biotin biosynthesis I

MetaCyc:BIOTIN-BIOSYNTHESIS-PWY

The complete 14-reaction BioC/BioH-dependent route in E. coli K-12/MG1655 converts malonyl-ACP through two fatty-acid elongation cycles and BioF/BioA/BioD/BioB ring assembly to biotin. Both native MetaCyc children are retained. The first condensation reaction is present without an assigned catalyst: current inspected evidence excludes the old ACP-incompatible FabH proposal but does not establish a unique FabB/F catalyst. Native downstream FAS assignments retain their indirect evidence grade. Seven intermediate ACP classes have no authoritative empirical formula; all are whole protein states, not isolated reactive residues. Six current Rhea equations provide normalized charge/stereochemistry; eight native FAS equations preserve source orientation and NADH versus NADPH. BioB retains the formal Rhea generic sulfur-carrier/ferredoxin equation, while E. coli primary assays use flavodoxin; no exact physiological donor or cluster-repair cycle is inferred. Selected protein identities are K-12, native complexes MG1655, and primary assays include engineered strains and non-E. coli BioC homologues as explicitly qualified. Malonyl-ACP formation, broader fatty-acid synthesis, BirA ligation/regulation and Fe-S-cluster regeneration lie outside this named pathway.

Pathway type
biotin biosynthesis
Organism scope

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Pathway network

74 nodes · 126 asserted directed edges

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Pathway network: biotin biosynthesis I 74 nodes · 126 asserted directed edges. Every arrow links to its evidence table row; nodes link to their component details. Isolated declared components are retained. RHEA-COMP:9623 — consumes → RHEA:17106; Evidence: RHEA:17106consumes CHEBI:59789 — consumes → RHEA:17106; Evidence: RHEA:17106consumes RHEA:17106 — produces → RHEA-COMP:9954; Evidence: RHEA:17106produces RHEA:17106 — produces → CHEBI:57856; Evidence: RHEA:17106produces RHEA-COMP:9954 — consumes → MetaCyc:RXN-11474; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11474, RHEA:17106consumes RHEA-COMP:9623 — consumes → MetaCyc:RXN-11474; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11474, RHEA:17106consumes CHEBI:15378 — consumes → MetaCyc:RXN-11474; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11474consumes MetaCyc:RXN-11474 — produces → MetaCyc:3-Ketoglutaryl-ACP-methyl-ester; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11474produces MetaCyc:RXN-11474 — produces → CHEBI:16526; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11474produces MetaCyc:RXN-11474 — produces → RHEA-COMP:9685; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11474, RHEA:42289produces MetaCyc:RXN-11476 — produces → MetaCyc:3-Hydroxyglutaryl-ACP-methyl-ester; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11476produces MetaCyc:RXN-11476 — produces → CHEBI:58349; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11476produces MetaCyc:3-Ketoglutaryl-ACP-methyl-ester — consumes → MetaCyc:RXN-11476; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11476consumes CHEBI:57783 — consumes → MetaCyc:RXN-11476; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11476consumes CHEBI:15378 — consumes → MetaCyc:RXN-11476; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11476consumes MetaCyc:3-Hydroxyglutaryl-ACP-methyl-ester — consumes → MetaCyc:RXN-11477; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11477consumes MetaCyc:RXN-11477 — produces → MetaCyc:Enoylglutaryl-ACP-methyl-esters; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11477produces MetaCyc:RXN-11477 — produces → CHEBI:15377; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11477produces MetaCyc:RXN-11478 — produces → MetaCyc:Glutaryl-ACP-methyl-esters; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11478produces MetaCyc:RXN-11478 — produces → CHEBI:57540; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11478produces MetaCyc:Enoylglutaryl-ACP-methyl-esters — consumes → MetaCyc:RXN-11478; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11478consumes CHEBI:57945 — consumes → MetaCyc:RXN-11478; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11478consumes CHEBI:15378 — consumes → MetaCyc:RXN-11478; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11478consumes MetaCyc:Glutaryl-ACP-methyl-esters — consumes → MetaCyc:RXN-11479; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11479consumes RHEA-COMP:9623 — consumes → MetaCyc:RXN-11479; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11479, RHEA:17106consumes CHEBI:15378 — consumes → MetaCyc:RXN-11479; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11479consumes MetaCyc:RXN-11479 — produces → MetaCyc:3-Ketopimeloyl-ACP-methyl-esters; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11479produces MetaCyc:RXN-11479 — produces → CHEBI:16526; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11479produces MetaCyc:RXN-11479 — produces → RHEA-COMP:9685; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11479, RHEA:42289produces MetaCyc:RXN-11480 — produces → MetaCyc:3-hydroxypimeloyl-ACP-methyl-esters; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11480produces MetaCyc:RXN-11480 — produces → CHEBI:58349; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11480produces MetaCyc:3-Ketopimeloyl-ACP-methyl-esters — consumes → MetaCyc:RXN-11480; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11480consumes CHEBI:57783 — consumes → MetaCyc:RXN-11480; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11480consumes CHEBI:15378 — consumes → MetaCyc:RXN-11480; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11480consumes MetaCyc:3-hydroxypimeloyl-ACP-methyl-esters — consumes → MetaCyc:RXN-11481; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11481consumes MetaCyc:RXN-11481 — produces → MetaCyc:Enoylpimeloyl-ACP-methyl-esters; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11481produces MetaCyc:RXN-11481 — produces → CHEBI:15377; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11481produces MetaCyc:RXN-11482 — produces → RHEA-COMP:10186; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11482, RHEA:42701produces MetaCyc:RXN-11482 — produces → CHEBI:57540; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11482produces MetaCyc:Enoylpimeloyl-ACP-methyl-esters — consumes → MetaCyc:RXN-11482; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11482consumes CHEBI:57945 — consumes → MetaCyc:RXN-11482; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11482consumes CHEBI:15378 — consumes → MetaCyc:RXN-11482; Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.; Evidence: MetaCyc:RXN-11482consumes RHEA-COMP:10186 — consumes → RHEA:42701; Evidence: RHEA:42701consumes CHEBI:15377 — consumes → RHEA:42701; Evidence: RHEA:42701consumes RHEA:42701 — produces → RHEA-COMP:9955; Evidence: RHEA:42701produces RHEA:42701 — produces → CHEBI:17790; Evidence: RHEA:42701produces RHEA:42701 — produces → CHEBI:15378; Evidence: RHEA:42701produces RHEA-COMP:9955 — consumes → RHEA:42289; Evidence: RHEA:42289consumes CHEBI:57972 — consumes → RHEA:42289; Evidence: RHEA:42289consumes CHEBI:15378 — consumes → RHEA:42289; Evidence: RHEA:42289consumes RHEA:42289 — produces → CHEBI:149468; Evidence: RHEA:42289produces RHEA:42289 — produces → RHEA-COMP:9685; Evidence: RHEA:42289produces RHEA:42289 — produces → CHEBI:16526; Evidence: RHEA:42289produces CHEBI:149468 — consumes → RHEA:16862; Evidence: RHEA:16862consumes CHEBI:59789 — consumes → RHEA:16862; Evidence: RHEA:16862consumes RHEA:16862 — produces → CHEBI:16490; Evidence: RHEA:16862produces RHEA:16862 — produces → CHEBI:149469; Evidence: RHEA:16862produces CHEBI:149469 — consumes → RHEA:15806; Evidence: RHEA:15806consumes CHEBI:16526 — consumes → RHEA:15806; Evidence: RHEA:15806consumes CHEBI:30616 — consumes → RHEA:15806; Evidence: RHEA:15806consumes RHEA:15806 — produces → CHEBI:149473; Evidence: RHEA:15806produces RHEA:15806 — produces → CHEBI:456216; Evidence: RHEA:15806produces RHEA:15806 — produces → CHEBI:43474; Evidence: RHEA:15806produces RHEA:15806 — produces → CHEBI:15378; Evidence: RHEA:15806produces CHEBI:149473 — consumes → RHEA:22061; Formal Rhea sulfur-carrier/ferredoxin equation; the E. coli primary assay uses flavodoxin with ferredoxin/flavodoxin-NADP reductase and NADPH. These generic states do not identify that physiological donor or a specific sulfur-donor protein.; Evidence: RHEA:22061consumes RHEA-COMP:14737 — consumes → RHEA:22061; Formal Rhea sulfur-carrier/ferredoxin equation; the E. coli primary assay uses flavodoxin with ferredoxin/flavodoxin-NADP reductase and NADPH. These generic states do not identify that physiological donor or a specific sulfur-donor protein.; Evidence: RHEA:22061consumes RHEA-COMP:10001 — consumes → RHEA:22061; Formal Rhea sulfur-carrier/ferredoxin equation; the E. coli primary assay uses flavodoxin with ferredoxin/flavodoxin-NADP reductase and NADPH. These generic states do not identify that physiological donor or a specific sulfur-donor protein.; Evidence: RHEA:22061consumes CHEBI:59789 — consumes → RHEA:22061; Formal Rhea sulfur-carrier/ferredoxin equation; the E. coli primary assay uses flavodoxin with ferredoxin/flavodoxin-NADP reductase and NADPH. These generic states do not identify that physiological donor or a specific sulfur-donor protein.; Evidence: RHEA:22061consumes RHEA:22061 — produces → RHEA-COMP:14739; Formal Rhea sulfur-carrier/ferredoxin equation; the E. coli primary assay uses flavodoxin with ferredoxin/flavodoxin-NADP reductase and NADPH. These generic states do not identify that physiological donor or a specific sulfur-donor protein.; Evidence: RHEA:22061produces RHEA:22061 — produces → CHEBI:57586; Formal Rhea sulfur-carrier/ferredoxin equation; the E. coli primary assay uses flavodoxin with ferredoxin/flavodoxin-NADP reductase and NADPH. These generic states do not identify that physiological donor or a specific sulfur-donor protein.; Evidence: RHEA:22061produces RHEA:22061 — produces → CHEBI:17319; Formal Rhea sulfur-carrier/ferredoxin equation; the E. coli primary assay uses flavodoxin with ferredoxin/flavodoxin-NADP reductase and NADPH. These generic states do not identify that physiological donor or a specific sulfur-donor protein.; Evidence: RHEA:22061produces RHEA:22061 — produces → CHEBI:57844; Formal Rhea sulfur-carrier/ferredoxin equation; the E. coli primary assay uses flavodoxin with ferredoxin/flavodoxin-NADP reductase and NADPH. These generic states do not identify that physiological donor or a specific sulfur-donor protein.; Evidence: RHEA:22061produces RHEA:22061 — produces → RHEA-COMP:10000; Formal Rhea sulfur-carrier/ferredoxin equation; the E. coli primary assay uses flavodoxin with ferredoxin/flavodoxin-NADP reductase and NADPH. These generic states do not identify that physiological donor or a specific sulfur-donor protein.; Evidence: RHEA:22061produces RHEA:17106 — part_of → MetaCyc:BIOTIN-BIOSYNTHESIS-PWY; Evidence: MetaCyc:PWY-6519, MetaCyc:BIOTIN-BIOSYNTHESIS-PWY, MetaCyc:RXN-11475, RHEA:17106part of MetaCyc:RXN-11474 — part_of → MetaCyc:BIOTIN-BIOSYNTHESIS-PWY; Evidence: MetaCyc:PWY-6519, MetaCyc:BIOTIN-BIOSYNTHESIS-PWYpart of MetaCyc:RXN-11476 — part_of → MetaCyc:BIOTIN-BIOSYNTHESIS-PWY; Evidence: MetaCyc:PWY-6519, MetaCyc:BIOTIN-BIOSYNTHESIS-PWYpart of MetaCyc:RXN-11477 — part_of → MetaCyc:BIOTIN-BIOSYNTHESIS-PWY; Evidence: MetaCyc:PWY-6519, MetaCyc:BIOTIN-BIOSYNTHESIS-PWYpart of MetaCyc:RXN-11478 — part_of → MetaCyc:BIOTIN-BIOSYNTHESIS-PWY; Evidence: MetaCyc:PWY-6519, MetaCyc:BIOTIN-BIOSYNTHESIS-PWYpart of MetaCyc:RXN-11479 — part_of → MetaCyc:BIOTIN-BIOSYNTHESIS-PWY; Evidence: MetaCyc:PWY-6519, MetaCyc:BIOTIN-BIOSYNTHESIS-PWYpart of MetaCyc:RXN-11480 — part_of → MetaCyc:BIOTIN-BIOSYNTHESIS-PWY; Evidence: MetaCyc:PWY-6519, MetaCyc:BIOTIN-BIOSYNTHESIS-PWYpart of MetaCyc:RXN-11481 — part_of → MetaCyc:BIOTIN-BIOSYNTHESIS-PWY; Evidence: MetaCyc:PWY-6519, MetaCyc:BIOTIN-BIOSYNTHESIS-PWYpart of MetaCyc:RXN-11482 — part_of → MetaCyc:BIOTIN-BIOSYNTHESIS-PWY; Evidence: MetaCyc:PWY-6519, MetaCyc:BIOTIN-BIOSYNTHESIS-PWYpart of RHEA:42701 — part_of → MetaCyc:BIOTIN-BIOSYNTHESIS-PWY; Evidence: MetaCyc:PWY-6519, MetaCyc:BIOTIN-BIOSYNTHESIS-PWY, MetaCyc:RXN-11483, RHEA:42701part of RHEA:42289 — part_of → MetaCyc:BIOTIN-BIOSYNTHESIS-PWY; Evidence: MetaCyc:PWY-6519, MetaCyc:BIOTIN-BIOSYNTHESIS-PWY, MetaCyc:RXN-11484, RHEA:42289part of RHEA:16862 — part_of → MetaCyc:BIOTIN-BIOSYNTHESIS-PWY; Evidence: MetaCyc:PWY0-1507, MetaCyc:BIOTIN-BIOSYNTHESIS-PWY, MetaCyc:DAPASYN-RXN, RHEA:16862part of RHEA:15806 — part_of → MetaCyc:BIOTIN-BIOSYNTHESIS-PWY; Evidence: MetaCyc:PWY0-1507, MetaCyc:BIOTIN-BIOSYNTHESIS-PWY, MetaCyc:DETHIOBIOTIN-SYN-RXN, RHEA:15806part of RHEA:22061 — part_of → MetaCyc:BIOTIN-BIOSYNTHESIS-PWY; Evidence: MetaCyc:PWY0-1507, MetaCyc:BIOTIN-BIOSYNTHESIS-PWY, MetaCyc:2.8.1.6-RXN, RHEA:22061part of RHEA:17106 — precedes → MetaCyc:RXN-11474; Sequential intermediate: RHEA-COMP:9954. This ordering does not assert physical substrate channeling.; Evidence: MetaCyc:PWY-6519, RHEA:17106, MetaCyc:RXN-11474, RHEA:17106precedes MetaCyc:RXN-11474 — precedes → MetaCyc:RXN-11476; Sequential intermediate: MetaCyc:3-Ketoglutaryl-ACP-methyl-ester. This ordering does not assert physical substrate channeling.; Evidence: MetaCyc:PWY-6519, MetaCyc:RXN-11474, MetaCyc:RXN-11476precedes MetaCyc:RXN-11476 — precedes → MetaCyc:RXN-11477; Sequential intermediate: MetaCyc:3-Hydroxyglutaryl-ACP-methyl-ester. This ordering does not assert physical substrate channeling.; Evidence: MetaCyc:PWY-6519, MetaCyc:RXN-11476, MetaCyc:RXN-11477precedes MetaCyc:RXN-11477 — precedes → MetaCyc:RXN-11478; Sequential intermediate: MetaCyc:Enoylglutaryl-ACP-methyl-esters. This ordering does not assert physical substrate channeling.; Evidence: MetaCyc:PWY-6519, MetaCyc:RXN-11477, MetaCyc:RXN-11478precedes MetaCyc:RXN-11478 — precedes → MetaCyc:RXN-11479; Sequential intermediate: MetaCyc:Glutaryl-ACP-methyl-esters. This ordering does not assert physical substrate channeling.; Evidence: MetaCyc:PWY-6519, MetaCyc:RXN-11478, MetaCyc:RXN-11479precedes MetaCyc:RXN-11479 — precedes → MetaCyc:RXN-11480; Sequential intermediate: MetaCyc:3-Ketopimeloyl-ACP-methyl-esters. This ordering does not assert physical substrate channeling.; Evidence: MetaCyc:PWY-6519, MetaCyc:RXN-11479, MetaCyc:RXN-11480precedes MetaCyc:RXN-11480 — precedes → MetaCyc:RXN-11481; Sequential intermediate: MetaCyc:3-hydroxypimeloyl-ACP-methyl-esters. This ordering does not assert physical substrate channeling.; Evidence: MetaCyc:PWY-6519, MetaCyc:RXN-11480, MetaCyc:RXN-11481precedes MetaCyc:RXN-11481 — precedes → MetaCyc:RXN-11482; Sequential intermediate: MetaCyc:Enoylpimeloyl-ACP-methyl-esters. This ordering does not assert physical substrate channeling.; Evidence: MetaCyc:PWY-6519, MetaCyc:RXN-11481, MetaCyc:RXN-11482precedes MetaCyc:RXN-11482 — precedes → RHEA:42701; Sequential intermediate: RHEA-COMP:10186. This ordering does not assert physical substrate channeling.; Evidence: MetaCyc:PWY-6519, MetaCyc:RXN-11482, RHEA:42701, RHEA:42701precedes RHEA:42701 — precedes → RHEA:42289; Sequential intermediate: RHEA-COMP:9955. This ordering does not assert physical substrate channeling.; Evidence: MetaCyc:PWY-6519, RHEA:42701, RHEA:42289precedes RHEA:42289 — precedes → RHEA:16862; Sequential intermediate: CHEBI:149468. This ordering does not assert physical substrate channeling.; Evidence: MetaCyc:BIOTIN-BIOSYNTHESIS-PWY, RHEA:42289, RHEA:16862precedes RHEA:16862 — precedes → RHEA:15806; Sequential intermediate: CHEBI:149469. This ordering does not assert physical substrate channeling.; Evidence: MetaCyc:PWY0-1507, RHEA:16862, RHEA:15806precedes RHEA:15806 — precedes → RHEA:22061; Sequential intermediate: CHEBI:149473. This ordering does not assert physical substrate channeling.; Evidence: MetaCyc:PWY0-1507, RHEA:15806, RHEA:22061precedes MetaCyc:7KAPSYN-CPLX — has_part → UniProtKB:P12998; Native assembly stoichiometry; no claim that an isolated subunit is catalytically sufficient.; Evidence: MetaCyc:7KAPSYN-CPLX, MetaCyc:7KAPSYN-MONOMERhas part MetaCyc:DAPASYN-CPLX — has_part → UniProtKB:P12995; Native assembly stoichiometry; no claim that an isolated subunit is catalytically sufficient.; Evidence: MetaCyc:DAPASYN-CPLX, MetaCyc:DAPASYN-MONOMERhas part MetaCyc:DETHIOBIOTIN-SYN-CPLX — has_part → UniProtKB:P13000; Native assembly stoichiometry; no claim that an isolated subunit is catalytically sufficient.; Evidence: MetaCyc:DETHIOBIOTIN-SYN-CPLX, MetaCyc:DETHIOBIOTIN-SYN-MONOMERhas part MetaCyc:BIOTIN-SYN-CPLX — has_part → UniProtKB:P12996; Native assembly stoichiometry; no claim that an isolated subunit is catalytically sufficient.; Evidence: MetaCyc:BIOTIN-SYN-CPLX, MetaCyc:BIOTIN-SYN-MONOMERhas part MetaCyc:CPLX0-8005 — has_part → UniProtKB:P0AEK2; Native assembly stoichiometry; no claim that an isolated subunit is catalytically sufficient.; Evidence: MetaCyc:CPLX0-8005, MetaCyc:3-OXOACYL-ACP-REDUCT-MONOMERhas part MetaCyc:FABZ-CPLX — has_part → UniProtKB:P0A6Q6; Native assembly stoichiometry; no claim that an isolated subunit is catalytically sufficient. Hexamer assignment is based on E. coli His-tagged protein gel filtration, not the P. aeruginosa crystal as an E. coli measurement.; Evidence: MetaCyc:FABZ-CPLX, MetaCyc:FABZ-MONOMERhas part MetaCyc:CPLX0-8006 — has_part → UniProtKB:P0AEK4; Native assembly stoichiometry; no claim that an isolated subunit is catalytically sufficient.; Evidence: MetaCyc:CPLX0-8006, MetaCyc:ENOYL-ACP-REDUCT-NADH-MONOMERhas part MetaCyc:FABB-CPLX — has_part → UniProtKB:P0A953; Native assembly stoichiometry; no claim that an isolated subunit is catalytically sufficient.; Evidence: MetaCyc:FABB-CPLX, MetaCyc:FABB-MONOMERhas part UniProtKB:P12999 — enables → RHEA:17106; E. coli BioC supports the route genetically and in a weak refolded coupled assay. Direct purified malonyl-ACP methyltransferase experiments used B. cereus BioC; those data do not establish an E. coli oligomer.; Evidence: MetaCyc:ENZRXN-17863, MetaCyc:EG10119-MONOMER, UniProtKB:P12999, PMID:22965231enables MetaCyc:CPLX0-8005 — enables → MetaCyc:RXN-11476; Source-supported functional role, not a purified-substrate assay or isolated-subunit sufficiency claim. Native FAS assignments are supported by pathway genetics/inhibition and general enzyme specificity.; Evidence: MetaCyc:ENZRXN-17867, UniProtKB:P0AEK2enables MetaCyc:FABZ-CPLX — enables → MetaCyc:RXN-11477; Source-supported functional role, not a purified-substrate assay or isolated-subunit sufficiency claim. Native FAS assignments are supported by pathway genetics/inhibition and general enzyme specificity.; Evidence: MetaCyc:ENZRXN-17869, UniProtKB:P0A6Q6enables MetaCyc:CPLX0-8006 — enables → MetaCyc:RXN-11478; Source-supported functional role, not a purified-substrate assay or isolated-subunit sufficiency claim. Native FAS assignments are supported by pathway genetics/inhibition and general enzyme specificity.; Evidence: MetaCyc:ENZRXN-17871, UniProtKB:P0AEK4enables MetaCyc:FABB-CPLX — enables → MetaCyc:RXN-11479; Source-supported functional role, not a purified-substrate assay or isolated-subunit sufficiency claim. Native FAS assignments are supported by pathway genetics/inhibition and general enzyme specificity.; Evidence: MetaCyc:ENZRXN-17873, UniProtKB:P0A953enables MetaCyc:CPLX0-8005 — enables → MetaCyc:RXN-11480; Source-supported functional role, not a purified-substrate assay or isolated-subunit sufficiency claim. Native FAS assignments are supported by pathway genetics/inhibition and general enzyme specificity.; Evidence: MetaCyc:ENZRXN-17868, UniProtKB:P0AEK2enables MetaCyc:FABZ-CPLX — enables → MetaCyc:RXN-11481; Source-supported functional role, not a purified-substrate assay or isolated-subunit sufficiency claim. Native FAS assignments are supported by pathway genetics/inhibition and general enzyme specificity.; Evidence: MetaCyc:ENZRXN-17870, UniProtKB:P0A6Q6enables MetaCyc:CPLX0-8006 — enables → MetaCyc:RXN-11482; Source-supported functional role, not a purified-substrate assay or isolated-subunit sufficiency claim. Native FAS assignments are supported by pathway genetics/inhibition and general enzyme specificity.; Evidence: MetaCyc:ENZRXN-17872, UniProtKB:P0AEK4enables UniProtKB:P13001 — catalyzes → RHEA:42701; Evidence: MetaCyc:ENZRXN-17864, MetaCyc:EG10122-MONOMER, UniProtKB:P13001, PMID:23045647catalyzes MetaCyc:7KAPSYN-CPLX — catalyzes → RHEA:42289; Evidence: MetaCyc:ENZRXN-17865, UniProtKB:P12998, PMID:20693992, PMID:10642176catalyzes MetaCyc:DAPASYN-CPLX — catalyzes → RHEA:16862; Evidence: MetaCyc:DAPASYN-ENZRXN, UniProtKB:P12995, PMID:1092681catalyzes MetaCyc:DETHIOBIOTIN-SYN-CPLX — catalyzes → RHEA:15806; Evidence: MetaCyc:DETHIOBIOTIN-SYN-ENZRXN, UniProtKB:P13000, PMID:7669755catalyzes MetaCyc:BIOTIN-SYN-CPLX — catalyzes → RHEA:22061; Formal Rhea net chemistry retains generic sulfur-carrier and ferredoxin states. E. coli BioB assays use flavodoxin/reductase/NADPH; no specific ferredoxin identity or entire cluster-repair mechanism is asserted.; Evidence: MetaCyc:BIOTIN-SYN-ENZRXN, UniProtKB:P12996, PMID:20961145catalyzes MetaCyc:7KAPSYN-CPLX — has_cofactor → CHEBI:597326; Evidence: UniProtKB:P12998has cofactor MetaCyc:DAPASYN-CPLX — has_cofactor → CHEBI:597326; Evidence: UniProtKB:P12995has cofactor MetaCyc:DETHIOBIOTIN-SYN-CPLX — has_cofactor → CHEBI:18420; Evidence: UniProtKB:P13000has cofactor MetaCyc:BIOTIN-SYN-CPLX — has_cofactor → CHEBI:49883; Evidence: UniProtKB:P12996, PMID:14704425has cofactor MetaCyc:BIOTIN-SYN-CPLX — has_cofactor → CHEBI:190135; Evidence: UniProtKB:P12996, PMID:14704425has cofactor (8S)-8-amino-7-oxononanoic acid zwitterion; CHEBI:149468; Declared type: small_molecule small molecule (8S)-8-amino-7-oxononanoic acid zwitterion (7R,8S)-7,8-diammoniononanoate; CHEBI:149469; Declared type: small_molecule small molecule (7R,8S)-7,8- diammoniononanoate (4R,5S)-dethiobiotin(1-); CHEBI:149473; Declared type: small_molecule small molecule (4R,5S)-dethiobiotin(1-) water; CHEBI:15377; Declared type: small_molecule small molecule water hydron; CHEBI:15378; Declared type: small_molecule small molecule hydron S-adenosyl-4-methylthio-2-oxobutanoate; CHEBI:16490; Declared type: small_molecule small molecule S-adenosyl-4-methylthio-2- oxobutanoate carbon dioxide; CHEBI:16526; Declared type: small_molecule small molecule carbon dioxide 5'-deoxyadenosine; CHEBI:17319; Declared type: small_molecule small molecule 5'-deoxyadenosine methanol; CHEBI:17790; Declared type: small_molecule small molecule methanol magnesium(2+); CHEBI:18420; Declared type: cofactor cofactor magnesium(2+) di-mu-sulfido-diiron; CHEBI:190135; Declared type: cofactor cofactor di-mu-sulfido-diiron ATP(4-); CHEBI:30616; Declared type: small_molecule small molecule ATP(4-) hydrogenphosphate; CHEBI:43474; Declared type: small_molecule small molecule hydrogenphosphate ADP(3-); CHEBI:456216; Declared type: small_molecule small molecule ADP(3-) tetra-mu3-sulfido-tetrairon; CHEBI:49883; Declared type: cofactor cofactor tetra-mu3-sulfido-tetrairon NAD(1-); CHEBI:57540; Declared type: small_molecule small molecule NAD(1-) biotinate; CHEBI:57586; Declared type: small_molecule small molecule biotinate NADPH(4-); CHEBI:57783; Declared type: small_molecule small molecule NADPH(4-) L-methionine zwitterion; CHEBI:57844; Declared type: small_molecule small molecule L-methionine zwitterion S-adenosyl-L-homocysteine zwitterion; CHEBI:57856; Declared type: small_molecule small molecule S-adenosyl-L-homocysteine zwitterion NADH(2-); CHEBI:57945; Declared type: small_molecule small molecule NADH(2-) L-alanine zwitterion; CHEBI:57972; Declared type: small_molecule small molecule L-alanine zwitterion NADP(3-); CHEBI:58349; Declared type: small_molecule small molecule NADP(3-) pyridoxal 5'-phosphate(2-); CHEBI:597326; Declared type: cofactor cofactor pyridoxal 5'-phosphate(2-) S-adenosyl-L-methionine zwitterion; CHEBI:59789; Declared type: small_molecule small molecule S-adenosyl-L-methionine zwitterion oxidized [2Fe-2S]-[ferredoxin]; RHEA-COMP:10000; Declared type: protein protein oxidized [2Fe-2S]-[ferredoxin] reduced [2Fe-2S]-[ferredoxin]; RHEA-COMP:10001; Declared type: protein protein reduced [2Fe-2S]-[ferredoxin] 6-carboxyhexanoyl-[ACP] methyl ester; RHEA-COMP:10186; Declared type: protein protein 6-carboxyhexanoyl-[ACP] methyl ester (sulfur carrier)-SH; RHEA-COMP:14737; Declared type: protein protein (sulfur carrier)-SH (sulfur carrier)-H; RHEA-COMP:14739; Declared type: protein protein (sulfur carrier)-H malonyl-[ACP]; RHEA-COMP:9623; Declared type: protein protein malonyl-[ACP] holo-[ACP]; RHEA-COMP:9685; Declared type: protein protein holo-[ACP] malonyl-[ACP] methyl ester; RHEA-COMP:9954; Declared type: protein protein malonyl-[ACP] methyl ester 6-carboxyhexanoyl-[ACP]; RHEA-COMP:9955; Declared type: protein protein 6-carboxyhexanoyl-[ACP] a (3R)-3-hydroxyglutaryl-[acp] methyl ester; MetaCyc:3-Hydroxyglutaryl-ACP-methyl-ester; Declared type: protein protein a (3R)-3-hydroxyglutaryl-[acp] methyl ester a 3-oxoglutaryl-[acp] methyl ester; MetaCyc:3-Ketoglutaryl-ACP-methyl-ester; Declared type: protein protein a 3-oxoglutaryl-[acp] methyl ester a 3-oxopimeloyl-[acp] methyl ester; MetaCyc:3-Ketopimeloyl-ACP-methyl-esters; Declared type: protein protein a 3-oxopimeloyl-[acp] methyl ester a (3R)-3-hydroxypimeloyl-[acp] methyl ester; MetaCyc:3-hydroxypimeloyl-ACP-methyl-esters; Declared type: protein protein a (3R)-3-hydroxypimeloyl-[acp] methyl ester an enoylglutaryl-[acp] methyl ester; MetaCyc:Enoylglutaryl-ACP-methyl-esters; Declared type: protein protein an enoylglutaryl-[acp] methyl ester an enoylpimeloyl-[acp] methyl ester; MetaCyc:Enoylpimeloyl-ACP-methyl-esters; Declared type: protein protein an enoylpimeloyl-[acp] methyl ester a glutaryl-[acp] methyl ester; MetaCyc:Glutaryl-ACP-methyl-esters; Declared type: protein protein a glutaryl-[acp] methyl ester Pimeloyl-[acyl-carrier protein] methyl ester esterase; UniProtKB:P13001; Declared type: protein protein Pimeloyl-[acyl-carrier protein] methyl ester esterase 8-amino-7-oxononanoate synthase; UniProtKB:P12998; Declared type: protein protein 8-amino-7-oxononanoate synthase Adenosylmethionine-8-amino-7-oxononanoate aminotransferase; UniProtKB:P12995; Declared type: protein protein Adenosylmethionine-8-amino- 7-oxononanoate aminotransferase Biotin synthase; UniProtKB:P12996; Declared type: protein protein Biotin synthase Malonyl-[acyl-carrier protein] O-methyltransferase; UniProtKB:P12999; Declared type: protein protein Malonyl-[acyl-carrier protein] O-methyltransferase 3-oxoacyl-[acyl-carrier-protein] synthase 1; UniProtKB:P0A953; Declared type: protein protein 3-oxoacyl-[acyl-carrier- protein] synthase 1 Enoyl-[acyl-carrier-protein] reductase [NADH] FabI; UniProtKB:P0AEK4; Declared type: protein protein Enoyl-[acyl-carrier-protein] reductase [NADH] FabI 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ; UniProtKB:P0A6Q6; Declared type: protein protein 3-hydroxyacyl-[acyl-carrier- protein] dehydratase FabZ 3-oxoacyl-[acyl-carrier-protein] reductase FabG; UniProtKB:P0AEK2; Declared type: protein protein 3-oxoacyl-[acyl-carrier- protein] reductase FabG ATP-dependent dethiobiotin synthetase BioD 1; UniProtKB:P13000; Declared type: protein protein ATP-dependent dethiobiotin synthetase BioD 1 8-amino-7-oxononanoate synthase; MetaCyc:7KAPSYN-CPLX; Declared type: complex complex 8-amino-7-oxononanoate synthase adenosylmethionine-8-amino-7-oxononanoate aminotransferase; MetaCyc:DAPASYN-CPLX; Declared type: complex complex adenosylmethionine-8-amino- 7-oxononanoate aminotransferase dethiobiotin synthetase; MetaCyc:DETHIOBIOTIN-SYN-CPLX; Declared type: complex complex dethiobiotin synthetase biotin synthase; MetaCyc:BIOTIN-SYN-CPLX; Declared type: complex complex biotin synthase 3-oxoacyl-[acyl-carrier-protein] reductase FabG; MetaCyc:CPLX0-8005; Declared type: complex complex 3-oxoacyl-[acyl-carrier- protein] reductase FabG 3-hydroxy-acyl-[acyl-carrier-protein] dehydratase; MetaCyc:FABZ-CPLX; Declared type: complex complex 3-hydroxy-acyl-[acyl- carrier-protein] dehydratase enoyl-[acyl-carrier-protein] reductase; MetaCyc:CPLX0-8006; Declared type: complex complex enoyl-[acyl-carrier-protein] reductase beta-ketoacyl-[acyl carrier protein] synthase I; MetaCyc:FABB-CPLX; Declared type: complex complex beta-ketoacyl-[acyl carrier protein] synthase I malonyl-[ACP] + S-adenosyl-L-methionine => malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine; RHEA:17106; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity malonyl-[ACP] + S-adenosyl- L-methionine => malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine a malonyl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxoglutaryl-[acp] methyl ester + CO2 + acyl-carrier protein; MetaCyc:RXN-11474; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity a malonyl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxoglutaryl-[acp] methyl ester + CO2 + acyl-carrier protein a (3R)-3-hydroxyglutaryl-[acp] methyl ester + NADP+ <- a 3-oxoglutaryl-[acp] methyl ester + NADPH + H+; MetaCyc:RXN-11476; Declared type: molecular_activity; Source reaction direction: right_to_left molecular activity a (3R)-3-hydroxyglutaryl-[acp] methyl ester + NADP+ <- a 3-oxoglutaryl-[acp] methyl ester + NADPH + H+ a (3R)-3-hydroxyglutaryl-[acp] methyl ester -> an enoylglutaryl-[acp] methyl ester + H2O; MetaCyc:RXN-11477; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity a (3R)-3-hydroxyglutaryl-[acp] methyl ester -> an enoylglutaryl-[acp] methyl ester + H2O a glutaryl-[acp] methyl ester + NAD+ <- an enoylglutaryl-[acp] methyl ester + NADH + H+; MetaCyc:RXN-11478; Declared type: molecular_activity; Source reaction direction: right_to_left molecular activity a glutaryl-[acp] methyl ester + NAD+ <- an enoylglutaryl-[acp] methyl ester + NADH + H+ a glutaryl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxopimeloyl-[acp] methyl ester + CO2 + acyl-carrier protein; MetaCyc:RXN-11479; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity a glutaryl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxopimeloyl-[acp] methyl ester + CO2 + acyl- carrier protein a (3R)-3-hydroxypimeloyl-[acp] methyl ester + NADP+ <- a 3-oxopimeloyl-[acp] methyl ester + NADPH + H+; MetaCyc:RXN-11480; Declared type: molecular_activity; Source reaction direction: right_to_left molecular activity a (3R)-3-hydroxypimeloyl-[acp] methyl ester + NADP+ <- a 3-oxopimeloyl-[acp] methyl ester + NADPH + H+ a (3R)-3-hydroxypimeloyl-[acp] methyl ester -> an enoylpimeloyl-[acp] methyl ester + H2O; MetaCyc:RXN-11481; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity a (3R)-3-hydroxypimeloyl-[acp] methyl ester -> an enoylpimeloyl-[acp] methyl ester + H2O a pimeloyl-[acp] methyl ester + NAD+ <- an enoylpimeloyl-[acp] methyl ester + NADH + H+; MetaCyc:RXN-11482; Declared type: molecular_activity; Source reaction direction: right_to_left molecular activity a pimeloyl-[acp] methyl ester + NAD+ <- an enoylpimeloyl-[acp] methyl ester + NADH + H+ 6-carboxyhexanoyl-[ACP] methyl ester + H2O => 6-carboxyhexanoyl-[ACP] + methanol + H(+); RHEA:42701; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity 6-carboxyhexanoyl-[ACP] methyl ester + H2O => 6-carboxyhexanoyl-[ACP] + methanol + H(+) 6-carboxyhexanoyl-[ACP] + L-alanine + H(+) => (8S)-8-amino-7-oxononanoate + holo-[ACP] + CO2; RHEA:42289; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity 6-carboxyhexanoyl-[ACP] + L-alanine + H(+) => (8S)-8-amino-7-oxononanoate + holo-[ACP] + CO2 (8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine => S-adenosyl-4-methylsulfanyl-2-oxobutanoate + (7R,8S)-7,8-diammoniononanoate; RHEA:16862; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity (8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine => S-adenosyl-4-methylsulfanyl- 2-oxobutanoate + (7R,8S)- 7,8-diammoniononanoate (7R,8S)-7,8-diammoniononanoate + CO2 + ATP => (4R,5S)-dethiobiotin + ADP + phosphate + 3 H(+); RHEA:15806; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity (7R,8S)-7,8- diammoniononanoate + CO2 + ATP => (4R,5S)-dethiobiotin + ADP + phosphate + 3 H(+) (4R,5S)-dethiobiotin + (sulfur carrier)-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine => (sulfur carrier)-H + biotin + 2 5'-deoxyadenosine + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]; RHEA:22061; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity (4R,5S)-dethiobiotin + (sulfur carrier)-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine => (sulfur carrier)-H + biotin + 2 5'-deoxyadenosine + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] biotin biosynthesis I; MetaCyc:BIOTIN-BIOSYNTHESIS-PWY; Declared type: pathway pathway biotin biosynthesis I

Components and activities

Declared biological components and source reaction directions
NodeKind or roleSource direction
Escherichia coli K-12
NCBITaxon:83333		taxon
Escherichia coli str. K-12 substr. MG1655
NCBITaxon:511145		taxon
(8S)-8-amino-7-oxononanoic acid zwitterion
CHEBI:149468		small molecule
(7R,8S)-7,8-diammoniononanoate
CHEBI:149469		small molecule
(4R,5S)-dethiobiotin(1-)
CHEBI:149473		small molecule
water
CHEBI:15377		small molecule
hydron
CHEBI:15378		small molecule
S-adenosyl-4-methylthio-2-oxobutanoate
CHEBI:16490		small molecule
carbon dioxide
CHEBI:16526		small molecule
5'-deoxyadenosine
CHEBI:17319		small molecule
methanol
CHEBI:17790		small molecule
magnesium(2+)
CHEBI:18420		cofactor
di-mu-sulfido-diiron
CHEBI:190135		cofactor
ATP(4-)
CHEBI:30616		small molecule
hydrogenphosphate
CHEBI:43474		small molecule
ADP(3-)
CHEBI:456216		small molecule
tetra-mu3-sulfido-tetrairon
CHEBI:49883		cofactor
NAD(1-)
CHEBI:57540		small molecule
biotinate
CHEBI:57586		small molecule
NADPH(4-)
CHEBI:57783		small molecule
L-methionine zwitterion
CHEBI:57844		small molecule
S-adenosyl-L-homocysteine zwitterion
CHEBI:57856		small molecule
NADH(2-)
CHEBI:57945		small molecule
L-alanine zwitterion
CHEBI:57972		small molecule
NADP(3-)
CHEBI:58349		small molecule
pyridoxal 5'-phosphate(2-)
CHEBI:597326		cofactor
S-adenosyl-L-methionine zwitterion
CHEBI:59789		small molecule
oxidized [2Fe-2S]-[ferredoxin]
RHEA-COMP:10000		protein
reduced [2Fe-2S]-[ferredoxin]
RHEA-COMP:10001		protein
6-carboxyhexanoyl-[ACP] methyl ester
RHEA-COMP:10186		protein
(sulfur carrier)-SH
RHEA-COMP:14737		protein
(sulfur carrier)-H
RHEA-COMP:14739		protein
malonyl-[ACP]
RHEA-COMP:9623		protein
holo-[ACP]
RHEA-COMP:9685		protein
malonyl-[ACP] methyl ester
RHEA-COMP:9954		protein
6-carboxyhexanoyl-[ACP]
RHEA-COMP:9955		protein
a (3R)-3-hydroxyglutaryl-[acp] methyl ester
MetaCyc:3-Hydroxyglutaryl-ACP-methyl-ester		protein
a 3-oxoglutaryl-[acp] methyl ester
MetaCyc:3-Ketoglutaryl-ACP-methyl-ester		protein
a 3-oxopimeloyl-[acp] methyl ester
MetaCyc:3-Ketopimeloyl-ACP-methyl-esters		protein
a (3R)-3-hydroxypimeloyl-[acp] methyl ester
MetaCyc:3-hydroxypimeloyl-ACP-methyl-esters		protein
an enoylglutaryl-[acp] methyl ester
MetaCyc:Enoylglutaryl-ACP-methyl-esters		protein
an enoylpimeloyl-[acp] methyl ester
MetaCyc:Enoylpimeloyl-ACP-methyl-esters		protein
a glutaryl-[acp] methyl ester
MetaCyc:Glutaryl-ACP-methyl-esters		protein
Pimeloyl-[acyl-carrier protein] methyl ester esterase
UniProtKB:P13001		protein
8-amino-7-oxononanoate synthase
UniProtKB:P12998		protein
Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
UniProtKB:P12995		protein
Biotin synthase
UniProtKB:P12996		protein
Malonyl-[acyl-carrier protein] O-methyltransferase
UniProtKB:P12999		protein
3-oxoacyl-[acyl-carrier-protein] synthase 1
UniProtKB:P0A953		protein
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI
UniProtKB:P0AEK4		protein
3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
UniProtKB:P0A6Q6		protein
3-oxoacyl-[acyl-carrier-protein] reductase FabG
UniProtKB:P0AEK2		protein
ATP-dependent dethiobiotin synthetase BioD 1
UniProtKB:P13000		protein
8-amino-7-oxononanoate synthase
MetaCyc:7KAPSYN-CPLX		complex
adenosylmethionine-8-amino-7-oxononanoate aminotransferase
MetaCyc:DAPASYN-CPLX		complex
dethiobiotin synthetase
MetaCyc:DETHIOBIOTIN-SYN-CPLX		complex
biotin synthase
MetaCyc:BIOTIN-SYN-CPLX		complex
3-oxoacyl-[acyl-carrier-protein] reductase FabG
MetaCyc:CPLX0-8005		complex
3-hydroxy-acyl-[acyl-carrier-protein] dehydratase
MetaCyc:FABZ-CPLX		complex
enoyl-[acyl-carrier-protein] reductase
MetaCyc:CPLX0-8006		complex
beta-ketoacyl-[acyl carrier protein] synthase I
MetaCyc:FABB-CPLX		complex
malonyl-[ACP] + S-adenosyl-L-methionine => malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
RHEA:17106		molecular activityleft to right
a malonyl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxoglutaryl-[acp] methyl ester + CO2 + acyl-carrier protein
MetaCyc:RXN-11474		molecular activityleft to right
a (3R)-3-hydroxyglutaryl-[acp] methyl ester + NADP+ <- a 3-oxoglutaryl-[acp] methyl ester + NADPH + H+
MetaCyc:RXN-11476		molecular activityright to left
a (3R)-3-hydroxyglutaryl-[acp] methyl ester -> an enoylglutaryl-[acp] methyl ester + H2O
MetaCyc:RXN-11477		molecular activityleft to right
a glutaryl-[acp] methyl ester + NAD+ <- an enoylglutaryl-[acp] methyl ester + NADH + H+
MetaCyc:RXN-11478		molecular activityright to left
a glutaryl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxopimeloyl-[acp] methyl ester + CO2 + acyl-carrier protein
MetaCyc:RXN-11479		molecular activityleft to right
a (3R)-3-hydroxypimeloyl-[acp] methyl ester + NADP+ <- a 3-oxopimeloyl-[acp] methyl ester + NADPH + H+
MetaCyc:RXN-11480		molecular activityright to left
a (3R)-3-hydroxypimeloyl-[acp] methyl ester -> an enoylpimeloyl-[acp] methyl ester + H2O
MetaCyc:RXN-11481		molecular activityleft to right
a pimeloyl-[acp] methyl ester + NAD+ <- an enoylpimeloyl-[acp] methyl ester + NADH + H+
MetaCyc:RXN-11482		molecular activityright to left
6-carboxyhexanoyl-[ACP] methyl ester + H2O => 6-carboxyhexanoyl-[ACP] + methanol + H(+)
RHEA:42701		molecular activityleft to right
6-carboxyhexanoyl-[ACP] + L-alanine + H(+) => (8S)-8-amino-7-oxononanoate + holo-[ACP] + CO2
RHEA:42289		molecular activityleft to right
(8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine => S-adenosyl-4-methylsulfanyl-2-oxobutanoate + (7R,8S)-7,8-diammoniononanoate
RHEA:16862		molecular activityleft to right
(7R,8S)-7,8-diammoniononanoate + CO2 + ATP => (4R,5S)-dethiobiotin + ADP + phosphate + 3 H(+)
RHEA:15806		molecular activityleft to right
(4R,5S)-dethiobiotin + (sulfur carrier)-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine => (sulfur carrier)-H + biotin + 2 5'-deoxyadenosine + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
RHEA:22061		molecular activityleft to right

Mechanistic edges

Mechanistic edges and their cited evidence
SubjectPredicate and descriptionObjectEvidence
malonyl-[ACP]
RHEA-COMP:9623		consumes

malonyl-[ACP] + S-adenosyl-L-methionine => malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
RHEA:17106
  • RHEA:17106

    Source assertion: RHEA:17106 assigns RHEA-COMP:9623 to substrates, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/17106 rh:substrates; http://rdf.rhea-db.org/17105_L rh:contains1 http://rdf.rhea-db.org/Participant_17105_compound_9623; rh:compound http://rdf.rhea-db.org/Compound_9623
S-adenosyl-L-methionine zwitterion
CHEBI:59789		consumes

malonyl-[ACP] + S-adenosyl-L-methionine => malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
RHEA:17106
  • RHEA:17106

    Source assertion: RHEA:17106 assigns CHEBI:59789 to substrates, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/17106 rh:substrates; http://rdf.rhea-db.org/17105_L rh:contains1 http://rdf.rhea-db.org/Participant_17105_compound_6127; rh:compound http://rdf.rhea-db.org/Compound_6127
malonyl-[ACP] + S-adenosyl-L-methionine => malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
RHEA:17106		produces

malonyl-[ACP] methyl ester
RHEA-COMP:9954
  • RHEA:17106

    Source assertion: RHEA:17106 assigns RHEA-COMP:9954 to products, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/17106 rh:products; http://rdf.rhea-db.org/17105_R rh:contains1 http://rdf.rhea-db.org/Participant_17105_compound_9954; rh:compound http://rdf.rhea-db.org/Compound_9954
malonyl-[ACP] + S-adenosyl-L-methionine => malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
RHEA:17106		produces

S-adenosyl-L-homocysteine zwitterion
CHEBI:57856
  • RHEA:17106

    Source assertion: RHEA:17106 assigns CHEBI:57856 to products, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/17106 rh:products; http://rdf.rhea-db.org/17105_R rh:contains1 http://rdf.rhea-db.org/Participant_17105_compound_4281; rh:compound http://rdf.rhea-db.org/Compound_4281
malonyl-[ACP] methyl ester
RHEA-COMP:9954		consumes

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a malonyl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxoglutaryl-[acp] methyl ester + CO2 + acyl-carrier protein
MetaCyc:RXN-11474
  • MetaCyc:RXN-11474

    Source assertion: Native RXN-11474 has Malonyl-acp-methyl-ester on left, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11474']/left/*[@frameid='Malonyl-acp-methyl-ester']; sibling coefficient (absent means 1); reaction-direction
  • RHEA:17106

    Source assertion: Independent Rhea whole-carrier identity used for the native ACP state: RHEA-COMP:9954; reactive-part ChEBI is not the whole carrier.

    Source locationhttp://rdf.rhea-db.org/Compound_9954 rh:name; rh:reactivePart
malonyl-[ACP]
RHEA-COMP:9623		consumes

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a malonyl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxoglutaryl-[acp] methyl ester + CO2 + acyl-carrier protein
MetaCyc:RXN-11474
  • MetaCyc:RXN-11474

    Source assertion: Native RXN-11474 has MALONYL-ACP on left, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11474']/left/*[@frameid='MALONYL-ACP']; sibling coefficient (absent means 1); reaction-direction
  • RHEA:17106

    Source assertion: Independent Rhea whole-carrier identity used for the native ACP state: RHEA-COMP:9623; reactive-part ChEBI is not the whole carrier.

    Source locationhttp://rdf.rhea-db.org/Compound_9623 rh:name; rh:reactivePart
hydron
CHEBI:15378		consumes

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a malonyl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxoglutaryl-[acp] methyl ester + CO2 + acyl-carrier protein
MetaCyc:RXN-11474
  • MetaCyc:RXN-11474

    Source assertion: Native RXN-11474 has PROTON on left, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11474']/left/*[@frameid='PROTON']; sibling coefficient (absent means 1); reaction-direction
a malonyl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxoglutaryl-[acp] methyl ester + CO2 + acyl-carrier protein
MetaCyc:RXN-11474		produces

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a 3-oxoglutaryl-[acp] methyl ester
MetaCyc:3-Ketoglutaryl-ACP-methyl-ester
  • MetaCyc:RXN-11474

    Source assertion: Native RXN-11474 has 3-Ketoglutaryl-ACP-methyl-ester on right, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11474']/right/*[@frameid='3-Ketoglutaryl-ACP-methyl-ester']; sibling coefficient (absent means 1); reaction-direction
a malonyl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxoglutaryl-[acp] methyl ester + CO2 + acyl-carrier protein
MetaCyc:RXN-11474		produces

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

carbon dioxide
CHEBI:16526
  • MetaCyc:RXN-11474

    Source assertion: Native RXN-11474 has CARBON-DIOXIDE on right, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11474']/right/*[@frameid='CARBON-DIOXIDE']; sibling coefficient (absent means 1); reaction-direction
a malonyl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxoglutaryl-[acp] methyl ester + CO2 + acyl-carrier protein
MetaCyc:RXN-11474		produces

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

holo-[ACP]
RHEA-COMP:9685
  • MetaCyc:RXN-11474

    Source assertion: Native RXN-11474 has ACP on right, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11474']/right/*[@frameid='ACP']; sibling coefficient (absent means 1); reaction-direction
  • RHEA:42289

    Source assertion: Independent Rhea whole-carrier identity used for the native ACP state: RHEA-COMP:9685; reactive-part ChEBI is not the whole carrier.

    Source locationhttp://rdf.rhea-db.org/Compound_9685 rh:name; rh:reactivePart
a (3R)-3-hydroxyglutaryl-[acp] methyl ester + NADP+ <- a 3-oxoglutaryl-[acp] methyl ester + NADPH + H+
MetaCyc:RXN-11476		produces

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a (3R)-3-hydroxyglutaryl-[acp] methyl ester
MetaCyc:3-Hydroxyglutaryl-ACP-methyl-ester
  • MetaCyc:RXN-11476

    Source assertion: Native RXN-11476 has 3-Hydroxyglutaryl-ACP-methyl-ester on left, coefficient 1; physiological direction PHYSIOL-RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11476']/left/*[@frameid='3-Hydroxyglutaryl-ACP-methyl-ester']; sibling coefficient (absent means 1); reaction-direction
a (3R)-3-hydroxyglutaryl-[acp] methyl ester + NADP+ <- a 3-oxoglutaryl-[acp] methyl ester + NADPH + H+
MetaCyc:RXN-11476		produces

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

NADP(3-)
CHEBI:58349
  • MetaCyc:RXN-11476

    Source assertion: Native RXN-11476 has NADP on left, coefficient 1; physiological direction PHYSIOL-RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11476']/left/*[@frameid='NADP']; sibling coefficient (absent means 1); reaction-direction
a 3-oxoglutaryl-[acp] methyl ester
MetaCyc:3-Ketoglutaryl-ACP-methyl-ester		consumes

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a (3R)-3-hydroxyglutaryl-[acp] methyl ester + NADP+ <- a 3-oxoglutaryl-[acp] methyl ester + NADPH + H+
MetaCyc:RXN-11476
  • MetaCyc:RXN-11476

    Source assertion: Native RXN-11476 has 3-Ketoglutaryl-ACP-methyl-ester on right, coefficient 1; physiological direction PHYSIOL-RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11476']/right/*[@frameid='3-Ketoglutaryl-ACP-methyl-ester']; sibling coefficient (absent means 1); reaction-direction
NADPH(4-)
CHEBI:57783		consumes

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a (3R)-3-hydroxyglutaryl-[acp] methyl ester + NADP+ <- a 3-oxoglutaryl-[acp] methyl ester + NADPH + H+
MetaCyc:RXN-11476
  • MetaCyc:RXN-11476

    Source assertion: Native RXN-11476 has NADPH on right, coefficient 1; physiological direction PHYSIOL-RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11476']/right/*[@frameid='NADPH']; sibling coefficient (absent means 1); reaction-direction
hydron
CHEBI:15378		consumes

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a (3R)-3-hydroxyglutaryl-[acp] methyl ester + NADP+ <- a 3-oxoglutaryl-[acp] methyl ester + NADPH + H+
MetaCyc:RXN-11476
  • MetaCyc:RXN-11476

    Source assertion: Native RXN-11476 has PROTON on right, coefficient 1; physiological direction PHYSIOL-RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11476']/right/*[@frameid='PROTON']; sibling coefficient (absent means 1); reaction-direction
a (3R)-3-hydroxyglutaryl-[acp] methyl ester
MetaCyc:3-Hydroxyglutaryl-ACP-methyl-ester		consumes

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a (3R)-3-hydroxyglutaryl-[acp] methyl ester -> an enoylglutaryl-[acp] methyl ester + H2O
MetaCyc:RXN-11477
  • MetaCyc:RXN-11477

    Source assertion: Native RXN-11477 has 3-Hydroxyglutaryl-ACP-methyl-ester on left, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11477']/left/*[@frameid='3-Hydroxyglutaryl-ACP-methyl-ester']; sibling coefficient (absent means 1); reaction-direction
a (3R)-3-hydroxyglutaryl-[acp] methyl ester -> an enoylglutaryl-[acp] methyl ester + H2O
MetaCyc:RXN-11477		produces

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

an enoylglutaryl-[acp] methyl ester
MetaCyc:Enoylglutaryl-ACP-methyl-esters
  • MetaCyc:RXN-11477

    Source assertion: Native RXN-11477 has Enoylglutaryl-ACP-methyl-esters on right, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11477']/right/*[@frameid='Enoylglutaryl-ACP-methyl-esters']; sibling coefficient (absent means 1); reaction-direction
a (3R)-3-hydroxyglutaryl-[acp] methyl ester -> an enoylglutaryl-[acp] methyl ester + H2O
MetaCyc:RXN-11477		produces

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

water
CHEBI:15377
  • MetaCyc:RXN-11477

    Source assertion: Native RXN-11477 has WATER on right, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11477']/right/*[@frameid='WATER']; sibling coefficient (absent means 1); reaction-direction
a glutaryl-[acp] methyl ester + NAD+ <- an enoylglutaryl-[acp] methyl ester + NADH + H+
MetaCyc:RXN-11478		produces

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a glutaryl-[acp] methyl ester
MetaCyc:Glutaryl-ACP-methyl-esters
  • MetaCyc:RXN-11478

    Source assertion: Native RXN-11478 has Glutaryl-ACP-methyl-esters on left, coefficient 1; physiological direction RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11478']/left/*[@frameid='Glutaryl-ACP-methyl-esters']; sibling coefficient (absent means 1); reaction-direction
a glutaryl-[acp] methyl ester + NAD+ <- an enoylglutaryl-[acp] methyl ester + NADH + H+
MetaCyc:RXN-11478		produces

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

NAD(1-)
CHEBI:57540
  • MetaCyc:RXN-11478

    Source assertion: Native RXN-11478 has NAD on left, coefficient 1; physiological direction RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11478']/left/*[@frameid='NAD']; sibling coefficient (absent means 1); reaction-direction
an enoylglutaryl-[acp] methyl ester
MetaCyc:Enoylglutaryl-ACP-methyl-esters		consumes

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a glutaryl-[acp] methyl ester + NAD+ <- an enoylglutaryl-[acp] methyl ester + NADH + H+
MetaCyc:RXN-11478
  • MetaCyc:RXN-11478

    Source assertion: Native RXN-11478 has Enoylglutaryl-ACP-methyl-esters on right, coefficient 1; physiological direction RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11478']/right/*[@frameid='Enoylglutaryl-ACP-methyl-esters']; sibling coefficient (absent means 1); reaction-direction
NADH(2-)
CHEBI:57945		consumes

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a glutaryl-[acp] methyl ester + NAD+ <- an enoylglutaryl-[acp] methyl ester + NADH + H+
MetaCyc:RXN-11478
  • MetaCyc:RXN-11478

    Source assertion: Native RXN-11478 has NADH on right, coefficient 1; physiological direction RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11478']/right/*[@frameid='NADH']; sibling coefficient (absent means 1); reaction-direction
hydron
CHEBI:15378		consumes

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a glutaryl-[acp] methyl ester + NAD+ <- an enoylglutaryl-[acp] methyl ester + NADH + H+
MetaCyc:RXN-11478
  • MetaCyc:RXN-11478

    Source assertion: Native RXN-11478 has PROTON on right, coefficient 1; physiological direction RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11478']/right/*[@frameid='PROTON']; sibling coefficient (absent means 1); reaction-direction
a glutaryl-[acp] methyl ester
MetaCyc:Glutaryl-ACP-methyl-esters		consumes

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a glutaryl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxopimeloyl-[acp] methyl ester + CO2 + acyl-carrier protein
MetaCyc:RXN-11479
  • MetaCyc:RXN-11479

    Source assertion: Native RXN-11479 has Glutaryl-ACP-methyl-esters on left, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11479']/left/*[@frameid='Glutaryl-ACP-methyl-esters']; sibling coefficient (absent means 1); reaction-direction
malonyl-[ACP]
RHEA-COMP:9623		consumes

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a glutaryl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxopimeloyl-[acp] methyl ester + CO2 + acyl-carrier protein
MetaCyc:RXN-11479
  • MetaCyc:RXN-11479

    Source assertion: Native RXN-11479 has MALONYL-ACP on left, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11479']/left/*[@frameid='MALONYL-ACP']; sibling coefficient (absent means 1); reaction-direction
  • RHEA:17106

    Source assertion: Independent Rhea whole-carrier identity used for the native ACP state: RHEA-COMP:9623; reactive-part ChEBI is not the whole carrier.

    Source locationhttp://rdf.rhea-db.org/Compound_9623 rh:name; rh:reactivePart
hydron
CHEBI:15378		consumes

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a glutaryl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxopimeloyl-[acp] methyl ester + CO2 + acyl-carrier protein
MetaCyc:RXN-11479
  • MetaCyc:RXN-11479

    Source assertion: Native RXN-11479 has PROTON on left, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11479']/left/*[@frameid='PROTON']; sibling coefficient (absent means 1); reaction-direction
a glutaryl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxopimeloyl-[acp] methyl ester + CO2 + acyl-carrier protein
MetaCyc:RXN-11479		produces

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a 3-oxopimeloyl-[acp] methyl ester
MetaCyc:3-Ketopimeloyl-ACP-methyl-esters
  • MetaCyc:RXN-11479

    Source assertion: Native RXN-11479 has 3-Ketopimeloyl-ACP-methyl-esters on right, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11479']/right/*[@frameid='3-Ketopimeloyl-ACP-methyl-esters']; sibling coefficient (absent means 1); reaction-direction
a glutaryl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxopimeloyl-[acp] methyl ester + CO2 + acyl-carrier protein
MetaCyc:RXN-11479		produces

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

carbon dioxide
CHEBI:16526
  • MetaCyc:RXN-11479

    Source assertion: Native RXN-11479 has CARBON-DIOXIDE on right, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11479']/right/*[@frameid='CARBON-DIOXIDE']; sibling coefficient (absent means 1); reaction-direction
a glutaryl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxopimeloyl-[acp] methyl ester + CO2 + acyl-carrier protein
MetaCyc:RXN-11479		produces

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

holo-[ACP]
RHEA-COMP:9685
  • MetaCyc:RXN-11479

    Source assertion: Native RXN-11479 has ACP on right, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11479']/right/*[@frameid='ACP']; sibling coefficient (absent means 1); reaction-direction
  • RHEA:42289

    Source assertion: Independent Rhea whole-carrier identity used for the native ACP state: RHEA-COMP:9685; reactive-part ChEBI is not the whole carrier.

    Source locationhttp://rdf.rhea-db.org/Compound_9685 rh:name; rh:reactivePart
a (3R)-3-hydroxypimeloyl-[acp] methyl ester + NADP+ <- a 3-oxopimeloyl-[acp] methyl ester + NADPH + H+
MetaCyc:RXN-11480		produces

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a (3R)-3-hydroxypimeloyl-[acp] methyl ester
MetaCyc:3-hydroxypimeloyl-ACP-methyl-esters
  • MetaCyc:RXN-11480

    Source assertion: Native RXN-11480 has 3-hydroxypimeloyl-ACP-methyl-esters on left, coefficient 1; physiological direction PHYSIOL-RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11480']/left/*[@frameid='3-hydroxypimeloyl-ACP-methyl-esters']; sibling coefficient (absent means 1); reaction-direction
a (3R)-3-hydroxypimeloyl-[acp] methyl ester + NADP+ <- a 3-oxopimeloyl-[acp] methyl ester + NADPH + H+
MetaCyc:RXN-11480		produces

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

NADP(3-)
CHEBI:58349
  • MetaCyc:RXN-11480

    Source assertion: Native RXN-11480 has NADP on left, coefficient 1; physiological direction PHYSIOL-RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11480']/left/*[@frameid='NADP']; sibling coefficient (absent means 1); reaction-direction
a 3-oxopimeloyl-[acp] methyl ester
MetaCyc:3-Ketopimeloyl-ACP-methyl-esters		consumes

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a (3R)-3-hydroxypimeloyl-[acp] methyl ester + NADP+ <- a 3-oxopimeloyl-[acp] methyl ester + NADPH + H+
MetaCyc:RXN-11480
  • MetaCyc:RXN-11480

    Source assertion: Native RXN-11480 has 3-Ketopimeloyl-ACP-methyl-esters on right, coefficient 1; physiological direction PHYSIOL-RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11480']/right/*[@frameid='3-Ketopimeloyl-ACP-methyl-esters']; sibling coefficient (absent means 1); reaction-direction
NADPH(4-)
CHEBI:57783		consumes

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a (3R)-3-hydroxypimeloyl-[acp] methyl ester + NADP+ <- a 3-oxopimeloyl-[acp] methyl ester + NADPH + H+
MetaCyc:RXN-11480
  • MetaCyc:RXN-11480

    Source assertion: Native RXN-11480 has NADPH on right, coefficient 1; physiological direction PHYSIOL-RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11480']/right/*[@frameid='NADPH']; sibling coefficient (absent means 1); reaction-direction
hydron
CHEBI:15378		consumes

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a (3R)-3-hydroxypimeloyl-[acp] methyl ester + NADP+ <- a 3-oxopimeloyl-[acp] methyl ester + NADPH + H+
MetaCyc:RXN-11480
  • MetaCyc:RXN-11480

    Source assertion: Native RXN-11480 has PROTON on right, coefficient 1; physiological direction PHYSIOL-RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11480']/right/*[@frameid='PROTON']; sibling coefficient (absent means 1); reaction-direction
a (3R)-3-hydroxypimeloyl-[acp] methyl ester
MetaCyc:3-hydroxypimeloyl-ACP-methyl-esters		consumes

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a (3R)-3-hydroxypimeloyl-[acp] methyl ester -> an enoylpimeloyl-[acp] methyl ester + H2O
MetaCyc:RXN-11481
  • MetaCyc:RXN-11481

    Source assertion: Native RXN-11481 has 3-hydroxypimeloyl-ACP-methyl-esters on left, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11481']/left/*[@frameid='3-hydroxypimeloyl-ACP-methyl-esters']; sibling coefficient (absent means 1); reaction-direction
a (3R)-3-hydroxypimeloyl-[acp] methyl ester -> an enoylpimeloyl-[acp] methyl ester + H2O
MetaCyc:RXN-11481		produces

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

an enoylpimeloyl-[acp] methyl ester
MetaCyc:Enoylpimeloyl-ACP-methyl-esters
  • MetaCyc:RXN-11481

    Source assertion: Native RXN-11481 has Enoylpimeloyl-ACP-methyl-esters on right, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11481']/right/*[@frameid='Enoylpimeloyl-ACP-methyl-esters']; sibling coefficient (absent means 1); reaction-direction
a (3R)-3-hydroxypimeloyl-[acp] methyl ester -> an enoylpimeloyl-[acp] methyl ester + H2O
MetaCyc:RXN-11481		produces

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

water
CHEBI:15377
  • MetaCyc:RXN-11481

    Source assertion: Native RXN-11481 has WATER on right, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11481']/right/*[@frameid='WATER']; sibling coefficient (absent means 1); reaction-direction
a pimeloyl-[acp] methyl ester + NAD+ <- an enoylpimeloyl-[acp] methyl ester + NADH + H+
MetaCyc:RXN-11482		produces

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

6-carboxyhexanoyl-[ACP] methyl ester
RHEA-COMP:10186
  • MetaCyc:RXN-11482

    Source assertion: Native RXN-11482 has Pimeloyl-ACP-methyl-esters on left, coefficient 1; physiological direction RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11482']/left/*[@frameid='Pimeloyl-ACP-methyl-esters']; sibling coefficient (absent means 1); reaction-direction
  • RHEA:42701

    Source assertion: Independent Rhea whole-carrier identity used for the native ACP state: RHEA-COMP:10186; reactive-part ChEBI is not the whole carrier.

    Source locationhttp://rdf.rhea-db.org/Compound_10186 rh:name; rh:reactivePart
a pimeloyl-[acp] methyl ester + NAD+ <- an enoylpimeloyl-[acp] methyl ester + NADH + H+
MetaCyc:RXN-11482		produces

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

NAD(1-)
CHEBI:57540
  • MetaCyc:RXN-11482

    Source assertion: Native RXN-11482 has NAD on left, coefficient 1; physiological direction RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11482']/left/*[@frameid='NAD']; sibling coefficient (absent means 1); reaction-direction
an enoylpimeloyl-[acp] methyl ester
MetaCyc:Enoylpimeloyl-ACP-methyl-esters		consumes

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a pimeloyl-[acp] methyl ester + NAD+ <- an enoylpimeloyl-[acp] methyl ester + NADH + H+
MetaCyc:RXN-11482
  • MetaCyc:RXN-11482

    Source assertion: Native RXN-11482 has Enoylpimeloyl-ACP-methyl-esters on right, coefficient 1; physiological direction RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11482']/right/*[@frameid='Enoylpimeloyl-ACP-methyl-esters']; sibling coefficient (absent means 1); reaction-direction
NADH(2-)
CHEBI:57945		consumes

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a pimeloyl-[acp] methyl ester + NAD+ <- an enoylpimeloyl-[acp] methyl ester + NADH + H+
MetaCyc:RXN-11482
  • MetaCyc:RXN-11482

    Source assertion: Native RXN-11482 has NADH on right, coefficient 1; physiological direction RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11482']/right/*[@frameid='NADH']; sibling coefficient (absent means 1); reaction-direction
hydron
CHEBI:15378		consumes

Native reaction retained because no exact specific Rhea reaction was verified. Formal protonation of free NAD(P)(H), water, CO2 and hydron follows active ChEBI identities; native ACP classes lack empirical formulas.

a pimeloyl-[acp] methyl ester + NAD+ <- an enoylpimeloyl-[acp] methyl ester + NADH + H+
MetaCyc:RXN-11482
  • MetaCyc:RXN-11482

    Source assertion: Native RXN-11482 has PROTON on right, coefficient 1; physiological direction RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11482']/right/*[@frameid='PROTON']; sibling coefficient (absent means 1); reaction-direction
6-carboxyhexanoyl-[ACP] methyl ester
RHEA-COMP:10186		consumes

6-carboxyhexanoyl-[ACP] methyl ester + H2O => 6-carboxyhexanoyl-[ACP] + methanol + H(+)
RHEA:42701
  • RHEA:42701

    Source assertion: RHEA:42701 assigns RHEA-COMP:10186 to substrates, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/42701 rh:substrates; http://rdf.rhea-db.org/42700_L rh:contains1 http://rdf.rhea-db.org/Participant_42700_compound_10186; rh:compound http://rdf.rhea-db.org/Compound_10186
water
CHEBI:15377		consumes

6-carboxyhexanoyl-[ACP] methyl ester + H2O => 6-carboxyhexanoyl-[ACP] + methanol + H(+)
RHEA:42701
  • RHEA:42701

    Source assertion: RHEA:42701 assigns CHEBI:15377 to substrates, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/42701 rh:substrates; http://rdf.rhea-db.org/42700_L rh:contains1 http://rdf.rhea-db.org/Participant_42700_compound_1283; rh:compound http://rdf.rhea-db.org/Compound_1283
6-carboxyhexanoyl-[ACP] methyl ester + H2O => 6-carboxyhexanoyl-[ACP] + methanol + H(+)
RHEA:42701		produces

6-carboxyhexanoyl-[ACP]
RHEA-COMP:9955
  • RHEA:42701

    Source assertion: RHEA:42701 assigns RHEA-COMP:9955 to products, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/42701 rh:products; http://rdf.rhea-db.org/42700_R rh:contains1 http://rdf.rhea-db.org/Participant_42700_compound_9955; rh:compound http://rdf.rhea-db.org/Compound_9955
6-carboxyhexanoyl-[ACP] methyl ester + H2O => 6-carboxyhexanoyl-[ACP] + methanol + H(+)
RHEA:42701		produces

methanol
CHEBI:17790
  • RHEA:42701

    Source assertion: RHEA:42701 assigns CHEBI:17790 to products, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/42701 rh:products; http://rdf.rhea-db.org/42700_R rh:contains1 http://rdf.rhea-db.org/Participant_42700_compound_3528; rh:compound http://rdf.rhea-db.org/Compound_3528
6-carboxyhexanoyl-[ACP] methyl ester + H2O => 6-carboxyhexanoyl-[ACP] + methanol + H(+)
RHEA:42701		produces

hydron
CHEBI:15378
  • RHEA:42701

    Source assertion: RHEA:42701 assigns CHEBI:15378 to products, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/42701 rh:products; http://rdf.rhea-db.org/42700_R rh:contains1 http://rdf.rhea-db.org/Participant_42700_compound_3249; rh:compound http://rdf.rhea-db.org/Compound_3249
6-carboxyhexanoyl-[ACP]
RHEA-COMP:9955		consumes

6-carboxyhexanoyl-[ACP] + L-alanine + H(+) => (8S)-8-amino-7-oxononanoate + holo-[ACP] + CO2
RHEA:42289
  • RHEA:42289

    Source assertion: RHEA:42289 assigns RHEA-COMP:9955 to substrates, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/42289 rh:substrates; http://rdf.rhea-db.org/42288_L rh:contains1 http://rdf.rhea-db.org/Participant_42288_compound_9955; rh:compound http://rdf.rhea-db.org/Compound_9955
L-alanine zwitterion
CHEBI:57972		consumes

6-carboxyhexanoyl-[ACP] + L-alanine + H(+) => (8S)-8-amino-7-oxononanoate + holo-[ACP] + CO2
RHEA:42289
  • RHEA:42289

    Source assertion: RHEA:42289 assigns CHEBI:57972 to substrates, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/42289 rh:substrates; http://rdf.rhea-db.org/42288_L rh:contains1 http://rdf.rhea-db.org/Participant_42288_compound_3361; rh:compound http://rdf.rhea-db.org/Compound_3361
hydron
CHEBI:15378		consumes

6-carboxyhexanoyl-[ACP] + L-alanine + H(+) => (8S)-8-amino-7-oxononanoate + holo-[ACP] + CO2
RHEA:42289
  • RHEA:42289

    Source assertion: RHEA:42289 assigns CHEBI:15378 to substrates, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/42289 rh:substrates; http://rdf.rhea-db.org/42288_L rh:contains1 http://rdf.rhea-db.org/Participant_42288_compound_3249; rh:compound http://rdf.rhea-db.org/Compound_3249
6-carboxyhexanoyl-[ACP] + L-alanine + H(+) => (8S)-8-amino-7-oxononanoate + holo-[ACP] + CO2
RHEA:42289		produces

(8S)-8-amino-7-oxononanoic acid zwitterion
CHEBI:149468
  • RHEA:42289

    Source assertion: RHEA:42289 assigns CHEBI:149468 to products, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/42289 rh:products; http://rdf.rhea-db.org/42288_R rh:contains1 http://rdf.rhea-db.org/Participant_42288_compound_16402; rh:compound http://rdf.rhea-db.org/Compound_16402
6-carboxyhexanoyl-[ACP] + L-alanine + H(+) => (8S)-8-amino-7-oxononanoate + holo-[ACP] + CO2
RHEA:42289		produces

holo-[ACP]
RHEA-COMP:9685
  • RHEA:42289

    Source assertion: RHEA:42289 assigns RHEA-COMP:9685 to products, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/42289 rh:products; http://rdf.rhea-db.org/42288_R rh:contains1 http://rdf.rhea-db.org/Participant_42288_compound_9685; rh:compound http://rdf.rhea-db.org/Compound_9685
6-carboxyhexanoyl-[ACP] + L-alanine + H(+) => (8S)-8-amino-7-oxononanoate + holo-[ACP] + CO2
RHEA:42289		produces

carbon dioxide
CHEBI:16526
  • RHEA:42289

    Source assertion: RHEA:42289 assigns CHEBI:16526 to products, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/42289 rh:products; http://rdf.rhea-db.org/42288_R rh:contains1 http://rdf.rhea-db.org/Participant_42288_compound_4391; rh:compound http://rdf.rhea-db.org/Compound_4391
(8S)-8-amino-7-oxononanoic acid zwitterion
CHEBI:149468		consumes

(8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine => S-adenosyl-4-methylsulfanyl-2-oxobutanoate + (7R,8S)-7,8-diammoniononanoate
RHEA:16862
  • RHEA:16862

    Source assertion: RHEA:16862 assigns CHEBI:149468 to substrates, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/16862 rh:substrates; http://rdf.rhea-db.org/16861_L rh:contains1 http://rdf.rhea-db.org/Participant_16861_compound_16402; rh:compound http://rdf.rhea-db.org/Compound_16402
S-adenosyl-L-methionine zwitterion
CHEBI:59789		consumes

(8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine => S-adenosyl-4-methylsulfanyl-2-oxobutanoate + (7R,8S)-7,8-diammoniononanoate
RHEA:16862
  • RHEA:16862

    Source assertion: RHEA:16862 assigns CHEBI:59789 to substrates, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/16862 rh:substrates; http://rdf.rhea-db.org/16861_L rh:contains1 http://rdf.rhea-db.org/Participant_16861_compound_6127; rh:compound http://rdf.rhea-db.org/Compound_6127
(8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine => S-adenosyl-4-methylsulfanyl-2-oxobutanoate + (7R,8S)-7,8-diammoniononanoate
RHEA:16862		produces

S-adenosyl-4-methylthio-2-oxobutanoate
CHEBI:16490
  • RHEA:16862

    Source assertion: RHEA:16862 assigns CHEBI:16490 to products, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/16862 rh:products; http://rdf.rhea-db.org/16861_R rh:contains1 http://rdf.rhea-db.org/Participant_16861_compound_5784; rh:compound http://rdf.rhea-db.org/Compound_5784
(8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine => S-adenosyl-4-methylsulfanyl-2-oxobutanoate + (7R,8S)-7,8-diammoniononanoate
RHEA:16862		produces

(7R,8S)-7,8-diammoniononanoate
CHEBI:149469
  • RHEA:16862

    Source assertion: RHEA:16862 assigns CHEBI:149469 to products, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/16862 rh:products; http://rdf.rhea-db.org/16861_R rh:contains1 http://rdf.rhea-db.org/Participant_16861_compound_16403; rh:compound http://rdf.rhea-db.org/Compound_16403
(7R,8S)-7,8-diammoniononanoate
CHEBI:149469		consumes

(7R,8S)-7,8-diammoniononanoate + CO2 + ATP => (4R,5S)-dethiobiotin + ADP + phosphate + 3 H(+)
RHEA:15806
  • RHEA:15806

    Source assertion: RHEA:15806 assigns CHEBI:149469 to substrates, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/15806 rh:substrates; http://rdf.rhea-db.org/15805_L rh:contains1 http://rdf.rhea-db.org/Participant_15805_compound_16403; rh:compound http://rdf.rhea-db.org/Compound_16403
carbon dioxide
CHEBI:16526		consumes

(7R,8S)-7,8-diammoniononanoate + CO2 + ATP => (4R,5S)-dethiobiotin + ADP + phosphate + 3 H(+)
RHEA:15806
  • RHEA:15806

    Source assertion: RHEA:15806 assigns CHEBI:16526 to substrates, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/15806 rh:substrates; http://rdf.rhea-db.org/15805_L rh:contains1 http://rdf.rhea-db.org/Participant_15805_compound_4391; rh:compound http://rdf.rhea-db.org/Compound_4391
ATP(4-)
CHEBI:30616		consumes

(7R,8S)-7,8-diammoniononanoate + CO2 + ATP => (4R,5S)-dethiobiotin + ADP + phosphate + 3 H(+)
RHEA:15806
  • RHEA:15806

    Source assertion: RHEA:15806 assigns CHEBI:30616 to substrates, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/15806 rh:substrates; http://rdf.rhea-db.org/15805_L rh:contains1 http://rdf.rhea-db.org/Participant_15805_compound_6372; rh:compound http://rdf.rhea-db.org/Compound_6372
(7R,8S)-7,8-diammoniononanoate + CO2 + ATP => (4R,5S)-dethiobiotin + ADP + phosphate + 3 H(+)
RHEA:15806		produces

(4R,5S)-dethiobiotin(1-)
CHEBI:149473
  • RHEA:15806

    Source assertion: RHEA:15806 assigns CHEBI:149473 to products, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/15806 rh:products; http://rdf.rhea-db.org/15805_R rh:contains1 http://rdf.rhea-db.org/Participant_15805_compound_16404; rh:compound http://rdf.rhea-db.org/Compound_16404
(7R,8S)-7,8-diammoniononanoate + CO2 + ATP => (4R,5S)-dethiobiotin + ADP + phosphate + 3 H(+)
RHEA:15806		produces

ADP(3-)
CHEBI:456216
  • RHEA:15806

    Source assertion: RHEA:15806 assigns CHEBI:456216 to products, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/15806 rh:products; http://rdf.rhea-db.org/15805_R rh:contains1 http://rdf.rhea-db.org/Participant_15805_compound_2710; rh:compound http://rdf.rhea-db.org/Compound_2710
(7R,8S)-7,8-diammoniononanoate + CO2 + ATP => (4R,5S)-dethiobiotin + ADP + phosphate + 3 H(+)
RHEA:15806		produces

hydrogenphosphate
CHEBI:43474
  • RHEA:15806

    Source assertion: RHEA:15806 assigns CHEBI:43474 to products, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/15806 rh:products; http://rdf.rhea-db.org/15805_R rh:contains1 http://rdf.rhea-db.org/Participant_15805_compound_5518; rh:compound http://rdf.rhea-db.org/Compound_5518
(7R,8S)-7,8-diammoniononanoate + CO2 + ATP => (4R,5S)-dethiobiotin + ADP + phosphate + 3 H(+)
RHEA:15806		produces

hydron
CHEBI:15378
  • RHEA:15806

    Source assertion: RHEA:15806 assigns CHEBI:15378 to products, coefficient 3; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/15806 rh:products; http://rdf.rhea-db.org/15805_R rh:contains3 http://rdf.rhea-db.org/Participant_15805_compound_3249; rh:compound http://rdf.rhea-db.org/Compound_3249
(4R,5S)-dethiobiotin(1-)
CHEBI:149473		consumes

Formal Rhea sulfur-carrier/ferredoxin equation; the E. coli primary assay uses flavodoxin with ferredoxin/flavodoxin-NADP reductase and NADPH. These generic states do not identify that physiological donor or a specific sulfur-donor protein.

(4R,5S)-dethiobiotin + (sulfur carrier)-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine => (sulfur carrier)-H + biotin + 2 5'-deoxyadenosine + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
RHEA:22061
  • RHEA:22061

    Source assertion: RHEA:22061 assigns CHEBI:149473 to substrates, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/22061 rh:substrates; http://rdf.rhea-db.org/22060_L rh:contains1 http://rdf.rhea-db.org/Participant_22060_compound_16404; rh:compound http://rdf.rhea-db.org/Compound_16404
(sulfur carrier)-SH
RHEA-COMP:14737		consumes

Formal Rhea sulfur-carrier/ferredoxin equation; the E. coli primary assay uses flavodoxin with ferredoxin/flavodoxin-NADP reductase and NADPH. These generic states do not identify that physiological donor or a specific sulfur-donor protein.

(4R,5S)-dethiobiotin + (sulfur carrier)-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine => (sulfur carrier)-H + biotin + 2 5'-deoxyadenosine + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
RHEA:22061
  • RHEA:22061

    Source assertion: RHEA:22061 assigns RHEA-COMP:14737 to substrates, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/22061 rh:substrates; http://rdf.rhea-db.org/22060_L rh:contains1 http://rdf.rhea-db.org/Participant_22060_compound_14737; rh:compound http://rdf.rhea-db.org/Compound_14737
reduced [2Fe-2S]-[ferredoxin]
RHEA-COMP:10001		consumes

Formal Rhea sulfur-carrier/ferredoxin equation; the E. coli primary assay uses flavodoxin with ferredoxin/flavodoxin-NADP reductase and NADPH. These generic states do not identify that physiological donor or a specific sulfur-donor protein.

(4R,5S)-dethiobiotin + (sulfur carrier)-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine => (sulfur carrier)-H + biotin + 2 5'-deoxyadenosine + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
RHEA:22061
  • RHEA:22061

    Source assertion: RHEA:22061 assigns RHEA-COMP:10001 to substrates, coefficient 2; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/22061 rh:substrates; http://rdf.rhea-db.org/22060_L rh:contains2 http://rdf.rhea-db.org/Participant_22060_compound_10001; rh:compound http://rdf.rhea-db.org/Compound_10001
S-adenosyl-L-methionine zwitterion
CHEBI:59789		consumes

Formal Rhea sulfur-carrier/ferredoxin equation; the E. coli primary assay uses flavodoxin with ferredoxin/flavodoxin-NADP reductase and NADPH. These generic states do not identify that physiological donor or a specific sulfur-donor protein.

(4R,5S)-dethiobiotin + (sulfur carrier)-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine => (sulfur carrier)-H + biotin + 2 5'-deoxyadenosine + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
RHEA:22061
  • RHEA:22061

    Source assertion: RHEA:22061 assigns CHEBI:59789 to substrates, coefficient 2; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/22061 rh:substrates; http://rdf.rhea-db.org/22060_L rh:contains2 http://rdf.rhea-db.org/Participant_22060_compound_6127; rh:compound http://rdf.rhea-db.org/Compound_6127
(4R,5S)-dethiobiotin + (sulfur carrier)-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine => (sulfur carrier)-H + biotin + 2 5'-deoxyadenosine + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
RHEA:22061		produces

Formal Rhea sulfur-carrier/ferredoxin equation; the E. coli primary assay uses flavodoxin with ferredoxin/flavodoxin-NADP reductase and NADPH. These generic states do not identify that physiological donor or a specific sulfur-donor protein.

(sulfur carrier)-H
RHEA-COMP:14739
  • RHEA:22061

    Source assertion: RHEA:22061 assigns RHEA-COMP:14739 to products, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/22061 rh:products; http://rdf.rhea-db.org/22060_R rh:contains1 http://rdf.rhea-db.org/Participant_22060_compound_14739; rh:compound http://rdf.rhea-db.org/Compound_14739
(4R,5S)-dethiobiotin + (sulfur carrier)-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine => (sulfur carrier)-H + biotin + 2 5'-deoxyadenosine + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
RHEA:22061		produces

Formal Rhea sulfur-carrier/ferredoxin equation; the E. coli primary assay uses flavodoxin with ferredoxin/flavodoxin-NADP reductase and NADPH. These generic states do not identify that physiological donor or a specific sulfur-donor protein.

biotinate
CHEBI:57586
  • RHEA:22061

    Source assertion: RHEA:22061 assigns CHEBI:57586 to products, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/22061 rh:products; http://rdf.rhea-db.org/22060_R rh:contains1 http://rdf.rhea-db.org/Participant_22060_compound_2770; rh:compound http://rdf.rhea-db.org/Compound_2770
(4R,5S)-dethiobiotin + (sulfur carrier)-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine => (sulfur carrier)-H + biotin + 2 5'-deoxyadenosine + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
RHEA:22061		produces

Formal Rhea sulfur-carrier/ferredoxin equation; the E. coli primary assay uses flavodoxin with ferredoxin/flavodoxin-NADP reductase and NADPH. These generic states do not identify that physiological donor or a specific sulfur-donor protein.

5'-deoxyadenosine
CHEBI:17319
  • RHEA:22061

    Source assertion: RHEA:22061 assigns CHEBI:17319 to products, coefficient 2; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/22061 rh:products; http://rdf.rhea-db.org/22060_R rh:contains2 http://rdf.rhea-db.org/Participant_22060_compound_2028; rh:compound http://rdf.rhea-db.org/Compound_2028
(4R,5S)-dethiobiotin + (sulfur carrier)-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine => (sulfur carrier)-H + biotin + 2 5'-deoxyadenosine + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
RHEA:22061		produces

Formal Rhea sulfur-carrier/ferredoxin equation; the E. coli primary assay uses flavodoxin with ferredoxin/flavodoxin-NADP reductase and NADPH. These generic states do not identify that physiological donor or a specific sulfur-donor protein.

L-methionine zwitterion
CHEBI:57844
  • RHEA:22061

    Source assertion: RHEA:22061 assigns CHEBI:57844 to products, coefficient 2; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/22061 rh:products; http://rdf.rhea-db.org/22060_R rh:contains2 http://rdf.rhea-db.org/Participant_22060_compound_2530; rh:compound http://rdf.rhea-db.org/Compound_2530
(4R,5S)-dethiobiotin + (sulfur carrier)-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine => (sulfur carrier)-H + biotin + 2 5'-deoxyadenosine + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
RHEA:22061		produces

Formal Rhea sulfur-carrier/ferredoxin equation; the E. coli primary assay uses flavodoxin with ferredoxin/flavodoxin-NADP reductase and NADPH. These generic states do not identify that physiological donor or a specific sulfur-donor protein.

oxidized [2Fe-2S]-[ferredoxin]
RHEA-COMP:10000
  • RHEA:22061

    Source assertion: RHEA:22061 assigns RHEA-COMP:10000 to products, coefficient 2; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/22061 rh:products; http://rdf.rhea-db.org/22060_R rh:contains2 http://rdf.rhea-db.org/Participant_22060_compound_10000; rh:compound http://rdf.rhea-db.org/Compound_10000
malonyl-[ACP] + S-adenosyl-L-methionine => malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
RHEA:17106		part_of

MetaCyc:BIOTIN-BIOSYNTHESIS-PWY
  • MetaCyc:PWY-6519

    Source assertion: The native child pathway lists RXN-11475 as a reaction member.

    Source locationPathway[@frameid='PWY-6519']/reaction-list/Reaction[@frameid='RXN-11475']
  • MetaCyc:BIOTIN-BIOSYNTHESIS-PWY

    Source assertion: The complete parent contains child pathways PWY-6519 and PWY0-1507; PWY-6519 is one of these two members.

    Source locationPathway[@frameid='BIOTIN-BIOSYNTHESIS-PWY']/sub-pathways; reaction-list
  • MetaCyc:RXN-11475

    Source assertion: Native reaction RXN-11475 defines the corresponding substrate/product transformation; its Rhea cross-reference is 34900, not an assertion of a different current identifier.

    Source locationReaction[@frameid='RXN-11475']/left; right; dblink[dblink-db='RHEA']
  • RHEA:17106

    Source assertion: Current directed RHEA:17106 supplies the independently inspected normalized equation for this step; correspondence uses substrate/product chemistry and the current catalyst annotation.

    Source locationhttp://rdf.rhea-db.org/17106 rdfs:label; rh:substrates; rh:products
a malonyl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxoglutaryl-[acp] methyl ester + CO2 + acyl-carrier protein
MetaCyc:RXN-11474		part_of

MetaCyc:BIOTIN-BIOSYNTHESIS-PWY
  • MetaCyc:PWY-6519

    Source assertion: The native child pathway lists RXN-11474 as a reaction member.

    Source locationPathway[@frameid='PWY-6519']/reaction-list/Reaction[@frameid='RXN-11474']
  • MetaCyc:BIOTIN-BIOSYNTHESIS-PWY

    Source assertion: The complete parent contains child pathways PWY-6519 and PWY0-1507; PWY-6519 is one of these two members.

    Source locationPathway[@frameid='BIOTIN-BIOSYNTHESIS-PWY']/sub-pathways; reaction-list
a (3R)-3-hydroxyglutaryl-[acp] methyl ester + NADP+ <- a 3-oxoglutaryl-[acp] methyl ester + NADPH + H+
MetaCyc:RXN-11476		part_of

MetaCyc:BIOTIN-BIOSYNTHESIS-PWY
  • MetaCyc:PWY-6519

    Source assertion: The native child pathway lists RXN-11476 as a reaction member.

    Source locationPathway[@frameid='PWY-6519']/reaction-list/Reaction[@frameid='RXN-11476']
  • MetaCyc:BIOTIN-BIOSYNTHESIS-PWY

    Source assertion: The complete parent contains child pathways PWY-6519 and PWY0-1507; PWY-6519 is one of these two members.

    Source locationPathway[@frameid='BIOTIN-BIOSYNTHESIS-PWY']/sub-pathways; reaction-list
a (3R)-3-hydroxyglutaryl-[acp] methyl ester -> an enoylglutaryl-[acp] methyl ester + H2O
MetaCyc:RXN-11477		part_of

MetaCyc:BIOTIN-BIOSYNTHESIS-PWY
  • MetaCyc:PWY-6519

    Source assertion: The native child pathway lists RXN-11477 as a reaction member.

    Source locationPathway[@frameid='PWY-6519']/reaction-list/Reaction[@frameid='RXN-11477']
  • MetaCyc:BIOTIN-BIOSYNTHESIS-PWY

    Source assertion: The complete parent contains child pathways PWY-6519 and PWY0-1507; PWY-6519 is one of these two members.

    Source locationPathway[@frameid='BIOTIN-BIOSYNTHESIS-PWY']/sub-pathways; reaction-list
a glutaryl-[acp] methyl ester + NAD+ <- an enoylglutaryl-[acp] methyl ester + NADH + H+
MetaCyc:RXN-11478		part_of

MetaCyc:BIOTIN-BIOSYNTHESIS-PWY
  • MetaCyc:PWY-6519

    Source assertion: The native child pathway lists RXN-11478 as a reaction member.

    Source locationPathway[@frameid='PWY-6519']/reaction-list/Reaction[@frameid='RXN-11478']
  • MetaCyc:BIOTIN-BIOSYNTHESIS-PWY

    Source assertion: The complete parent contains child pathways PWY-6519 and PWY0-1507; PWY-6519 is one of these two members.

    Source locationPathway[@frameid='BIOTIN-BIOSYNTHESIS-PWY']/sub-pathways; reaction-list
a glutaryl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxopimeloyl-[acp] methyl ester + CO2 + acyl-carrier protein
MetaCyc:RXN-11479		part_of

MetaCyc:BIOTIN-BIOSYNTHESIS-PWY
  • MetaCyc:PWY-6519

    Source assertion: The native child pathway lists RXN-11479 as a reaction member.

    Source locationPathway[@frameid='PWY-6519']/reaction-list/Reaction[@frameid='RXN-11479']
  • MetaCyc:BIOTIN-BIOSYNTHESIS-PWY

    Source assertion: The complete parent contains child pathways PWY-6519 and PWY0-1507; PWY-6519 is one of these two members.

    Source locationPathway[@frameid='BIOTIN-BIOSYNTHESIS-PWY']/sub-pathways; reaction-list
a (3R)-3-hydroxypimeloyl-[acp] methyl ester + NADP+ <- a 3-oxopimeloyl-[acp] methyl ester + NADPH + H+
MetaCyc:RXN-11480		part_of

MetaCyc:BIOTIN-BIOSYNTHESIS-PWY
  • MetaCyc:PWY-6519

    Source assertion: The native child pathway lists RXN-11480 as a reaction member.

    Source locationPathway[@frameid='PWY-6519']/reaction-list/Reaction[@frameid='RXN-11480']
  • MetaCyc:BIOTIN-BIOSYNTHESIS-PWY

    Source assertion: The complete parent contains child pathways PWY-6519 and PWY0-1507; PWY-6519 is one of these two members.

    Source locationPathway[@frameid='BIOTIN-BIOSYNTHESIS-PWY']/sub-pathways; reaction-list
a (3R)-3-hydroxypimeloyl-[acp] methyl ester -> an enoylpimeloyl-[acp] methyl ester + H2O
MetaCyc:RXN-11481		part_of

MetaCyc:BIOTIN-BIOSYNTHESIS-PWY
  • MetaCyc:PWY-6519

    Source assertion: The native child pathway lists RXN-11481 as a reaction member.

    Source locationPathway[@frameid='PWY-6519']/reaction-list/Reaction[@frameid='RXN-11481']
  • MetaCyc:BIOTIN-BIOSYNTHESIS-PWY

    Source assertion: The complete parent contains child pathways PWY-6519 and PWY0-1507; PWY-6519 is one of these two members.

    Source locationPathway[@frameid='BIOTIN-BIOSYNTHESIS-PWY']/sub-pathways; reaction-list
a pimeloyl-[acp] methyl ester + NAD+ <- an enoylpimeloyl-[acp] methyl ester + NADH + H+
MetaCyc:RXN-11482		part_of

MetaCyc:BIOTIN-BIOSYNTHESIS-PWY
  • MetaCyc:PWY-6519

    Source assertion: The native child pathway lists RXN-11482 as a reaction member.

    Source locationPathway[@frameid='PWY-6519']/reaction-list/Reaction[@frameid='RXN-11482']
  • MetaCyc:BIOTIN-BIOSYNTHESIS-PWY

    Source assertion: The complete parent contains child pathways PWY-6519 and PWY0-1507; PWY-6519 is one of these two members.

    Source locationPathway[@frameid='BIOTIN-BIOSYNTHESIS-PWY']/sub-pathways; reaction-list
6-carboxyhexanoyl-[ACP] methyl ester + H2O => 6-carboxyhexanoyl-[ACP] + methanol + H(+)
RHEA:42701		part_of

MetaCyc:BIOTIN-BIOSYNTHESIS-PWY
  • MetaCyc:PWY-6519

    Source assertion: The native child pathway lists RXN-11483 as a reaction member.

    Source locationPathway[@frameid='PWY-6519']/reaction-list/Reaction[@frameid='RXN-11483']
  • MetaCyc:BIOTIN-BIOSYNTHESIS-PWY

    Source assertion: The complete parent contains child pathways PWY-6519 and PWY0-1507; PWY-6519 is one of these two members.

    Source locationPathway[@frameid='BIOTIN-BIOSYNTHESIS-PWY']/sub-pathways; reaction-list
  • MetaCyc:RXN-11483

    Source assertion: Native reaction RXN-11483 defines the corresponding substrate/product transformation; its Rhea cross-reference is 42701, not an assertion of a different current identifier.

    Source locationReaction[@frameid='RXN-11483']/left; right; dblink[dblink-db='RHEA']
  • RHEA:42701

    Source assertion: Current directed RHEA:42701 supplies the independently inspected normalized equation for this step; correspondence uses substrate/product chemistry and the current catalyst annotation.

    Source locationhttp://rdf.rhea-db.org/42701 rdfs:label; rh:substrates; rh:products
6-carboxyhexanoyl-[ACP] + L-alanine + H(+) => (8S)-8-amino-7-oxononanoate + holo-[ACP] + CO2
RHEA:42289		part_of

MetaCyc:BIOTIN-BIOSYNTHESIS-PWY
  • MetaCyc:PWY-6519

    Source assertion: The native child pathway lists RXN-11484 as a reaction member.

    Source locationPathway[@frameid='PWY-6519']/reaction-list/Reaction[@frameid='RXN-11484']
  • MetaCyc:BIOTIN-BIOSYNTHESIS-PWY

    Source assertion: The complete parent contains child pathways PWY-6519 and PWY0-1507; PWY-6519 is one of these two members.

    Source locationPathway[@frameid='BIOTIN-BIOSYNTHESIS-PWY']/sub-pathways; reaction-list
  • MetaCyc:RXN-11484

    Source assertion: Native reaction RXN-11484 defines the corresponding substrate/product transformation; its Rhea cross-reference is 42289, not an assertion of a different current identifier.

    Source locationReaction[@frameid='RXN-11484']/left; right; dblink[dblink-db='RHEA']
  • RHEA:42289

    Source assertion: Current directed RHEA:42289 supplies the independently inspected normalized equation for this step; correspondence uses substrate/product chemistry and the current catalyst annotation.

    Source locationhttp://rdf.rhea-db.org/42289 rdfs:label; rh:substrates; rh:products
(8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine => S-adenosyl-4-methylsulfanyl-2-oxobutanoate + (7R,8S)-7,8-diammoniononanoate
RHEA:16862		part_of

MetaCyc:BIOTIN-BIOSYNTHESIS-PWY
  • MetaCyc:PWY0-1507

    Source assertion: The native child pathway lists DAPASYN-RXN as a reaction member.

    Source locationPathway[@frameid='PWY0-1507']/reaction-list/Reaction[@frameid='DAPASYN-RXN']
  • MetaCyc:BIOTIN-BIOSYNTHESIS-PWY

    Source assertion: The complete parent contains child pathways PWY-6519 and PWY0-1507; PWY0-1507 is one of these two members.

    Source locationPathway[@frameid='BIOTIN-BIOSYNTHESIS-PWY']/sub-pathways; reaction-list
  • MetaCyc:DAPASYN-RXN

    Source assertion: Native reaction DAPASYN-RXN defines the corresponding substrate/product transformation; its Rhea cross-reference is 16864, not an assertion of a different current identifier.

    Source locationReaction[@frameid='DAPASYN-RXN']/left; right; dblink[dblink-db='RHEA']
  • RHEA:16862

    Source assertion: Current directed RHEA:16862 supplies the independently inspected normalized equation for this step; correspondence uses substrate/product chemistry and the current catalyst annotation.

    Source locationhttp://rdf.rhea-db.org/16862 rdfs:label; rh:substrates; rh:products
(7R,8S)-7,8-diammoniononanoate + CO2 + ATP => (4R,5S)-dethiobiotin + ADP + phosphate + 3 H(+)
RHEA:15806		part_of

MetaCyc:BIOTIN-BIOSYNTHESIS-PWY
  • MetaCyc:PWY0-1507

    Source assertion: The native child pathway lists DETHIOBIOTIN-SYN-RXN as a reaction member.

    Source locationPathway[@frameid='PWY0-1507']/reaction-list/Reaction[@frameid='DETHIOBIOTIN-SYN-RXN']
  • MetaCyc:BIOTIN-BIOSYNTHESIS-PWY

    Source assertion: The complete parent contains child pathways PWY-6519 and PWY0-1507; PWY0-1507 is one of these two members.

    Source locationPathway[@frameid='BIOTIN-BIOSYNTHESIS-PWY']/sub-pathways; reaction-list
  • MetaCyc:DETHIOBIOTIN-SYN-RXN

    Source assertion: Native reaction DETHIOBIOTIN-SYN-RXN defines the corresponding substrate/product transformation; its Rhea cross-reference is 15805, not an assertion of a different current identifier.

    Source locationReaction[@frameid='DETHIOBIOTIN-SYN-RXN']/left; right; dblink[dblink-db='RHEA']
  • RHEA:15806

    Source assertion: Current directed RHEA:15806 supplies the independently inspected normalized equation for this step; correspondence uses substrate/product chemistry and the current catalyst annotation.

    Source locationhttp://rdf.rhea-db.org/15806 rdfs:label; rh:substrates; rh:products
(4R,5S)-dethiobiotin + (sulfur carrier)-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine => (sulfur carrier)-H + biotin + 2 5'-deoxyadenosine + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
RHEA:22061		part_of

MetaCyc:BIOTIN-BIOSYNTHESIS-PWY
  • MetaCyc:PWY0-1507

    Source assertion: The native child pathway lists 2.8.1.6-RXN as a reaction member.

    Source locationPathway[@frameid='PWY0-1507']/reaction-list/Reaction[@frameid='2.8.1.6-RXN']
  • MetaCyc:BIOTIN-BIOSYNTHESIS-PWY

    Source assertion: The complete parent contains child pathways PWY-6519 and PWY0-1507; PWY0-1507 is one of these two members.

    Source locationPathway[@frameid='BIOTIN-BIOSYNTHESIS-PWY']/sub-pathways; reaction-list
  • MetaCyc:2.8.1.6-RXN

    Source assertion: Native reaction 2.8.1.6-RXN defines the corresponding substrate/product transformation; its Rhea cross-reference is 22061, not an assertion of a different current identifier.

    Source locationReaction[@frameid='2.8.1.6-RXN']/left; right; dblink[dblink-db='RHEA']
  • RHEA:22061

    Source assertion: Current directed RHEA:22061 supplies the independently inspected normalized equation for this step; correspondence uses substrate/product chemistry and the current catalyst annotation.

    Source locationhttp://rdf.rhea-db.org/22061 rdfs:label; rh:substrates; rh:products
malonyl-[ACP] + S-adenosyl-L-methionine => malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
RHEA:17106		precedes

Sequential intermediate: RHEA-COMP:9954. This ordering does not assert physical substrate channeling.

a malonyl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxoglutaryl-[acp] methyl ester + CO2 + acyl-carrier protein
MetaCyc:RXN-11474
  • MetaCyc:PWY-6519

    Source assertion: Native reaction-ordering places RXN-11475 before RXN-11474; the separately cited chemical sides identify the shared intermediate.

    Source locationPathway[@frameid='PWY-6519']/reaction-ordering[Reaction/@frameid='RXN-11474']/predecessor-reactions/Reaction[@frameid='RXN-11475']
  • RHEA:17106

    Source assertion: RHEA:17106 assigns RHEA-COMP:9954 to products, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/17106 rh:products; http://rdf.rhea-db.org/17105_R rh:contains1 http://rdf.rhea-db.org/Participant_17105_compound_9954; rh:compound http://rdf.rhea-db.org/Compound_9954
  • MetaCyc:RXN-11474

    Source assertion: Native RXN-11474 has Malonyl-acp-methyl-ester on left, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11474']/left/*[@frameid='Malonyl-acp-methyl-ester']; sibling coefficient (absent means 1); reaction-direction
  • RHEA:17106

    Source assertion: Independent Rhea whole-carrier identity used for the native ACP state: RHEA-COMP:9954; reactive-part ChEBI is not the whole carrier.

    Source locationhttp://rdf.rhea-db.org/Compound_9954 rh:name; rh:reactivePart
a malonyl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxoglutaryl-[acp] methyl ester + CO2 + acyl-carrier protein
MetaCyc:RXN-11474		precedes

Sequential intermediate: MetaCyc:3-Ketoglutaryl-ACP-methyl-ester. This ordering does not assert physical substrate channeling.

a (3R)-3-hydroxyglutaryl-[acp] methyl ester + NADP+ <- a 3-oxoglutaryl-[acp] methyl ester + NADPH + H+
MetaCyc:RXN-11476
  • MetaCyc:PWY-6519

    Source assertion: Native reaction-ordering places RXN-11474 before RXN-11476; the separately cited chemical sides identify the shared intermediate.

    Source locationPathway[@frameid='PWY-6519']/reaction-ordering[Reaction/@frameid='RXN-11476']/predecessor-reactions/Reaction[@frameid='RXN-11474']
  • MetaCyc:RXN-11474

    Source assertion: Native RXN-11474 has 3-Ketoglutaryl-ACP-methyl-ester on right, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11474']/right/*[@frameid='3-Ketoglutaryl-ACP-methyl-ester']; sibling coefficient (absent means 1); reaction-direction
  • MetaCyc:RXN-11476

    Source assertion: Native RXN-11476 has 3-Ketoglutaryl-ACP-methyl-ester on right, coefficient 1; physiological direction PHYSIOL-RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11476']/right/*[@frameid='3-Ketoglutaryl-ACP-methyl-ester']; sibling coefficient (absent means 1); reaction-direction
a (3R)-3-hydroxyglutaryl-[acp] methyl ester + NADP+ <- a 3-oxoglutaryl-[acp] methyl ester + NADPH + H+
MetaCyc:RXN-11476		precedes

Sequential intermediate: MetaCyc:3-Hydroxyglutaryl-ACP-methyl-ester. This ordering does not assert physical substrate channeling.

a (3R)-3-hydroxyglutaryl-[acp] methyl ester -> an enoylglutaryl-[acp] methyl ester + H2O
MetaCyc:RXN-11477
  • MetaCyc:PWY-6519

    Source assertion: Native reaction-ordering places RXN-11476 before RXN-11477; the separately cited chemical sides identify the shared intermediate.

    Source locationPathway[@frameid='PWY-6519']/reaction-ordering[Reaction/@frameid='RXN-11477']/predecessor-reactions/Reaction[@frameid='RXN-11476']
  • MetaCyc:RXN-11476

    Source assertion: Native RXN-11476 has 3-Hydroxyglutaryl-ACP-methyl-ester on left, coefficient 1; physiological direction PHYSIOL-RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11476']/left/*[@frameid='3-Hydroxyglutaryl-ACP-methyl-ester']; sibling coefficient (absent means 1); reaction-direction
  • MetaCyc:RXN-11477

    Source assertion: Native RXN-11477 has 3-Hydroxyglutaryl-ACP-methyl-ester on left, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11477']/left/*[@frameid='3-Hydroxyglutaryl-ACP-methyl-ester']; sibling coefficient (absent means 1); reaction-direction
a (3R)-3-hydroxyglutaryl-[acp] methyl ester -> an enoylglutaryl-[acp] methyl ester + H2O
MetaCyc:RXN-11477		precedes

Sequential intermediate: MetaCyc:Enoylglutaryl-ACP-methyl-esters. This ordering does not assert physical substrate channeling.

a glutaryl-[acp] methyl ester + NAD+ <- an enoylglutaryl-[acp] methyl ester + NADH + H+
MetaCyc:RXN-11478
  • MetaCyc:PWY-6519

    Source assertion: Native reaction-ordering places RXN-11477 before RXN-11478; the separately cited chemical sides identify the shared intermediate.

    Source locationPathway[@frameid='PWY-6519']/reaction-ordering[Reaction/@frameid='RXN-11478']/predecessor-reactions/Reaction[@frameid='RXN-11477']
  • MetaCyc:RXN-11477

    Source assertion: Native RXN-11477 has Enoylglutaryl-ACP-methyl-esters on right, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11477']/right/*[@frameid='Enoylglutaryl-ACP-methyl-esters']; sibling coefficient (absent means 1); reaction-direction
  • MetaCyc:RXN-11478

    Source assertion: Native RXN-11478 has Enoylglutaryl-ACP-methyl-esters on right, coefficient 1; physiological direction RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11478']/right/*[@frameid='Enoylglutaryl-ACP-methyl-esters']; sibling coefficient (absent means 1); reaction-direction
a glutaryl-[acp] methyl ester + NAD+ <- an enoylglutaryl-[acp] methyl ester + NADH + H+
MetaCyc:RXN-11478		precedes

Sequential intermediate: MetaCyc:Glutaryl-ACP-methyl-esters. This ordering does not assert physical substrate channeling.

a glutaryl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxopimeloyl-[acp] methyl ester + CO2 + acyl-carrier protein
MetaCyc:RXN-11479
  • MetaCyc:PWY-6519

    Source assertion: Native reaction-ordering places RXN-11478 before RXN-11479; the separately cited chemical sides identify the shared intermediate.

    Source locationPathway[@frameid='PWY-6519']/reaction-ordering[Reaction/@frameid='RXN-11479']/predecessor-reactions/Reaction[@frameid='RXN-11478']
  • MetaCyc:RXN-11478

    Source assertion: Native RXN-11478 has Glutaryl-ACP-methyl-esters on left, coefficient 1; physiological direction RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11478']/left/*[@frameid='Glutaryl-ACP-methyl-esters']; sibling coefficient (absent means 1); reaction-direction
  • MetaCyc:RXN-11479

    Source assertion: Native RXN-11479 has Glutaryl-ACP-methyl-esters on left, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11479']/left/*[@frameid='Glutaryl-ACP-methyl-esters']; sibling coefficient (absent means 1); reaction-direction
a glutaryl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxopimeloyl-[acp] methyl ester + CO2 + acyl-carrier protein
MetaCyc:RXN-11479		precedes

Sequential intermediate: MetaCyc:3-Ketopimeloyl-ACP-methyl-esters. This ordering does not assert physical substrate channeling.

a (3R)-3-hydroxypimeloyl-[acp] methyl ester + NADP+ <- a 3-oxopimeloyl-[acp] methyl ester + NADPH + H+
MetaCyc:RXN-11480
  • MetaCyc:PWY-6519

    Source assertion: Native reaction-ordering places RXN-11479 before RXN-11480; the separately cited chemical sides identify the shared intermediate.

    Source locationPathway[@frameid='PWY-6519']/reaction-ordering[Reaction/@frameid='RXN-11480']/predecessor-reactions/Reaction[@frameid='RXN-11479']
  • MetaCyc:RXN-11479

    Source assertion: Native RXN-11479 has 3-Ketopimeloyl-ACP-methyl-esters on right, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11479']/right/*[@frameid='3-Ketopimeloyl-ACP-methyl-esters']; sibling coefficient (absent means 1); reaction-direction
  • MetaCyc:RXN-11480

    Source assertion: Native RXN-11480 has 3-Ketopimeloyl-ACP-methyl-esters on right, coefficient 1; physiological direction PHYSIOL-RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11480']/right/*[@frameid='3-Ketopimeloyl-ACP-methyl-esters']; sibling coefficient (absent means 1); reaction-direction
a (3R)-3-hydroxypimeloyl-[acp] methyl ester + NADP+ <- a 3-oxopimeloyl-[acp] methyl ester + NADPH + H+
MetaCyc:RXN-11480		precedes

Sequential intermediate: MetaCyc:3-hydroxypimeloyl-ACP-methyl-esters. This ordering does not assert physical substrate channeling.

a (3R)-3-hydroxypimeloyl-[acp] methyl ester -> an enoylpimeloyl-[acp] methyl ester + H2O
MetaCyc:RXN-11481
  • MetaCyc:PWY-6519

    Source assertion: Native reaction-ordering places RXN-11480 before RXN-11481; the separately cited chemical sides identify the shared intermediate.

    Source locationPathway[@frameid='PWY-6519']/reaction-ordering[Reaction/@frameid='RXN-11481']/predecessor-reactions/Reaction[@frameid='RXN-11480']
  • MetaCyc:RXN-11480

    Source assertion: Native RXN-11480 has 3-hydroxypimeloyl-ACP-methyl-esters on left, coefficient 1; physiological direction PHYSIOL-RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11480']/left/*[@frameid='3-hydroxypimeloyl-ACP-methyl-esters']; sibling coefficient (absent means 1); reaction-direction
  • MetaCyc:RXN-11481

    Source assertion: Native RXN-11481 has 3-hydroxypimeloyl-ACP-methyl-esters on left, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11481']/left/*[@frameid='3-hydroxypimeloyl-ACP-methyl-esters']; sibling coefficient (absent means 1); reaction-direction
a (3R)-3-hydroxypimeloyl-[acp] methyl ester -> an enoylpimeloyl-[acp] methyl ester + H2O
MetaCyc:RXN-11481		precedes

Sequential intermediate: MetaCyc:Enoylpimeloyl-ACP-methyl-esters. This ordering does not assert physical substrate channeling.

a pimeloyl-[acp] methyl ester + NAD+ <- an enoylpimeloyl-[acp] methyl ester + NADH + H+
MetaCyc:RXN-11482
  • MetaCyc:PWY-6519

    Source assertion: Native reaction-ordering places RXN-11481 before RXN-11482; the separately cited chemical sides identify the shared intermediate.

    Source locationPathway[@frameid='PWY-6519']/reaction-ordering[Reaction/@frameid='RXN-11482']/predecessor-reactions/Reaction[@frameid='RXN-11481']
  • MetaCyc:RXN-11481

    Source assertion: Native RXN-11481 has Enoylpimeloyl-ACP-methyl-esters on right, coefficient 1; physiological direction LEFT-TO-RIGHT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11481']/right/*[@frameid='Enoylpimeloyl-ACP-methyl-esters']; sibling coefficient (absent means 1); reaction-direction
  • MetaCyc:RXN-11482

    Source assertion: Native RXN-11482 has Enoylpimeloyl-ACP-methyl-esters on right, coefficient 1; physiological direction RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11482']/right/*[@frameid='Enoylpimeloyl-ACP-methyl-esters']; sibling coefficient (absent means 1); reaction-direction
a pimeloyl-[acp] methyl ester + NAD+ <- an enoylpimeloyl-[acp] methyl ester + NADH + H+
MetaCyc:RXN-11482		precedes

Sequential intermediate: RHEA-COMP:10186. This ordering does not assert physical substrate channeling.

6-carboxyhexanoyl-[ACP] methyl ester + H2O => 6-carboxyhexanoyl-[ACP] + methanol + H(+)
RHEA:42701
  • MetaCyc:PWY-6519

    Source assertion: Native reaction-ordering places RXN-11482 before RXN-11483; the separately cited chemical sides identify the shared intermediate.

    Source locationPathway[@frameid='PWY-6519']/reaction-ordering[Reaction/@frameid='RXN-11483']/predecessor-reactions/Reaction[@frameid='RXN-11482']
  • MetaCyc:RXN-11482

    Source assertion: Native RXN-11482 has Pimeloyl-ACP-methyl-esters on left, coefficient 1; physiological direction RIGHT-TO-LEFT. Whole ACP classes are preserved.

    Source locationReaction[@frameid='RXN-11482']/left/*[@frameid='Pimeloyl-ACP-methyl-esters']; sibling coefficient (absent means 1); reaction-direction
  • RHEA:42701

    Source assertion: Independent Rhea whole-carrier identity used for the native ACP state: RHEA-COMP:10186; reactive-part ChEBI is not the whole carrier.

    Source locationhttp://rdf.rhea-db.org/Compound_10186 rh:name; rh:reactivePart
  • RHEA:42701

    Source assertion: RHEA:42701 assigns RHEA-COMP:10186 to substrates, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/42701 rh:substrates; http://rdf.rhea-db.org/42700_L rh:contains1 http://rdf.rhea-db.org/Participant_42700_compound_10186; rh:compound http://rdf.rhea-db.org/Compound_10186
6-carboxyhexanoyl-[ACP] methyl ester + H2O => 6-carboxyhexanoyl-[ACP] + methanol + H(+)
RHEA:42701		precedes

Sequential intermediate: RHEA-COMP:9955. This ordering does not assert physical substrate channeling.

6-carboxyhexanoyl-[ACP] + L-alanine + H(+) => (8S)-8-amino-7-oxononanoate + holo-[ACP] + CO2
RHEA:42289
  • MetaCyc:PWY-6519

    Source assertion: Native reaction-ordering places RXN-11483 before RXN-11484; the separately cited chemical sides identify the shared intermediate.

    Source locationPathway[@frameid='PWY-6519']/reaction-ordering[Reaction/@frameid='RXN-11484']/predecessor-reactions/Reaction[@frameid='RXN-11483']
  • RHEA:42701

    Source assertion: RHEA:42701 assigns RHEA-COMP:9955 to products, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/42701 rh:products; http://rdf.rhea-db.org/42700_R rh:contains1 http://rdf.rhea-db.org/Participant_42700_compound_9955; rh:compound http://rdf.rhea-db.org/Compound_9955
  • RHEA:42289

    Source assertion: RHEA:42289 assigns RHEA-COMP:9955 to substrates, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/42289 rh:substrates; http://rdf.rhea-db.org/42288_L rh:contains1 http://rdf.rhea-db.org/Participant_42288_compound_9955; rh:compound http://rdf.rhea-db.org/Compound_9955
6-carboxyhexanoyl-[ACP] + L-alanine + H(+) => (8S)-8-amino-7-oxononanoate + holo-[ACP] + CO2
RHEA:42289		precedes

Sequential intermediate: CHEBI:149468. This ordering does not assert physical substrate channeling.

(8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine => S-adenosyl-4-methylsulfanyl-2-oxobutanoate + (7R,8S)-7,8-diammoniononanoate
RHEA:16862
  • MetaCyc:BIOTIN-BIOSYNTHESIS-PWY

    Source assertion: Native reaction-ordering places RXN-11484 before DAPASYN-RXN; the separately cited chemical sides identify the shared intermediate.

    Source locationPathway[@frameid='BIOTIN-BIOSYNTHESIS-PWY']/reaction-ordering[Reaction/@frameid='DAPASYN-RXN']/predecessor-reactions/Reaction[@frameid='RXN-11484']
  • RHEA:42289

    Source assertion: RHEA:42289 assigns CHEBI:149468 to products, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/42289 rh:products; http://rdf.rhea-db.org/42288_R rh:contains1 http://rdf.rhea-db.org/Participant_42288_compound_16402; rh:compound http://rdf.rhea-db.org/Compound_16402
  • RHEA:16862

    Source assertion: RHEA:16862 assigns CHEBI:149468 to substrates, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/16862 rh:substrates; http://rdf.rhea-db.org/16861_L rh:contains1 http://rdf.rhea-db.org/Participant_16861_compound_16402; rh:compound http://rdf.rhea-db.org/Compound_16402
(8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine => S-adenosyl-4-methylsulfanyl-2-oxobutanoate + (7R,8S)-7,8-diammoniononanoate
RHEA:16862		precedes

Sequential intermediate: CHEBI:149469. This ordering does not assert physical substrate channeling.

(7R,8S)-7,8-diammoniononanoate + CO2 + ATP => (4R,5S)-dethiobiotin + ADP + phosphate + 3 H(+)
RHEA:15806
  • MetaCyc:PWY0-1507

    Source assertion: Native reaction-ordering places DAPASYN-RXN before DETHIOBIOTIN-SYN-RXN; the separately cited chemical sides identify the shared intermediate.

    Source locationPathway[@frameid='PWY0-1507']/reaction-ordering[Reaction/@frameid='DETHIOBIOTIN-SYN-RXN']/predecessor-reactions/Reaction[@frameid='DAPASYN-RXN']
  • RHEA:16862

    Source assertion: RHEA:16862 assigns CHEBI:149469 to products, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/16862 rh:products; http://rdf.rhea-db.org/16861_R rh:contains1 http://rdf.rhea-db.org/Participant_16861_compound_16403; rh:compound http://rdf.rhea-db.org/Compound_16403
  • RHEA:15806

    Source assertion: RHEA:15806 assigns CHEBI:149469 to substrates, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/15806 rh:substrates; http://rdf.rhea-db.org/15805_L rh:contains1 http://rdf.rhea-db.org/Participant_15805_compound_16403; rh:compound http://rdf.rhea-db.org/Compound_16403
(7R,8S)-7,8-diammoniononanoate + CO2 + ATP => (4R,5S)-dethiobiotin + ADP + phosphate + 3 H(+)
RHEA:15806		precedes

Sequential intermediate: CHEBI:149473. This ordering does not assert physical substrate channeling.

(4R,5S)-dethiobiotin + (sulfur carrier)-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine => (sulfur carrier)-H + biotin + 2 5'-deoxyadenosine + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
RHEA:22061
  • MetaCyc:PWY0-1507

    Source assertion: Native reaction-ordering places DETHIOBIOTIN-SYN-RXN before 2.8.1.6-RXN; the separately cited chemical sides identify the shared intermediate.

    Source locationPathway[@frameid='PWY0-1507']/reaction-ordering[Reaction/@frameid='2.8.1.6-RXN']/predecessor-reactions/Reaction[@frameid='DETHIOBIOTIN-SYN-RXN']
  • RHEA:15806

    Source assertion: RHEA:15806 assigns CHEBI:149473 to products, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/15806 rh:products; http://rdf.rhea-db.org/15805_R rh:contains1 http://rdf.rhea-db.org/Participant_15805_compound_16404; rh:compound http://rdf.rhea-db.org/Compound_16404
  • RHEA:22061

    Source assertion: RHEA:22061 assigns CHEBI:149473 to substrates, coefficient 1; generic polypeptide states remain whole carriers.

    Source locationhttp://rdf.rhea-db.org/22061 rh:substrates; http://rdf.rhea-db.org/22060_L rh:contains1 http://rdf.rhea-db.org/Participant_22060_compound_16404; rh:compound http://rdf.rhea-db.org/Compound_16404
8-amino-7-oxononanoate synthase
MetaCyc:7KAPSYN-CPLX		has_part

Native assembly stoichiometry; no claim that an isolated subunit is catalytically sufficient.

8-amino-7-oxononanoate synthase
UniProtKB:P12998
  • MetaCyc:7KAPSYN-CPLX

    Source assertion: Native complex has 2 copies of 7KAPSYN-MONOMER; the species frame is E. coli MG1655.

    Source locationProtein[@frameid='7KAPSYN-CPLX']/component; coefficient; species/Organism[@frameid='TAX-511145']
  • MetaCyc:7KAPSYN-MONOMER

    Source assertion: Native subunit cross-reference identifies UniProtKB:P12998.

    Source locationProtein[@frameid='7KAPSYN-MONOMER']/dblink[dblink-db='UNIPROT']
adenosylmethionine-8-amino-7-oxononanoate aminotransferase
MetaCyc:DAPASYN-CPLX		has_part

Native assembly stoichiometry; no claim that an isolated subunit is catalytically sufficient.

Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
UniProtKB:P12995
  • MetaCyc:DAPASYN-CPLX

    Source assertion: Native complex has 2 copies of DAPASYN-MONOMER; the species frame is E. coli MG1655.

    Source locationProtein[@frameid='DAPASYN-CPLX']/component; coefficient; species/Organism[@frameid='TAX-511145']
  • MetaCyc:DAPASYN-MONOMER

    Source assertion: Native subunit cross-reference identifies UniProtKB:P12995.

    Source locationProtein[@frameid='DAPASYN-MONOMER']/dblink[dblink-db='UNIPROT']
dethiobiotin synthetase
MetaCyc:DETHIOBIOTIN-SYN-CPLX		has_part

Native assembly stoichiometry; no claim that an isolated subunit is catalytically sufficient.

ATP-dependent dethiobiotin synthetase BioD 1
UniProtKB:P13000
  • MetaCyc:DETHIOBIOTIN-SYN-CPLX

    Source assertion: Native complex has 2 copies of DETHIOBIOTIN-SYN-MONOMER; the species frame is E. coli MG1655.

    Source locationProtein[@frameid='DETHIOBIOTIN-SYN-CPLX']/component; coefficient; species/Organism[@frameid='TAX-511145']
  • MetaCyc:DETHIOBIOTIN-SYN-MONOMER

    Source assertion: Native subunit cross-reference identifies UniProtKB:P13000.

    Source locationProtein[@frameid='DETHIOBIOTIN-SYN-MONOMER']/dblink[dblink-db='UNIPROT']
biotin synthase
MetaCyc:BIOTIN-SYN-CPLX		has_part

Native assembly stoichiometry; no claim that an isolated subunit is catalytically sufficient.

Biotin synthase
UniProtKB:P12996
  • MetaCyc:BIOTIN-SYN-CPLX

    Source assertion: Native complex has 2 copies of BIOTIN-SYN-MONOMER; the species frame is E. coli MG1655.

    Source locationProtein[@frameid='BIOTIN-SYN-CPLX']/component; coefficient; species/Organism[@frameid='TAX-511145']
  • MetaCyc:BIOTIN-SYN-MONOMER

    Source assertion: Native subunit cross-reference identifies UniProtKB:P12996.

    Source locationProtein[@frameid='BIOTIN-SYN-MONOMER']/dblink[dblink-db='UNIPROT']
3-oxoacyl-[acyl-carrier-protein] reductase FabG
MetaCyc:CPLX0-8005		has_part

Native assembly stoichiometry; no claim that an isolated subunit is catalytically sufficient.

3-oxoacyl-[acyl-carrier-protein] reductase FabG
UniProtKB:P0AEK2
  • MetaCyc:CPLX0-8005

    Source assertion: Native complex has 4 copies of 3-OXOACYL-ACP-REDUCT-MONOMER; the species frame is E. coli MG1655.

    Source locationProtein[@frameid='CPLX0-8005']/component; coefficient; species/Organism[@frameid='TAX-511145']
  • MetaCyc:3-OXOACYL-ACP-REDUCT-MONOMER

    Source assertion: Native subunit cross-reference identifies UniProtKB:P0AEK2.

    Source locationProtein[@frameid='3-OXOACYL-ACP-REDUCT-MONOMER']/dblink[dblink-db='UNIPROT']
3-hydroxy-acyl-[acyl-carrier-protein] dehydratase
MetaCyc:FABZ-CPLX		has_part

Native assembly stoichiometry; no claim that an isolated subunit is catalytically sufficient. Hexamer assignment is based on E. coli His-tagged protein gel filtration, not the P. aeruginosa crystal as an E. coli measurement.

3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
UniProtKB:P0A6Q6
  • MetaCyc:FABZ-CPLX

    Source assertion: Native complex has 6 copies of FABZ-MONOMER; the species frame is E. coli MG1655.

    Source locationProtein[@frameid='FABZ-CPLX']/component; coefficient; species/Organism[@frameid='TAX-511145']
  • MetaCyc:FABZ-MONOMER

    Source assertion: Native subunit cross-reference identifies UniProtKB:P0A6Q6.

    Source locationProtein[@frameid='FABZ-MONOMER']/dblink[dblink-db='UNIPROT']
enoyl-[acyl-carrier-protein] reductase
MetaCyc:CPLX0-8006		has_part

Native assembly stoichiometry; no claim that an isolated subunit is catalytically sufficient.

Enoyl-[acyl-carrier-protein] reductase [NADH] FabI
UniProtKB:P0AEK4
  • MetaCyc:CPLX0-8006

    Source assertion: Native complex has 4 copies of ENOYL-ACP-REDUCT-NADH-MONOMER; the species frame is E. coli MG1655.

    Source locationProtein[@frameid='CPLX0-8006']/component; coefficient; species/Organism[@frameid='TAX-511145']
  • MetaCyc:ENOYL-ACP-REDUCT-NADH-MONOMER

    Source assertion: Native subunit cross-reference identifies UniProtKB:P0AEK4.

    Source locationProtein[@frameid='ENOYL-ACP-REDUCT-NADH-MONOMER']/dblink[dblink-db='UNIPROT']
beta-ketoacyl-[acyl carrier protein] synthase I
MetaCyc:FABB-CPLX		has_part

Native assembly stoichiometry; no claim that an isolated subunit is catalytically sufficient.

3-oxoacyl-[acyl-carrier-protein] synthase 1
UniProtKB:P0A953
  • MetaCyc:FABB-CPLX

    Source assertion: Native complex has 2 copies of FABB-MONOMER; the species frame is E. coli MG1655.

    Source locationProtein[@frameid='FABB-CPLX']/component; coefficient; species/Organism[@frameid='TAX-511145']
  • MetaCyc:FABB-MONOMER

    Source assertion: Native subunit cross-reference identifies UniProtKB:P0A953.

    Source locationProtein[@frameid='FABB-MONOMER']/dblink[dblink-db='UNIPROT']
Malonyl-[acyl-carrier protein] O-methyltransferase
UniProtKB:P12999		enables

E. coli BioC supports the route genetically and in a weak refolded coupled assay. Direct purified malonyl-ACP methyltransferase experiments used B. cereus BioC; those data do not establish an E. coli oligomer.

malonyl-[ACP] + S-adenosyl-L-methionine => malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
RHEA:17106
  • MetaCyc:ENZRXN-17863

    Source assertion: Native enzymatic-reaction connects EG10119-MONOMER to RXN-11475. The biotin-specific FAS/BioC assignment is indirect where its native evidence is EV-EXP-IMP or reaction-blocked.

    Source locationEnzymatic-Reaction[@frameid='ENZRXN-17863']/enzyme; reaction; citation
  • MetaCyc:EG10119-MONOMER

    Source assertion: Native protein cross-reference identifies UniProtKB:P12999.

    Source locationProtein[@frameid='EG10119-MONOMER']/dblink[dblink-db='UNIPROT']
  • UniProtKB:P12999

    Source assertion: Current reviewed catalytic-activity annotation links P12999 to RHEA:17105; exact directed chemistry is separately grounded in Rhea 142. Annotation evidence codes remain in the protein source projection.

    Source locationresults[primaryAccession='P12999'].comments[commentType='CATALYTIC ACTIVITY'].reaction.reactionCrossReferences
  • PMID:22965231

    Source assertion: Purified B. cereus BioC complemented E. coli bioC and favored malonyl-ACP over malonyl-CoA. Active E. coli BioC purification remained problematic; the direct enzyme assay was not on the E. coli protein.

    Source locationAbstract; Results, paragraph beginning We tested malonyl-ACP and malonyl-CoA
3-oxoacyl-[acyl-carrier-protein] reductase FabG
MetaCyc:CPLX0-8005		enables

Source-supported functional role, not a purified-substrate assay or isolated-subunit sufficiency claim. Native FAS assignments are supported by pathway genetics/inhibition and general enzyme specificity.

a (3R)-3-hydroxyglutaryl-[acp] methyl ester + NADP+ <- a 3-oxoglutaryl-[acp] methyl ester + NADPH + H+
MetaCyc:RXN-11476
  • MetaCyc:ENZRXN-17867

    Source assertion: Native enzymatic-reaction connects CPLX0-8005 to RXN-11476. The biotin-specific FAS/BioC assignment is indirect where its native evidence is EV-EXP-IMP or reaction-blocked.

    Source locationEnzymatic-Reaction[@frameid='ENZRXN-17867']/enzyme; reaction; citation
  • UniProtKB:P0AEK2

    Source assertion: Reviewed FUNCTION annotation describes the protein fatty-acid synthesis activity (ECO:0000269). It does not by itself establish the exact biotin methyl-ester substrate; that assignment is separately sourced to MetaCyc.

    Source locationresults[primaryAccession='P0AEK2'].comments[commentType='FUNCTION']
3-hydroxy-acyl-[acyl-carrier-protein] dehydratase
MetaCyc:FABZ-CPLX		enables

Source-supported functional role, not a purified-substrate assay or isolated-subunit sufficiency claim. Native FAS assignments are supported by pathway genetics/inhibition and general enzyme specificity.

a (3R)-3-hydroxyglutaryl-[acp] methyl ester -> an enoylglutaryl-[acp] methyl ester + H2O
MetaCyc:RXN-11477
  • MetaCyc:ENZRXN-17869

    Source assertion: Native enzymatic-reaction connects FABZ-CPLX to RXN-11477. The biotin-specific FAS/BioC assignment is indirect where its native evidence is EV-EXP-IMP or reaction-blocked.

    Source locationEnzymatic-Reaction[@frameid='ENZRXN-17869']/enzyme; reaction; citation
  • UniProtKB:P0A6Q6

    Source assertion: Reviewed FUNCTION annotation describes the protein fatty-acid synthesis activity (ECO:0000269). It does not by itself establish the exact biotin methyl-ester substrate; that assignment is separately sourced to MetaCyc.

    Source locationresults[primaryAccession='P0A6Q6'].comments[commentType='FUNCTION']
enoyl-[acyl-carrier-protein] reductase
MetaCyc:CPLX0-8006		enables

Source-supported functional role, not a purified-substrate assay or isolated-subunit sufficiency claim. Native FAS assignments are supported by pathway genetics/inhibition and general enzyme specificity.

a glutaryl-[acp] methyl ester + NAD+ <- an enoylglutaryl-[acp] methyl ester + NADH + H+
MetaCyc:RXN-11478
  • MetaCyc:ENZRXN-17871

    Source assertion: Native enzymatic-reaction connects CPLX0-8006 to RXN-11478. The biotin-specific FAS/BioC assignment is indirect where its native evidence is EV-EXP-IMP or reaction-blocked.

    Source locationEnzymatic-Reaction[@frameid='ENZRXN-17871']/enzyme; reaction; citation
  • UniProtKB:P0AEK4

    Source assertion: Reviewed FUNCTION annotation describes the protein fatty-acid synthesis activity (ECO:0000269). It does not by itself establish the exact biotin methyl-ester substrate; that assignment is separately sourced to MetaCyc.

    Source locationresults[primaryAccession='P0AEK4'].comments[commentType='FUNCTION']
beta-ketoacyl-[acyl carrier protein] synthase I
MetaCyc:FABB-CPLX		enables

Source-supported functional role, not a purified-substrate assay or isolated-subunit sufficiency claim. Native FAS assignments are supported by pathway genetics/inhibition and general enzyme specificity.

a glutaryl-[acp] methyl ester + a malonyl-[acp] + H+ -> a 3-oxopimeloyl-[acp] methyl ester + CO2 + acyl-carrier protein
MetaCyc:RXN-11479
  • MetaCyc:ENZRXN-17873

    Source assertion: Native enzymatic-reaction connects FABB-CPLX to RXN-11479. The biotin-specific FAS/BioC assignment is indirect where its native evidence is EV-EXP-IMP or reaction-blocked.

    Source locationEnzymatic-Reaction[@frameid='ENZRXN-17873']/enzyme; reaction; citation
  • UniProtKB:P0A953

    Source assertion: Reviewed FUNCTION annotation describes the protein fatty-acid synthesis activity (ECO:0000269). It does not by itself establish the exact biotin methyl-ester substrate; that assignment is separately sourced to MetaCyc.

    Source locationresults[primaryAccession='P0A953'].comments[commentType='FUNCTION']
3-oxoacyl-[acyl-carrier-protein] reductase FabG
MetaCyc:CPLX0-8005		enables

Source-supported functional role, not a purified-substrate assay or isolated-subunit sufficiency claim. Native FAS assignments are supported by pathway genetics/inhibition and general enzyme specificity.

a (3R)-3-hydroxypimeloyl-[acp] methyl ester + NADP+ <- a 3-oxopimeloyl-[acp] methyl ester + NADPH + H+
MetaCyc:RXN-11480
  • MetaCyc:ENZRXN-17868

    Source assertion: Native enzymatic-reaction connects CPLX0-8005 to RXN-11480. The biotin-specific FAS/BioC assignment is indirect where its native evidence is EV-EXP-IMP or reaction-blocked.

    Source locationEnzymatic-Reaction[@frameid='ENZRXN-17868']/enzyme; reaction; citation
  • UniProtKB:P0AEK2

    Source assertion: Reviewed FUNCTION annotation describes the protein fatty-acid synthesis activity (ECO:0000269). It does not by itself establish the exact biotin methyl-ester substrate; that assignment is separately sourced to MetaCyc.

    Source locationresults[primaryAccession='P0AEK2'].comments[commentType='FUNCTION']
3-hydroxy-acyl-[acyl-carrier-protein] dehydratase
MetaCyc:FABZ-CPLX		enables

Source-supported functional role, not a purified-substrate assay or isolated-subunit sufficiency claim. Native FAS assignments are supported by pathway genetics/inhibition and general enzyme specificity.

a (3R)-3-hydroxypimeloyl-[acp] methyl ester -> an enoylpimeloyl-[acp] methyl ester + H2O
MetaCyc:RXN-11481
  • MetaCyc:ENZRXN-17870

    Source assertion: Native enzymatic-reaction connects FABZ-CPLX to RXN-11481. The biotin-specific FAS/BioC assignment is indirect where its native evidence is EV-EXP-IMP or reaction-blocked.

    Source locationEnzymatic-Reaction[@frameid='ENZRXN-17870']/enzyme; reaction; citation
  • UniProtKB:P0A6Q6

    Source assertion: Reviewed FUNCTION annotation describes the protein fatty-acid synthesis activity (ECO:0000269). It does not by itself establish the exact biotin methyl-ester substrate; that assignment is separately sourced to MetaCyc.

    Source locationresults[primaryAccession='P0A6Q6'].comments[commentType='FUNCTION']
enoyl-[acyl-carrier-protein] reductase
MetaCyc:CPLX0-8006		enables

Source-supported functional role, not a purified-substrate assay or isolated-subunit sufficiency claim. Native FAS assignments are supported by pathway genetics/inhibition and general enzyme specificity.

a pimeloyl-[acp] methyl ester + NAD+ <- an enoylpimeloyl-[acp] methyl ester + NADH + H+
MetaCyc:RXN-11482
  • MetaCyc:ENZRXN-17872

    Source assertion: Native enzymatic-reaction connects CPLX0-8006 to RXN-11482. The biotin-specific FAS/BioC assignment is indirect where its native evidence is EV-EXP-IMP or reaction-blocked.

    Source locationEnzymatic-Reaction[@frameid='ENZRXN-17872']/enzyme; reaction; citation
  • UniProtKB:P0AEK4

    Source assertion: Reviewed FUNCTION annotation describes the protein fatty-acid synthesis activity (ECO:0000269). It does not by itself establish the exact biotin methyl-ester substrate; that assignment is separately sourced to MetaCyc.

    Source locationresults[primaryAccession='P0AEK4'].comments[commentType='FUNCTION']
Pimeloyl-[acyl-carrier protein] methyl ester esterase
UniProtKB:P13001		catalyzes

6-carboxyhexanoyl-[ACP] methyl ester + H2O => 6-carboxyhexanoyl-[ACP] + methanol + H(+)
RHEA:42701
  • MetaCyc:ENZRXN-17864

    Source assertion: Native enzymatic-reaction connects EG10122-MONOMER to RXN-11483. The biotin-specific FAS/BioC assignment is indirect where its native evidence is EV-EXP-IMP or reaction-blocked.

    Source locationEnzymatic-Reaction[@frameid='ENZRXN-17864']/enzyme; reaction; citation
  • MetaCyc:EG10122-MONOMER

    Source assertion: Native protein cross-reference identifies UniProtKB:P13001.

    Source locationProtein[@frameid='EG10122-MONOMER']/dblink[dblink-db='UNIPROT']
  • UniProtKB:P13001

    Source assertion: Current reviewed catalytic-activity annotation links P13001 to RHEA:42700; exact directed chemistry is separately grounded in Rhea 142. Annotation evidence codes remain in the protein source projection.

    Source locationresults[primaryAccession='P13001'].comments[commentType='CATALYTIC ACTIVITY'].reaction.reactionCrossReferences
  • PMID:23045647

    Source assertion: BioH S82A was crystallized with pimeloyl-ACP methyl ester; biochemical mutagenesis and E. coli complementation establish the native BioH gatekeeper substrate. The trapped enzyme-substrate complex is not a permanent oligomer.

    Source locationAbstract; Results, BioH:ACP Interactions; Discussion
8-amino-7-oxononanoate synthase
MetaCyc:7KAPSYN-CPLX		catalyzes

6-carboxyhexanoyl-[ACP] + L-alanine + H(+) => (8S)-8-amino-7-oxononanoate + holo-[ACP] + CO2
RHEA:42289
  • MetaCyc:ENZRXN-17865

    Source assertion: Native enzymatic-reaction connects 7KAPSYN-CPLX to RXN-11484. The biotin-specific FAS/BioC assignment is indirect where its native evidence is EV-EXP-IMP or reaction-blocked.

    Source locationEnzymatic-Reaction[@frameid='ENZRXN-17865']/enzyme; reaction; citation
  • UniProtKB:P12998

    Source assertion: Current reviewed catalytic-activity annotation links P12998 to RHEA:42288; exact directed chemistry is separately grounded in Rhea 142. Annotation evidence codes remain in the protein source projection.

    Source locationresults[primaryAccession='P12998'].comments[commentType='CATALYTIC ACTIVITY'].reaction.reactionCrossReferences
  • PMID:20693992

    Source assertion: E. coli growth bypass with AasS plus monomethyl pimelate or BioW plus pimelate argues that BioF accepts ACP and CoA thioesters. This is not purified BioF substrate kinetics; the native ACP-specific evidence is unpurified/coupled.

    Source locationResults, paragraph P6; Supplementary Fig. 3 as discussed in main text (supplement not independently inspected)
  • PMID:10642176

    Source assertion: E. coli AONS is PLP-dependent and forms the 8(S) product from L-alanine and pimeloyl-CoA; this older kinetic study does not directly prove ACP-substrate kinetics.

    Source locationIndexed abstract
adenosylmethionine-8-amino-7-oxononanoate aminotransferase
MetaCyc:DAPASYN-CPLX		catalyzes

(8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine => S-adenosyl-4-methylsulfanyl-2-oxobutanoate + (7R,8S)-7,8-diammoniononanoate
RHEA:16862
  • MetaCyc:DAPASYN-ENZRXN

    Source assertion: Native enzymatic-reaction connects DAPASYN-CPLX to DAPASYN-RXN. The biotin-specific FAS/BioC assignment is indirect where its native evidence is EV-EXP-IMP or reaction-blocked.

    Source locationEnzymatic-Reaction[@frameid='DAPASYN-ENZRXN']/enzyme; reaction; citation
  • UniProtKB:P12995

    Source assertion: Current reviewed catalytic-activity annotation links P12995 to RHEA:16861; exact directed chemistry is separately grounded in Rhea 142. Annotation evidence codes remain in the protein source projection.

    Source locationresults[primaryAccession='P12995'].comments[commentType='CATALYTIC ACTIVITY'].reaction.reactionCrossReferences
  • PMID:1092681

    Source assertion: The E. coli aminotransferase uses SAM as amino donor, has a PLP cofactor and an estimated 94 kDa dimer of 47 kDa subunits; the preparation was estimated 86% homogeneous.

    Source locationIndexed abstract
dethiobiotin synthetase
MetaCyc:DETHIOBIOTIN-SYN-CPLX		catalyzes

(7R,8S)-7,8-diammoniononanoate + CO2 + ATP => (4R,5S)-dethiobiotin + ADP + phosphate + 3 H(+)
RHEA:15806
  • MetaCyc:DETHIOBIOTIN-SYN-ENZRXN

    Source assertion: Native enzymatic-reaction connects DETHIOBIOTIN-SYN-CPLX to DETHIOBIOTIN-SYN-RXN. The biotin-specific FAS/BioC assignment is indirect where its native evidence is EV-EXP-IMP or reaction-blocked.

    Source locationEnzymatic-Reaction[@frameid='DETHIOBIOTIN-SYN-ENZRXN']/enzyme; reaction; citation
  • UniProtKB:P13000

    Source assertion: Current reviewed catalytic-activity annotation links P13000 to RHEA:15805; exact directed chemistry is separately grounded in Rhea 142. Annotation evidence codes remain in the protein source projection.

    Source locationcomments[commentType='CATALYTIC ACTIVITY'].reaction.reactionCrossReferences
  • PMID:7669755

    Source assertion: Only the N7-carbamate of (7R,8S)-diaminononanoate is the cyclization intermediate; commitment occurs upon MgATP addition. CO2 is the net Rhea substrate, not a separately inserted bicarbonate reaction.

    Source locationIndexed abstract (publisher abstract is truncated)
biotin synthase
MetaCyc:BIOTIN-SYN-CPLX		catalyzes

Formal Rhea net chemistry retains generic sulfur-carrier and ferredoxin states. E. coli BioB assays use flavodoxin/reductase/NADPH; no specific ferredoxin identity or entire cluster-repair mechanism is asserted.

(4R,5S)-dethiobiotin + (sulfur carrier)-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine => (sulfur carrier)-H + biotin + 2 5'-deoxyadenosine + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
RHEA:22061
  • MetaCyc:BIOTIN-SYN-ENZRXN

    Source assertion: Native enzymatic-reaction connects BIOTIN-SYN-CPLX to 2.8.1.6-RXN. The biotin-specific FAS/BioC assignment is indirect where its native evidence is EV-EXP-IMP or reaction-blocked.

    Source locationEnzymatic-Reaction[@frameid='BIOTIN-SYN-ENZRXN']/enzyme; reaction; citation
  • UniProtKB:P12996

    Source assertion: Current reviewed catalytic-activity annotation links P12996 to RHEA:22060; exact directed chemistry is separately grounded in Rhea 142. Annotation evidence codes remain in the protein source projection.

    Source locationresults[primaryAccession='P12996'].comments[commentType='CATALYTIC ACTIVITY'].reaction.reactionCrossReferences
  • PMID:20961145

    Source assertion: Optimized anaerobic assays with purified SAM and MTAN relieve product inhibition and show multiple BioB turnovers. The electron-transfer assay uses flavodoxin, ferredoxin/flavodoxin-NADP reductase and NADPH.

    Source locationMethods, Biotin Synthase Activity Assay, P9; Results/Discussion on multiple turnovers
8-amino-7-oxononanoate synthase
MetaCyc:7KAPSYN-CPLX		has_cofactor

pyridoxal 5'-phosphate(2-)
CHEBI:597326
  • UniProtKB:P12998

    Source assertion: BioF is annotated to bind pyridoxal phosphate; current COFACTOR evidence includes direct E. coli kinetic/structural studies.

    Source locationresults[primaryAccession='P12998'].comments[commentType='COFACTOR']
adenosylmethionine-8-amino-7-oxononanoate aminotransferase
MetaCyc:DAPASYN-CPLX		has_cofactor

pyridoxal 5'-phosphate(2-)
CHEBI:597326
  • UniProtKB:P12995

    Source assertion: BioA is annotated to bind pyridoxal phosphate; primary E. coli purification and kinetic studies establish the cofactor.

    Source locationresults[primaryAccession='P12995'].comments[commentType='COFACTOR']
dethiobiotin synthetase
MetaCyc:DETHIOBIOTIN-SYN-CPLX		has_cofactor

magnesium(2+)
CHEBI:18420
  • UniProtKB:P13000

    Source assertion: BioD1 binds one Mg(2+) per subunit; one structure shows a second Mg(2+). Direct-study annotation must not be simplified to a fixed universal two-metal stoichiometry.

    Source locationcomments[commentType='COFACTOR']
biotin synthase
MetaCyc:BIOTIN-SYN-CPLX		has_cofactor

tetra-mu3-sulfido-tetrairon
CHEBI:49883
  • UniProtKB:P12996

    Source assertion: BioB binds one radical-SAM [4Fe-4S] cluster per subunit; the distinct [2Fe-2S] cluster is separately represented.

    Source locationresults[primaryAccession='P12996'].comments[commentType='COFACTOR']
  • PMID:14704425

    Source assertion: The E. coli structure contains both Fe-S clusters and positions SAM and dethiobiotin between them. The structure favors a cluster-based sulfur mechanism and does not support a PLP-binding site.

    Source locationP7-P8; Figure 1
biotin synthase
MetaCyc:BIOTIN-SYN-CPLX		has_cofactor

di-mu-sulfido-diiron
CHEBI:190135
  • UniProtKB:P12996

    Source assertion: BioB binds one [2Fe-2S] cluster per subunit; this sulfur-associated cluster is distinct from the radical-SAM [4Fe-4S] cluster.

    Source locationresults[primaryAccession='P12996'].comments[commentType='COFACTOR']
  • PMID:14704425

    Source assertion: The E. coli structure contains both Fe-S clusters and positions SAM and dethiobiotin between them. The structure favors a cluster-based sulfur mechanism and does not support a PLP-binding site.

    Source locationP7-P8; Figure 1

References

Curation history