunit.

    Source locationXPath /ptools-xml/Protein/component/Protein[@frameid="YJFT-MONOMER"]; sibling coefficient
  • UniProtKB:P69822

    Source assertion: Exact reviewed entry UniProtKB:P69822 identifies the corresponding Ula gene product.

    Source locationJSON results[primaryAccession]; genes; BioCyc cross-reference
Ascorbate-specific PTS system EIIA component
UniProtKB:P69820		part_of

Native MetaCyc:EIISGA contains 1 copy of YJFU-MONOMER, resolved to UniProtKB:P69820. The complete native EIISGA composition is two UlaA, one UlaB and one UlaC subunit.

L-ascorbate specific PTS enzyme II
MetaCyc:EIISGA
  • MetaCyc:EIISGA

    Source assertion: Native MetaCyc:EIISGA contains 1 copy of YJFU-MONOMER, resolved to UniProtKB:P69820. The complete native EIISGA composition is two UlaA, one UlaB and one UlaC subunit.

    Source locationXPath /ptools-xml/Protein/component/Protein[@frameid="YJFU-MONOMER"]; sibling coefficient
  • UniProtKB:P69820

    Source assertion: Exact reviewed entry UniProtKB:P69820 identifies the corresponding Ula gene product.

    Source locationJSON results[primaryAccession]; genes; BioCyc cross-reference
L-ascorbate-6-phosphate lactonase
MetaCyc:CPLX0-7848		has_cofactor

The 2010 primary abstract reports that Mn2+- or Co2+-loaded UlaG hydrolyses L-ascorbate 6-phosphate. These are alternative active metal-loaded states, not a requirement that both metals bind simultaneously. Full methods/figures remain unavailable.

manganese(2+)
CHEBI:29035
  • PMID:20359483

    Source assertion: The 2010 primary abstract reports that Mn2+- or Co2+-loaded UlaG hydrolyses L-ascorbate 6-phosphate. These are alternative active metal-loaded states, not a requirement that both metals bind simultaneously. Full methods/figures remain unavailable.

    Source locationEuropePMC result PMID20359483/abstractText
L-ascorbate-6-phosphate lactonase
MetaCyc:CPLX0-7848		has_cofactor

The 2010 primary abstract reports that Mn2+- or Co2+-loaded UlaG hydrolyses L-ascorbate 6-phosphate. These are alternative active metal-loaded states, not a requirement that both metals bind simultaneously. Full methods/figures remain unavailable.

cobalt(2+)
CHEBI:48828
  • PMID:20359483

    Source assertion: The 2010 primary abstract reports that Mn2+- or Co2+-loaded UlaG hydrolyses L-ascorbate 6-phosphate. These are alternative active metal-loaded states, not a requirement that both metals bind simultaneously. Full methods/figures remain unavailable.

    Source locationEuropePMC result PMID20359483/abstractText
3-keto-L-gulonate-6-phosphate decarboxylase UlaD
MetaCyc:CPLX0-7744		has_cofactor

Reviewed UlaD binds one Mg2+ per subunit; native structural commentary describes the Mg-stabilized enediolate. This assignment is not inferred merely from Mg present in a coupled assay.

magnesium(2+)
CHEBI:18420
  • UniProtKB:P39304

    Source assertion: Reviewed UlaD binds one Mg2+ per subunit; native structural commentary describes the Mg-stabilized enediolate. This assignment is not inferred merely from Mg present in a coupled assay.

    Source locationJSON results[primaryAccession=P39304].comments[COFACTOR]
  • MetaCyc:CPLX0-7744

    Source assertion: Reviewed UlaD binds one Mg2+ per subunit; native structural commentary describes the Mg-stabilized enediolate. This assignment is not inferred merely from Mg present in a coupled assay.

    Source locationXPath /ptools-xml/Protein/comment
L-ribulose-5-phosphate 4-epimerase UlaF
UniProtKB:P39306		has_cofactor

UniProt annotates one Zn2+ per UlaF subunit by similarity to AraD and HAMAP, not a direct UlaF metal experiment. The 2002 Mg-containing coupled assay does not independently establish the physiological UlaF metal.

zinc(2+)
CHEBI:29105
  • UniProtKB:P39306

    Source assertion: UniProt annotates one Zn2+ per UlaF subunit by similarity to AraD and HAMAP, not a direct UlaF metal experiment. The 2002 Mg-containing coupled assay does not independently establish the physiological UlaF metal.

    Source locationJSON results[primaryAccession=P39306].comments[COFACTOR]; ECO:0000250 and ECO:0000255
Phosphocarrier protein HPr
UniProtKB:P0AA04		enables

Native EIISGA requires HPr and enzyme I. The primary comparison used JM101 and its PB11 derivative carrying the combined ptsHIcrr deletion; PB11 lacked uptake and growth. This is not a BW25113 comparison or a test of individual ptsH or ptsI knockouts, and does not establish direct HPr-to-sugar transfer.

EC 2.7.1.194
MetaCyc:RXN0-2461
  • MetaCyc:EIISGA

    Source assertion: Native EIISGA describes dependence on the general PTS proteins HPr (PtsH) and enzyme I (PtsI), with phosphoryl transfer relayed through the UlaABC system.

    Source locationXPath /ptools-xml/Protein/comment; general PTS requirement and relay
  • PMID:12644495

    Source assertion: The general PTS experiment compared JM101 with PB11, its combined ptsHIcrr-deletion derivative. PB11 lacked ascorbate uptake and growth; added cAMP did not rescue. These data do not isolate individual ptsH or ptsI knockout effects.

    Source locationMaterials and Methods, Bacterial strains; Table 1; Results, Enzyme I and HPr are required for L-ascorbate transport
Phosphoenolpyruvate-protein phosphotransferase
UniProtKB:P08839		enables

Native EIISGA requires HPr and enzyme I. The primary comparison used JM101 and its PB11 derivative carrying the combined ptsHIcrr deletion; PB11 lacked uptake and growth. This is not a BW25113 comparison or a test of individual ptsH or ptsI knockouts, and does not establish direct HPr-to-sugar transfer.

EC 2.7.1.194
MetaCyc:RXN0-2461
  • MetaCyc:EIISGA

    Source assertion: Native EIISGA describes dependence on the general PTS proteins HPr (PtsH) and enzyme I (PtsI), with phosphoryl transfer relayed through the UlaABC system.

    Source locationXPath /ptools-xml/Protein/comment; general PTS requirement and relay
  • PMID:12644495

    Source assertion: The general PTS experiment compared JM101 with PB11, its combined ptsHIcrr-deletion derivative. PB11 lacked ascorbate uptake and growth; added cAMP did not rescue. These data do not isolate individual ptsH or ptsI knockout effects.

    Source locationMaterials and Methods, Bacterial strains; Table 1; Results, Enzyme I and HPr are required for L-ascorbate transport
Ascorbate-specific PTS system EIIC component
UniProtKB:P39301		located_in

Reviewed UlaA is an integral multi-pass cell inner membrane protein.

plasma membrane
GO:0005886
  • UniProtKB:P39301

    Source assertion: Reviewed UlaA is an integral multi-pass cell inner membrane protein.

    Source locationJSON results[primaryAccession=P39301].comments[SUBCELLULAR LOCATION]
Ascorbate-specific PTS system EIIB component
UniProtKB:P69822		located_in

Reviewed UlaB is cytoplasmic; annotation is inferred, not direct imaging.

cytoplasm
GO:0005737
  • UniProtKB:P69822

    Source assertion: Reviewed UlaB is cytoplasmic; annotation is inferred, not direct imaging.

    Source locationJSON results[primaryAccession=P69822].comments[SUBCELLULAR LOCATION]
Ascorbate-specific PTS system EIIA component
UniProtKB:P69820		located_in

Reviewed UlaC is cytoplasmic; annotation is inferred, not direct imaging.

cytoplasm
GO:0005737
  • UniProtKB:P69820

    Source assertion: Reviewed UlaC is cytoplasmic; annotation is inferred, not direct imaging.

    Source locationJSON results[primaryAccession=P69820].comments[SUBCELLULAR LOCATION]
Probable L-ascorbate-6-phosphate lactonase UlaG
UniProtKB:P39300		located_in

Reviewed UlaG cytoplasmic location is inferred; the 2003 lack of an N-terminal export signal is supporting context.

cytoplasm
GO:0005737
  • UniProtKB:P39300

    Source assertion: Reviewed UlaG cytoplasmic location is inferred; the 2003 lack of an N-terminal export signal is supporting context.

    Source locationJSON results[primaryAccession=P39300].comments[SUBCELLULAR LOCATION]
HTH-type transcriptional regulator UlaR
UniProtKB:P0A9W0

experimental construct: Supporting DNA-binding assays used NusA/His6-UlaR after thrombin tag removal. The separate promoter reporter experiments used JA134-derived cells; no engineered tag is attributed to their chromosomal UlaR.

Qualification evidence
  • PMID:14996803

    Source assertion: Purified recombinant UlaR was produced from pET43c+ in BL21(DE3), its tag removed with thrombin, and tested by gel retardation. Promoter reporter strains derive from JA134.

    Source locationMaterials and Methods, overexpression and purification of UlaR; Table 1
inhibits

UlaR represses this promoter-bearing gene. The ulaA promoter controls the six-gene ulaABCDEF operon. Reporter and binding experiments used JA134 derivatives and tag-cleaved recombinant UlaR; DNA-looping was proposed rather than directly visualized.

ulaG
Entrez:948705
  • PMID:14996803

    Source assertion: UlaR represses this promoter-bearing gene. The ulaA promoter controls the six-gene ulaABCDEF operon. Reporter and binding experiments used JA134 derivatives and tag-cleaved recombinant UlaR; DNA-looping was proposed rather than directly visualized.

    Source locationTable 2; Figures 3–5 and7; regulation by UlaR
HTH-type transcriptional regulator UlaR
UniProtKB:P0A9W0

experimental construct: Supporting DNA-binding assays used NusA/His6-UlaR after thrombin tag removal. The separate promoter reporter experiments used JA134-derived cells; no engineered tag is attributed to their chromosomal UlaR.

Qualification evidence
  • PMID:14996803

    Source assertion: Purified recombinant UlaR was produced from pET43c+ in BL21(DE3), its tag removed with thrombin, and tested by gel retardation. Promoter reporter strains derive from JA134.

    Source locationMaterials and Methods, overexpression and purification of UlaR; Table 1
inhibits

UlaR represses this promoter-bearing gene. The ulaA promoter controls the six-gene ulaABCDEF operon. Reporter and binding experiments used JA134 derivatives and tag-cleaved recombinant UlaR; DNA-looping was proposed rather than directly visualized.

ulaA
Entrez:948717
  • PMID:14996803

    Source assertion: UlaR represses this promoter-bearing gene. The ulaA promoter controls the six-gene ulaABCDEF operon. Reporter and binding experiments used JA134 derivatives and tag-cleaved recombinant UlaR; DNA-looping was proposed rather than directly visualized.

    Source locationTable 2; Figures 3–5 and7; regulation by UlaR
CRP-cyclic-AMP DNA-binding transcriptional dual regulator
EcoCyc:CPLX0-226		activates

cAMP-CRP directly binds and activates the ulaA promoter controlling ulaABCDEF. ulaG expression was not CRP-dependent in the same reporter conditions; no CRP→ulaG activation is asserted.

ulaA
Entrez:948717
  • PMID:14996803

    Source assertion: cAMP-CRP directly binds and activates the ulaA promoter controlling ulaABCDEF. ulaG expression was not CRP-dependent in the same reporter conditions; no CRP→ulaG activation is asserted.

    Source locationTable 2; Figure 6B; Figure 7; CRP-binding-site mutation
DNA-binding transcriptional dual regulator IHF
EcoCyc:PC00027		inhibits

IHF contributes to repression of basal expression at this divergent ula promoter in JA134 derivatives, especially ulaA. The effect is regulatory context for UlaR-dependent promoter organization; no direct inhibition of catalytic protein is implied.

ulaG
Entrez:948705
  • PMID:14996803

    Source assertion: IHF contributes to repression of basal expression at this divergent ula promoter in JA134 derivatives, especially ulaA. The effect is regulatory context for UlaR-dependent promoter organization; no direct inhibition of catalytic protein is implied.

    Source locationTable 2; Figure 6C; Discussion, IHF mutant basal expression
DNA-binding transcriptional dual regulator IHF
EcoCyc:PC00027		inhibits

IHF contributes to repression of basal expression at this divergent ula promoter in JA134 derivatives, especially ulaA. The effect is regulatory context for UlaR-dependent promoter organization; no direct inhibition of catalytic protein is implied.

ulaA
Entrez:948717
  • PMID:14996803

    Source assertion: IHF contributes to repression of basal expression at this divergent ula promoter in JA134 derivatives, especially ulaA. The effect is regulatory context for UlaR-dependent promoter organization; no direct inhibition of catalytic protein is implied.

    Source locationTable 2; Figure 6C; Discussion, IHF mutant basal expression
D-glucose
CHEBI:17634		inhibits

Glucose strongly represses the ula promoter reporter under tested JA134 conditions. Added cAMP did not fully relieve repression, so a second mechanism was proposed; glucose binding to UlaR or a particular inducer-exclusion step was not demonstrated.

ulaG
Entrez:948705
  • PMID:14996803

    Source assertion: Glucose strongly represses the ula promoter reporter under tested JA134 conditions. Added cAMP did not fully relieve repression, so a second mechanism was proposed; glucose binding to UlaR or a particular inducer-exclusion step was not demonstrated.

    Source locationFigure 7 expression matrix; Discussion, glucose repression
D-glucose
CHEBI:17634		inhibits

Glucose strongly represses the ula promoter reporter under tested JA134 conditions. Added cAMP did not fully relieve repression, so a second mechanism was proposed; glucose binding to UlaR or a particular inducer-exclusion step was not demonstrated.

ulaA
Entrez:948717
  • PMID:14996803

    Source assertion: Glucose strongly represses the ula promoter reporter under tested JA134 conditions. Added cAMP did not fully relieve repression, so a second mechanism was proposed; glucose binding to UlaR or a particular inducer-exclusion step was not demonstrated.

    Source locationFigure 7 expression matrix; Discussion, glucose repression
L-ascorbate 6-phosphate(3-)
CHEBI:61698		inhibits

The 2008 primary abstract identifies L-ascorbate 6-phosphate as direct UlaR effector, shifting the DNA-bound tetramer toward a DNA-free dimer and relieving repression. Fullbody/construct details were unavailable. Free L-ascorbate is not substituted for its 6-phosphate.

HTH-type transcriptional regulator UlaR
UniProtKB:P0A9W0
  • PMID:18844374

    Source assertion: The 2008 primary abstract identifies L-ascorbate 6-phosphate as direct UlaR effector, shifting the DNA-bound tetramer toward a DNA-free dimer and relieving repression. Fullbody/construct details were unavailable. Free L-ascorbate is not substituted for its 6-phosphate.

    Source locationEuropePMC result PMID18844374/abstractText
ulaG
Entrez:948705		enables

Expression of this ula gene supplies its encoded Ula protein. Gene deletion impairs L-ascorbate utilization; this edge connects the promoter regulation context to the corresponding pathway component.

L-ascorbate 6-phosphate + H2O => 3-dehydro-L-gulonate 6-phosphate
RHEA:28804
  • UniProtKB:P39300

    Source assertion: Expression of this ula gene supplies its encoded Ula protein. Gene deletion impairs L-ascorbate utilization; this edge connects the promoter regulation context to the corresponding pathway component.

    Source locationJSON exact geneName and FUNCTION/DISRUPTION PHENOTYPE comments
  • PMID:12644495

    Source assertion: Expression of this ula gene supplies its encoded Ula protein. Gene deletion impairs L-ascorbate utilization; this edge connects the promoter regulation context to the corresponding pathway component.

    Source locationResults, UlaABC mutant tests and proposed UlaG role
ulaA
Entrez:948717		enables

Expression of this ula gene supplies its encoded Ula protein. Gene deletion impairs L-ascorbate utilization; this edge connects the promoter regulation context to the corresponding pathway component.

EC 2.7.1.194
MetaCyc:RXN0-2461
  • UniProtKB:P39301

    Source assertion: Expression of this ula gene supplies its encoded Ula protein. Gene deletion impairs L-ascorbate utilization; this edge connects the promoter regulation context to the corresponding pathway component.

    Source locationJSON exact geneName and FUNCTION/DISRUPTION PHENOTYPE comments
  • PMID:12644495

    Source assertion: Expression of this ula gene supplies its encoded Ula protein. Gene deletion impairs L-ascorbate utilization; this edge connects the promoter regulation context to the corresponding pathway component.

    Source locationResults, UlaABC mutant tests and proposed UlaG role
L-ribulose 5-phosphate => D-xylulose 5-phosphate
RHEA:22369		provides_input_for

The native pathway-link routes the D-xylulose5P product into the non-oxidative pentose phosphate pathway. This is an interface; downstream pentose-phosphate reactions are outside the selected five-event core.

pentose phosphate pathway (non-oxidative branch)
MetaCyc:NONOXIPENT-PWY
  • MetaCyc:PWY0-301

    Source assertion: The native pathway-link routes the D-xylulose5P product into the non-oxidative pentose phosphate pathway. This is an interface; downstream pentose-phosphate reactions are outside the selected five-event core.

    Source locationXPath /ptools-xml/Pathway/pathway-link containing XYLULOSE-5-PHOSPHATE and NONOXIPENT-PWY

References

Curation history