ADP-L-glycero-beta-D-manno-heptose biosynthesis

MetaCyc:PWY0-1241

The complete five-reaction MetaCyc route converts sedoheptulose 7-phosphate to ADP-L-glycero-beta-D-manno-heptose using GmhA, the two activities of HldE, GmhB and HldD. The selected proteins are E. coli K-12; native complexes are MG1655 assignments. The 2002 HldE/GmhB experiments used K-12 gene products with an Aneurinibacillus GmhA reagent, whereas later GmhA work directly examines E. coli. Current Rhea represents GmhA as two substrate molecules giving one alpha and one beta heptose 7-phosphate; both products and the coefficient are retained, without asserting an experimentally fixed 1:1 physiological product ratio. Only the beta branch continues to ADP-heptose. GmhA, HldE and HldD are represented by source-defined tetramer, dimer and pentamer assemblies; GmhB is monomeric. GmhA zinc is a similarity-based annotation. GmhB catalytic magnesium and manganese/cobalt alternatives are distinguished from its bound zinc loop site, whose physiological role remains unresolved. HldD recycles bound NADP during epimerization; NAD is a lower-activity substitute, not an additional required cofactor. Sedoheptulose generation, alpha-GDP-heptose synthesis, LPS incorporation and host sensing are outside this native boundary. No obligatory growth phenotype, universal strain activity or compensating GmhB phosphatase is inferred.

Pathway type
adp l glycero beta d manno heptose biosynthesis
Organism scope

Read the source YAML

Pathway network

32 nodes · 43 asserted directed edges

Arrows show recorded subject → object relationships, not necessarily metabolic flow. Select a node for details or an arrow for evidence. Scroll, zoom or find a node to explore.

Pathway network: ADP-L-glycero-beta-D-manno-heptose biosynthesis 32 nodes · 43 asserted directed edges. Every arrow links to its evidence table row; nodes link to their component details. Isolated declared components are retained. CHEBI:57483 — consumes → RHEA:27490; This is the formal Rhea two-anomer equation, not a measured fixed in vivo product ratio.; Evidence: RHEA:27490consumes RHEA:27490 — produces → CHEBI:60203; This is the formal Rhea two-anomer equation, not a measured fixed in vivo product ratio.; Evidence: RHEA:27490produces RHEA:27490 — produces → CHEBI:60204; This is the formal Rhea two-anomer equation, not a measured fixed in vivo product ratio.; Evidence: RHEA:27490produces CHEBI:60204 — consumes → RHEA:27474; Evidence: RHEA:27474consumes CHEBI:30616 — consumes → RHEA:27474; Evidence: RHEA:27474consumes RHEA:27474 — produces → CHEBI:60208; Evidence: RHEA:27474produces RHEA:27474 — produces → CHEBI:456216; Evidence: RHEA:27474produces RHEA:27474 — produces → CHEBI:15378; Evidence: RHEA:27474produces CHEBI:60208 — consumes → RHEA:28519; Evidence: RHEA:28519consumes CHEBI:15377 — consumes → RHEA:28519; Evidence: RHEA:28519consumes RHEA:28519 — produces → CHEBI:61593; Evidence: RHEA:28519produces RHEA:28519 — produces → CHEBI:43474; Evidence: RHEA:28519produces CHEBI:61593 — consumes → RHEA:27466; Evidence: RHEA:27466consumes CHEBI:30616 — consumes → RHEA:27466; Evidence: RHEA:27466consumes CHEBI:15378 — consumes → RHEA:27466; Evidence: RHEA:27466consumes RHEA:27466 — produces → CHEBI:59967; Evidence: RHEA:27466produces RHEA:27466 — produces → CHEBI:33019; Evidence: RHEA:27466produces CHEBI:59967 — consumes → RHEA:17578; Evidence: RHEA:17578consumes RHEA:17578 — produces → CHEBI:61506; Evidence: RHEA:17578produces MetaCyc:CPLX0-7660 — catalyzes → RHEA:27490; The selected biosynthetic direction does not assert irreversible chemistry.; Evidence: MetaCyc:CPLX0-7660, UniProtKB:P63224, RHEA:27490, PMID:18056714catalyzes MetaCyc:CPLX0-3661 — catalyzes → RHEA:27474; Evidence: MetaCyc:CPLX0-3661, UniProtKB:P76658, RHEA:27474, PMID:11751812catalyzes UniProtKB:P63228 — catalyzes → RHEA:28519; Evidence: UniProtKB:P63228, RHEA:28519, PMID:20050615, PMID:20050614catalyzes MetaCyc:CPLX0-3661 — catalyzes → RHEA:27466; Evidence: MetaCyc:CPLX0-3661, UniProtKB:P76658, RHEA:27466, PMID:11751812catalyzes MetaCyc:CPLX0-3681 — catalyzes → RHEA:17578; The selected biosynthetic direction does not assert irreversible chemistry.; Evidence: MetaCyc:CPLX0-3681, UniProtKB:P67910, RHEA:17578, PMID:7929099catalyzes UniProtKB:P63224 — part_of → MetaCyc:CPLX0-7660; The native complex contains 4 identical subunits; the protein node is not independently assigned monomeric catalytic sufficiency.; Evidence: MetaCyc:CPLX0-7660, MetaCyc:G6106-MONOMER, UniProtKB:P63224, PMID:18056714part of UniProtKB:P76658 — part_of → MetaCyc:CPLX0-3661; The native complex contains 2 identical subunits; the protein node is not independently assigned monomeric catalytic sufficiency.; Evidence: MetaCyc:CPLX0-3661, MetaCyc:G7590-MONOMER, UniProtKB:P76658, PMID:16030223part of UniProtKB:P67910 — part_of → MetaCyc:CPLX0-3681; The native complex contains 5 identical subunits; the protein node is not independently assigned monomeric catalytic sufficiency.; Evidence: MetaCyc:CPLX0-3681, MetaCyc:EG10838-MONOMER, UniProtKB:P67910, PMID:10896473part of MetaCyc:CPLX0-7660 — has_cofactor → CHEBI:29105; Similarity-based cofactor annotation is retained with its evidence grade; no direct K-12 zinc requirement is inferred.; Evidence: UniProtKB:P63224has cofactor UniProtKB:P63228 — has_cofactor → CHEBI:18420; Catalytic divalent-metal alternatives are not simultaneous required occupancy. Dominant in vivo metal is not established by these annotations.; Evidence: UniProtKB:P63228, PMID:20050614has cofactor UniProtKB:P63228 — has_cofactor → CHEBI:29035; Catalytic divalent-metal alternatives are not simultaneous required occupancy. Dominant in vivo metal is not established by these annotations.; Evidence: UniProtKB:P63228has cofactor UniProtKB:P63228 — has_cofactor → CHEBI:48828; Catalytic divalent-metal alternatives are not simultaneous required occupancy. Dominant in vivo metal is not established by these annotations.; Evidence: UniProtKB:P63228has cofactor UniProtKB:P63228 — has_cofactor → CHEBI:29105; This bound Zn site is distinct from catalytic Mg. No universal Zn requirement or established physiological regulatory role is asserted.; Evidence: UniProtKB:P63228, PMID:20050614has cofactor MetaCyc:CPLX0-3681 — has_cofactor → CHEBI:58349; NADP is the physiological bound cofactor; NAD is an alternative with lower activity. Neither is consumed in the balanced net epimerization.; Evidence: UniProtKB:P67910, PMID:11313358, PMID:17316025has cofactor MetaCyc:CPLX0-3681 — has_cofactor → CHEBI:57540; NADP is the physiological bound cofactor; NAD is an alternative with lower activity. Neither is consumed in the balanced net epimerization.; Evidence: UniProtKB:P67910, PMID:11313358, PMID:17316025has cofactor RHEA:27490 — part_of → MetaCyc:PWY0-1241; Evidence: MetaCyc:PWY0-1241, MetaCyc:RXN0-4301part of RHEA:27474 — part_of → MetaCyc:PWY0-1241; Evidence: MetaCyc:PWY0-1241, MetaCyc:RXN0-4341part of RHEA:28519 — part_of → MetaCyc:PWY0-1241; Evidence: MetaCyc:PWY0-1241, MetaCyc:RXN0-4361part of RHEA:27466 — part_of → MetaCyc:PWY0-1241; Evidence: MetaCyc:PWY0-1241, MetaCyc:RXN0-4342part of RHEA:17578 — part_of → MetaCyc:PWY0-1241; Evidence: MetaCyc:PWY0-1241, MetaCyc:5.1.3.20-RXNpart of RHEA:27490 — provides_input_for → RHEA:27474; A shared chemical and native predecessor relation establish this sequence; no physical channeling or obligatory enzyme complex is inferred.; Evidence: MetaCyc:PWY0-1241, RHEA:27490, RHEA:27474provides input for RHEA:27474 — provides_input_for → RHEA:28519; A shared chemical and native predecessor relation establish this sequence; no physical channeling or obligatory enzyme complex is inferred.; Evidence: MetaCyc:PWY0-1241, RHEA:27474, RHEA:28519provides input for RHEA:28519 — provides_input_for → RHEA:27466; A shared chemical and native predecessor relation establish this sequence; no physical channeling or obligatory enzyme complex is inferred.; Evidence: MetaCyc:PWY0-1241, RHEA:28519, RHEA:27466provides input for RHEA:27466 — provides_input_for → RHEA:17578; A shared chemical and native predecessor relation establish this sequence; no physical channeling or obligatory enzyme complex is inferred.; Evidence: MetaCyc:PWY0-1241, RHEA:27466, RHEA:17578provides input for water; CHEBI:15377; Declared type: small_molecule small molecule water hydron; CHEBI:15378; Declared type: small_molecule small molecule hydron magnesium(2+); CHEBI:18420; Declared type: cofactor cofactor magnesium(2+) manganese(2+); CHEBI:29035; Declared type: cofactor cofactor manganese(2+) zinc(2+); CHEBI:29105; Declared type: cofactor cofactor zinc(2+) ATP(4-); CHEBI:30616; Declared type: small_molecule small molecule ATP(4-) diphosphate(3-); CHEBI:33019; Declared type: small_molecule small molecule diphosphate(3-) hydrogenphosphate; CHEBI:43474; Declared type: small_molecule small molecule hydrogenphosphate ADP(3-); CHEBI:456216; Declared type: small_molecule small molecule ADP(3-) cobalt(2+); CHEBI:48828; Declared type: cofactor cofactor cobalt(2+) sedoheptulose 7-phosphate(2-); CHEBI:57483; Declared type: small_molecule small molecule sedoheptulose 7-phosphate(2-) NAD(1-); CHEBI:57540; Declared type: cofactor cofactor NAD(1-) NADP(3-); CHEBI:58349; Declared type: cofactor cofactor NADP(3-) ADP-D-glycero-beta-D-manno-heptose(2-); CHEBI:59967; Declared type: small_molecule small molecule ADP-D-glycero-beta-D-manno- heptose(2-) D-glycero-alpha-D-manno-heptose 7-phosphate(2-); CHEBI:60203; Declared type: small_molecule small molecule D-glycero-alpha-D-manno- heptose 7-phosphate(2-) D-glycero-beta-D-manno-heptose 7-phosphate(2-); CHEBI:60204; Declared type: small_molecule small molecule D-glycero-beta-D-manno- heptose 7-phosphate(2-) D-glycero-beta-D-manno-heptose 1,7-bisphosphate(4-); CHEBI:60208; Declared type: small_molecule small molecule D-glycero-beta-D-manno- heptose 1,7-bisphosphate(4-) ADP-L-glycero-beta-D-manno-heptose(2-); CHEBI:61506; Declared type: small_molecule small molecule ADP-L-glycero-beta-D-manno- heptose(2-) D-glycero-beta-D-manno-heptose 1-phosphate(2-); CHEBI:61593; Declared type: small_molecule small molecule D-glycero-beta-D-manno- heptose 1-phosphate(2-) Phosphoheptose isomerase; UniProtKB:P63224; Declared type: protein protein Phosphoheptose isomerase Bifunctional protein HldE; UniProtKB:P76658; Declared type: protein protein Bifunctional protein HldE D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase; UniProtKB:P63228; Declared type: protein protein D-glycero-beta-D-manno- heptose-1,7-bisphosphate 7-phosphatase ADP-L-glycero-D-manno-heptose-6-epimerase; UniProtKB:P67910; Declared type: protein protein ADP-L-glycero-D-manno- heptose-6-epimerase D-sedoheptulose 7-phosphate isomerase; MetaCyc:CPLX0-7660; Declared type: complex complex D-sedoheptulose 7-phosphate isomerase fused heptose 7-phosphate kinase/heptose 1-phosphate adenyltransferase; MetaCyc:CPLX0-3661; Declared type: complex complex fused heptose 7-phosphate kinase/heptose 1-phosphate adenyltransferase ADP-L-glycero-D-mannoheptose 6-epimerase; MetaCyc:CPLX0-3681; Declared type: complex complex ADP-L-glycero-D-mannoheptose 6-epimerase 2 D-sedoheptulose 7-phosphate => D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate; RHEA:27490; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity 2 D-sedoheptulose 7-phosphate => D-glycero- alpha-D-manno-heptose 7-phosphate + D-glycero- beta-D-manno-heptose 7-phosphate D-glycero-beta-D-manno-heptose 7-phosphate + ATP => D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP + H(+); RHEA:27474; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity D-glycero-beta-D-manno- heptose 7-phosphate + ATP => D-glycero-beta-D-manno- heptose 1,7-bisphosphate + ADP + H(+) D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O => D-glycero-beta-D-manno-heptose 1-phosphate + phosphate; RHEA:28519; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity D-glycero-beta-D-manno- heptose 1,7-bisphosphate + H2O => D-glycero-beta-D- manno-heptose 1-phosphate + phosphate D-glycero-beta-D-manno-heptose 1-phosphate + ATP + H(+) => ADP-D-glycero-beta-D-manno-heptose + diphosphate; RHEA:27466; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity D-glycero-beta-D-manno- heptose 1-phosphate + ATP + H(+) => ADP-D-glycero-beta- D-manno-heptose + diphosphate ADP-D-glycero-beta-D-manno-heptose => ADP-L-glycero-beta-D-manno-heptose; RHEA:17578; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity ADP-D-glycero-beta-D-manno- heptose => ADP-L-glycero- beta-D-manno-heptose ADP-L-glycero-beta-D-manno-heptose biosynthesis; MetaCyc:PWY0-1241; Declared type: pathway pathway ADP-L-glycero-beta-D-manno- heptose biosynthesis

Components and activities

Declared biological components and source reaction directions
NodeKind or roleSource direction
Escherichia coli K-12
NCBITaxon:83333
taxon
water
CHEBI:15377
small molecule
hydron
CHEBI:15378
small molecule
magnesium(2+)
CHEBI:18420
cofactor
manganese(2+)
CHEBI:29035
cofactor
zinc(2+)
CHEBI:29105
cofactor
ATP(4-)
CHEBI:30616
small molecule
diphosphate(3-)
CHEBI:33019
small molecule
hydrogenphosphate
CHEBI:43474
small molecule
ADP(3-)
CHEBI:456216
small molecule
cobalt(2+)
CHEBI:48828
cofactor
sedoheptulose 7-phosphate(2-)
CHEBI:57483
small molecule
NAD(1-)
CHEBI:57540
cofactor
NADP(3-)
CHEBI:58349
cofactor
ADP-D-glycero-beta-D-manno-heptose(2-)
CHEBI:59967
small molecule
D-glycero-alpha-D-manno-heptose 7-phosphate(2-)
CHEBI:60203
small molecule
D-glycero-beta-D-manno-heptose 7-phosphate(2-)
CHEBI:60204
small molecule
D-glycero-beta-D-manno-heptose 1,7-bisphosphate(4-)
CHEBI:60208
small molecule
ADP-L-glycero-beta-D-manno-heptose(2-)
CHEBI:61506
small molecule
D-glycero-beta-D-manno-heptose 1-phosphate(2-)
CHEBI:61593
small molecule
Phosphoheptose isomerase
UniProtKB:P63224
protein
Bifunctional protein HldE
UniProtKB:P76658
protein
D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase
UniProtKB:P63228
protein
ADP-L-glycero-D-manno-heptose-6-epimerase
UniProtKB:P67910
protein
D-sedoheptulose 7-phosphate isomerase
MetaCyc:CPLX0-7660
complex
fused heptose 7-phosphate kinase/heptose 1-phosphate adenyltransferase
MetaCyc:CPLX0-3661
complex
ADP-L-glycero-D-mannoheptose 6-epimerase
MetaCyc:CPLX0-3681
complex
2 D-sedoheptulose 7-phosphate => D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate
RHEA:27490
molecular activityleft to right
D-glycero-beta-D-manno-heptose 7-phosphate + ATP => D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP + H(+)
RHEA:27474
molecular activityleft to right
D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O => D-glycero-beta-D-manno-heptose 1-phosphate + phosphate
RHEA:28519
molecular activityleft to right
D-glycero-beta-D-manno-heptose 1-phosphate + ATP + H(+) => ADP-D-glycero-beta-D-manno-heptose + diphosphate
RHEA:27466
molecular activityleft to right
ADP-D-glycero-beta-D-manno-heptose => ADP-L-glycero-beta-D-manno-heptose
RHEA:17578
molecular activityleft to right

Mechanistic edges

Mechanistic edges and their cited evidence
SubjectPredicate and descriptionObjectEvidence
sedoheptulose 7-phosphate(2-)
CHEBI:57483
consumes

This is the formal Rhea two-anomer equation, not a measured fixed in vivo product ratio.

2 D-sedoheptulose 7-phosphate => D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate
RHEA:27490
  • RHEA:27490

    Source assertion: RHEA:27490 assigns CHEBI:57483 to its substrates, coefficient 2 via rh:contains2.

    Source locationhttp://rdf.rhea-db.org/27490 rh:substrates; http://rdf.rhea-db.org/27489_L rh:contains2 http://rdf.rhea-db.org/Participant_27489_compound_3830; http://rdf.rhea-db.org/Participant_27489_compound_3830 rh:compound http://rdf.rhea-db.org/Compound_3830; rh:chebi
2 D-sedoheptulose 7-phosphate => D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate
RHEA:27490
produces

This is the formal Rhea two-anomer equation, not a measured fixed in vivo product ratio.

D-glycero-alpha-D-manno-heptose 7-phosphate(2-)
CHEBI:60203
  • RHEA:27490

    Source assertion: RHEA:27490 assigns CHEBI:60203 to its products, coefficient 1 via rh:contains1.

    Source locationhttp://rdf.rhea-db.org/27490 rh:products; http://rdf.rhea-db.org/27489_R rh:contains1 http://rdf.rhea-db.org/Participant_27489_compound_6236; http://rdf.rhea-db.org/Participant_27489_compound_6236 rh:compound http://rdf.rhea-db.org/Compound_6236; rh:chebi
2 D-sedoheptulose 7-phosphate => D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate
RHEA:27490
produces

This is the formal Rhea two-anomer equation, not a measured fixed in vivo product ratio.

D-glycero-beta-D-manno-heptose 7-phosphate(2-)
CHEBI:60204
  • RHEA:27490

    Source assertion: RHEA:27490 assigns CHEBI:60204 to its products, coefficient 1 via rh:contains1.

    Source locationhttp://rdf.rhea-db.org/27490 rh:products; http://rdf.rhea-db.org/27489_R rh:contains1 http://rdf.rhea-db.org/Participant_27489_compound_6311; http://rdf.rhea-db.org/Participant_27489_compound_6311 rh:compound http://rdf.rhea-db.org/Compound_6311; rh:chebi
D-glycero-beta-D-manno-heptose 7-phosphate(2-)
CHEBI:60204
consumes

D-glycero-beta-D-manno-heptose 7-phosphate + ATP => D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP + H(+)
RHEA:27474
  • RHEA:27474

    Source assertion: RHEA:27474 assigns CHEBI:60204 to its substrates, coefficient 1 via rh:contains1.

    Source locationhttp://rdf.rhea-db.org/27474 rh:substrates; http://rdf.rhea-db.org/27473_L rh:contains1 http://rdf.rhea-db.org/Participant_27473_compound_6311; http://rdf.rhea-db.org/Participant_27473_compound_6311 rh:compound http://rdf.rhea-db.org/Compound_6311; rh:chebi
ATP(4-)
CHEBI:30616
consumes

D-glycero-beta-D-manno-heptose 7-phosphate + ATP => D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP + H(+)
RHEA:27474
  • RHEA:27474

    Source assertion: RHEA:27474 assigns CHEBI:30616 to its substrates, coefficient 1 via rh:contains1.

    Source locationhttp://rdf.rhea-db.org/27474 rh:substrates; http://rdf.rhea-db.org/27473_L rh:contains1 http://rdf.rhea-db.org/Participant_27473_compound_6372; http://rdf.rhea-db.org/Participant_27473_compound_6372 rh:compound http://rdf.rhea-db.org/Compound_6372; rh:chebi
D-glycero-beta-D-manno-heptose 7-phosphate + ATP => D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP + H(+)
RHEA:27474
produces

D-glycero-beta-D-manno-heptose 1,7-bisphosphate(4-)
CHEBI:60208
  • RHEA:27474

    Source assertion: RHEA:27474 assigns CHEBI:60208 to its products, coefficient 1 via rh:contains1.

    Source locationhttp://rdf.rhea-db.org/27474 rh:products; http://rdf.rhea-db.org/27473_R rh:contains1 http://rdf.rhea-db.org/Participant_27473_compound_6310; http://rdf.rhea-db.org/Participant_27473_compound_6310 rh:compound http://rdf.rhea-db.org/Compound_6310; rh:chebi
D-glycero-beta-D-manno-heptose 7-phosphate + ATP => D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP + H(+)
RHEA:27474
produces

ADP(3-)
CHEBI:456216
  • RHEA:27474

    Source assertion: RHEA:27474 assigns CHEBI:456216 to its products, coefficient 1 via rh:contains1.

    Source locationhttp://rdf.rhea-db.org/27474 rh:products; http://rdf.rhea-db.org/27473_R rh:contains1 http://rdf.rhea-db.org/Participant_27473_compound_2710; http://rdf.rhea-db.org/Participant_27473_compound_2710 rh:compound http://rdf.rhea-db.org/Compound_2710; rh:chebi
D-glycero-beta-D-manno-heptose 7-phosphate + ATP => D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP + H(+)
RHEA:27474
produces

hydron
CHEBI:15378
  • RHEA:27474

    Source assertion: RHEA:27474 assigns CHEBI:15378 to its products, coefficient 1 via rh:contains1.

    Source locationhttp://rdf.rhea-db.org/27474 rh:products; http://rdf.rhea-db.org/27473_R rh:contains1 http://rdf.rhea-db.org/Participant_27473_compound_3249; http://rdf.rhea-db.org/Participant_27473_compound_3249 rh:compound http://rdf.rhea-db.org/Compound_3249; rh:chebi
D-glycero-beta-D-manno-heptose 1,7-bisphosphate(4-)
CHEBI:60208
consumes

D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O => D-glycero-beta-D-manno-heptose 1-phosphate + phosphate
RHEA:28519
  • RHEA:28519

    Source assertion: RHEA:28519 assigns CHEBI:60208 to its substrates, coefficient 1 via rh:contains1.

    Source locationhttp://rdf.rhea-db.org/28519 rh:substrates; http://rdf.rhea-db.org/28518_L rh:contains1 http://rdf.rhea-db.org/Participant_28518_compound_6310; http://rdf.rhea-db.org/Participant_28518_compound_6310 rh:compound http://rdf.rhea-db.org/Compound_6310; rh:chebi
water
CHEBI:15377
consumes

D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O => D-glycero-beta-D-manno-heptose 1-phosphate + phosphate
RHEA:28519
  • RHEA:28519

    Source assertion: RHEA:28519 assigns CHEBI:15377 to its substrates, coefficient 1 via rh:contains1.

    Source locationhttp://rdf.rhea-db.org/28519 rh:substrates; http://rdf.rhea-db.org/28518_L rh:contains1 http://rdf.rhea-db.org/Participant_28518_compound_1283; http://rdf.rhea-db.org/Participant_28518_compound_1283 rh:compound http://rdf.rhea-db.org/Compound_1283; rh:chebi
D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O => D-glycero-beta-D-manno-heptose 1-phosphate + phosphate
RHEA:28519
produces

D-glycero-beta-D-manno-heptose 1-phosphate(2-)
CHEBI:61593
  • RHEA:28519

    Source assertion: RHEA:28519 assigns CHEBI:61593 to its products, coefficient 1 via rh:contains1.

    Source locationhttp://rdf.rhea-db.org/28519 rh:products; http://rdf.rhea-db.org/28518_R rh:contains1 http://rdf.rhea-db.org/Participant_28518_compound_6538; http://rdf.rhea-db.org/Participant_28518_compound_6538 rh:compound http://rdf.rhea-db.org/Compound_6538; rh:chebi
D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O => D-glycero-beta-D-manno-heptose 1-phosphate + phosphate
RHEA:28519
produces

hydrogenphosphate
CHEBI:43474
  • RHEA:28519

    Source assertion: RHEA:28519 assigns CHEBI:43474 to its products, coefficient 1 via rh:contains1.

    Source locationhttp://rdf.rhea-db.org/28519 rh:products; http://rdf.rhea-db.org/28518_R rh:contains1 http://rdf.rhea-db.org/Participant_28518_compound_5518; http://rdf.rhea-db.org/Participant_28518_compound_5518 rh:compound http://rdf.rhea-db.org/Compound_5518; rh:chebi
D-glycero-beta-D-manno-heptose 1-phosphate(2-)
CHEBI:61593
consumes

D-glycero-beta-D-manno-heptose 1-phosphate + ATP + H(+) => ADP-D-glycero-beta-D-manno-heptose + diphosphate
RHEA:27466
  • RHEA:27466

    Source assertion: RHEA:27466 assigns CHEBI:61593 to its substrates, coefficient 1 via rh:contains1.

    Source locationhttp://rdf.rhea-db.org/27466 rh:substrates; http://rdf.rhea-db.org/27465_L rh:contains1 http://rdf.rhea-db.org/Participant_27465_compound_6538; http://rdf.rhea-db.org/Participant_27465_compound_6538 rh:compound http://rdf.rhea-db.org/Compound_6538; rh:chebi
ATP(4-)
CHEBI:30616
consumes

D-glycero-beta-D-manno-heptose 1-phosphate + ATP + H(+) => ADP-D-glycero-beta-D-manno-heptose + diphosphate
RHEA:27466
  • RHEA:27466

    Source assertion: RHEA:27466 assigns CHEBI:30616 to its substrates, coefficient 1 via rh:contains1.

    Source locationhttp://rdf.rhea-db.org/27466 rh:substrates; http://rdf.rhea-db.org/27465_L rh:contains1 http://rdf.rhea-db.org/Participant_27465_compound_6372; http://rdf.rhea-db.org/Participant_27465_compound_6372 rh:compound http://rdf.rhea-db.org/Compound_6372; rh:chebi
hydron
CHEBI:15378
consumes

D-glycero-beta-D-manno-heptose 1-phosphate + ATP + H(+) => ADP-D-glycero-beta-D-manno-heptose + diphosphate
RHEA:27466
  • RHEA:27466

    Source assertion: RHEA:27466 assigns CHEBI:15378 to its substrates, coefficient 1 via rh:contains1.

    Source locationhttp://rdf.rhea-db.org/27466 rh:substrates; http://rdf.rhea-db.org/27465_L rh:contains1 http://rdf.rhea-db.org/Participant_27465_compound_3249; http://rdf.rhea-db.org/Participant_27465_compound_3249 rh:compound http://rdf.rhea-db.org/Compound_3249; rh:chebi
D-glycero-beta-D-manno-heptose 1-phosphate + ATP + H(+) => ADP-D-glycero-beta-D-manno-heptose + diphosphate
RHEA:27466
produces

ADP-D-glycero-beta-D-manno-heptose(2-)
CHEBI:59967
  • RHEA:27466

    Source assertion: RHEA:27466 assigns CHEBI:59967 to its products, coefficient 1 via rh:contains1.

    Source locationhttp://rdf.rhea-db.org/27466 rh:products; http://rdf.rhea-db.org/27465_R rh:contains1 http://rdf.rhea-db.org/Participant_27465_compound_6139; http://rdf.rhea-db.org/Participant_27465_compound_6139 rh:compound http://rdf.rhea-db.org/Compound_6139; rh:chebi
D-glycero-beta-D-manno-heptose 1-phosphate + ATP + H(+) => ADP-D-glycero-beta-D-manno-heptose + diphosphate
RHEA:27466
produces

diphosphate(3-)
CHEBI:33019
  • RHEA:27466

    Source assertion: RHEA:27466 assigns CHEBI:33019 to its products, coefficient 1 via rh:contains1.

    Source locationhttp://rdf.rhea-db.org/27466 rh:products; http://rdf.rhea-db.org/27465_R rh:contains1 http://rdf.rhea-db.org/Participant_27465_compound_2106; http://rdf.rhea-db.org/Participant_27465_compound_2106 rh:compound http://rdf.rhea-db.org/Compound_2106; rh:chebi
ADP-D-glycero-beta-D-manno-heptose(2-)
CHEBI:59967
consumes

ADP-D-glycero-beta-D-manno-heptose => ADP-L-glycero-beta-D-manno-heptose
RHEA:17578
  • RHEA:17578

    Source assertion: RHEA:17578 assigns CHEBI:59967 to its substrates, coefficient 1 via rh:contains1.

    Source locationhttp://rdf.rhea-db.org/17578 rh:substrates; http://rdf.rhea-db.org/17577_L rh:contains1 http://rdf.rhea-db.org/Participant_17577_compound_6139; http://rdf.rhea-db.org/Participant_17577_compound_6139 rh:compound http://rdf.rhea-db.org/Compound_6139; rh:chebi
ADP-D-glycero-beta-D-manno-heptose => ADP-L-glycero-beta-D-manno-heptose
RHEA:17578
produces

ADP-L-glycero-beta-D-manno-heptose(2-)
CHEBI:61506
  • RHEA:17578

    Source assertion: RHEA:17578 assigns CHEBI:61506 to its products, coefficient 1 via rh:contains1.

    Source locationhttp://rdf.rhea-db.org/17578 rh:products; http://rdf.rhea-db.org/17577_R rh:contains1 http://rdf.rhea-db.org/Participant_17577_compound_6453; http://rdf.rhea-db.org/Participant_17577_compound_6453 rh:compound http://rdf.rhea-db.org/Compound_6453; rh:chebi
D-sedoheptulose 7-phosphate isomerase
MetaCyc:CPLX0-7660
catalyzes

The selected biosynthetic direction does not assert irreversible chemistry.

2 D-sedoheptulose 7-phosphate => D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate
RHEA:27490
  • MetaCyc:CPLX0-7660

    Source assertion: CPLX0-7660 has an explicit catalytic assignment to RXN0-4301.

    Source locationProtein[@frameid="CPLX0-7660"]/catalyzes/Enzymatic-Reaction/reaction/Reaction[@frameid="RXN0-4301"]
  • UniProtKB:P63224

    Source assertion: Reviewed K-12 P63224 CATALYTIC ACTIVITY gives RHEA:27489 and the corresponding equation with experimental ECO:0000269 evidence.

    Source location/organism/taxonId; /comments/1/reaction
  • RHEA:27490

    Source assertion: Master RHEA:27489 explicitly links directionalReaction RHEA:27490, the left-to-right member in release 142.

    Source locationhttp://rdf.rhea-db.org/27489 rh:directionalReaction http://rdf.rhea-db.org/27490; rhea-directions.tsv RHEA_ID_LR
  • PMID:18056714

    Source assertion: The primary abstract reports E. coli and P. aeruginosa GmhA structures in apo, substrate and product forms, with mutant biochemistry and in vivo LPS analysis. It supports the E. coli isomerase assignment, without making the 2002 heterologous GmhA reagent an E. coli experiment.

    Source location/resultList/result[id="18056714"]/abstractText
fused heptose 7-phosphate kinase/heptose 1-phosphate adenyltransferase
MetaCyc:CPLX0-3661
catalyzes

D-glycero-beta-D-manno-heptose 7-phosphate + ATP => D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP + H(+)
RHEA:27474
  • MetaCyc:CPLX0-3661

    Source assertion: CPLX0-3661 has an explicit catalytic assignment to RXN0-4341.

    Source locationProtein[@frameid="CPLX0-3661"]/catalyzes/Enzymatic-Reaction/reaction/Reaction[@frameid="RXN0-4341"]
  • UniProtKB:P76658

    Source assertion: Reviewed K-12 P76658 CATALYTIC ACTIVITY gives RHEA:27473 and the corresponding equation with experimental ECO:0000269 evidence.

    Source location/organism/taxonId; /comments/2/reaction
  • RHEA:27474

    Source assertion: Master RHEA:27473 explicitly links directionalReaction RHEA:27474, the left-to-right member in release 142.

    Source locationhttp://rdf.rhea-db.org/27473 rh:directionalReaction http://rdf.rhea-db.org/27474; rhea-directions.tsv RHEA_ID_LR
  • PMID:11751812

    Source assertion: Purified K-12 HldE and ATP generate beta-heptose 1,7-bisphosphate in coupled HPAEC experiments; the upstream GmhA reagent was from A. thermoaerophilus. The assay contained 10 mM MgCl2, which alone is not a separate HldE metal-binding measurement.

    Source locationPMC139585 HTML (//article//p)[14,19,21]; Results/Biochemical characterization of the biosynthetic pathway; Figure 2
D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase
UniProtKB:P63228
catalyzes

D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O => D-glycero-beta-D-manno-heptose 1-phosphate + phosphate
RHEA:28519
  • UniProtKB:P63228

    Source assertion: Reviewed K-12 P63228 CATALYTIC ACTIVITY gives RHEA:28518 and the corresponding equation with experimental ECO:0000269 evidence.

    Source location/organism/taxonId; /comments/1/reaction
  • RHEA:28519

    Source assertion: Master RHEA:28518 explicitly links directionalReaction RHEA:28519, the left-to-right member in release 142.

    Source locationhttp://rdf.rhea-db.org/28518 rh:directionalReaction http://rdf.rhea-db.org/28519; rhea-directions.tsv RHEA_ID_LR
  • PMID:20050615

    Source assertion: E. coli K-12 GmhB selectively removes the C7 phosphate. Kinetics favor the beta over the alpha bisphosphate by about 100-fold; this is preference, not absolute alpha inactivity. The monophosphate product is not further hydrolyzed.

    Source locationPMC2844805 HTML (//article//p)[43]; Results/Substrate specificity; Tables 1 and 2
  • PMID:20050614

    Source assertion: Solution size-exclusion analysis supports monomeric E. coli GmhB; its substrate/Mg structure and catalytic-site analysis support C7 dephosphorylation. The paper prints an incorrect Swiss-Prot accession P63288; identity is independently grounded by native P63228 and current UniProt.

    Source locationPMC2844806 BioC passages offsets6284,12476,15508,28097
fused heptose 7-phosphate kinase/heptose 1-phosphate adenyltransferase
MetaCyc:CPLX0-3661
catalyzes

D-glycero-beta-D-manno-heptose 1-phosphate + ATP + H(+) => ADP-D-glycero-beta-D-manno-heptose + diphosphate
RHEA:27466
  • MetaCyc:CPLX0-3661

    Source assertion: CPLX0-3661 has an explicit catalytic assignment to RXN0-4342.

    Source locationProtein[@frameid="CPLX0-3661"]/catalyzes/Enzymatic-Reaction/reaction/Reaction[@frameid="RXN0-4342"]
  • UniProtKB:P76658

    Source assertion: Reviewed K-12 P76658 CATALYTIC ACTIVITY gives RHEA:27465 and the corresponding equation with experimental ECO:0000269 evidence.

    Source location/organism/taxonId; /comments/3/reaction
  • RHEA:27466

    Source assertion: Master RHEA:27465 explicitly links directionalReaction RHEA:27466, the left-to-right member in release 142.

    Source locationhttp://rdf.rhea-db.org/27465 rh:directionalReaction http://rdf.rhea-db.org/27466; rhea-directions.tsv RHEA_ID_LR
  • PMID:11751812

    Source assertion: K-12 HldE plus ATP activates synthetic beta-heptose 1-phosphate; alpha-heptose 1-phosphate and GTP controls do not yield the corresponding activation. Phosphatase activity is needed upstream in the coupled system. This is AMP transfer with diphosphate release.

    Source locationPMC139585 HTML (//article//p)[23,25,29]; Figure 3
ADP-L-glycero-D-mannoheptose 6-epimerase
MetaCyc:CPLX0-3681
catalyzes

The selected biosynthetic direction does not assert irreversible chemistry.

ADP-D-glycero-beta-D-manno-heptose => ADP-L-glycero-beta-D-manno-heptose
RHEA:17578
  • MetaCyc:CPLX0-3681

    Source assertion: CPLX0-3681 has an explicit catalytic assignment to 5.1.3.20-RXN.

    Source locationProtein[@frameid="CPLX0-3681"]/catalyzes/Enzymatic-Reaction/reaction/Reaction[@frameid="5.1.3.20-RXN"]
  • UniProtKB:P67910

    Source assertion: Reviewed K-12 P67910 CATALYTIC ACTIVITY gives RHEA:17577 and the corresponding equation with experimental ECO:0000269 evidence.

    Source location/organism/taxonId; /comments/1/reaction
  • RHEA:17578

    Source assertion: Master RHEA:17577 explicitly links directionalReaction RHEA:17578, the left-to-right member in release 142.

    Source locationhttp://rdf.rhea-db.org/17577 rh:directionalReaction http://rdf.rhea-db.org/17578; rhea-directions.tsv RHEA_ID_LR
  • PMID:7929099

    Source assertion: The indexed primary abstract reports purified E. coli K-12 RfaD/HldD interconversion of the ADP-D- and ADP-L-glycero-D-manno-heptose epimers. Its historical NAD identification was subsequently refined by the 2001 NADP study.

    Source location/resultList/result[id="7929099"]/abstractText
Phosphoheptose isomerase
UniProtKB:P63224
part_of

The native complex contains 4 identical subunits; the protein node is not independently assigned monomeric catalytic sufficiency.

D-sedoheptulose 7-phosphate isomerase
MetaCyc:CPLX0-7660
  • MetaCyc:CPLX0-7660

    Source assertion: The native assembly contains 4 copies of G6106-MONOMER.

    Source locationProtein[@frameid="CPLX0-7660"]/component/Protein; component/coefficient
  • MetaCyc:G6106-MONOMER

    Source assertion: G6106-MONOMER explicitly unifies with UniProt P63224; the native organism is E. coli K-12 MG1655.

    Source locationProtein[@frameid="G6106-MONOMER"]/dblink[dblink-db="UNIPROT"]; species/Organism
  • UniProtKB:P63224

    Source assertion: SUBUNIT gives the 4-subunit homo-assembly with ECO:0000269 literature evidence.

    Source location/comments/5
  • PMID:18056714

    Source assertion: Current curated assembly evidence cites the GmhA structural study; the inspected abstract describes quaternary rearrangement but does not independently specify tetramer stoichiometry.

    Source location/resultList/result[id="18056714"]/abstractText
Bifunctional protein HldE
UniProtKB:P76658
part_of

The native complex contains 2 identical subunits; the protein node is not independently assigned monomeric catalytic sufficiency.

fused heptose 7-phosphate kinase/heptose 1-phosphate adenyltransferase
MetaCyc:CPLX0-3661
  • MetaCyc:CPLX0-3661

    Source assertion: The native assembly contains 2 copies of G7590-MONOMER.

    Source locationProtein[@frameid="CPLX0-3661"]/component/Protein; component/coefficient
  • MetaCyc:G7590-MONOMER

    Source assertion: G7590-MONOMER explicitly unifies with UniProt P76658; the native organism is E. coli K-12 MG1655.

    Source locationProtein[@frameid="G7590-MONOMER"]/dblink[dblink-db="UNIPROT"]; species/Organism
  • UniProtKB:P76658

    Source assertion: SUBUNIT gives the 2-subunit homo-assembly with ECO:0000269 literature evidence.

    Source location/comments/7
  • PMID:16030223

    Source assertion: Copurification and dominant-negative experiments support a functional HldE dimer. The gel-filtration dimer measurement in the abstract is specifically the isolated HldE1 kinase domain, not an independently repeated full-length HldE measurement.

    Source location/resultList/result[id="16030223"]/abstractText
ADP-L-glycero-D-manno-heptose-6-epimerase
UniProtKB:P67910
part_of

The native complex contains 5 identical subunits; the protein node is not independently assigned monomeric catalytic sufficiency.

ADP-L-glycero-D-mannoheptose 6-epimerase
MetaCyc:CPLX0-3681
  • MetaCyc:CPLX0-3681

    Source assertion: The native assembly contains 5 copies of EG10838-MONOMER.

    Source locationProtein[@frameid="CPLX0-3681"]/component/Protein; component/coefficient
  • MetaCyc:EG10838-MONOMER

    Source assertion: EG10838-MONOMER explicitly unifies with UniProt P67910; the native organism is E. coli K-12 MG1655.

    Source locationProtein[@frameid="EG10838-MONOMER"]/dblink[dblink-db="UNIPROT"]; species/Organism
  • UniProtKB:P67910

    Source assertion: SUBUNIT gives the 5-subunit homo-assembly with ECO:0000269 literature evidence.

    Source location/comments/7
  • PMID:10896473

    Source assertion: The primary structure is a homopentamer with two pentamers in the crystallographic asymmetric unit; that is not evidence for a physiological decamer. Earlier apparent native mass does not itself resolve this stoichiometry.

    Source location/resultList/result[id="10896473"]/abstractText
D-sedoheptulose 7-phosphate isomerase
MetaCyc:CPLX0-7660
has_cofactor

Similarity-based cofactor annotation is retained with its evidence grade; no direct K-12 zinc requirement is inferred.

zinc(2+)
CHEBI:29105
  • UniProtKB:P63224

    Source assertion: COFACTOR annotates Zn(2+) and one zinc ion per subunit with ECO:0000250, an inference by similarity rather than direct evidence for zinc binding in this K-12 protein.

    Source location/comments/2/cofactors; /comments/2/note
D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase
UniProtKB:P63228
has_cofactor

Catalytic divalent-metal alternatives are not simultaneous required occupancy. Dominant in vivo metal is not established by these annotations.

magnesium(2+)
CHEBI:18420
  • UniProtKB:P63228

    Source assertion: COFACTOR explicitly includes Mg(2+); the note names magnesium and manganese/cobalt alternatives with ECO:0000269 PMID:16990279.

    Source location/comments/2/cofactors; /comments/2/note
  • PMID:20050614

    Source assertion: The E. coli GmhB substrate/product structures show the catalytic Mg coordination site. It is distinct from the Zn-binding loop site.

    Source locationPMC2844806 BioC passages offsets15508,16641,17361; Figures 3-5
D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase
UniProtKB:P63228
has_cofactor

Catalytic divalent-metal alternatives are not simultaneous required occupancy. Dominant in vivo metal is not established by these annotations.

manganese(2+)
CHEBI:29035
  • UniProtKB:P63228

    Source assertion: COFACTOR explicitly includes Mn(2+); the note names magnesium and manganese/cobalt alternatives with ECO:0000269 PMID:16990279.

    Source location/comments/2/cofactors; /comments/2/note
D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase
UniProtKB:P63228
has_cofactor

Catalytic divalent-metal alternatives are not simultaneous required occupancy. Dominant in vivo metal is not established by these annotations.

cobalt(2+)
CHEBI:48828
  • UniProtKB:P63228

    Source assertion: COFACTOR explicitly includes Co(2+); the note names magnesium and manganese/cobalt alternatives with ECO:0000269 PMID:16990279.

    Source location/comments/2/cofactors; /comments/2/note
D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase
UniProtKB:P63228
has_cofactor

This bound Zn site is distinct from catalytic Mg. No universal Zn requirement or established physiological regulatory role is asserted.

zinc(2+)
CHEBI:29105
  • UniProtKB:P63228

    Source assertion: A separate COFACTOR statement annotates Zn(2+) with ECO:0000269 PMID:16990279.

    Source location/comments/3/cofactors
  • PMID:20050614

    Source assertion: E. coli GmhB has a Zn-bound loop; Zn does not contact substrate or directly participate in catalysis in the inspected structure. Mutating coordinating residues is detrimental, but the paper leaves the origin and function of the motif unresolved.

    Source locationPMC2844806 BioC passages offsets20251,21102,23631; Figure 6
ADP-L-glycero-D-mannoheptose 6-epimerase
MetaCyc:CPLX0-3681
has_cofactor

NADP is the physiological bound cofactor; NAD is an alternative with lower activity. Neither is consumed in the balanced net epimerization.

NADP(3-)
CHEBI:58349
  • UniProtKB:P67910

    Source assertion: COFACTOR includes NADP(+); the note specifies one NADP per subunit and reduced activity when NAD substitutes, with experimental ECO:0000269 citations.

    Source location/comments/2/cofactors; /comments/2/note
  • PMID:11313358

    Source assertion: Apoenzyme reconstitution accepts NADP or NAD, but not FAD. Purified-enzyme extract analysis identifies NADP in vivo, refining the earlier NAD-only assignment.

    Source location/resultList/result[id="11313358"]/abstractText
  • PMID:17316025

    Source assertion: The E. coli K-12 mechanistic study describes initial C6 oxidation by bound NADP and subsequent reduction of the rotated keto intermediate; this is cofactor recycling during epimerization.

    Source location/resultList/result[id="17316025"]/abstractText
ADP-L-glycero-D-mannoheptose 6-epimerase
MetaCyc:CPLX0-3681
has_cofactor

NADP is the physiological bound cofactor; NAD is an alternative with lower activity. Neither is consumed in the balanced net epimerization.

NAD(1-)
CHEBI:57540
  • UniProtKB:P67910

    Source assertion: COFACTOR includes NAD(+); the note specifies one NADP per subunit and reduced activity when NAD substitutes, with experimental ECO:0000269 citations.

    Source location/comments/2/cofactors; /comments/2/note
  • PMID:11313358

    Source assertion: Apoenzyme reconstitution accepts NADP or NAD, but not FAD. Purified-enzyme extract analysis identifies NADP in vivo, refining the earlier NAD-only assignment.

    Source location/resultList/result[id="11313358"]/abstractText
  • PMID:17316025

    Source assertion: The E. coli K-12 mechanistic study describes initial C6 oxidation by bound NADP and subsequent reduction of the rotated keto intermediate; this is cofactor recycling during epimerization.

    Source location/resultList/result[id="17316025"]/abstractText
2 D-sedoheptulose 7-phosphate => D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate
RHEA:27490
part_of

MetaCyc:PWY0-1241
  • MetaCyc:PWY0-1241

    Source assertion: PWY0-1241 explicitly includes RXN0-4301; the native reaction layout selects L2R.

    Source locationPathway[@frameid="PWY0-1241"]/reaction-list; reaction-layout[Reaction/@frameid="RXN0-4301"]/direction
  • MetaCyc:RXN0-4301

    Source assertion: RXN0-4301 has explicit RHEA 27490 unification cross-reference.

    Source locationReaction[@frameid="RXN0-4301"]/dblink[dblink-db="RHEA"]/dblink-oid; dblink-relationship
D-glycero-beta-D-manno-heptose 7-phosphate + ATP => D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP + H(+)
RHEA:27474
part_of

MetaCyc:PWY0-1241
  • MetaCyc:PWY0-1241

    Source assertion: PWY0-1241 explicitly includes RXN0-4341; the native reaction layout selects L2R.

    Source locationPathway[@frameid="PWY0-1241"]/reaction-list; reaction-layout[Reaction/@frameid="RXN0-4341"]/direction
  • MetaCyc:RXN0-4341

    Source assertion: RXN0-4341 has explicit RHEA 27474 unification cross-reference.

    Source locationReaction[@frameid="RXN0-4341"]/dblink[dblink-db="RHEA"]/dblink-oid; dblink-relationship
D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O => D-glycero-beta-D-manno-heptose 1-phosphate + phosphate
RHEA:28519
part_of

MetaCyc:PWY0-1241
  • MetaCyc:PWY0-1241

    Source assertion: PWY0-1241 explicitly includes RXN0-4361; the native reaction layout selects L2R.

    Source locationPathway[@frameid="PWY0-1241"]/reaction-list; reaction-layout[Reaction/@frameid="RXN0-4361"]/direction
  • MetaCyc:RXN0-4361

    Source assertion: RXN0-4361 has explicit RHEA 28519 unification cross-reference.

    Source locationReaction[@frameid="RXN0-4361"]/dblink[dblink-db="RHEA"]/dblink-oid; dblink-relationship
D-glycero-beta-D-manno-heptose 1-phosphate + ATP + H(+) => ADP-D-glycero-beta-D-manno-heptose + diphosphate
RHEA:27466
part_of

MetaCyc:PWY0-1241
  • MetaCyc:PWY0-1241

    Source assertion: PWY0-1241 explicitly includes RXN0-4342; the native reaction layout selects L2R.

    Source locationPathway[@frameid="PWY0-1241"]/reaction-list; reaction-layout[Reaction/@frameid="RXN0-4342"]/direction
  • MetaCyc:RXN0-4342

    Source assertion: RXN0-4342 has explicit RHEA 27466 unification cross-reference.

    Source locationReaction[@frameid="RXN0-4342"]/dblink[dblink-db="RHEA"]/dblink-oid; dblink-relationship
ADP-D-glycero-beta-D-manno-heptose => ADP-L-glycero-beta-D-manno-heptose
RHEA:17578
part_of

MetaCyc:PWY0-1241
  • MetaCyc:PWY0-1241

    Source assertion: PWY0-1241 explicitly includes 5.1.3.20-RXN; the native reaction layout selects L2R.

    Source locationPathway[@frameid="PWY0-1241"]/reaction-list; reaction-layout[Reaction/@frameid="5.1.3.20-RXN"]/direction
  • MetaCyc:5.1.3.20-RXN

    Source assertion: 5.1.3.20-RXN has explicit RHEA 17578 unification cross-reference.

    Source locationReaction[@frameid="5.1.3.20-RXN"]/dblink[dblink-db="RHEA"]/dblink-oid; dblink-relationship
2 D-sedoheptulose 7-phosphate => D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate
RHEA:27490
provides_input_for

A shared chemical and native predecessor relation establish this sequence; no physical channeling or obligatory enzyme complex is inferred.

D-glycero-beta-D-manno-heptose 7-phosphate + ATP => D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP + H(+)
RHEA:27474
  • MetaCyc:PWY0-1241

    Source assertion: RXN0-4341 has RXN0-4301 as its explicit predecessor in PWY0-1241.

    Source locationPathway[@frameid="PWY0-1241"]/reaction-ordering
  • RHEA:27490

    Source assertion: RHEA:27490 produces CHEBI:60204, the shared intermediate consumed by the next selected reaction.

    Source locationhttp://rdf.rhea-db.org/27490 rh:products; rh:contains1
  • RHEA:27474

    Source assertion: RHEA:27474 consumes CHEBI:60204.

    Source locationhttp://rdf.rhea-db.org/27474 rh:substrates; rh:contains1
D-glycero-beta-D-manno-heptose 7-phosphate + ATP => D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP + H(+)
RHEA:27474
provides_input_for

A shared chemical and native predecessor relation establish this sequence; no physical channeling or obligatory enzyme complex is inferred.

D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O => D-glycero-beta-D-manno-heptose 1-phosphate + phosphate
RHEA:28519
  • MetaCyc:PWY0-1241

    Source assertion: RXN0-4361 has RXN0-4341 as its explicit predecessor in PWY0-1241.

    Source locationPathway[@frameid="PWY0-1241"]/reaction-ordering
  • RHEA:27474

    Source assertion: RHEA:27474 produces CHEBI:60208, the shared intermediate consumed by the next selected reaction.

    Source locationhttp://rdf.rhea-db.org/27474 rh:products; rh:contains1
  • RHEA:28519

    Source assertion: RHEA:28519 consumes CHEBI:60208.

    Source locationhttp://rdf.rhea-db.org/28519 rh:substrates; rh:contains1
D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O => D-glycero-beta-D-manno-heptose 1-phosphate + phosphate
RHEA:28519
provides_input_for

A shared chemical and native predecessor relation establish this sequence; no physical channeling or obligatory enzyme complex is inferred.

D-glycero-beta-D-manno-heptose 1-phosphate + ATP + H(+) => ADP-D-glycero-beta-D-manno-heptose + diphosphate
RHEA:27466
  • MetaCyc:PWY0-1241

    Source assertion: RXN0-4342 has RXN0-4361 as its explicit predecessor in PWY0-1241.

    Source locationPathway[@frameid="PWY0-1241"]/reaction-ordering
  • RHEA:28519

    Source assertion: RHEA:28519 produces CHEBI:61593, the shared intermediate consumed by the next selected reaction.

    Source locationhttp://rdf.rhea-db.org/28519 rh:products; rh:contains1
  • RHEA:27466

    Source assertion: RHEA:27466 consumes CHEBI:61593.

    Source locationhttp://rdf.rhea-db.org/27466 rh:substrates; rh:contains1
D-glycero-beta-D-manno-heptose 1-phosphate + ATP + H(+) => ADP-D-glycero-beta-D-manno-heptose + diphosphate
RHEA:27466
provides_input_for

A shared chemical and native predecessor relation establish this sequence; no physical channeling or obligatory enzyme complex is inferred.

ADP-D-glycero-beta-D-manno-heptose => ADP-L-glycero-beta-D-manno-heptose
RHEA:17578
  • MetaCyc:PWY0-1241

    Source assertion: 5.1.3.20-RXN has RXN0-4342 as its explicit predecessor in PWY0-1241.

    Source locationPathway[@frameid="PWY0-1241"]/reaction-ordering
  • RHEA:27466

    Source assertion: RHEA:27466 produces CHEBI:59967, the shared intermediate consumed by the next selected reaction.

    Source locationhttp://rdf.rhea-db.org/27466 rh:products; rh:contains1
  • RHEA:17578

    Source assertion: RHEA:17578 consumes CHEBI:59967.

    Source locationhttp://rdf.rhea-db.org/17578 rh:substrates; rh:contains1

References

Curation history