7-cyano-7-deazaguanine biosynthetic process

GO:0097288

The complete four-transformation route from GTP to preQ0 in Escherichia coli K-12, independently defined by MetaCyc PWY-6703. FolE and QueD form dihydroneopterin triphosphate and carboxytetrahydropterin, QueE contracts the ring to carboxydeazaguanine, and QueC forms the nitrile. Current Rhea chemistry assigns two ATP-to-AMP activations to the QueC net step, superseding the obsolete one-ATP/ADP accounting in the retained native releases. The net QueE reaction regenerates SAM; radical activation and its physiological electron donor are not additional stoichiometric transformations here. Direct E. coli FolE/QueD assays, mixed-species pathway reconstruction, E. coli genetics and inferred K-12 QueE/QueC activities are distinguished. The native QueD hexamer represents a crystallographic assembly; reviewed solution trimers and dodecamers remain an unresolved assembly difference. The pathway ends at free preQ0: its reduction to preQ1, tRNA incorporation, queuosine maturation, transport and antibiotic branches are separate processes. Anaerobic purified-enzyme assay conditions protect oxygen-sensitive intermediates and clusters and do not establish that the cellular pathway operates only anaerobically.

Pathway type
deazapurine biosynthesis
Organism scope

Read the source YAML

Pathway network

29 nodes · 41 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: 7-cyano-7-deazaguanine biosynthetic process 29 nodes · 41 asserted directed edges. Every arrow links to its evidence table row; nodes link to their component details. Isolated declared components are retained. CHEBI:37565 — consumes → RHEA:17474; Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.; Evidence: RHEA:17473consumes CHEBI:15377 — consumes → RHEA:17474; Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.; Evidence: RHEA:17473consumes RHEA:17474 — produces → CHEBI:58462; Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.; Evidence: RHEA:17473produces RHEA:17474 — produces → CHEBI:15740; Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.; Evidence: RHEA:17473produces RHEA:17474 — produces → CHEBI:15378; Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.; Evidence: RHEA:17473produces CHEBI:58462 — consumes → RHEA:27967; Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.; Evidence: RHEA:27966consumes CHEBI:15377 — consumes → RHEA:27967; Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.; Evidence: RHEA:27966consumes RHEA:27967 — produces → CHEBI:61032; Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.; Evidence: RHEA:27966produces RHEA:27967 — produces → CHEBI:18036; Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.; Evidence: RHEA:27966produces RHEA:27967 — produces → CHEBI:15343; Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.; Evidence: RHEA:27966produces RHEA:27967 — produces → CHEBI:15378; Coefficient 2 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.; Evidence: RHEA:27966produces CHEBI:61032 — consumes → RHEA:27975; Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.; Evidence: RHEA:27974consumes CHEBI:15378 — consumes → RHEA:27975; Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.; Evidence: RHEA:27974consumes RHEA:27975 — produces → CHEBI:61036; Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.; Evidence: RHEA:27974produces RHEA:27975 — produces → CHEBI:28938; Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.; Evidence: RHEA:27974produces CHEBI:61036 — consumes → RHEA:27983; Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained. The current two-ATP net equation supersedes the obsolete one-ATP/ADP equation in MetaCyc 22.5 and PathBank; no component reactions are double counted.; Evidence: RHEA:27982consumes CHEBI:28938 — consumes → RHEA:27983; Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained. The current two-ATP net equation supersedes the obsolete one-ATP/ADP equation in MetaCyc 22.5 and PathBank; no component reactions are double counted.; Evidence: RHEA:27982consumes CHEBI:30616 — consumes → RHEA:27983; Coefficient 2 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained. The current two-ATP net equation supersedes the obsolete one-ATP/ADP equation in MetaCyc 22.5 and PathBank; no component reactions are double counted.; Evidence: RHEA:27982consumes RHEA:27983 — produces → CHEBI:45075; Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained. The current two-ATP net equation supersedes the obsolete one-ATP/ADP equation in MetaCyc 22.5 and PathBank; no component reactions are double counted.; Evidence: RHEA:27982produces RHEA:27983 — produces → CHEBI:456215; Coefficient 2 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained. The current two-ATP net equation supersedes the obsolete one-ATP/ADP equation in MetaCyc 22.5 and PathBank; no component reactions are double counted.; Evidence: RHEA:27982produces RHEA:27983 — produces → CHEBI:33019; Coefficient 2 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained. The current two-ATP net equation supersedes the obsolete one-ATP/ADP equation in MetaCyc 22.5 and PathBank; no component reactions are double counted.; Evidence: RHEA:27982produces RHEA:27983 — produces → CHEBI:15378; Coefficient 2 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained. The current two-ATP net equation supersedes the obsolete one-ATP/ADP equation in MetaCyc 22.5 and PathBank; no component reactions are double counted.; Evidence: RHEA:27982produces UniProtKB:P0A6T5 — part_of → MetaCyc:FOLE-CPLX; FolE is a subunit of the independently identified native homodecamer; ten polypeptides form the assembly.; Evidence: MetaCyc:FOLE-CPLX, UniProtKB:P0A6T5part of UniProtKB:P65870 — part_of → MetaCyc:CPLX0-8123; The selected native QueD assembly contains six subunits and corresponds to the crystallographic hexamer. Reviewed UniProt also reports trimers and dodecamers in solution; this edge does not assert a unique assembly under all conditions.; Evidence: MetaCyc:CPLX0-8123, MetaCyc:G7431-MONOMER, UniProtKB:P65870part of MetaCyc:FOLE-CPLX — catalyzes → RHEA:17474; The FolE assembly provides the first transformation shared with folate and other pterin pathways.; Evidence: MetaCyc:FOLE-CPLX, UniProtKB:P0A6T5, PMID:19231875catalyzes MetaCyc:CPLX0-8123 — catalyzes → RHEA:27967; QueD forms carboxytetrahydropterin, not the mammalian pyruvoyltetrahydropterin product. The native crystallographic assembly is retained without excluding other solution assemblies.; Evidence: MetaCyc:CPLX0-8123, UniProtKB:P65870, PMID:19231875catalyzes UniProtKB:P64554 — enables → RHEA:27975; E. coli QueE is assigned this catalytic role by reviewed HAMAP inference, not by transferring a purified Bacillus experiment to E. coli. UniProt infers a homodimer; no monomer sufficiency is asserted. The net reaction does not consume SAM, which is regenerated in the mechanistically characterized Bacillus enzyme.; Evidence: UniProtKB:P64554, PMID:19354300, PMID:23194065enables UniProtKB:P77756 — enables → RHEA:27983; The E. coli QueC gene product is assigned the current two-ATP nitrile-forming net activity by reviewed HAMAP inference. Genetic complementation supports its upstream role; it does not independently measure the exact stoichiometry or establish monomer sufficiency. The two-adenylation mechanism was experimentally resolved for Streptomyces ToyM.; Evidence: UniProtKB:P77756, PMID:16199558, PMID:26228534enables UniProtKB:P0A6T5 — has_cofactor → CHEBI:29105; The FolE protein binds catalytically active zinc; binding-site annotation is not evidence for additional free divalent-metal cofactors.; Evidence: UniProtKB:P0A6T5, MetaCyc:FOLE-CPLXhas cofactor UniProtKB:P65870 — has_cofactor → CHEBI:29105; QueD binds one zinc ion per subunit; the directly measured stoichiometry is approximately one equivalent, rather than proof of one invariant oligomeric state.; Evidence: UniProtKB:P65870, PMID:19231875has cofactor UniProtKB:P64554 — has_cofactor → CHEBI:49883; The E. coli QueE cofactor assignment is explicitly automatic HAMAP inference; direct mechanistic cofactor measurements were made on B. subtilis QueE.; Evidence: UniProtKB:P64554, PMID:23194065has cofactor UniProtKB:P64554 — has_cofactor → CHEBI:59789; The E. coli QueE cofactor assignment is explicitly automatic HAMAP inference; direct mechanistic cofactor measurements were made on B. subtilis QueE. SAM is catalytic and regenerated in that experiment, so it is not a net substrate or product.; Evidence: UniProtKB:P64554, PMID:23194065has cofactor UniProtKB:P64554 — has_cofactor → CHEBI:18420; The E. coli QueE cofactor assignment is explicitly automatic HAMAP inference; direct mechanistic cofactor measurements were made on B. subtilis QueE.; Evidence: UniProtKB:P64554, PMID:23194065has cofactor UniProtKB:P77756 — has_cofactor → CHEBI:29105; QueC zinc binding is a reviewed HAMAP inference for E. coli; the inspected primary zinc measurements concern B. subtilis QueC and S. rimosus ToyM.; Evidence: UniProtKB:P77756, PMID:19354300has cofactor RHEA:17474 — part_of → GO:0097288; This is one complete native transformation in the exact PreQ0-forming process.; Evidence: MetaCyc:PWY-6703, MetaCyc:GTP-CYCLOHYDRO-I-RXN, RHEA:17473, GO:0097288part of RHEA:27967 — part_of → GO:0097288; This is one complete native transformation in the exact PreQ0-forming process.; Evidence: MetaCyc:PWY-6703, MetaCyc:RXN0-5507, RHEA:27966part of RHEA:27975 — part_of → GO:0097288; This is one complete native transformation in the exact PreQ0-forming process.; Evidence: MetaCyc:PWY-6703, MetaCyc:RXN0-6575, RHEA:27974part of RHEA:27983 — part_of → GO:0097288; This is one complete native transformation in the exact PreQ0-forming process. The preserved native cross-reference identifies the updated reaction, but MetaCyc 22.5 retains an obsolete one-ATP/ADP equation; current Rhea 142 supplies the chemistry.; Evidence: MetaCyc:PWY-6703, MetaCyc:RXN-12093, RHEA:27982part of RHEA:17474 — provides_input_for → RHEA:27967; The exact charged intermediate connects the two selected biosynthetic reactions; there is no additional net or decomposition reaction.; Evidence: RHEA:17473, RHEA:27966provides input for RHEA:27967 — provides_input_for → RHEA:27975; The exact charged intermediate connects the two selected biosynthetic reactions; there is no additional net or decomposition reaction.; Evidence: RHEA:27966, RHEA:27974provides input for RHEA:27975 — provides_input_for → RHEA:27983; The exact charged intermediate connects the two selected biosynthetic reactions; there is no additional net or decomposition reaction.; Evidence: RHEA:27974, RHEA:27982provides input for GTP(4-); CHEBI:37565; Declared type: small_molecule small molecule GTP(4-) water; CHEBI:15377; Declared type: small_molecule small molecule water 7,8-dihydroneopterin 3'-triphosphate(4-); CHEBI:58462; Declared type: small_molecule small molecule 7,8-dihydroneopterin 3'-triphosphate(4-) formate; CHEBI:15740; Declared type: small_molecule small molecule formate hydron; CHEBI:15378; Declared type: small_molecule small molecule hydron 5,6,7,8-tetrahydropterin-6-carboxylate; CHEBI:61032; Declared type: small_molecule small molecule 5,6,7,8-tetrahydropterin-6- carboxylate triphosphate(5-); CHEBI:18036; Declared type: small_molecule small molecule triphosphate(5-) acetaldehyde; CHEBI:15343; Declared type: small_molecule small molecule acetaldehyde 7-carboxylato-7-deazaguanine; CHEBI:61036; Declared type: small_molecule small molecule 7-carboxylato-7-deazaguanine ammonium; CHEBI:28938; Declared type: small_molecule small molecule ammonium ATP(4-); CHEBI:30616; Declared type: small_molecule small molecule ATP(4-) 7-cyano-7-deazaguanine; CHEBI:45075; Declared type: small_molecule small molecule 7-cyano-7-deazaguanine adenosine 5'-monophosphate(2-); CHEBI:456215; Declared type: small_molecule small molecule adenosine 5'-monophosphate(2-) diphosphate(3-); CHEBI:33019; Declared type: small_molecule small molecule diphosphate(3-) zinc(2+); CHEBI:29105; Declared type: cofactor cofactor zinc(2+) tetra-mu3-sulfido-tetrairon; CHEBI:49883; Declared type: cofactor cofactor tetra-mu3-sulfido-tetrairon S-adenosyl-L-methionine zwitterion; CHEBI:59789; Declared type: cofactor cofactor S-adenosyl-L-methionine zwitterion magnesium(2+); CHEBI:18420; Declared type: cofactor cofactor magnesium(2+) GTP cyclohydrolase 1; UniProtKB:P0A6T5; Declared type: protein protein GTP cyclohydrolase 1 6-carboxy-5,6,7,8-tetrahydropterin synthase; UniProtKB:P65870; Declared type: protein protein 6-carboxy-5,6,7,8- tetrahydropterin synthase 7-carboxy-7-deazaguanine synthase; UniProtKB:P64554; Declared type: protein protein 7-carboxy-7-deazaguanine synthase 7-cyano-7-deazaguanine synthase; UniProtKB:P77756; Declared type: protein protein 7-cyano-7-deazaguanine synthase GTP cyclohydrolase 1; MetaCyc:FOLE-CPLX; Declared type: complex complex GTP cyclohydrolase 1 6-carboxy-5,6,7,8-tetrahydropterin synthase; MetaCyc:CPLX0-8123; Declared type: complex complex 6-carboxy-5,6,7,8- tetrahydropterin synthase GTP + H2O => 7,8-dihydroneopterin 3'-triphosphate + formate + H(+); RHEA:17474; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity GTP + H2O => 7,8-dihydroneopterin 3'-triphosphate + formate + H(+) 7,8-dihydroneopterin 3'-triphosphate + H2O => 6-carboxy-5,6,7,8-tetrahydropterin + triphosphate + acetaldehyde + 2 H(+); RHEA:27967; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity 7,8-dihydroneopterin 3'-triphosphate + H2O => 6- carboxy-5,6,7,8- tetrahydropterin + triphosphate + acetaldehyde + 2 H(+) 6-carboxy-5,6,7,8-tetrahydropterin + H(+) => 7-carboxy-7-carbaguanine + NH4(+); RHEA:27975; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity 6-carboxy-5,6,7,8- tetrahydropterin + H(+) => 7-carboxy-7-carbaguanine + NH4(+) 7-carboxy-7-carbaguanine + NH4(+) + 2 ATP => 7-cyano-7-carbaguanine + 2 AMP + 2 diphosphate + 2 H(+); RHEA:27983; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity 7-carboxy-7-carbaguanine + NH4(+) + 2 ATP => 7-cyano-7-carbaguanine + 2 AMP + 2 diphosphate + 2 H(+) 7-cyano-7-deazaguanine biosynthetic process; GO:0097288; Declared type: pathway pathway 7-cyano-7-deazaguanine biosynthetic process

Components and activities

Declared biological components and source reaction directions
NodeKind or roleSource direction
Escherichia coli K-12
NCBITaxon:83333		taxon
GTP(4-)
CHEBI:37565		small molecule
water
CHEBI:15377		small molecule
7,8-dihydroneopterin 3'-triphosphate(4-)
CHEBI:58462		small molecule
formate
CHEBI:15740		small molecule
hydron
CHEBI:15378		small molecule
5,6,7,8-tetrahydropterin-6-carboxylate
CHEBI:61032		small molecule
triphosphate(5-)
CHEBI:18036		small molecule
acetaldehyde
CHEBI:15343		small molecule
7-carboxylato-7-deazaguanine
CHEBI:61036		small molecule
ammonium
CHEBI:28938		small molecule
ATP(4-)
CHEBI:30616		small molecule
7-cyano-7-deazaguanine
CHEBI:45075		small molecule
adenosine 5'-monophosphate(2-)
CHEBI:456215		small molecule
diphosphate(3-)
CHEBI:33019		small molecule
zinc(2+)
CHEBI:29105		cofactor
tetra-mu3-sulfido-tetrairon
CHEBI:49883		cofactor
S-adenosyl-L-methionine zwitterion
CHEBI:59789		cofactor
magnesium(2+)
CHEBI:18420		cofactor
GTP cyclohydrolase 1
UniProtKB:P0A6T5		protein
6-carboxy-5,6,7,8-tetrahydropterin synthase
UniProtKB:P65870		protein
7-carboxy-7-deazaguanine synthase
UniProtKB:P64554		protein
7-cyano-7-deazaguanine synthase
UniProtKB:P77756		protein
GTP cyclohydrolase 1
MetaCyc:FOLE-CPLX		complex
6-carboxy-5,6,7,8-tetrahydropterin synthase
MetaCyc:CPLX0-8123		complex
GTP + H2O => 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
RHEA:17474		molecular activityleft to right
7,8-dihydroneopterin 3'-triphosphate + H2O => 6-carboxy-5,6,7,8-tetrahydropterin + triphosphate + acetaldehyde + 2 H(+)
RHEA:27967		molecular activityleft to right
6-carboxy-5,6,7,8-tetrahydropterin + H(+) => 7-carboxy-7-carbaguanine + NH4(+)
RHEA:27975		molecular activityleft to right
7-carboxy-7-carbaguanine + NH4(+) + 2 ATP => 7-cyano-7-carbaguanine + 2 AMP + 2 diphosphate + 2 H(+)
RHEA:27983		molecular activityleft to right

Mechanistic edges

Mechanistic edges and their cited evidence
SubjectPredicate and descriptionObjectEvidence
GTP(4-)
CHEBI:37565		consumes

Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.

GTP + H2O => 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
RHEA:17474
  • RHEA:17473

    Source assertion: RHEA:17474 substrates side 17473_L has coefficient 1 for Participant_17473_compound_6355; its compound accession is CHEBI:37565.

    Source locationhttp://rdf.rhea-db.org/17474 rh:substrates; http://rdf.rhea-db.org/17473_L rh:contains1 http://rdf.rhea-db.org/Participant_17473_compound_6355; rh:compound http://rdf.rhea-db.org/Compound_6355; rh:accession
water
CHEBI:15377		consumes

Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.

GTP + H2O => 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
RHEA:17474
  • RHEA:17473

    Source assertion: RHEA:17474 substrates side 17473_L has coefficient 1 for Participant_17473_compound_1283; its compound accession is CHEBI:15377.

    Source locationhttp://rdf.rhea-db.org/17474 rh:substrates; http://rdf.rhea-db.org/17473_L rh:contains1 http://rdf.rhea-db.org/Participant_17473_compound_1283; rh:compound http://rdf.rhea-db.org/Compound_1283; rh:accession
GTP + H2O => 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
RHEA:17474		produces

Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.

7,8-dihydroneopterin 3'-triphosphate(4-)
CHEBI:58462
  • RHEA:17473

    Source assertion: RHEA:17474 products side 17473_R has coefficient 1 for Participant_17473_compound_2443; its compound accession is CHEBI:58462.

    Source locationhttp://rdf.rhea-db.org/17474 rh:products; http://rdf.rhea-db.org/17473_R rh:contains1 http://rdf.rhea-db.org/Participant_17473_compound_2443; rh:compound http://rdf.rhea-db.org/Compound_2443; rh:accession
GTP + H2O => 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
RHEA:17474		produces

Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.

formate
CHEBI:15740
  • RHEA:17473

    Source assertion: RHEA:17474 products side 17473_R has coefficient 1 for Participant_17473_compound_3001; its compound accession is CHEBI:15740.

    Source locationhttp://rdf.rhea-db.org/17474 rh:products; http://rdf.rhea-db.org/17473_R rh:contains1 http://rdf.rhea-db.org/Participant_17473_compound_3001; rh:compound http://rdf.rhea-db.org/Compound_3001; rh:accession
GTP + H2O => 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
RHEA:17474		produces

Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.

hydron
CHEBI:15378
  • RHEA:17473

    Source assertion: RHEA:17474 products side 17473_R has coefficient 1 for Participant_17473_compound_3249; its compound accession is CHEBI:15378.

    Source locationhttp://rdf.rhea-db.org/17474 rh:products; http://rdf.rhea-db.org/17473_R rh:contains1 http://rdf.rhea-db.org/Participant_17473_compound_3249; rh:compound http://rdf.rhea-db.org/Compound_3249; rh:accession
7,8-dihydroneopterin 3'-triphosphate(4-)
CHEBI:58462		consumes

Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.

7,8-dihydroneopterin 3'-triphosphate + H2O => 6-carboxy-5,6,7,8-tetrahydropterin + triphosphate + acetaldehyde + 2 H(+)
RHEA:27967
  • RHEA:27966

    Source assertion: RHEA:27967 substrates side 27966_L has coefficient 1 for Participant_27966_compound_2443; its compound accession is CHEBI:58462.

    Source locationhttp://rdf.rhea-db.org/27967 rh:substrates; http://rdf.rhea-db.org/27966_L rh:contains1 http://rdf.rhea-db.org/Participant_27966_compound_2443; rh:compound http://rdf.rhea-db.org/Compound_2443; rh:accession
water
CHEBI:15377		consumes

Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.

7,8-dihydroneopterin 3'-triphosphate + H2O => 6-carboxy-5,6,7,8-tetrahydropterin + triphosphate + acetaldehyde + 2 H(+)
RHEA:27967
  • RHEA:27966

    Source assertion: RHEA:27967 substrates side 27966_L has coefficient 1 for Participant_27966_compound_1283; its compound accession is CHEBI:15377.

    Source locationhttp://rdf.rhea-db.org/27967 rh:substrates; http://rdf.rhea-db.org/27966_L rh:contains1 http://rdf.rhea-db.org/Participant_27966_compound_1283; rh:compound http://rdf.rhea-db.org/Compound_1283; rh:accession
7,8-dihydroneopterin 3'-triphosphate + H2O => 6-carboxy-5,6,7,8-tetrahydropterin + triphosphate + acetaldehyde + 2 H(+)
RHEA:27967		produces

Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.

5,6,7,8-tetrahydropterin-6-carboxylate
CHEBI:61032
  • RHEA:27966

    Source assertion: RHEA:27967 products side 27966_R has coefficient 1 for Participant_27966_compound_6305; its compound accession is CHEBI:61032.

    Source locationhttp://rdf.rhea-db.org/27967 rh:products; http://rdf.rhea-db.org/27966_R rh:contains1 http://rdf.rhea-db.org/Participant_27966_compound_6305; rh:compound http://rdf.rhea-db.org/Compound_6305; rh:accession
7,8-dihydroneopterin 3'-triphosphate + H2O => 6-carboxy-5,6,7,8-tetrahydropterin + triphosphate + acetaldehyde + 2 H(+)
RHEA:27967		produces

Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.

triphosphate(5-)
CHEBI:18036
  • RHEA:27966

    Source assertion: RHEA:27967 products side 27966_R has coefficient 1 for Participant_27966_compound_5288; its compound accession is CHEBI:18036.

    Source locationhttp://rdf.rhea-db.org/27967 rh:products; http://rdf.rhea-db.org/27966_R rh:contains1 http://rdf.rhea-db.org/Participant_27966_compound_5288; rh:compound http://rdf.rhea-db.org/Compound_5288; rh:accession
7,8-dihydroneopterin 3'-triphosphate + H2O => 6-carboxy-5,6,7,8-tetrahydropterin + triphosphate + acetaldehyde + 2 H(+)
RHEA:27967		produces

Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.

acetaldehyde
CHEBI:15343
  • RHEA:27966

    Source assertion: RHEA:27967 products side 27966_R has coefficient 1 for Participant_27966_compound_3952; its compound accession is CHEBI:15343.

    Source locationhttp://rdf.rhea-db.org/27967 rh:products; http://rdf.rhea-db.org/27966_R rh:contains1 http://rdf.rhea-db.org/Participant_27966_compound_3952; rh:compound http://rdf.rhea-db.org/Compound_3952; rh:accession
7,8-dihydroneopterin 3'-triphosphate + H2O => 6-carboxy-5,6,7,8-tetrahydropterin + triphosphate + acetaldehyde + 2 H(+)
RHEA:27967		produces

Coefficient 2 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.

hydron
CHEBI:15378
  • RHEA:27966

    Source assertion: RHEA:27967 products side 27966_R has coefficient 2 for Participant_27966_compound_3249; its compound accession is CHEBI:15378.

    Source locationhttp://rdf.rhea-db.org/27967 rh:products; http://rdf.rhea-db.org/27966_R rh:contains2 http://rdf.rhea-db.org/Participant_27966_compound_3249; rh:compound http://rdf.rhea-db.org/Compound_3249; rh:accession
5,6,7,8-tetrahydropterin-6-carboxylate
CHEBI:61032		consumes

Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.

6-carboxy-5,6,7,8-tetrahydropterin + H(+) => 7-carboxy-7-carbaguanine + NH4(+)
RHEA:27975
  • RHEA:27974

    Source assertion: RHEA:27975 substrates side 27974_L has coefficient 1 for Participant_27974_compound_6305; its compound accession is CHEBI:61032.

    Source locationhttp://rdf.rhea-db.org/27975 rh:substrates; http://rdf.rhea-db.org/27974_L rh:contains1 http://rdf.rhea-db.org/Participant_27974_compound_6305; rh:compound http://rdf.rhea-db.org/Compound_6305; rh:accession
hydron
CHEBI:15378		consumes

Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.

6-carboxy-5,6,7,8-tetrahydropterin + H(+) => 7-carboxy-7-carbaguanine + NH4(+)
RHEA:27975
  • RHEA:27974

    Source assertion: RHEA:27975 substrates side 27974_L has coefficient 1 for Participant_27974_compound_3249; its compound accession is CHEBI:15378.

    Source locationhttp://rdf.rhea-db.org/27975 rh:substrates; http://rdf.rhea-db.org/27974_L rh:contains1 http://rdf.rhea-db.org/Participant_27974_compound_3249; rh:compound http://rdf.rhea-db.org/Compound_3249; rh:accession
6-carboxy-5,6,7,8-tetrahydropterin + H(+) => 7-carboxy-7-carbaguanine + NH4(+)
RHEA:27975		produces

Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.

7-carboxylato-7-deazaguanine
CHEBI:61036
  • RHEA:27974

    Source assertion: RHEA:27975 products side 27974_R has coefficient 1 for Participant_27974_compound_6307; its compound accession is CHEBI:61036.

    Source locationhttp://rdf.rhea-db.org/27975 rh:products; http://rdf.rhea-db.org/27974_R rh:contains1 http://rdf.rhea-db.org/Participant_27974_compound_6307; rh:compound http://rdf.rhea-db.org/Compound_6307; rh:accession
6-carboxy-5,6,7,8-tetrahydropterin + H(+) => 7-carboxy-7-carbaguanine + NH4(+)
RHEA:27975		produces

Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained.

ammonium
CHEBI:28938
  • RHEA:27974

    Source assertion: RHEA:27975 products side 27974_R has coefficient 1 for Participant_27974_compound_1012; its compound accession is CHEBI:28938.

    Source locationhttp://rdf.rhea-db.org/27975 rh:products; http://rdf.rhea-db.org/27974_R rh:contains1 http://rdf.rhea-db.org/Participant_27974_compound_1012; rh:compound http://rdf.rhea-db.org/Compound_1012; rh:accession
7-carboxylato-7-deazaguanine
CHEBI:61036		consumes

Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained. The current two-ATP net equation supersedes the obsolete one-ATP/ADP equation in MetaCyc 22.5 and PathBank; no component reactions are double counted.

7-carboxy-7-carbaguanine + NH4(+) + 2 ATP => 7-cyano-7-carbaguanine + 2 AMP + 2 diphosphate + 2 H(+)
RHEA:27983
  • RHEA:27982

    Source assertion: RHEA:27983 substrates side 27982_L has coefficient 1 for Participant_27982_compound_6307; its compound accession is CHEBI:61036.

    Source locationhttp://rdf.rhea-db.org/27983 rh:substrates; http://rdf.rhea-db.org/27982_L rh:contains1 http://rdf.rhea-db.org/Participant_27982_compound_6307; rh:compound http://rdf.rhea-db.org/Compound_6307; rh:accession
ammonium
CHEBI:28938		consumes

Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained. The current two-ATP net equation supersedes the obsolete one-ATP/ADP equation in MetaCyc 22.5 and PathBank; no component reactions are double counted.

7-carboxy-7-carbaguanine + NH4(+) + 2 ATP => 7-cyano-7-carbaguanine + 2 AMP + 2 diphosphate + 2 H(+)
RHEA:27983
  • RHEA:27982

    Source assertion: RHEA:27983 substrates side 27982_L has coefficient 1 for Participant_27982_compound_1012; its compound accession is CHEBI:28938.

    Source locationhttp://rdf.rhea-db.org/27983 rh:substrates; http://rdf.rhea-db.org/27982_L rh:contains1 http://rdf.rhea-db.org/Participant_27982_compound_1012; rh:compound http://rdf.rhea-db.org/Compound_1012; rh:accession
ATP(4-)
CHEBI:30616		consumes

Coefficient 2 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained. The current two-ATP net equation supersedes the obsolete one-ATP/ADP equation in MetaCyc 22.5 and PathBank; no component reactions are double counted.

7-carboxy-7-carbaguanine + NH4(+) + 2 ATP => 7-cyano-7-carbaguanine + 2 AMP + 2 diphosphate + 2 H(+)
RHEA:27983
  • RHEA:27982

    Source assertion: RHEA:27983 substrates side 27982_L has coefficient 2 for Participant_27982_compound_6372; its compound accession is CHEBI:30616.

    Source locationhttp://rdf.rhea-db.org/27983 rh:substrates; http://rdf.rhea-db.org/27982_L rh:contains2 http://rdf.rhea-db.org/Participant_27982_compound_6372; rh:compound http://rdf.rhea-db.org/Compound_6372; rh:accession
7-carboxy-7-carbaguanine + NH4(+) + 2 ATP => 7-cyano-7-carbaguanine + 2 AMP + 2 diphosphate + 2 H(+)
RHEA:27983		produces

Coefficient 1 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained. The current two-ATP net equation supersedes the obsolete one-ATP/ADP equation in MetaCyc 22.5 and PathBank; no component reactions are double counted.

7-cyano-7-deazaguanine
CHEBI:45075
  • RHEA:27982

    Source assertion: RHEA:27983 products side 27982_R has coefficient 1 for Participant_27982_compound_5843; its compound accession is CHEBI:45075.

    Source locationhttp://rdf.rhea-db.org/27983 rh:products; http://rdf.rhea-db.org/27982_R rh:contains1 http://rdf.rhea-db.org/Participant_27982_compound_5843; rh:compound http://rdf.rhea-db.org/Compound_5843; rh:accession
7-carboxy-7-carbaguanine + NH4(+) + 2 ATP => 7-cyano-7-carbaguanine + 2 AMP + 2 diphosphate + 2 H(+)
RHEA:27983		produces

Coefficient 2 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained. The current two-ATP net equation supersedes the obsolete one-ATP/ADP equation in MetaCyc 22.5 and PathBank; no component reactions are double counted.

adenosine 5'-monophosphate(2-)
CHEBI:456215
  • RHEA:27982

    Source assertion: RHEA:27983 products side 27982_R has coefficient 2 for Participant_27982_compound_2590; its compound accession is CHEBI:456215.

    Source locationhttp://rdf.rhea-db.org/27983 rh:products; http://rdf.rhea-db.org/27982_R rh:contains2 http://rdf.rhea-db.org/Participant_27982_compound_2590; rh:compound http://rdf.rhea-db.org/Compound_2590; rh:accession
7-carboxy-7-carbaguanine + NH4(+) + 2 ATP => 7-cyano-7-carbaguanine + 2 AMP + 2 diphosphate + 2 H(+)
RHEA:27983		produces

Coefficient 2 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained. The current two-ATP net equation supersedes the obsolete one-ATP/ADP equation in MetaCyc 22.5 and PathBank; no component reactions are double counted.

diphosphate(3-)
CHEBI:33019
  • RHEA:27982

    Source assertion: RHEA:27983 products side 27982_R has coefficient 2 for Participant_27982_compound_2106; its compound accession is CHEBI:33019.

    Source locationhttp://rdf.rhea-db.org/27983 rh:products; http://rdf.rhea-db.org/27982_R rh:contains2 http://rdf.rhea-db.org/Participant_27982_compound_2106; rh:compound http://rdf.rhea-db.org/Compound_2106; rh:accession
7-carboxy-7-carbaguanine + NH4(+) + 2 ATP => 7-cyano-7-carbaguanine + 2 AMP + 2 diphosphate + 2 H(+)
RHEA:27983		produces

Coefficient 2 in the selected Rhea 142 biosynthetic direction; the exact charge form is retained. The current two-ATP net equation supersedes the obsolete one-ATP/ADP equation in MetaCyc 22.5 and PathBank; no component reactions are double counted.

hydron
CHEBI:15378
  • RHEA:27982

    Source assertion: RHEA:27983 products side 27982_R has coefficient 2 for Participant_27982_compound_3249; its compound accession is CHEBI:15378.

    Source locationhttp://rdf.rhea-db.org/27983 rh:products; http://rdf.rhea-db.org/27982_R rh:contains2 http://rdf.rhea-db.org/Participant_27982_compound_3249; rh:compound http://rdf.rhea-db.org/Compound_3249; rh:accession
GTP cyclohydrolase 1
UniProtKB:P0A6T5		part_of

FolE is a subunit of the independently identified native homodecamer; ten polypeptides form the assembly.

GTP cyclohydrolase 1
MetaCyc:FOLE-CPLX
  • MetaCyc:FOLE-CPLX

    Source assertion: FOLE-CPLX contains ten copies of GTP-CYCLOHYDRO-I-MONOMER.

    Source locationProtein[@frameid="FOLE-CPLX"]/component/Protein; component/coefficient
  • UniProtKB:P0A6T5

    Source assertion: The reviewed entry explicitly cross-references MetaCyc:GTP-CYCLOHYDRO-I-MONOMER and annotates a toroid-shaped homodecamer, with ECO:0000269 citations.

    Source locationuniProtKBCrossReferences[database="BioCyc"]; comments[3]
6-carboxy-5,6,7,8-tetrahydropterin synthase
UniProtKB:P65870		part_of

The selected native QueD assembly contains six subunits and corresponds to the crystallographic hexamer. Reviewed UniProt also reports trimers and dodecamers in solution; this edge does not assert a unique assembly under all conditions.

6-carboxy-5,6,7,8-tetrahydropterin synthase
MetaCyc:CPLX0-8123
  • MetaCyc:CPLX0-8123

    Source assertion: CPLX0-8123 contains six copies of G7431-MONOMER and describes a hexamer of interacting trimers.

    Source locationProtein[@frameid="CPLX0-8123"]/component; comment
  • MetaCyc:G7431-MONOMER

    Source assertion: G7431-MONOMER has an explicit UNIPROT unification cross-reference to P65870.

    Source locationProtein[@frameid="G7431-MONOMER"]/dblink[dblink-db="UNIPROT"]
  • UniProtKB:P65870

    Source assertion: The reviewed entry reports homotrimers and homododecamers in solution (PMID:24816091), and six active sites at trimer interfaces in the crystal homohexamer (PMID:24990950); both are ECO:0000269 statements.

    Source locationcomments[7]; comments[8]
GTP cyclohydrolase 1
MetaCyc:FOLE-CPLX		catalyzes

The FolE assembly provides the first transformation shared with folate and other pterin pathways.

GTP + H2O => 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
RHEA:17474
  • MetaCyc:FOLE-CPLX

    Source assertion: FOLE-CPLX catalyzes GTP-CYCLOHYDRO-I-RXN through GTP-CYCLOHYDRO-I-ENZRXN.

    Source locationProtein/catalyzes/Enzymatic-Reaction/reaction
  • UniProtKB:P0A6T5

    Source assertion: The reviewed catalytic activity names RHEA:17473, GTP hydrolysis to dihydroneopterin triphosphate, formate and H+.

    Source locationcomments[0]/reaction
  • PMID:19231875

    Source assertion: Recombinant E. coli FolE generated dihydroneopterin triphosphate quantitatively from GTP for the QueD assays.

    Source locationPMC3227869 BioC passage[5]; Figure 2A and caption passage[17]
6-carboxy-5,6,7,8-tetrahydropterin synthase
MetaCyc:CPLX0-8123		catalyzes

QueD forms carboxytetrahydropterin, not the mammalian pyruvoyltetrahydropterin product. The native crystallographic assembly is retained without excluding other solution assemblies.

7,8-dihydroneopterin 3'-triphosphate + H2O => 6-carboxy-5,6,7,8-tetrahydropterin + triphosphate + acetaldehyde + 2 H(+)
RHEA:27967
  • MetaCyc:CPLX0-8123

    Source assertion: CPLX0-8123 catalyzes RXN0-5507 through ENZRXN0-6612.

    Source locationProtein/catalyzes/Enzymatic-Reaction/reaction
  • UniProtKB:P65870

    Source assertion: The RHEA:27966 catalytic activity has ECO:0000269 support from PMID:19231875 and PMID:24990950; physiological direction RHEA:27967 is ECO:0000305.

    Source locationcomments[1]/reaction; comments[1]/physiologicalReactions
  • PMID:19231875

    Source assertion: E. coli QueD forms CPH4 from H2NTP; isotope-resolved mass spectra, fragmentation and co-elution with chemically reduced carboxypterin establish product identity.

    Source locationPMC3227869 BioC passages[5-8]; Figure 2D
7-carboxy-7-deazaguanine synthase
UniProtKB:P64554		enables

E. coli QueE is assigned this catalytic role by reviewed HAMAP inference, not by transferring a purified Bacillus experiment to E. coli. UniProt infers a homodimer; no monomer sufficiency is asserted. The net reaction does not consume SAM, which is regenerated in the mechanistically characterized Bacillus enzyme.

6-carboxy-5,6,7,8-tetrahydropterin + H(+) => 7-carboxy-7-carbaguanine + NH4(+)
RHEA:27975
  • UniProtKB:P64554

    Source assertion: The reviewed QueE entry assigns RHEA:27974 and a homodimer with ECO:0000255 HAMAP-Rule MF_00917 evidence.

    Source locationcomments[1]/reaction; comments[6]
  • PMID:19354300

    Source assertion: B. subtilis QueE converted CPH4 to CDG in the mixed-species reconstruction; the cloned and assayed QueE was Bacillus, not the E. coli expression host.

    Source locationPMC2693876 BioC passages[9-14], [34-36]; Figure 2
  • PMID:23194065

    Source assertion: For B. subtilis QueE, product formed in 15-fold excess over supplied SAM, demonstrating regeneration of the cofactor rather than stoichiometric consumption.

    Source locationPMC4022186 BioC passage[58]; Figure 3e
7-cyano-7-deazaguanine synthase
UniProtKB:P77756		enables

The E. coli QueC gene product is assigned the current two-ATP nitrile-forming net activity by reviewed HAMAP inference. Genetic complementation supports its upstream role; it does not independently measure the exact stoichiometry or establish monomer sufficiency. The two-adenylation mechanism was experimentally resolved for Streptomyces ToyM.

7-carboxy-7-carbaguanine + NH4(+) + 2 ATP => 7-cyano-7-carbaguanine + 2 AMP + 2 diphosphate + 2 H(+)
RHEA:27983
  • UniProtKB:P77756

    Source assertion: The current reviewed net RHEA:27982 reaction and physiological RHEA:27983 direction consume two ATP and yield two AMP plus two diphosphate, assigned with ECO:0000255 HAMAP-Rule MF_01633.

    Source locationcomments[1]/reaction; comments[1]/physiologicalReactions
  • PMID:16199558

    Source assertion: Plasmid-borne queC restored Q modification in E. coli B105; mutant analyses place QueC before preQ0, providing genetic evidence rather than a purified E. coli enzyme assay.

    Source locationEurope PMC resultList/result[0]/abstractText
  • PMID:26228534

    Source assertion: Streptomyces rimosus ToyM activates CDG and the amide intermediate through two ATP-dependent half-reactions; AMP and pyrophosphate are produced with both substrates.

    Source locationPMC4767005 BioC passages[3], [5-9]; Figures 3-5
GTP cyclohydrolase 1
UniProtKB:P0A6T5		has_cofactor

The FolE protein binds catalytically active zinc; binding-site annotation is not evidence for additional free divalent-metal cofactors.

zinc(2+)
CHEBI:29105
  • UniProtKB:P0A6T5

    Source assertion: The entry annotates zinc-binding sites at residues 111, 114 and 182 with explicit ChEBI:29105 ligand cross-references.

    Source locationfeatures[2]; features[3]; features[4]
  • MetaCyc:FOLE-CPLX

    Source assertion: The native enzyme comment identifies a catalytically active zinc ion; cited residue numbering differs by one from the current UniProt sequence.

    Source locationProtein[@frameid="FOLE-CPLX"]/comment, paragraph on catalytic zinc
6-carboxy-5,6,7,8-tetrahydropterin synthase
UniProtKB:P65870		has_cofactor

QueD binds one zinc ion per subunit; the directly measured stoichiometry is approximately one equivalent, rather than proof of one invariant oligomeric state.

zinc(2+)
CHEBI:29105
  • UniProtKB:P65870

    Source assertion: QueD binds one zinc per subunit, with ECO:0000269 support from PMID:19231875, PMID:24816091 and PMID:24990950.

    Source locationcomments[4]/cofactors; comments[4]/note
  • PMID:19231875
    revealed the presence of 1.1 equivalents of Zn per monomer.
    Source locationPMC3227869 BioC passage[9]
7-carboxy-7-deazaguanine synthase
UniProtKB:P64554		has_cofactor

The E. coli QueE cofactor assignment is explicitly automatic HAMAP inference; direct mechanistic cofactor measurements were made on B. subtilis QueE.

tetra-mu3-sulfido-tetrairon
CHEBI:49883
  • UniProtKB:P64554

    Source assertion: QueE is annotated with one [4Fe-4S] cluster coordinated by three cysteines and exchangeable SAM; ECO:0000255 HAMAP-Rule MF_00917.

    Source locationcomments[2]/cofactors; comments[2]/note
  • PMID:23194065

    Source assertion: B. subtilis QueE is a homodimer with a [4Fe-4S] cluster per monomer, magnesium dependence and a SAM cofactor regenerated through multiple turnovers.

    Source locationPMC4022186 BioC passage[1]; passages[47], [58], [68]
7-carboxy-7-deazaguanine synthase
UniProtKB:P64554		has_cofactor

The E. coli QueE cofactor assignment is explicitly automatic HAMAP inference; direct mechanistic cofactor measurements were made on B. subtilis QueE. SAM is catalytic and regenerated in that experiment, so it is not a net substrate or product.

S-adenosyl-L-methionine zwitterion
CHEBI:59789
  • UniProtKB:P64554

    Source assertion: QueE is annotated with one S-adenosyl-L-methionine per subunit; ECO:0000255 HAMAP-Rule MF_00917.

    Source locationcomments[3]/cofactors; comments[3]/note
  • PMID:23194065

    Source assertion: B. subtilis QueE is a homodimer with a [4Fe-4S] cluster per monomer, magnesium dependence and a SAM cofactor regenerated through multiple turnovers.

    Source locationPMC4022186 BioC passage[1]; passages[47], [58], [68]
7-carboxy-7-deazaguanine synthase
UniProtKB:P64554		has_cofactor

The E. coli QueE cofactor assignment is explicitly automatic HAMAP inference; direct mechanistic cofactor measurements were made on B. subtilis QueE.

magnesium(2+)
CHEBI:18420
  • UniProtKB:P64554

    Source assertion: QueE is annotated with Mg(2+) as a cofactor; ECO:0000255 HAMAP-Rule MF_00917.

    Source locationcomments[4]/cofactors
  • PMID:23194065

    Source assertion: B. subtilis QueE is a homodimer with a [4Fe-4S] cluster per monomer, magnesium dependence and a SAM cofactor regenerated through multiple turnovers.

    Source locationPMC4022186 BioC passage[1]; passages[47], [58], [68]
7-cyano-7-deazaguanine synthase
UniProtKB:P77756		has_cofactor

QueC zinc binding is a reviewed HAMAP inference for E. coli; the inspected primary zinc measurements concern B. subtilis QueC and S. rimosus ToyM.

zinc(2+)
CHEBI:29105
  • UniProtKB:P77756

    Source assertion: The current entry assigns one zinc per subunit with ECO:0000255 HAMAP-Rule MF_01633.

    Source locationcomments[6]/cofactors; comments[6]/note
  • PMID:19354300

    Source assertion: ICP-OES measured 0.88 zinc equivalents per monomer for B. subtilis QueC and 0.80 for S. rimosus ToyM.

    Source locationPMC2693876 BioC passage[38]
GTP + H2O => 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
RHEA:17474		part_of

This is one complete native transformation in the exact PreQ0-forming process.

GO:0097288
  • MetaCyc:PWY-6703

    Source assertion: PWY-6703 explicitly lists GTP-CYCLOHYDRO-I-RXN among its four reaction members.

    Source locationPathway[@frameid="PWY-6703"]/reaction-list
  • MetaCyc:GTP-CYCLOHYDRO-I-RXN

    Source assertion: The native reaction explicitly cross-references Rhea 17473; its source direction is LEFT-TO-RIGHT.

    Source locationReaction[@frameid="GTP-CYCLOHYDRO-I-RXN"]/dblink[dblink-db="RHEA"]; reaction-direction
  • RHEA:17473

    Source assertion: Master RHEA:17473 declares RHEA:17474 as a directional reaction; the selected full RDF equation is the source for its chemistry.

    Source locationhttp://rdf.rhea-db.org/17473 rh:directionalReaction; http://rdf.rhea-db.org/17474 rh:substrates; rh:products
  • GO:0097288

    Source assertion: GO:0097288 denotes reactions and pathways forming 7-cyano-7-deazaguanine (preQ0), matching the endpoint of the full four-step native route.

    Source locationresults[0]/definition/text
7,8-dihydroneopterin 3'-triphosphate + H2O => 6-carboxy-5,6,7,8-tetrahydropterin + triphosphate + acetaldehyde + 2 H(+)
RHEA:27967		part_of

This is one complete native transformation in the exact PreQ0-forming process.

GO:0097288
  • MetaCyc:PWY-6703

    Source assertion: PWY-6703 explicitly lists RXN0-5507 among its four reaction members.

    Source locationPathway[@frameid="PWY-6703"]/reaction-list
  • MetaCyc:RXN0-5507

    Source assertion: The native reaction explicitly cross-references Rhea 27967; its source direction is LEFT-TO-RIGHT.

    Source locationReaction[@frameid="RXN0-5507"]/dblink[dblink-db="RHEA"]; reaction-direction
  • RHEA:27966

    Source assertion: Master RHEA:27966 declares RHEA:27967 as a directional reaction; the selected full RDF equation is the source for its chemistry.

    Source locationhttp://rdf.rhea-db.org/27966 rh:directionalReaction; http://rdf.rhea-db.org/27967 rh:substrates; rh:products
6-carboxy-5,6,7,8-tetrahydropterin + H(+) => 7-carboxy-7-carbaguanine + NH4(+)
RHEA:27975		part_of

This is one complete native transformation in the exact PreQ0-forming process.

GO:0097288
  • MetaCyc:PWY-6703

    Source assertion: PWY-6703 explicitly lists RXN0-6575 among its four reaction members.

    Source locationPathway[@frameid="PWY-6703"]/reaction-list
  • MetaCyc:RXN0-6575

    Source assertion: The native reaction explicitly cross-references Rhea 27975; its source direction is LEFT-TO-RIGHT.

    Source locationReaction[@frameid="RXN0-6575"]/dblink[dblink-db="RHEA"]; reaction-direction
  • RHEA:27974

    Source assertion: Master RHEA:27974 declares RHEA:27975 as a directional reaction; the selected full RDF equation is the source for its chemistry.

    Source locationhttp://rdf.rhea-db.org/27974 rh:directionalReaction; http://rdf.rhea-db.org/27975 rh:substrates; rh:products
7-carboxy-7-carbaguanine + NH4(+) + 2 ATP => 7-cyano-7-carbaguanine + 2 AMP + 2 diphosphate + 2 H(+)
RHEA:27983		part_of

This is one complete native transformation in the exact PreQ0-forming process. The preserved native cross-reference identifies the updated reaction, but MetaCyc 22.5 retains an obsolete one-ATP/ADP equation; current Rhea 142 supplies the chemistry.

GO:0097288
  • MetaCyc:PWY-6703

    Source assertion: PWY-6703 explicitly lists RXN-12093 among its four reaction members.

    Source locationPathway[@frameid="PWY-6703"]/reaction-list
  • MetaCyc:RXN-12093

    Source assertion: The native reaction explicitly cross-references Rhea 27983; its source direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationReaction[@frameid="RXN-12093"]/dblink[dblink-db="RHEA"]; reaction-direction
  • RHEA:27982

    Source assertion: Master RHEA:27982 declares RHEA:27983 as a directional reaction; the selected full RDF equation is the source for its chemistry. The current equation has two ATP, two AMP and two diphosphate.

    Source locationhttp://rdf.rhea-db.org/27982 rh:directionalReaction; http://rdf.rhea-db.org/27983 rh:substrates; rh:products
GTP + H2O => 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
RHEA:17474		provides_input_for

The exact charged intermediate connects the two selected biosynthetic reactions; there is no additional net or decomposition reaction.

7,8-dihydroneopterin 3'-triphosphate + H2O => 6-carboxy-5,6,7,8-tetrahydropterin + triphosphate + acetaldehyde + 2 H(+)
RHEA:27967
  • RHEA:17473

    Source assertion: RHEA:17474 produces CHEBI:58462.

    Source locationhttp://rdf.rhea-db.org/17474 rh:products; http://rdf.rhea-db.org/17473_R rh:contains1 http://rdf.rhea-db.org/Participant_17473_compound_2443; rh:compound http://rdf.rhea-db.org/Compound_2443; rh:accession
  • RHEA:27966

    Source assertion: RHEA:27967 consumes CHEBI:58462.

    Source locationhttp://rdf.rhea-db.org/27967 rh:substrates; http://rdf.rhea-db.org/27966_L rh:contains1 http://rdf.rhea-db.org/Participant_27966_compound_2443; rh:compound http://rdf.rhea-db.org/Compound_2443; rh:accession
7,8-dihydroneopterin 3'-triphosphate + H2O => 6-carboxy-5,6,7,8-tetrahydropterin + triphosphate + acetaldehyde + 2 H(+)
RHEA:27967		provides_input_for

The exact charged intermediate connects the two selected biosynthetic reactions; there is no additional net or decomposition reaction.

6-carboxy-5,6,7,8-tetrahydropterin + H(+) => 7-carboxy-7-carbaguanine + NH4(+)
RHEA:27975
  • RHEA:27966

    Source assertion: RHEA:27967 produces CHEBI:61032.

    Source locationhttp://rdf.rhea-db.org/27967 rh:products; http://rdf.rhea-db.org/27966_R rh:contains1 http://rdf.rhea-db.org/Participant_27966_compound_6305; rh:compound http://rdf.rhea-db.org/Compound_6305; rh:accession
  • RHEA:27974

    Source assertion: RHEA:27975 consumes CHEBI:61032.

    Source locationhttp://rdf.rhea-db.org/27975 rh:substrates; http://rdf.rhea-db.org/27974_L rh:contains1 http://rdf.rhea-db.org/Participant_27974_compound_6305; rh:compound http://rdf.rhea-db.org/Compound_6305; rh:accession
6-carboxy-5,6,7,8-tetrahydropterin + H(+) => 7-carboxy-7-carbaguanine + NH4(+)
RHEA:27975		provides_input_for

The exact charged intermediate connects the two selected biosynthetic reactions; there is no additional net or decomposition reaction.

7-carboxy-7-carbaguanine + NH4(+) + 2 ATP => 7-cyano-7-carbaguanine + 2 AMP + 2 diphosphate + 2 H(+)
RHEA:27983
  • RHEA:27974

    Source assertion: RHEA:27975 produces CHEBI:61036.

    Source locationhttp://rdf.rhea-db.org/27975 rh:products; http://rdf.rhea-db.org/27974_R rh:contains1 http://rdf.rhea-db.org/Participant_27974_compound_6307; rh:compound http://rdf.rhea-db.org/Compound_6307; rh:accession
  • RHEA:27982

    Source assertion: RHEA:27983 consumes CHEBI:61036.

    Source locationhttp://rdf.rhea-db.org/27983 rh:substrates; http://rdf.rhea-db.org/27982_L rh:contains1 http://rdf.rhea-db.org/Participant_27982_compound_6307; rh:compound http://rdf.rhea-db.org/Compound_6307; rh:accession

References

Curation history