nitrate reduction I (denitrification)

MetaCyc:DENITRIFICATION-PWY

Complete native nitrate-to-dinitrogen route with five listed objects: vectorial Nar nitrate reduction, nitrate/nitrite exchange, c551-dependent nitrite reduction, cytochrome-c-dependent NO reduction and N2O reduction. PAO1 experiments support the respiratory system; strict NarK2 antiport versus uniport remains unresolved, so native antiport is explicitly a database convention and has no assigned PAO1 catalyst. Whole carrier classes and side-specific proton coefficients are retained without choosing a quinone species or a unique NosZ donor. Functional gene-product edges do not imply isolated subunit catalysis. Other-species native complex IDs are not transferred; NirS/NosZ dimer and Nar/Nor assembly annotations retain source-specific evidence tiers. Current NorB proton-pump annotation conflicts with cNOR structural evidence and is excluded; RCSB 3O0R has source-PAO1 protein sequences differing from current entries. Inferred cofactors retain their evidence tiers; ligand-state IDs do not fix catalytic redox state. Native background nitrite-to-ammonium prose, Nap compensation, qNOR variants, assimilatory reduction, electron-carrier regeneration and ATP synthesis are outside this selected route.

Pathway type
anaerobic respiration
Organism scope

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Pathway network

45 nodes · 75 asserted directed edges

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Pathway network: nitrate reduction I (denitrification) 45 nodes · 75 asserted directed edges. Every arrow links to its evidence table row; nodes link to their component details. Isolated declared components are retained. MetaCyc:DENITRIFICATION-PWY — has_part → MetaCyc:RXN-11236; Complete native route member; source reaction direction is retained separately from the pathway L2R traversal.; Evidence: MetaCyc:DENITRIFICATION-PWYhas part MetaCyc:DENITRIFICATION-PWY — has_part → MetaCyc:TRANS-RXN0-239; Native nitrate/nitrite antiport convention is retained as a complete source-defined step. PAO1 transport function is experimentally supported, but strict antiport versus uniport and its exact catalyst assignment remain unresolved.; Evidence: MetaCyc:DENITRIFICATION-PWY, PMID:16391109has part MetaCyc:DENITRIFICATION-PWY — has_part → MetaCyc:RXN-15838; Complete native route member; source reaction direction is retained separately from the pathway L2R traversal.; Evidence: MetaCyc:DENITRIFICATION-PWYhas part MetaCyc:DENITRIFICATION-PWY — has_part → MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN; Complete native route member; source reaction direction is retained separately from the pathway L2R traversal.; Evidence: MetaCyc:DENITRIFICATION-PWYhas part MetaCyc:DENITRIFICATION-PWY — has_part → MetaCyc:RXN-12130; Complete native route member; source reaction direction is retained separately from the pathway L2R traversal.; Evidence: MetaCyc:DENITRIFICATION-PWYhas part MetaCyc:ETR-Quinols — consumes → MetaCyc:RXN-11236; Coefficient 1; membrane electron-transfer class; side not specified. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:RXN-11236, MetaCyc:ETR-Quinolsconsumes CHEBI:17632 — consumes → MetaCyc:RXN-11236; Coefficient 1; cytoplasmic side. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:RXN-11236, MetaCyc:NITRATE, CHEBI:17632consumes CHEBI:15378 — consumes → MetaCyc:RXN-11236; Coefficient 2; cytoplasmic side. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:RXN-11236, MetaCyc:PROTON, CHEBI:15378consumes MetaCyc:RXN-11236 — produces → MetaCyc:ETR-Quinones; Coefficient 1; membrane electron-transfer class; side not specified. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:RXN-11236, MetaCyc:ETR-Quinonesproduces MetaCyc:RXN-11236 — produces → CHEBI:15378; Coefficient 2; periplasmic side. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:RXN-11236, MetaCyc:PROTON, CHEBI:15378produces MetaCyc:RXN-11236 — produces → CHEBI:16301; Coefficient 1; cytoplasmic side. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:RXN-11236, MetaCyc:NITRITE, CHEBI:16301produces MetaCyc:RXN-11236 — produces → CHEBI:15377; Coefficient 1; cytoplasmic side. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:RXN-11236, MetaCyc:WATER, CHEBI:15377produces MetaCyc:TRANS-RXN0-239 — has_input → CHEBI:17632; Coefficient 1; periplasmic side. Native compartmental equation and class identity retained. Formal antiport convention; exact PAO1 mode/catalyst is unassigned, not experimentally established stoichiometry.; Evidence: MetaCyc:TRANS-RXN0-239, MetaCyc:NITRATE, CHEBI:17632has input MetaCyc:TRANS-RXN0-239 — has_input → CHEBI:16301; Coefficient 1; cytoplasmic side. Native compartmental equation and class identity retained. Formal antiport convention; exact PAO1 mode/catalyst is unassigned, not experimentally established stoichiometry.; Evidence: MetaCyc:TRANS-RXN0-239, MetaCyc:NITRITE, CHEBI:16301has input MetaCyc:TRANS-RXN0-239 — has_output → CHEBI:17632; Coefficient 1; cytoplasmic side. Native compartmental equation and class identity retained. Formal antiport convention; exact PAO1 mode/catalyst is unassigned, not experimentally established stoichiometry.; Evidence: MetaCyc:TRANS-RXN0-239, MetaCyc:NITRATE, CHEBI:17632has output MetaCyc:TRANS-RXN0-239 — has_output → CHEBI:16301; Coefficient 1; periplasmic side. Native compartmental equation and class identity retained. Formal antiport convention; exact PAO1 mode/catalyst is unassigned, not experimentally established stoichiometry.; Evidence: MetaCyc:TRANS-RXN0-239, MetaCyc:NITRITE, CHEBI:16301has output CHEBI:16301 — consumes → MetaCyc:RXN-15838; Coefficient 1; periplasmic side. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:RXN-15838, MetaCyc:NITRITE, CHEBI:16301consumes MetaCyc:Reduced-cytochromes-c551 — consumes → MetaCyc:RXN-15838; Coefficient 1; periplasmic side. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:RXN-15838, MetaCyc:Reduced-cytochromes-c551consumes CHEBI:15378 — consumes → MetaCyc:RXN-15838; Coefficient 2; periplasmic side. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:RXN-15838, MetaCyc:PROTON, CHEBI:15378consumes MetaCyc:RXN-15838 — produces → CHEBI:15377; Coefficient 1; periplasmic side. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:RXN-15838, MetaCyc:WATER, CHEBI:15377produces MetaCyc:RXN-15838 — produces → CHEBI:16480; Coefficient 1; periplasmic side. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:RXN-15838, MetaCyc:NITRIC-OXIDE, CHEBI:16480produces MetaCyc:RXN-15838 — produces → MetaCyc:Oxidized-cytochromes-c551; Coefficient 1; periplasmic side. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:RXN-15838, MetaCyc:Oxidized-cytochromes-c551produces MetaCyc:Cytochromes-C-Reduced — consumes → MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN; Coefficient 2; periplasmic side. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN, MetaCyc:Cytochromes-C-Reducedconsumes CHEBI:16480 — consumes → MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN; Coefficient 2; periplasmic side. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN, MetaCyc:NITRIC-OXIDE, CHEBI:16480consumes CHEBI:15378 — consumes → MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN; Coefficient 2; periplasmic side. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN, MetaCyc:PROTON, CHEBI:15378consumes MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN — produces → CHEBI:17045; Coefficient 1; periplasmic side. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN, MetaCyc:NITROUS-OXIDE, CHEBI:17045produces MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN — produces → MetaCyc:Cytochromes-C-Oxidized; Coefficient 2; periplasmic side. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN, MetaCyc:Cytochromes-C-Oxidizedproduces MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN — produces → CHEBI:15377; Coefficient 1; periplasmic side. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN, MetaCyc:WATER, CHEBI:15377produces MetaCyc:Cytochromes-C-Reduced — consumes → MetaCyc:RXN-12130; Coefficient 2; periplasmic side. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:RXN-12130, MetaCyc:Cytochromes-C-Reducedconsumes CHEBI:17045 — consumes → MetaCyc:RXN-12130; Coefficient 1; periplasmic side. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:RXN-12130, MetaCyc:NITROUS-OXIDE, CHEBI:17045consumes CHEBI:15378 — consumes → MetaCyc:RXN-12130; Coefficient 2; periplasmic side. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:RXN-12130, MetaCyc:PROTON, CHEBI:15378consumes MetaCyc:RXN-12130 — produces → MetaCyc:Cytochromes-C-Oxidized; Coefficient 2; periplasmic side. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:RXN-12130, MetaCyc:Cytochromes-C-Oxidizedproduces MetaCyc:RXN-12130 — produces → CHEBI:15377; Coefficient 1; periplasmic side. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:RXN-12130, MetaCyc:WATER, CHEBI:15377produces MetaCyc:RXN-12130 — produces → CHEBI:17997; Coefficient 1; periplasmic side. Native compartmental equation and class identity retained. ; Evidence: MetaCyc:RXN-12130, MetaCyc:NITROGEN-MOLECULE, CHEBI:17997produces MetaCyc:RXN-11236 — precedes → MetaCyc:TRANS-RXN0-239; Source-defined reaction ordering; transport is coupled to nitrate reduction and no exclusive temporal separation or in vivo flux is inferred.; Evidence: MetaCyc:DENITRIFICATION-PWYprecedes MetaCyc:TRANS-RXN0-239 — precedes → MetaCyc:RXN-15838; Source-defined reaction ordering; transport is coupled to nitrate reduction and no exclusive temporal separation or in vivo flux is inferred.; Evidence: MetaCyc:DENITRIFICATION-PWYprecedes MetaCyc:RXN-15838 — precedes → MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN; Source-defined reaction ordering; transport is coupled to nitrate reduction and no exclusive temporal separation or in vivo flux is inferred.; Evidence: MetaCyc:DENITRIFICATION-PWYprecedes MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN — precedes → MetaCyc:RXN-12130; Source-defined reaction ordering; transport is coupled to nitrate reduction and no exclusive temporal separation or in vivo flux is inferred.; Evidence: MetaCyc:DENITRIFICATION-PWYprecedes UniProtKB:G3XCX1 — enables → MetaCyc:RXN-11236; Gene-product component of the Nar respiratory ensemble, not isolated-subunit catalysis. Current activity is ARBA inference; the source vectorial proton convention is not derived from that chemical-class annotation.; Evidence: UniProtKB:G3XCX1, UniProtKB:G3XCX1, PMID:16391109enables UniProtKB:G3XD87 — enables → MetaCyc:RXN-11236; Gene-product component of the Nar respiratory ensemble, not isolated-subunit catalysis. Current activity is ARBA inference; the source vectorial proton convention is not derived from that chemical-class annotation.; Evidence: UniProtKB:G3XD87, UniProtKB:G3XD87, PMID:16391109enables UniProtKB:G3XD18 — enables → MetaCyc:RXN-11236; Gene-product component of the Nar respiratory ensemble, not isolated-subunit catalysis. Current activity is ARBA inference; the source vectorial proton convention is not derived from that chemical-class annotation.; Evidence: UniProtKB:G3XD18, UniProtKB:G3XD18, PMID:16391109enables UniProtKB:P24474 — enables → MetaCyc:RXN-15838; Current NirS nitrite-reductase activity with source c551 donor convention; the protein is reported as a homodimer, but no other-species MetaCyc complex ID is transferred.; Evidence: UniProtKB:P24474, UniProtKB:P24474, PMID:25386171enables UniProtKB:Q59647 — enables → MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN; Subunit function in the NorBC ensemble, not isolated-subunit catalysis. Current NorB proton-pump prose is excluded. RCSB 3O0R PAO1 preparations differ from current sequences (NorB lacks current R301; NorC K100 versus N100), so no exact construct equivalence is asserted.; Evidence: UniProtKB:Q59647, UniProtKB:Q59647, UniProtKB:Q59647, PMID:21109633, DOI:10.2210/pdb3o0r/pdb, UniProtKB:Q59647, DOI:10.1126/science.1195591enables UniProtKB:Q59646 — enables → MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN; Subunit function in the NorBC ensemble, not isolated-subunit catalysis. Current NorB proton-pump prose is excluded. RCSB 3O0R PAO1 preparations differ from current sequences (NorB lacks current R301; NorC K100 versus N100), so no exact construct equivalence is asserted.; Evidence: UniProtKB:Q59646, UniProtKB:Q59646, PMID:21109633, DOI:10.2210/pdb3o0r/pdbenables UniProtKB:Q9HYL2 — enables → MetaCyc:RXN-12130; NosZ activity is annotated by HAMAP; PAO1 deletion physiology independently supports terminal N2O reduction. Generic c-type electron donor is a source reaction convention, not a uniquely identified physiological partner.; Evidence: UniProtKB:Q9HYL2, UniProtKB:Q9HYL2, PMID:30093706, PMID:25386171enables UniProtKB:Q9HXD4 — enables → MetaCyc:DENITRIFICATION-PWY; Nitrate/nitrite transport contribution to the complete pathway; this edge does not assign strict 1:1 antiport or isolated exact transport stoichiometry. NarK2 has the dominant phenotype and NarK1 a smaller contribution in the tested PAO1 conditions.; Evidence: UniProtKB:Q9HXD4, PMID:16391109, PMID:16391109enables UniProtKB:G3XD60 — enables → MetaCyc:DENITRIFICATION-PWY; Nitrate/nitrite transport contribution to the complete pathway; this edge does not assign strict 1:1 antiport or isolated exact transport stoichiometry. NarK2 has the dominant phenotype and NarK1 a smaller contribution in the tested PAO1 conditions.; Evidence: UniProtKB:G3XD60, PMID:16391109, PMID:16391109enables UniProtKB:P00099 — enables → MetaCyc:RXN-15838; NirM electron-donor contribution to nitrite reduction, not catalytic nitrite-reductase assignment. The whole c551 redox classes remain distinct from the sequence entry.; Evidence: UniProtKB:P00099, UniProtKB:P00099enables UniProtKB:G3XCX1 — has_cofactor → CHEBI:60539; Current entry annotation of Mo-bisMGD; ECO:0000256 ARBA. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.; Evidence: UniProtKB:G3XCX1has cofactor UniProtKB:G3XCX1 — has_cofactor → CHEBI:49883; Current entry annotation of [4Fe-4S]; ECO:0000256 ARBA. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.; Evidence: UniProtKB:G3XCX1has cofactor UniProtKB:G3XD87 — has_cofactor → CHEBI:21137; Current entry annotation of [3Fe-4S]; ECO:0000256 ARBA. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.; Evidence: UniProtKB:G3XD87has cofactor UniProtKB:G3XD87 — has_cofactor → CHEBI:49883; Current entry annotation of [4Fe-4S]; ECO:0000256 ARBA. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.; Evidence: UniProtKB:G3XD87has cofactor UniProtKB:G3XD18 — has_cofactor → CHEBI:60344; Current entry annotation of heme b; ECO:0000256 PIRSR. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.; Evidence: UniProtKB:G3XD18has cofactor UniProtKB:P24474 — has_cofactor → CHEBI:61717; Current entry annotation of heme c; ECO:0000269 PMID9331415. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.; Evidence: UniProtKB:P24474has cofactor UniProtKB:P24474 — has_cofactor → CHEBI:60549; Current entry annotation of heme d1; ECO:0000269 PMID9331415 and PDB mapping. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.; Evidence: UniProtKB:P24474has cofactor UniProtKB:Q59647 — has_cofactor → CHEBI:60344; Current entry annotation of heme b; ECO:0000305 curator inference. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.; Evidence: UniProtKB:Q59647has cofactor UniProtKB:Q59647 — has_cofactor → CHEBI:24875; Current entry annotation of non-heme Fe cation; ECO:0000305 curator inference. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.; Evidence: UniProtKB:Q59647has cofactor UniProtKB:Q59646 — has_cofactor → CHEBI:61717; Current entry annotation of heme c; ECO:0000255 PROSITE. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.; Evidence: UniProtKB:Q59646has cofactor UniProtKB:Q9HYL2 — has_cofactor → CHEBI:47357; Current entry annotation of CuA binuclear copper center; ECO:0000255 HAMAP. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.; Evidence: UniProtKB:Q9HYL2has cofactor UniProtKB:Q9HYL2 — has_cofactor → CHEBI:33730; Current entry annotation of CuZ [4Cu-S] cluster; ECO:0000255 HAMAP. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.; Evidence: UniProtKB:Q9HYL2has cofactor UniProtKB:Q9HYL2 — has_cofactor → CHEBI:29108; Current entry annotation of Ca2+; ECO:0000255 HAMAP. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.; Evidence: UniProtKB:Q9HYL2has cofactor UniProtKB:P00099 — has_cofactor → CHEBI:61717; Covalently attached heme c; the whole redox carrier is retained separately. Current heme annotation does not assert a permanently reduced in vivo state.; Evidence: UniProtKB:P00099, UniProtKB:P00099has cofactor UniProtKB:P23926 — regulates → MetaCyc:DENITRIFICATION-PWY; Expression-level regulatory support under tested PAO1 nitrate/anaerobic conditions; no direct catalytic activation/inhibition or IHF CHA-A2 strain transfer is inferred.; Evidence: UniProtKB:P23926, PMID:17400734regulates UniProtKB:G3XCW6 — regulates → MetaCyc:DENITRIFICATION-PWY; Expression-level regulatory support under tested PAO1 nitrate/anaerobic conditions; no direct catalytic activation/inhibition or IHF CHA-A2 strain transfer is inferred.; Evidence: UniProtKB:G3XCW6, PMID:17400734regulates UniProtKB:Q9HXD3 — regulates → MetaCyc:DENITRIFICATION-PWY; Expression-level regulatory support under tested PAO1 nitrate/anaerobic conditions; no direct catalytic activation/inhibition or IHF CHA-A2 strain transfer is inferred.; Evidence: UniProtKB:Q9HXD3, PMID:17400734regulates UniProtKB:P24474 — located_in → GO:0042597; Current entry localization; inferred/rule-based scope remains as in the cited source. Membrane role does not itself demonstrate proton pumping.; Evidence: UniProtKB:P24474located in UniProtKB:Q59647 — located_in → GO:0005886; Current entry localization; inferred/rule-based scope remains as in the cited source. Membrane role does not itself demonstrate proton pumping.; Evidence: UniProtKB:Q59647located in UniProtKB:Q59646 — located_in → GO:0005886; Current entry localization; inferred/rule-based scope remains as in the cited source. Membrane role does not itself demonstrate proton pumping.; Evidence: UniProtKB:Q59646located in UniProtKB:Q9HYL2 — located_in → GO:0042597; Current entry localization; inferred/rule-based scope remains as in the cited source. Membrane role does not itself demonstrate proton pumping.; Evidence: UniProtKB:Q9HYL2located in UniProtKB:G3XCX1 — located_in → GO:0005886; Current entry localization; inferred/rule-based scope remains as in the cited source. Membrane role does not itself demonstrate proton pumping.; Evidence: UniProtKB:G3XCX1located in UniProtKB:G3XD87 — located_in → GO:0005886; Current entry localization; inferred/rule-based scope remains as in the cited source. Membrane role does not itself demonstrate proton pumping.; Evidence: UniProtKB:G3XD87located in UniProtKB:G3XD18 — located_in → GO:0005886; Current entry localization; inferred/rule-based scope remains as in the cited source. Membrane role does not itself demonstrate proton pumping.; Evidence: UniProtKB:G3XD18located in UniProtKB:Q9HXD4 — located_in → GO:0005886; Current entry localization; inferred/rule-based scope remains as in the cited source. Membrane role does not itself demonstrate proton pumping.; Evidence: UniProtKB:Q9HXD4located in UniProtKB:G3XD60 — located_in → GO:0016020; Generic membrane localization and multipass topology are inferred by ARBA (ECO:0000256). The current entry does not specify the inner/plasma membrane; no direct localization assay or proton-pumping role is inferred.; Evidence: UniProtKB:G3XD60, GO:0016020located in UniProtKB:P00099 — located_in → GO:0042597; Current entry localization; inferred/rule-based scope remains as in the cited source. Membrane role does not itself demonstrate proton pumping.; Evidence: UniProtKB:P00099located in nitrate; CHEBI:17632; Declared type: small_molecule small molecule nitrate nitrite; CHEBI:16301; Declared type: small_molecule small molecule nitrite nitric oxide; CHEBI:16480; Declared type: small_molecule small molecule nitric oxide dinitrogen oxide; CHEBI:17045; Declared type: small_molecule small molecule dinitrogen oxide dinitrogen; CHEBI:17997; Declared type: small_molecule small molecule dinitrogen water; CHEBI:15377; Declared type: small_molecule small molecule water hydron; CHEBI:15378; Declared type: small_molecule small molecule hydron Mo(=O)-bis(molybdopterin guanine dinucleotide)(4-); CHEBI:60539; Declared type: cofactor cofactor Mo(=O)-bis(molybdopterin guanine dinucleotide)(4-) tetra-mu3-sulfido-tetrairon; CHEBI:49883; Declared type: cofactor cofactor tetra-mu3-sulfido-tetrairon tri-mu-sulfido-mu3-sulfido-triiron; CHEBI:21137; Declared type: cofactor cofactor tri-mu-sulfido-mu3-sulfido- triiron ferroheme c(2-); CHEBI:61717; Declared type: cofactor cofactor ferroheme c(2-) ferroheme d1(4-); CHEBI:60549; Declared type: cofactor cofactor ferroheme d1(4-) ferroheme b(2-); CHEBI:60344; Declared type: cofactor cofactor ferroheme b(2-) iron cation; CHEBI:24875; Declared type: cofactor cofactor iron cation binuclear copper ion; CHEBI:47357; Declared type: cofactor cofactor binuclear copper ion mu4-sulfido-quadro-tetracopper; CHEBI:33730; Declared type: cofactor cofactor mu4-sulfido-quadro- tetracopper calcium(2+); CHEBI:29108; Declared type: cofactor cofactor calcium(2+) an electron-transfer quinol; MetaCyc:ETR-Quinols; Declared type: chemical_entity chemical entity an electron-transfer quinol an electron-transfer quinone; MetaCyc:ETR-Quinones; Declared type: chemical_entity chemical entity an electron-transfer quinone a reduced cytochrome c551; MetaCyc:Reduced-cytochromes-c551; Declared type: protein protein a reduced cytochrome c551 an oxidized cytochrome c551; MetaCyc:Oxidized-cytochromes-c551; Declared type: protein protein an oxidized cytochrome c551 a reduced c-type cytochrome; MetaCyc:Cytochromes-C-Reduced; Declared type: protein protein a reduced c-type cytochrome an oxidized c-type cytochrome; MetaCyc:Cytochromes-C-Oxidized; Declared type: protein protein an oxidized c-type cytochrome nitrate reductase (quinone); UniProtKB:G3XCX1; Declared type: protein protein nitrate reductase (quinone) nitrate reductase (quinone); UniProtKB:G3XD87; Declared type: protein protein nitrate reductase (quinone) nitrate reductase (quinone); UniProtKB:G3XD18; Declared type: protein protein nitrate reductase (quinone) Nitrite reductase; UniProtKB:P24474; Declared type: protein protein Nitrite reductase Nitric oxide reductase subunit B; UniProtKB:Q59647; Declared type: protein protein Nitric oxide reductase subunit B Nitric oxide reductase subunit C; UniProtKB:Q59646; Declared type: protein protein Nitric oxide reductase subunit C Nitrous-oxide reductase; UniProtKB:Q9HYL2; Declared type: protein protein Nitrous-oxide reductase Nitrate/nitrite transporter; UniProtKB:Q9HXD4; Declared type: protein protein Nitrate/nitrite transporter Nitrite extrusion protein 1; UniProtKB:G3XD60; Declared type: protein protein Nitrite extrusion protein 1 Cytochrome c-551; UniProtKB:P00099; Declared type: protein protein Cytochrome c-551 Transcriptional activator protein anr; UniProtKB:P23926; Declared type: protein protein Transcriptional activator protein anr Transcriptional regulator Dnr; UniProtKB:G3XCW6; Declared type: protein protein Transcriptional regulator Dnr Two-component response regulator NarL; UniProtKB:Q9HXD3; Declared type: protein protein Two-component response regulator NarL periplasmic space; GO:0042597; Declared type: cellular_component cellular component periplasmic space plasma membrane; GO:0005886; Declared type: cellular_component cellular component plasma membrane membrane; GO:0016020; Declared type: cellular_component cellular component membrane nitrate + an electron-transfer quinol[inner membrane] + 2 H+ nitrite + an electron-transfer quinone[inner membrane] + 2 H+[periplasm] + H2O; MetaCyc:RXN-11236; Declared type: reaction/activity; Source reaction direction: left_to_right reaction / activity nitrate + an electron- transfer quinol[inner membrane] + 2 H+ nitrite + an electron-transfer quinone[inner membrane] + 2 H+[periplasm] + H2O nitrate[periplasm] + nitrite[cytosol] -> nitrate[cytosol] + nitrite[periplasm]; MetaCyc:TRANS-RXN0-239; Declared type: reaction/activity; Source reaction direction: left_to_right reaction / activity nitrate[periplasm] + nitrite[cytosol] -> nitrate[cytosol] + nitrite[periplasm] nitrite[periplasm] + a reduced cytochrome c551[periplasm] + 2 H+[periplasm] nitric oxide[periplasm] + an oxidized cytochrome c551[periplasm] + H2O[periplasm]; MetaCyc:RXN-15838; Declared type: reaction/activity; Source reaction direction: left_to_right reaction / activity nitrite[periplasm] + a reduced cytochrome c551[periplasm] + 2 H+[periplasm] nitric oxide[periplasm] + an oxidized cytochrome c551[periplasm] + H2O[periplasm] 2 a reduced c-type cytochrome[periplasm] + 2 nitric oxide[periplasm] + 2 H+[periplasm] -> nitrous oxide[periplasm] + 2 an oxidized c-type cytochrome[periplasm] + H2O[periplasm]; MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN; Declared type: reaction/activity; Source reaction direction: left_to_right reaction / activity 2 a reduced c-type cytochrome[periplasm] + 2 nitric oxide[periplasm] + 2 H+[periplasm] -> nitrous oxide[periplasm] + 2 an oxidized c-type cytochrome[periplasm] + H2O[periplasm] 2 a reduced c-type cytochrome[periplasm] + nitrous oxide[periplasm] + 2 H+[periplasm] -> 2 an oxidized c-type cytochrome[periplasm] + N2[periplasm] + H2O[periplasm]; MetaCyc:RXN-12130; Declared type: reaction/activity; Source reaction direction: left_to_right reaction / activity 2 a reduced c-type cytochrome[periplasm] + nitrous oxide[periplasm] + 2 H+[periplasm] -> 2 an oxidized c-type cytochrome[periplasm] + N2[periplasm] + H2O[periplasm] nitrate reduction I (denitrification); MetaCyc:DENITRIFICATION-PWY; Declared type: pathway pathway nitrate reduction I (denitrification)

Components and activities

Declared biological components and source reaction directions
NodeKind or roleSource direction
Pseudomonas aeruginosa PAO1
NCBITaxon:208964
taxon
nitrate
CHEBI:17632
small molecule
nitrite
CHEBI:16301
small molecule
nitric oxide
CHEBI:16480
small molecule
dinitrogen oxide
CHEBI:17045
small molecule
dinitrogen
CHEBI:17997
small molecule
water
CHEBI:15377
small molecule
hydron
CHEBI:15378
small molecule
Mo(=O)-bis(molybdopterin guanine dinucleotide)(4-)
CHEBI:60539
cofactor
tetra-mu3-sulfido-tetrairon
CHEBI:49883
cofactor
tri-mu-sulfido-mu3-sulfido-triiron
CHEBI:21137
cofactor
ferroheme c(2-)
CHEBI:61717
cofactor
ferroheme d1(4-)
CHEBI:60549
cofactor
ferroheme b(2-)
CHEBI:60344
cofactor
iron cation
CHEBI:24875
cofactor
binuclear copper ion
CHEBI:47357
cofactor
mu4-sulfido-quadro-tetracopper
CHEBI:33730
cofactor
calcium(2+)
CHEBI:29108
cofactor
an electron-transfer quinol
MetaCyc:ETR-Quinols
chemical entity
an electron-transfer quinone
MetaCyc:ETR-Quinones
chemical entity
a reduced cytochrome c551
MetaCyc:Reduced-cytochromes-c551
protein
an oxidized cytochrome c551
MetaCyc:Oxidized-cytochromes-c551
protein
a reduced c-type cytochrome
MetaCyc:Cytochromes-C-Reduced
protein
an oxidized c-type cytochrome
MetaCyc:Cytochromes-C-Oxidized
protein
nitrate reductase (quinone)
UniProtKB:G3XCX1
protein
nitrate reductase (quinone)
UniProtKB:G3XD87
protein
nitrate reductase (quinone)
UniProtKB:G3XD18
protein
Nitrite reductase
UniProtKB:P24474
protein
Nitric oxide reductase subunit B
UniProtKB:Q59647
protein
Nitric oxide reductase subunit C
UniProtKB:Q59646
protein
Nitrous-oxide reductase
UniProtKB:Q9HYL2
protein
Nitrate/nitrite transporter
UniProtKB:Q9HXD4
protein
Nitrite extrusion protein 1
UniProtKB:G3XD60
protein
Cytochrome c-551
UniProtKB:P00099
protein
Transcriptional activator protein anr
UniProtKB:P23926
protein
Transcriptional regulator Dnr
UniProtKB:G3XCW6
protein
Two-component response regulator NarL
UniProtKB:Q9HXD3
protein
periplasmic space
GO:0042597
cellular component
plasma membrane
GO:0005886
cellular component
membrane
GO:0016020
cellular component
nitrate + an electron-transfer quinol[inner membrane] + 2 H+ nitrite + an electron-transfer quinone[inner membrane] + 2 H+[periplasm] + H2O
MetaCyc:RXN-11236
reactionleft to right
nitrate[periplasm] + nitrite[cytosol] -> nitrate[cytosol] + nitrite[periplasm]
MetaCyc:TRANS-RXN0-239
reactionleft to right
nitrite[periplasm] + a reduced cytochrome c551[periplasm] + 2 H+[periplasm] nitric oxide[periplasm] + an oxidized cytochrome c551[periplasm] + H2O[periplasm]
MetaCyc:RXN-15838
reactionleft to right
2 a reduced c-type cytochrome[periplasm] + 2 nitric oxide[periplasm] + 2 H+[periplasm] -> nitrous oxide[periplasm] + 2 an oxidized c-type cytochrome[periplasm] + H2O[periplasm]
MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN
reactionleft to right
2 a reduced c-type cytochrome[periplasm] + nitrous oxide[periplasm] + 2 H+[periplasm] -> 2 an oxidized c-type cytochrome[periplasm] + N2[periplasm] + H2O[periplasm]
MetaCyc:RXN-12130
reactionleft to right

Mechanistic edges

Mechanistic edges and their cited evidence
SubjectPredicate and descriptionObjectEvidence
MetaCyc:DENITRIFICATION-PWYhas_part

Complete native route member; source reaction direction is retained separately from the pathway L2R traversal.

nitrate + an electron-transfer quinol[inner membrane] + 2 H+ nitrite + an electron-transfer quinone[inner membrane] + 2 H+[periplasm] + H2O
MetaCyc:RXN-11236
  • MetaCyc:DENITRIFICATION-PWY

    Source assertion: The pathway explicitly lists RXN-11236 and assigns L2R traversal.

    Source locationXPath /ptools-xml/Pathway/reaction-list/Reaction[@frameid="RXN-11236"]; /ptools-xml/Pathway/reaction-layout[Reaction/@frameid="RXN-11236"]/direction
MetaCyc:DENITRIFICATION-PWYhas_part

Native nitrate/nitrite antiport convention is retained as a complete source-defined step. PAO1 transport function is experimentally supported, but strict antiport versus uniport and its exact catalyst assignment remain unresolved.

nitrate[periplasm] + nitrite[cytosol] -> nitrate[cytosol] + nitrite[periplasm]
MetaCyc:TRANS-RXN0-239
  • MetaCyc:DENITRIFICATION-PWY

    Source assertion: The pathway explicitly lists TRANS-RXN0-239 and assigns L2R traversal.

    Source locationXPath /ptools-xml/Pathway/reaction-list/Reaction[@frameid="TRANS-RXN0-239"]; /ptools-xml/Pathway/reaction-layout[Reaction/@frameid="TRANS-RXN0-239"]/direction
  • PMID:16391109

    Source assertion: The authors explicitly state that antiport versus uniport remains to be conclusively experimentally proven.

    Source locationXPath //article/section[2]/section/section[4]/p[5]
MetaCyc:DENITRIFICATION-PWYhas_part

Complete native route member; source reaction direction is retained separately from the pathway L2R traversal.

nitrite[periplasm] + a reduced cytochrome c551[periplasm] + 2 H+[periplasm] nitric oxide[periplasm] + an oxidized cytochrome c551[periplasm] + H2O[periplasm]
MetaCyc:RXN-15838
  • MetaCyc:DENITRIFICATION-PWY

    Source assertion: The pathway explicitly lists RXN-15838 and assigns L2R traversal.

    Source locationXPath /ptools-xml/Pathway/reaction-list/Reaction[@frameid="RXN-15838"]; /ptools-xml/Pathway/reaction-layout[Reaction/@frameid="RXN-15838"]/direction
MetaCyc:DENITRIFICATION-PWYhas_part

Complete native route member; source reaction direction is retained separately from the pathway L2R traversal.

2 a reduced c-type cytochrome[periplasm] + 2 nitric oxide[periplasm] + 2 H+[periplasm] -> nitrous oxide[periplasm] + 2 an oxidized c-type cytochrome[periplasm] + H2O[periplasm]
MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN
  • MetaCyc:DENITRIFICATION-PWY

    Source assertion: The pathway explicitly lists NITRIC-OXIDE-REDUCTASE-RXN and assigns L2R traversal.

    Source locationXPath /ptools-xml/Pathway/reaction-list/Reaction[@frameid="NITRIC-OXIDE-REDUCTASE-RXN"]; /ptools-xml/Pathway/reaction-layout[Reaction/@frameid="NITRIC-OXIDE-REDUCTASE-RXN"]/direction
MetaCyc:DENITRIFICATION-PWYhas_part

Complete native route member; source reaction direction is retained separately from the pathway L2R traversal.

2 a reduced c-type cytochrome[periplasm] + nitrous oxide[periplasm] + 2 H+[periplasm] -> 2 an oxidized c-type cytochrome[periplasm] + N2[periplasm] + H2O[periplasm]
MetaCyc:RXN-12130
  • MetaCyc:DENITRIFICATION-PWY

    Source assertion: The pathway explicitly lists RXN-12130 and assigns L2R traversal.

    Source locationXPath /ptools-xml/Pathway/reaction-list/Reaction[@frameid="RXN-12130"]; /ptools-xml/Pathway/reaction-layout[Reaction/@frameid="RXN-12130"]/direction
an electron-transfer quinol
MetaCyc:ETR-Quinols
consumes

Coefficient 1; membrane electron-transfer class; side not specified. Native compartmental equation and class identity retained.

nitrate + an electron-transfer quinol[inner membrane] + 2 H+ nitrite + an electron-transfer quinone[inner membrane] + 2 H+[periplasm] + H2O
MetaCyc:RXN-11236
  • MetaCyc:RXN-11236

    Source assertion: The left side contains coefficient 1 of ETR-Quinols; no side compartment is specified.

    Source locationXPath /ptools-xml/Reaction/left[1]
  • MetaCyc:ETR-Quinols

    Source assertion: The issuing native object identifies this whole class as an electron-transfer quinol; no unique molecular formula or sequence is asserted.

    Source locationXPath /ptools-xml/Compound/common-name
nitrate
CHEBI:17632
consumes

Coefficient 1; cytoplasmic side. Native compartmental equation and class identity retained.

nitrate + an electron-transfer quinol[inner membrane] + 2 H+ nitrite + an electron-transfer quinone[inner membrane] + 2 H+[periplasm] + H2O
MetaCyc:RXN-11236
  • MetaCyc:RXN-11236

    Source assertion: The left side contains coefficient 1 of NITRATE in CCO-IN.

    Source locationXPath /ptools-xml/Reaction/left[2]
  • MetaCyc:NITRATE

    Source assertion: The native NITRATE object has InChI InChI=1S/NO3/c2-1(3)4/q-1.

    Source locationXPath /ptools-xml/Compound/inchi
  • CHEBI:17632

    Source assertion: The selected ChEBI structure has the same InChI; formula NO3, charge -1.

    Source locationSemantic SQL statements: subject=CHEBI:17632; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge
hydron
CHEBI:15378
consumes

Coefficient 2; cytoplasmic side. Native compartmental equation and class identity retained.

nitrate + an electron-transfer quinol[inner membrane] + 2 H+ nitrite + an electron-transfer quinone[inner membrane] + 2 H+[periplasm] + H2O
MetaCyc:RXN-11236
  • MetaCyc:RXN-11236

    Source assertion: The left side contains coefficient 2 of PROTON in CCO-IN.

    Source locationXPath /ptools-xml/Reaction/left[3]
  • MetaCyc:PROTON

    Source assertion: The native PROTON object has InChI InChI=1S/p+1.

    Source locationXPath /ptools-xml/Compound/inchi
  • CHEBI:15378

    Source assertion: The selected ChEBI structure has the same InChI; formula H, charge 1.

    Source locationSemantic SQL statements: subject=CHEBI:15378; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge
nitrate + an electron-transfer quinol[inner membrane] + 2 H+ nitrite + an electron-transfer quinone[inner membrane] + 2 H+[periplasm] + H2O
MetaCyc:RXN-11236
produces

Coefficient 1; membrane electron-transfer class; side not specified. Native compartmental equation and class identity retained.

an electron-transfer quinone
MetaCyc:ETR-Quinones
  • MetaCyc:RXN-11236

    Source assertion: The right side contains coefficient 1 of ETR-Quinones; no side compartment is specified.

    Source locationXPath /ptools-xml/Reaction/right[1]
  • MetaCyc:ETR-Quinones

    Source assertion: The issuing native object identifies this whole class as an electron-transfer quinone; no unique molecular formula or sequence is asserted.

    Source locationXPath /ptools-xml/Compound/common-name
nitrate + an electron-transfer quinol[inner membrane] + 2 H+ nitrite + an electron-transfer quinone[inner membrane] + 2 H+[periplasm] + H2O
MetaCyc:RXN-11236
produces

Coefficient 2; periplasmic side. Native compartmental equation and class identity retained.

hydron
CHEBI:15378
  • MetaCyc:RXN-11236

    Source assertion: The right side contains coefficient 2 of PROTON in CCO-OUT.

    Source locationXPath /ptools-xml/Reaction/right[2]
  • MetaCyc:PROTON

    Source assertion: The native PROTON object has InChI InChI=1S/p+1.

    Source locationXPath /ptools-xml/Compound/inchi
  • CHEBI:15378

    Source assertion: The selected ChEBI structure has the same InChI; formula H, charge 1.

    Source locationSemantic SQL statements: subject=CHEBI:15378; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge
nitrate + an electron-transfer quinol[inner membrane] + 2 H+ nitrite + an electron-transfer quinone[inner membrane] + 2 H+[periplasm] + H2O
MetaCyc:RXN-11236
produces

Coefficient 1; cytoplasmic side. Native compartmental equation and class identity retained.

nitrite
CHEBI:16301
  • MetaCyc:RXN-11236

    Source assertion: The right side contains coefficient 1 of NITRITE in CCO-IN.

    Source locationXPath /ptools-xml/Reaction/right[3]
  • MetaCyc:NITRITE

    Source assertion: The native NITRITE object has InChI InChI=1S/HNO2/c2-1-3/h(H,2,3)/p-1.

    Source locationXPath /ptools-xml/Compound/inchi
  • CHEBI:16301

    Source assertion: The selected ChEBI structure has the same InChI; formula NO2, charge -1.

    Source locationSemantic SQL statements: subject=CHEBI:16301; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge
nitrate + an electron-transfer quinol[inner membrane] + 2 H+ nitrite + an electron-transfer quinone[inner membrane] + 2 H+[periplasm] + H2O
MetaCyc:RXN-11236
produces

Coefficient 1; cytoplasmic side. Native compartmental equation and class identity retained.

water
CHEBI:15377
  • MetaCyc:RXN-11236

    Source assertion: The right side contains coefficient 1 of WATER in CCO-IN.

    Source locationXPath /ptools-xml/Reaction/right[4]
  • MetaCyc:WATER

    Source assertion: The native WATER object has InChI InChI=1S/H2O/h1H2.

    Source locationXPath /ptools-xml/Compound/inchi
  • CHEBI:15377

    Source assertion: The selected ChEBI structure has the same InChI; formula H2O, charge 0.

    Source locationSemantic SQL statements: subject=CHEBI:15377; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge
nitrate[periplasm] + nitrite[cytosol] -> nitrate[cytosol] + nitrite[periplasm]
MetaCyc:TRANS-RXN0-239
has_input

Coefficient 1; periplasmic side. Native compartmental equation and class identity retained. Formal antiport convention; exact PAO1 mode/catalyst is unassigned, not experimentally established stoichiometry.

nitrate
CHEBI:17632
  • MetaCyc:TRANS-RXN0-239

    Source assertion: The left side contains coefficient 1 of NITRATE in CCO-OUT.

    Source locationXPath /ptools-xml/Reaction/left[1]
  • MetaCyc:NITRATE

    Source assertion: The native NITRATE object has InChI InChI=1S/NO3/c2-1(3)4/q-1.

    Source locationXPath /ptools-xml/Compound/inchi
  • CHEBI:17632

    Source assertion: The selected ChEBI structure has the same InChI; formula NO3, charge -1.

    Source locationSemantic SQL statements: subject=CHEBI:17632; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge
nitrate[periplasm] + nitrite[cytosol] -> nitrate[cytosol] + nitrite[periplasm]
MetaCyc:TRANS-RXN0-239
has_input

Coefficient 1; cytoplasmic side. Native compartmental equation and class identity retained. Formal antiport convention; exact PAO1 mode/catalyst is unassigned, not experimentally established stoichiometry.

nitrite
CHEBI:16301
  • MetaCyc:TRANS-RXN0-239

    Source assertion: The left side contains coefficient 1 of NITRITE in CCO-IN.

    Source locationXPath /ptools-xml/Reaction/left[2]
  • MetaCyc:NITRITE

    Source assertion: The native NITRITE object has InChI InChI=1S/HNO2/c2-1-3/h(H,2,3)/p-1.

    Source locationXPath /ptools-xml/Compound/inchi
  • CHEBI:16301

    Source assertion: The selected ChEBI structure has the same InChI; formula NO2, charge -1.

    Source locationSemantic SQL statements: subject=CHEBI:16301; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge
nitrate[periplasm] + nitrite[cytosol] -> nitrate[cytosol] + nitrite[periplasm]
MetaCyc:TRANS-RXN0-239
has_output

Coefficient 1; cytoplasmic side. Native compartmental equation and class identity retained. Formal antiport convention; exact PAO1 mode/catalyst is unassigned, not experimentally established stoichiometry.

nitrate
CHEBI:17632
  • MetaCyc:TRANS-RXN0-239

    Source assertion: The right side contains coefficient 1 of NITRATE in CCO-IN.

    Source locationXPath /ptools-xml/Reaction/right[1]
  • MetaCyc:NITRATE

    Source assertion: The native NITRATE object has InChI InChI=1S/NO3/c2-1(3)4/q-1.

    Source locationXPath /ptools-xml/Compound/inchi
  • CHEBI:17632

    Source assertion: The selected ChEBI structure has the same InChI; formula NO3, charge -1.

    Source locationSemantic SQL statements: subject=CHEBI:17632; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge
nitrate[periplasm] + nitrite[cytosol] -> nitrate[cytosol] + nitrite[periplasm]
MetaCyc:TRANS-RXN0-239
has_output

Coefficient 1; periplasmic side. Native compartmental equation and class identity retained. Formal antiport convention; exact PAO1 mode/catalyst is unassigned, not experimentally established stoichiometry.

nitrite
CHEBI:16301
  • MetaCyc:TRANS-RXN0-239

    Source assertion: The right side contains coefficient 1 of NITRITE in CCO-OUT.

    Source locationXPath /ptools-xml/Reaction/right[2]
  • MetaCyc:NITRITE

    Source assertion: The native NITRITE object has InChI InChI=1S/HNO2/c2-1-3/h(H,2,3)/p-1.

    Source locationXPath /ptools-xml/Compound/inchi
  • CHEBI:16301

    Source assertion: The selected ChEBI structure has the same InChI; formula NO2, charge -1.

    Source locationSemantic SQL statements: subject=CHEBI:16301; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge
nitrite
CHEBI:16301
consumes

Coefficient 1; periplasmic side. Native compartmental equation and class identity retained.

nitrite[periplasm] + a reduced cytochrome c551[periplasm] + 2 H+[periplasm] nitric oxide[periplasm] + an oxidized cytochrome c551[periplasm] + H2O[periplasm]
MetaCyc:RXN-15838
  • MetaCyc:RXN-15838

    Source assertion: The left side contains coefficient 1 of NITRITE in CCO-OUT.

    Source locationXPath /ptools-xml/Reaction/left[1]
  • MetaCyc:NITRITE

    Source assertion: The native NITRITE object has InChI InChI=1S/HNO2/c2-1-3/h(H,2,3)/p-1.

    Source locationXPath /ptools-xml/Compound/inchi
  • CHEBI:16301

    Source assertion: The selected ChEBI structure has the same InChI; formula NO2, charge -1.

    Source locationSemantic SQL statements: subject=CHEBI:16301; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge
a reduced cytochrome c551
MetaCyc:Reduced-cytochromes-c551
consumes

Coefficient 1; periplasmic side. Native compartmental equation and class identity retained.

nitrite[periplasm] + a reduced cytochrome c551[periplasm] + 2 H+[periplasm] nitric oxide[periplasm] + an oxidized cytochrome c551[periplasm] + H2O[periplasm]
MetaCyc:RXN-15838
  • MetaCyc:RXN-15838

    Source assertion: The left side contains coefficient 1 of Reduced-cytochromes-c551 in CCO-OUT.

    Source locationXPath /ptools-xml/Reaction/left[2]
  • MetaCyc:Reduced-cytochromes-c551

    Source assertion: The issuing native object identifies this whole class as a reduced cytochrome c551; no unique molecular formula or sequence is asserted.

    Source locationXPath /ptools-xml/Protein/common-name
hydron
CHEBI:15378
consumes

Coefficient 2; periplasmic side. Native compartmental equation and class identity retained.

nitrite[periplasm] + a reduced cytochrome c551[periplasm] + 2 H+[periplasm] nitric oxide[periplasm] + an oxidized cytochrome c551[periplasm] + H2O[periplasm]
MetaCyc:RXN-15838
  • MetaCyc:RXN-15838

    Source assertion: The left side contains coefficient 2 of PROTON in CCO-OUT.

    Source locationXPath /ptools-xml/Reaction/left[3]
  • MetaCyc:PROTON

    Source assertion: The native PROTON object has InChI InChI=1S/p+1.

    Source locationXPath /ptools-xml/Compound/inchi
  • CHEBI:15378

    Source assertion: The selected ChEBI structure has the same InChI; formula H, charge 1.

    Source locationSemantic SQL statements: subject=CHEBI:15378; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge
nitrite[periplasm] + a reduced cytochrome c551[periplasm] + 2 H+[periplasm] nitric oxide[periplasm] + an oxidized cytochrome c551[periplasm] + H2O[periplasm]
MetaCyc:RXN-15838
produces

Coefficient 1; periplasmic side. Native compartmental equation and class identity retained.

water
CHEBI:15377
  • MetaCyc:RXN-15838

    Source assertion: The right side contains coefficient 1 of WATER in CCO-OUT.

    Source locationXPath /ptools-xml/Reaction/right[1]
  • MetaCyc:WATER

    Source assertion: The native WATER object has InChI InChI=1S/H2O/h1H2.

    Source locationXPath /ptools-xml/Compound/inchi
  • CHEBI:15377

    Source assertion: The selected ChEBI structure has the same InChI; formula H2O, charge 0.

    Source locationSemantic SQL statements: subject=CHEBI:15377; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge
nitrite[periplasm] + a reduced cytochrome c551[periplasm] + 2 H+[periplasm] nitric oxide[periplasm] + an oxidized cytochrome c551[periplasm] + H2O[periplasm]
MetaCyc:RXN-15838
produces

Coefficient 1; periplasmic side. Native compartmental equation and class identity retained.

nitric oxide
CHEBI:16480
  • MetaCyc:RXN-15838

    Source assertion: The right side contains coefficient 1 of NITRIC-OXIDE in CCO-OUT.

    Source locationXPath /ptools-xml/Reaction/right[2]
  • MetaCyc:NITRIC-OXIDE

    Source assertion: The native NITRIC-OXIDE object has InChI InChI=1S/NO/c1-2.

    Source locationXPath /ptools-xml/Compound/inchi
  • CHEBI:16480

    Source assertion: The selected ChEBI structure has the same InChI; formula NO, charge 0.

    Source locationSemantic SQL statements: subject=CHEBI:16480; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge
nitrite[periplasm] + a reduced cytochrome c551[periplasm] + 2 H+[periplasm] nitric oxide[periplasm] + an oxidized cytochrome c551[periplasm] + H2O[periplasm]
MetaCyc:RXN-15838
produces

Coefficient 1; periplasmic side. Native compartmental equation and class identity retained.

an oxidized cytochrome c551
MetaCyc:Oxidized-cytochromes-c551
  • MetaCyc:RXN-15838

    Source assertion: The right side contains coefficient 1 of Oxidized-cytochromes-c551 in CCO-OUT.

    Source locationXPath /ptools-xml/Reaction/right[3]
  • MetaCyc:Oxidized-cytochromes-c551

    Source assertion: The issuing native object identifies this whole class as an oxidized cytochrome c551; no unique molecular formula or sequence is asserted.

    Source locationXPath /ptools-xml/Protein/common-name
a reduced c-type cytochrome
MetaCyc:Cytochromes-C-Reduced
consumes

Coefficient 2; periplasmic side. Native compartmental equation and class identity retained.

2 a reduced c-type cytochrome[periplasm] + 2 nitric oxide[periplasm] + 2 H+[periplasm] -> nitrous oxide[periplasm] + 2 an oxidized c-type cytochrome[periplasm] + H2O[periplasm]
MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN
  • MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN

    Source assertion: The left side contains coefficient 2 of Cytochromes-C-Reduced in CCO-OUT.

    Source locationXPath /ptools-xml/Reaction/left[1]
  • MetaCyc:Cytochromes-C-Reduced

    Source assertion: The issuing native object identifies this whole class as a reduced c-type cytochrome; no unique molecular formula or sequence is asserted.

    Source locationXPath /ptools-xml/Protein/common-name
nitric oxide
CHEBI:16480
consumes

Coefficient 2; periplasmic side. Native compartmental equation and class identity retained.

2 a reduced c-type cytochrome[periplasm] + 2 nitric oxide[periplasm] + 2 H+[periplasm] -> nitrous oxide[periplasm] + 2 an oxidized c-type cytochrome[periplasm] + H2O[periplasm]
MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN
  • MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN

    Source assertion: The left side contains coefficient 2 of NITRIC-OXIDE in CCO-OUT.

    Source locationXPath /ptools-xml/Reaction/left[2]
  • MetaCyc:NITRIC-OXIDE

    Source assertion: The native NITRIC-OXIDE object has InChI InChI=1S/NO/c1-2.

    Source locationXPath /ptools-xml/Compound/inchi
  • CHEBI:16480

    Source assertion: The selected ChEBI structure has the same InChI; formula NO, charge 0.

    Source locationSemantic SQL statements: subject=CHEBI:16480; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge
hydron
CHEBI:15378
consumes

Coefficient 2; periplasmic side. Native compartmental equation and class identity retained.

2 a reduced c-type cytochrome[periplasm] + 2 nitric oxide[periplasm] + 2 H+[periplasm] -> nitrous oxide[periplasm] + 2 an oxidized c-type cytochrome[periplasm] + H2O[periplasm]
MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN
  • MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN

    Source assertion: The left side contains coefficient 2 of PROTON in CCO-OUT.

    Source locationXPath /ptools-xml/Reaction/left[3]
  • MetaCyc:PROTON

    Source assertion: The native PROTON object has InChI InChI=1S/p+1.

    Source locationXPath /ptools-xml/Compound/inchi
  • CHEBI:15378

    Source assertion: The selected ChEBI structure has the same InChI; formula H, charge 1.

    Source locationSemantic SQL statements: subject=CHEBI:15378; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge
2 a reduced c-type cytochrome[periplasm] + 2 nitric oxide[periplasm] + 2 H+[periplasm] -> nitrous oxide[periplasm] + 2 an oxidized c-type cytochrome[periplasm] + H2O[periplasm]
MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN
produces

Coefficient 1; periplasmic side. Native compartmental equation and class identity retained.

dinitrogen oxide
CHEBI:17045
  • MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN

    Source assertion: The right side contains coefficient 1 of NITROUS-OXIDE in CCO-OUT.

    Source locationXPath /ptools-xml/Reaction/right[1]
  • MetaCyc:NITROUS-OXIDE

    Source assertion: The native NITROUS-OXIDE object has InChI InChI=1S/N2O/c1-2-3.

    Source locationXPath /ptools-xml/Compound/inchi
  • CHEBI:17045

    Source assertion: The selected ChEBI structure has the same InChI; formula N2O, charge 0.

    Source locationSemantic SQL statements: subject=CHEBI:17045; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge
2 a reduced c-type cytochrome[periplasm] + 2 nitric oxide[periplasm] + 2 H+[periplasm] -> nitrous oxide[periplasm] + 2 an oxidized c-type cytochrome[periplasm] + H2O[periplasm]
MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN
produces

Coefficient 2; periplasmic side. Native compartmental equation and class identity retained.

an oxidized c-type cytochrome
MetaCyc:Cytochromes-C-Oxidized
  • MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN

    Source assertion: The right side contains coefficient 2 of Cytochromes-C-Oxidized in CCO-OUT.

    Source locationXPath /ptools-xml/Reaction/right[2]
  • MetaCyc:Cytochromes-C-Oxidized

    Source assertion: The issuing native object identifies this whole class as an oxidized c-type cytochrome; no unique molecular formula or sequence is asserted.

    Source locationXPath /ptools-xml/Protein/common-name
2 a reduced c-type cytochrome[periplasm] + 2 nitric oxide[periplasm] + 2 H+[periplasm] -> nitrous oxide[periplasm] + 2 an oxidized c-type cytochrome[periplasm] + H2O[periplasm]
MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN
produces

Coefficient 1; periplasmic side. Native compartmental equation and class identity retained.

water
CHEBI:15377
  • MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN

    Source assertion: The right side contains coefficient 1 of WATER in CCO-OUT.

    Source locationXPath /ptools-xml/Reaction/right[3]
  • MetaCyc:WATER

    Source assertion: The native WATER object has InChI InChI=1S/H2O/h1H2.

    Source locationXPath /ptools-xml/Compound/inchi
  • CHEBI:15377

    Source assertion: The selected ChEBI structure has the same InChI; formula H2O, charge 0.

    Source locationSemantic SQL statements: subject=CHEBI:15377; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge
a reduced c-type cytochrome
MetaCyc:Cytochromes-C-Reduced
consumes

Coefficient 2; periplasmic side. Native compartmental equation and class identity retained.

2 a reduced c-type cytochrome[periplasm] + nitrous oxide[periplasm] + 2 H+[periplasm] -> 2 an oxidized c-type cytochrome[periplasm] + N2[periplasm] + H2O[periplasm]
MetaCyc:RXN-12130
  • MetaCyc:RXN-12130

    Source assertion: The left side contains coefficient 2 of Cytochromes-C-Reduced in CCO-OUT.

    Source locationXPath /ptools-xml/Reaction/left[1]
  • MetaCyc:Cytochromes-C-Reduced

    Source assertion: The issuing native object identifies this whole class as a reduced c-type cytochrome; no unique molecular formula or sequence is asserted.

    Source locationXPath /ptools-xml/Protein/common-name
dinitrogen oxide
CHEBI:17045
consumes

Coefficient 1; periplasmic side. Native compartmental equation and class identity retained.

2 a reduced c-type cytochrome[periplasm] + nitrous oxide[periplasm] + 2 H+[periplasm] -> 2 an oxidized c-type cytochrome[periplasm] + N2[periplasm] + H2O[periplasm]
MetaCyc:RXN-12130
  • MetaCyc:RXN-12130

    Source assertion: The left side contains coefficient 1 of NITROUS-OXIDE in CCO-OUT.

    Source locationXPath /ptools-xml/Reaction/left[2]
  • MetaCyc:NITROUS-OXIDE

    Source assertion: The native NITROUS-OXIDE object has InChI InChI=1S/N2O/c1-2-3.

    Source locationXPath /ptools-xml/Compound/inchi
  • CHEBI:17045

    Source assertion: The selected ChEBI structure has the same InChI; formula N2O, charge 0.

    Source locationSemantic SQL statements: subject=CHEBI:17045; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge
hydron
CHEBI:15378
consumes

Coefficient 2; periplasmic side. Native compartmental equation and class identity retained.

2 a reduced c-type cytochrome[periplasm] + nitrous oxide[periplasm] + 2 H+[periplasm] -> 2 an oxidized c-type cytochrome[periplasm] + N2[periplasm] + H2O[periplasm]
MetaCyc:RXN-12130
  • MetaCyc:RXN-12130

    Source assertion: The left side contains coefficient 2 of PROTON in CCO-OUT.

    Source locationXPath /ptools-xml/Reaction/left[3]
  • MetaCyc:PROTON

    Source assertion: The native PROTON object has InChI InChI=1S/p+1.

    Source locationXPath /ptools-xml/Compound/inchi
  • CHEBI:15378

    Source assertion: The selected ChEBI structure has the same InChI; formula H, charge 1.

    Source locationSemantic SQL statements: subject=CHEBI:15378; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge
2 a reduced c-type cytochrome[periplasm] + nitrous oxide[periplasm] + 2 H+[periplasm] -> 2 an oxidized c-type cytochrome[periplasm] + N2[periplasm] + H2O[periplasm]
MetaCyc:RXN-12130
produces

Coefficient 2; periplasmic side. Native compartmental equation and class identity retained.

an oxidized c-type cytochrome
MetaCyc:Cytochromes-C-Oxidized
  • MetaCyc:RXN-12130

    Source assertion: The right side contains coefficient 2 of Cytochromes-C-Oxidized in CCO-OUT.

    Source locationXPath /ptools-xml/Reaction/right[1]
  • MetaCyc:Cytochromes-C-Oxidized

    Source assertion: The issuing native object identifies this whole class as an oxidized c-type cytochrome; no unique molecular formula or sequence is asserted.

    Source locationXPath /ptools-xml/Protein/common-name
2 a reduced c-type cytochrome[periplasm] + nitrous oxide[periplasm] + 2 H+[periplasm] -> 2 an oxidized c-type cytochrome[periplasm] + N2[periplasm] + H2O[periplasm]
MetaCyc:RXN-12130
produces

Coefficient 1; periplasmic side. Native compartmental equation and class identity retained.

water
CHEBI:15377
  • MetaCyc:RXN-12130

    Source assertion: The right side contains coefficient 1 of WATER in CCO-OUT.

    Source locationXPath /ptools-xml/Reaction/right[2]
  • MetaCyc:WATER

    Source assertion: The native WATER object has InChI InChI=1S/H2O/h1H2.

    Source locationXPath /ptools-xml/Compound/inchi
  • CHEBI:15377

    Source assertion: The selected ChEBI structure has the same InChI; formula H2O, charge 0.

    Source locationSemantic SQL statements: subject=CHEBI:15377; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge
2 a reduced c-type cytochrome[periplasm] + nitrous oxide[periplasm] + 2 H+[periplasm] -> 2 an oxidized c-type cytochrome[periplasm] + N2[periplasm] + H2O[periplasm]
MetaCyc:RXN-12130
produces

Coefficient 1; periplasmic side. Native compartmental equation and class identity retained.

dinitrogen
CHEBI:17997
  • MetaCyc:RXN-12130

    Source assertion: The right side contains coefficient 1 of NITROGEN-MOLECULE in CCO-OUT.

    Source locationXPath /ptools-xml/Reaction/right[3]
  • MetaCyc:NITROGEN-MOLECULE

    Source assertion: The native NITROGEN-MOLECULE object has InChI InChI=1S/N2/c1-2.

    Source locationXPath /ptools-xml/Compound/inchi
  • CHEBI:17997

    Source assertion: The selected ChEBI structure has the same InChI; formula N2, charge 0.

    Source locationSemantic SQL statements: subject=CHEBI:17997; chemrof:inchi_string, chemrof:generalized_empirical_formula, chemrof:charge
nitrate + an electron-transfer quinol[inner membrane] + 2 H+ nitrite + an electron-transfer quinone[inner membrane] + 2 H+[periplasm] + H2O
MetaCyc:RXN-11236
precedes

Source-defined reaction ordering; transport is coupled to nitrate reduction and no exclusive temporal separation or in vivo flux is inferred.

nitrate[periplasm] + nitrite[cytosol] -> nitrate[cytosol] + nitrite[periplasm]
MetaCyc:TRANS-RXN0-239
  • MetaCyc:DENITRIFICATION-PWY

    Source assertion: The reaction-ordering object identifies RXN-11236 as a predecessor of TRANS-RXN0-239.

    Source locationXPath /ptools-xml/Pathway/reaction-ordering[Reaction/@frameid="TRANS-RXN0-239"]
nitrate[periplasm] + nitrite[cytosol] -> nitrate[cytosol] + nitrite[periplasm]
MetaCyc:TRANS-RXN0-239
precedes

Source-defined reaction ordering; transport is coupled to nitrate reduction and no exclusive temporal separation or in vivo flux is inferred.

nitrite[periplasm] + a reduced cytochrome c551[periplasm] + 2 H+[periplasm] nitric oxide[periplasm] + an oxidized cytochrome c551[periplasm] + H2O[periplasm]
MetaCyc:RXN-15838
  • MetaCyc:DENITRIFICATION-PWY

    Source assertion: The reaction-ordering object identifies TRANS-RXN0-239 as a predecessor of RXN-15838.

    Source locationXPath /ptools-xml/Pathway/reaction-ordering[Reaction/@frameid="RXN-15838"]
nitrite[periplasm] + a reduced cytochrome c551[periplasm] + 2 H+[periplasm] nitric oxide[periplasm] + an oxidized cytochrome c551[periplasm] + H2O[periplasm]
MetaCyc:RXN-15838
precedes

Source-defined reaction ordering; transport is coupled to nitrate reduction and no exclusive temporal separation or in vivo flux is inferred.

2 a reduced c-type cytochrome[periplasm] + 2 nitric oxide[periplasm] + 2 H+[periplasm] -> nitrous oxide[periplasm] + 2 an oxidized c-type cytochrome[periplasm] + H2O[periplasm]
MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN
  • MetaCyc:DENITRIFICATION-PWY

    Source assertion: The reaction-ordering object identifies RXN-15838 as a predecessor of NITRIC-OXIDE-REDUCTASE-RXN.

    Source locationXPath /ptools-xml/Pathway/reaction-ordering[Reaction/@frameid="NITRIC-OXIDE-REDUCTASE-RXN"]
2 a reduced c-type cytochrome[periplasm] + 2 nitric oxide[periplasm] + 2 H+[periplasm] -> nitrous oxide[periplasm] + 2 an oxidized c-type cytochrome[periplasm] + H2O[periplasm]
MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN
precedes

Source-defined reaction ordering; transport is coupled to nitrate reduction and no exclusive temporal separation or in vivo flux is inferred.

2 a reduced c-type cytochrome[periplasm] + nitrous oxide[periplasm] + 2 H+[periplasm] -> 2 an oxidized c-type cytochrome[periplasm] + N2[periplasm] + H2O[periplasm]
MetaCyc:RXN-12130
  • MetaCyc:DENITRIFICATION-PWY

    Source assertion: The reaction-ordering object identifies NITRIC-OXIDE-REDUCTASE-RXN as a predecessor of RXN-12130.

    Source locationXPath /ptools-xml/Pathway/reaction-ordering[Reaction/@frameid="RXN-12130"]
nitrate reductase (quinone)
UniProtKB:G3XCX1
enables

Gene-product component of the Nar respiratory ensemble, not isolated-subunit catalysis. Current activity is ARBA inference; the source vectorial proton convention is not derived from that chemical-class annotation.

nitrate + an electron-transfer quinol[inner membrane] + 2 H+ nitrite + an electron-transfer quinone[inner membrane] + 2 H+[periplasm] + H2O
MetaCyc:RXN-11236
  • UniProtKB:G3XCX1

    Source assertion: This current UniProtKB unreviewed (TrEMBL) entry assigns G3XCX1 to taxon 208964, narG / PA3875, with a 1261-residue sequence. It does not establish sequence identity to every historical preparation.

    Source locationJSON pointer /primaryAccession; /organism/taxonId; /genes; /sequence
  • UniProtKB:G3XCX1

    Source assertion: The unreviewed catalytic annotation cites Rhea 56144 with ECO:0000256 ARBA evidence; it supports the nitrate/quinol reaction class.

    Source locationJSON pointer /comments/0
  • PMID:16391109

    Source assertion: PAO1 narG mutant showed no nitrate uptake, connecting intracellular nitrite generation with uptake; this is physiological coupling, not a purified subunit assay.

    Source locationXPath //article/section[2]/section/section[4]/p[3]
nitrate reductase (quinone)
UniProtKB:G3XD87
enables

Gene-product component of the Nar respiratory ensemble, not isolated-subunit catalysis. Current activity is ARBA inference; the source vectorial proton convention is not derived from that chemical-class annotation.

nitrate + an electron-transfer quinol[inner membrane] + 2 H+ nitrite + an electron-transfer quinone[inner membrane] + 2 H+[periplasm] + H2O
MetaCyc:RXN-11236
  • UniProtKB:G3XD87

    Source assertion: This current UniProtKB unreviewed (TrEMBL) entry assigns G3XD87 to taxon 208964, narH / PA3874, with a 513-residue sequence. It does not establish sequence identity to every historical preparation.

    Source locationJSON pointer /primaryAccession; /organism/taxonId; /genes; /sequence
  • UniProtKB:G3XD87

    Source assertion: The unreviewed catalytic annotation cites Rhea 56144 with ECO:0000256 ARBA evidence; it supports the nitrate/quinol reaction class.

    Source locationJSON pointer /comments/0
  • PMID:16391109

    Source assertion: PAO1 narG mutant showed no nitrate uptake, connecting intracellular nitrite generation with uptake; this is physiological coupling, not a purified subunit assay.

    Source locationXPath //article/section[2]/section/section[4]/p[3]
nitrate reductase (quinone)
UniProtKB:G3XD18
enables

Gene-product component of the Nar respiratory ensemble, not isolated-subunit catalysis. Current activity is ARBA inference; the source vectorial proton convention is not derived from that chemical-class annotation.

nitrate + an electron-transfer quinol[inner membrane] + 2 H+ nitrite + an electron-transfer quinone[inner membrane] + 2 H+[periplasm] + H2O
MetaCyc:RXN-11236
  • UniProtKB:G3XD18

    Source assertion: This current UniProtKB unreviewed (TrEMBL) entry assigns G3XD18 to taxon 208964, narI / PA3872, with a 227-residue sequence. It does not establish sequence identity to every historical preparation.

    Source locationJSON pointer /primaryAccession; /organism/taxonId; /genes; /sequence
  • UniProtKB:G3XD18

    Source assertion: The unreviewed catalytic annotation cites Rhea 56144 with ECO:0000256 ARBA evidence; it supports the nitrate/quinol reaction class.

    Source locationJSON pointer /comments/0
  • PMID:16391109

    Source assertion: PAO1 narG mutant showed no nitrate uptake, connecting intracellular nitrite generation with uptake; this is physiological coupling, not a purified subunit assay.

    Source locationXPath //article/section[2]/section/section[4]/p[3]
Nitrite reductase
UniProtKB:P24474
enables

Current NirS nitrite-reductase activity with source c551 donor convention; the protein is reported as a homodimer, but no other-species MetaCyc complex ID is transferred.

nitrite[periplasm] + a reduced cytochrome c551[periplasm] + 2 H+[periplasm] nitric oxide[periplasm] + an oxidized cytochrome c551[periplasm] + H2O[periplasm]
MetaCyc:RXN-15838
  • UniProtKB:P24474

    Source assertion: This current UniProtKB reviewed (Swiss-Prot) entry assigns P24474 to taxon 208964, nirS / PA0519, with a 568-residue sequence. It does not establish sequence identity to every historical preparation.

    Source locationJSON pointer /primaryAccession; /organism/taxonId; /genes; /sequence
  • UniProtKB:P24474

    Source assertion: The reviewed entry records nitrite-reductase catalytic activity (Rhea 15233) and homodimeric subunit organization. The Rhea class uses generic cytochrome c, broader than native c551.

    Source locationJSON pointer /comments/0; /comments/4
  • PMID:25386171

    Source assertion: The study distinguishes PAO0001 reporter PAO1 from Holloway PAO1 wild-type and its nirS-N and nosZ deletion mutants; these are physiological strain preparations, not sequence-exact recombinant NirS assays.

    Source locationXPath /article/body/sec[2]/sec[1]/p[1]
Nitric oxide reductase subunit B
UniProtKB:Q59647
enables

Subunit function in the NorBC ensemble, not isolated-subunit catalysis. Current NorB proton-pump prose is excluded. RCSB 3O0R PAO1 preparations differ from current sequences (NorB lacks current R301; NorC K100 versus N100), so no exact construct equivalence is asserted.

2 a reduced c-type cytochrome[periplasm] + 2 nitric oxide[periplasm] + 2 H+[periplasm] -> nitrous oxide[periplasm] + 2 an oxidized c-type cytochrome[periplasm] + H2O[periplasm]
MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN
  • UniProtKB:Q59647

    Source assertion: This current UniProtKB reviewed (Swiss-Prot) entry assigns Q59647 to taxon 208964, norB / PA0524, with a 466-residue sequence. It does not establish sequence identity to every historical preparation.

    Source locationJSON pointer /primaryAccession; /organism/taxonId; /genes; /sequence
  • UniProtKB:Q59647

    Source assertion: The reviewed entry describes a heterodimer consisting of a large cytochrome b subunit and a small cytochrome c subunit.

    Source locationJSON pointer /comments/3
  • UniProtKB:Q59647

    Source assertion: The catalytic annotation is Rhea 30211, a cytochrome-c NO/N2O reaction class; reduction proceeds in its reverse direction.

    Source locationJSON pointer /comments/1
  • PMID:21109633

    Source assertion: The primary abstract reports a P. aeruginosa NOR structure, an FeB center with three His and one Glu ligands, and no D- or K-proton pathway; extracellular proton delivery is proposed.

    Source locationXPath //result[id="21109633"]/abstractText
  • DOI:10.2210/pdb3o0r/pdb

    Source assertion: The mmCIF assigns entity 3, NorB, a 465-residue sequence and natural PAO1 source.

    Source locationCIF category _entity_poly.; _entity_src_nat.
  • UniProtKB:Q59647

    Source assertion: The inferred FUNCTION annotation (ECO:0000250) states proton-pump activity. This source statement is retained as a conflict and is not adopted as a transport or energy-coupling assertion.

    Source locationJSON pointer /comments/0
  • DOI:10.1126/science.1195591

    Source assertion: The structural discussion states that no obvious D/K proton-pumping channel or hydrogen-bond network connects cytoplasm and periplasm, consistent with cNOR lacking proton-pumping ability.

    Source locationOriginal author-uploaded main article, Science 330 pp.1666–1670 (2010), final structural discussion paragraph beginning “Considering the regions of cNOR”; Figure 4 context; web-inspected text, no local full-text body
Nitric oxide reductase subunit C
UniProtKB:Q59646
enables

Subunit function in the NorBC ensemble, not isolated-subunit catalysis. Current NorB proton-pump prose is excluded. RCSB 3O0R PAO1 preparations differ from current sequences (NorB lacks current R301; NorC K100 versus N100), so no exact construct equivalence is asserted.

2 a reduced c-type cytochrome[periplasm] + 2 nitric oxide[periplasm] + 2 H+[periplasm] -> nitrous oxide[periplasm] + 2 an oxidized c-type cytochrome[periplasm] + H2O[periplasm]
MetaCyc:NITRIC-OXIDE-REDUCTASE-RXN
  • UniProtKB:Q59646

    Source assertion: This current UniProtKB reviewed (Swiss-Prot) entry assigns Q59646 to taxon 208964, norC / PA0523, with a 146-residue sequence. It does not establish sequence identity to every historical preparation.

    Source locationJSON pointer /primaryAccession; /organism/taxonId; /genes; /sequence
  • UniProtKB:Q59646

    Source assertion: The reviewed entry describes a heterodimer consisting of a large cytochrome b subunit and a small cytochrome c subunit.

    Source locationJSON pointer /comments/1
  • PMID:21109633

    Source assertion: The primary abstract reports a P. aeruginosa NOR structure, an FeB center with three His and one Glu ligands, and no D- or K-proton pathway; extracellular proton delivery is proposed.

    Source locationXPath //result[id="21109633"]/abstractText
  • DOI:10.2210/pdb3o0r/pdb

    Source assertion: The mmCIF assigns entity 4, NorC, a 146-residue sequence including K100 and natural PAO1 source.

    Source locationCIF category _entity_poly.; _entity_src_nat.
Nitrous-oxide reductase
UniProtKB:Q9HYL2
enables

NosZ activity is annotated by HAMAP; PAO1 deletion physiology independently supports terminal N2O reduction. Generic c-type electron donor is a source reaction convention, not a uniquely identified physiological partner.

2 a reduced c-type cytochrome[periplasm] + nitrous oxide[periplasm] + 2 H+[periplasm] -> 2 an oxidized c-type cytochrome[periplasm] + N2[periplasm] + H2O[periplasm]
MetaCyc:RXN-12130
  • UniProtKB:Q9HYL2

    Source assertion: This current UniProtKB reviewed (Swiss-Prot) entry assigns Q9HYL2 to taxon 208964, nosZ / PA3392, with a 636-residue sequence. It does not establish sequence identity to every historical preparation.

    Source locationJSON pointer /primaryAccession; /organism/taxonId; /genes; /sequence
  • UniProtKB:Q9HYL2

    Source assertion: The entry assigns nitrous-oxide reductase activity (Rhea 43108) using ECO:0000255 HAMAP-Rule MF_00716.

    Source locationJSON pointer /comments/1
  • PMID:30093706

    Source assertion: The PAO1 nosZ deletion strain accumulates N2O during denitrification; NosZ loss is the engineered physiological block.

    Source locationXPath /article/body/sec[2]/sec[1]/p[2]
  • PMID:25386171

    Source assertion: The nosZ mutant accumulates N2O under anoxia, whereas wild-type PAO1 produces less than 10 micromolar N2O under the experimental nitrate concentrations.

    Source locationXPath /article/body/sec[3]/sec[4]/p
Nitrate/nitrite transporter
UniProtKB:Q9HXD4
enables

Nitrate/nitrite transport contribution to the complete pathway; this edge does not assign strict 1:1 antiport or isolated exact transport stoichiometry. NarK2 has the dominant phenotype and NarK1 a smaller contribution in the tested PAO1 conditions.

MetaCyc:DENITRIFICATION-PWY
  • UniProtKB:Q9HXD4

    Source assertion: This current UniProtKB unreviewed (TrEMBL) entry assigns Q9HXD4 to taxon 208964, narK2 / PA3876, with a 468-residue sequence. It does not establish sequence identity to every historical preparation.

    Source locationJSON pointer /primaryAccession; /organism/taxonId; /genes; /sequence
  • PMID:16391109

    Source assertion: PAO1 narK1 deletion only slightly affected anaerobic growth, while narK2 and double deletion were severely compromised; all mutants retained nitrate-reductase activity.

    Source locationXPath //article/section[2]/section/section[4]/p[2]
  • PMID:16391109

    Source assertion: The authors explicitly leave antiport versus uniport experimentally unresolved.

    Source locationXPath //article/section[2]/section/section[4]/p[5]
Nitrite extrusion protein 1
UniProtKB:G3XD60
enables

Nitrate/nitrite transport contribution to the complete pathway; this edge does not assign strict 1:1 antiport or isolated exact transport stoichiometry. NarK2 has the dominant phenotype and NarK1 a smaller contribution in the tested PAO1 conditions.

MetaCyc:DENITRIFICATION-PWY
  • UniProtKB:G3XD60

    Source assertion: This current UniProtKB unreviewed (TrEMBL) entry assigns G3XD60 to taxon 208964, narK1 / PA3877, with a 431-residue sequence. It does not establish sequence identity to every historical preparation.

    Source locationJSON pointer /primaryAccession; /organism/taxonId; /genes; /sequence
  • PMID:16391109

    Source assertion: PAO1 narK1 deletion only slightly affected anaerobic growth, while narK2 and double deletion were severely compromised; all mutants retained nitrate-reductase activity.

    Source locationXPath //article/section[2]/section/section[4]/p[2]
  • PMID:16391109

    Source assertion: The authors explicitly leave antiport versus uniport experimentally unresolved.

    Source locationXPath //article/section[2]/section/section[4]/p[5]
Cytochrome c-551
UniProtKB:P00099
enables

NirM electron-donor contribution to nitrite reduction, not catalytic nitrite-reductase assignment. The whole c551 redox classes remain distinct from the sequence entry.

nitrite[periplasm] + a reduced cytochrome c551[periplasm] + 2 H+[periplasm] nitric oxide[periplasm] + an oxidized cytochrome c551[periplasm] + H2O[periplasm]
MetaCyc:RXN-15838
  • UniProtKB:P00099

    Source assertion: This current UniProtKB reviewed (Swiss-Prot) entry assigns P00099 to taxon 208964, nirM / PA0518, with a 104-residue sequence. It does not establish sequence identity to every historical preparation.

    Source locationJSON pointer /primaryAccession; /organism/taxonId; /genes; /sequence
  • UniProtKB:P00099

    Source assertion: The reviewed entry identifies cytochrome c-551 as an electron donor for cytochrome cd1 in nitrite and nitrate respiration.

    Source locationJSON pointer /comments/0
nitrate reductase (quinone)
UniProtKB:G3XCX1
has_cofactor

Current entry annotation of Mo-bisMGD; ECO:0000256 ARBA. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.

Mo(=O)-bis(molybdopterin guanine dinucleotide)(4-)
CHEBI:60539
  • UniProtKB:G3XCX1

    Source assertion: The exact annotation records Mo-bisMGD with ECO:0000256 ARBA; the selected ChEBI cofactor identifier is the entry-assigned ligand identity.

    Source locationJSON pointer /comments/1
nitrate reductase (quinone)
UniProtKB:G3XCX1
has_cofactor

Current entry annotation of [4Fe-4S]; ECO:0000256 ARBA. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.

tetra-mu3-sulfido-tetrairon
CHEBI:49883
  • UniProtKB:G3XCX1

    Source assertion: The exact annotation records [4Fe-4S] with ECO:0000256 ARBA; the selected ChEBI cofactor identifier is the entry-assigned ligand identity.

    Source locationJSON pointer /comments/2
nitrate reductase (quinone)
UniProtKB:G3XD87
has_cofactor

Current entry annotation of [3Fe-4S]; ECO:0000256 ARBA. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.

tri-mu-sulfido-mu3-sulfido-triiron
CHEBI:21137
  • UniProtKB:G3XD87

    Source assertion: The exact annotation records [3Fe-4S] with ECO:0000256 ARBA; the selected ChEBI cofactor identifier is the entry-assigned ligand identity.

    Source locationJSON pointer /comments/1
nitrate reductase (quinone)
UniProtKB:G3XD87
has_cofactor

Current entry annotation of [4Fe-4S]; ECO:0000256 ARBA. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.

tetra-mu3-sulfido-tetrairon
CHEBI:49883
  • UniProtKB:G3XD87

    Source assertion: The exact annotation records [4Fe-4S] with ECO:0000256 ARBA; the selected ChEBI cofactor identifier is the entry-assigned ligand identity.

    Source locationJSON pointer /comments/2
nitrate reductase (quinone)
UniProtKB:G3XD18
has_cofactor

Current entry annotation of heme b; ECO:0000256 PIRSR. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.

ferroheme b(2-)
CHEBI:60344
  • UniProtKB:G3XD18

    Source assertion: The exact annotation records heme b with ECO:0000256 PIRSR; the selected ChEBI cofactor identifier is the entry-assigned ligand identity.

    Source locationJSON pointer /features/6
Nitrite reductase
UniProtKB:P24474
has_cofactor

Current entry annotation of heme c; ECO:0000269 PMID9331415. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.

ferroheme c(2-)
CHEBI:61717
  • UniProtKB:P24474

    Source assertion: The exact annotation records heme c with ECO:0000269 PMID9331415; the selected ChEBI cofactor identifier is the entry-assigned ligand identity.

    Source locationJSON pointer /comments/2
Nitrite reductase
UniProtKB:P24474
has_cofactor

Current entry annotation of heme d1; ECO:0000269 PMID9331415 and PDB mapping. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.

ferroheme d1(4-)
CHEBI:60549
  • UniProtKB:P24474

    Source assertion: The exact annotation records heme d1 with ECO:0000269 PMID9331415 and PDB mapping; the selected ChEBI cofactor identifier is the entry-assigned ligand identity.

    Source locationJSON pointer /features/11
Nitric oxide reductase subunit B
UniProtKB:Q59647
has_cofactor

Current entry annotation of heme b; ECO:0000305 curator inference. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.

ferroheme b(2-)
CHEBI:60344
  • UniProtKB:Q59647

    Source assertion: The exact annotation records heme b with ECO:0000305 curator inference; the selected ChEBI cofactor identifier is the entry-assigned ligand identity.

    Source locationJSON pointer /features/13
Nitric oxide reductase subunit B
UniProtKB:Q59647
has_cofactor

Current entry annotation of non-heme Fe cation; ECO:0000305 curator inference. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.

iron cation
CHEBI:24875
  • UniProtKB:Q59647

    Source assertion: The exact annotation records non-heme Fe cation with ECO:0000305 curator inference; the selected ChEBI cofactor identifier is the entry-assigned ligand identity.

    Source locationJSON pointer /features/14
Nitric oxide reductase subunit C
UniProtKB:Q59646
has_cofactor

Current entry annotation of heme c; ECO:0000255 PROSITE. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.

ferroheme c(2-)
CHEBI:61717
  • UniProtKB:Q59646

    Source assertion: The exact annotation records heme c with ECO:0000255 PROSITE; the selected ChEBI cofactor identifier is the entry-assigned ligand identity.

    Source locationJSON pointer /features/3
Nitrous-oxide reductase
UniProtKB:Q9HYL2
has_cofactor

Current entry annotation of CuA binuclear copper center; ECO:0000255 HAMAP. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.

binuclear copper ion
CHEBI:47357
  • UniProtKB:Q9HYL2

    Source assertion: The exact annotation records CuA binuclear copper center with ECO:0000255 HAMAP; the selected ChEBI cofactor identifier is the entry-assigned ligand identity.

    Source locationJSON pointer /comments/2
Nitrous-oxide reductase
UniProtKB:Q9HYL2
has_cofactor

Current entry annotation of CuZ [4Cu-S] cluster; ECO:0000255 HAMAP. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.

mu4-sulfido-quadro-tetracopper
CHEBI:33730
  • UniProtKB:Q9HYL2

    Source assertion: The exact annotation records CuZ [4Cu-S] cluster with ECO:0000255 HAMAP; the selected ChEBI cofactor identifier is the entry-assigned ligand identity.

    Source locationJSON pointer /comments/3
Nitrous-oxide reductase
UniProtKB:Q9HYL2
has_cofactor

Current entry annotation of Ca2+; ECO:0000255 HAMAP. Issuing cofactor-state identifier is retained without asserting a fixed redox state throughout catalysis or direct measurement in every PAO1 preparation.

calcium(2+)
CHEBI:29108
  • UniProtKB:Q9HYL2

    Source assertion: The exact annotation records Ca2+ with ECO:0000255 HAMAP; the selected ChEBI cofactor identifier is the entry-assigned ligand identity.

    Source locationJSON pointer /comments/4
Cytochrome c-551
UniProtKB:P00099
has_cofactor

Covalently attached heme c; the whole redox carrier is retained separately. Current heme annotation does not assert a permanently reduced in vivo state.

ferroheme c(2-)
CHEBI:61717
  • UniProtKB:P00099

    Source assertion: The entry states that one heme c group is covalently bound per subunit.

    Source locationJSON pointer /comments/3
  • UniProtKB:P00099

    Source assertion: The current cytochrome c-551 heme-binding feature assigns CHEBI:61717.

    Source locationJSON pointer /features/2
Transcriptional activator protein anr
UniProtKB:P23926
regulates

Expression-level regulatory support under tested PAO1 nitrate/anaerobic conditions; no direct catalytic activation/inhibition or IHF CHA-A2 strain transfer is inferred.

MetaCyc:DENITRIFICATION-PWY
  • UniProtKB:P23926

    Source assertion: This current UniProtKB reviewed (Swiss-Prot) entry assigns P23926 to taxon 208964, anr / PA1544, with a 244-residue sequence. It does not establish sequence identity to every historical preparation.

    Source locationJSON pointer /primaryAccession; /organism/taxonId; /genes; /sequence
  • PMID:17400734

    Source assertion: Anr is essential for anaerobic narK1 promoter activity; promoter motif mutation and complementation support the expression effect.

    Source locationXPath //article/section[2]/section/section[4]/p[position() >= 1 and position() <= 2]
Transcriptional regulator Dnr
UniProtKB:G3XCW6
regulates

Expression-level regulatory support under tested PAO1 nitrate/anaerobic conditions; no direct catalytic activation/inhibition or IHF CHA-A2 strain transfer is inferred.

MetaCyc:DENITRIFICATION-PWY
  • UniProtKB:G3XCW6

    Source assertion: This current UniProtKB unreviewed (TrEMBL) entry assigns G3XCW6 to taxon 208964, dnr / PA0527, with a 227-residue sequence. It does not establish sequence identity to every historical preparation.

    Source locationJSON pointer /primaryAccession; /organism/taxonId; /genes; /sequence
  • PMID:17400734

    Source assertion: Dnr deletion decreases anaerobic narK1 promoter activity and complementation supports an enhancing expression role.

    Source locationXPath //article/section[2]/section/section[4]/p[1]
Two-component response regulator NarL
UniProtKB:Q9HXD3
regulates

Expression-level regulatory support under tested PAO1 nitrate/anaerobic conditions; no direct catalytic activation/inhibition or IHF CHA-A2 strain transfer is inferred.

MetaCyc:DENITRIFICATION-PWY
  • UniProtKB:Q9HXD3

    Source assertion: This current UniProtKB unreviewed (TrEMBL) entry assigns Q9HXD3 to taxon 208964, narL / PA3879, with a 219-residue sequence. It does not establish sequence identity to every historical preparation.

    Source locationJSON pointer /primaryAccession; /organism/taxonId; /genes; /sequence
  • PMID:17400734

    Source assertion: NarL deletion lowers narK1 promoter activity, complementation nearly restores it, and selected promoter-site mutations abolish reporter activity.

    Source locationXPath //article/section[2]/section/section[4]/p[2]
Nitrite reductase
UniProtKB:P24474
located_in

Current entry localization; inferred/rule-based scope remains as in the cited source. Membrane role does not itself demonstrate proton pumping.

periplasmic space
GO:0042597
  • UniProtKB:P24474

    Source assertion: The subcellular-location annotation places the protein in the periplasm.

    Source locationJSON pointer /comments/5
Nitric oxide reductase subunit B
UniProtKB:Q59647
located_in

Current entry localization; inferred/rule-based scope remains as in the cited source. Membrane role does not itself demonstrate proton pumping.

plasma membrane
GO:0005886
  • UniProtKB:Q59647

    Source assertion: The subcellular-location annotation places the protein in the cell/inner membrane.

    Source locationJSON pointer /comments/4
Nitric oxide reductase subunit C
UniProtKB:Q59646
located_in

Current entry localization; inferred/rule-based scope remains as in the cited source. Membrane role does not itself demonstrate proton pumping.

plasma membrane
GO:0005886
  • UniProtKB:Q59646

    Source assertion: The subcellular-location annotation places the protein in the cell/inner membrane.

    Source locationJSON pointer /comments/2
Nitrous-oxide reductase
UniProtKB:Q9HYL2
located_in

Current entry localization; inferred/rule-based scope remains as in the cited source. Membrane role does not itself demonstrate proton pumping.

periplasmic space
GO:0042597
  • UniProtKB:Q9HYL2

    Source assertion: The subcellular-location annotation places the protein in the periplasm.

    Source locationJSON pointer /comments/7
nitrate reductase (quinone)
UniProtKB:G3XCX1
located_in

Current entry localization; inferred/rule-based scope remains as in the cited source. Membrane role does not itself demonstrate proton pumping.

plasma membrane
GO:0005886
  • UniProtKB:G3XCX1

    Source assertion: The subcellular-location annotation places the protein in the cell/inner membrane.

    Source locationJSON pointer /comments/3
nitrate reductase (quinone)
UniProtKB:G3XD87
located_in

Current entry localization; inferred/rule-based scope remains as in the cited source. Membrane role does not itself demonstrate proton pumping.

plasma membrane
GO:0005886
  • UniProtKB:G3XD87

    Source assertion: The subcellular-location annotation places the protein in the cell/inner membrane.

    Source locationJSON pointer /comments/4
nitrate reductase (quinone)
UniProtKB:G3XD18
located_in

Current entry localization; inferred/rule-based scope remains as in the cited source. Membrane role does not itself demonstrate proton pumping.

plasma membrane
GO:0005886
  • UniProtKB:G3XD18

    Source assertion: The subcellular-location annotation places the protein in the cell/inner membrane.

    Source locationJSON pointer /comments/3
Nitrate/nitrite transporter
UniProtKB:Q9HXD4
located_in

Current entry localization; inferred/rule-based scope remains as in the cited source. Membrane role does not itself demonstrate proton pumping.

plasma membrane
GO:0005886
  • UniProtKB:Q9HXD4

    Source assertion: The subcellular-location annotation places the protein in the cell/inner membrane.

    Source locationJSON pointer /comments/0
Nitrite extrusion protein 1
UniProtKB:G3XD60
located_in

Generic membrane localization and multipass topology are inferred by ARBA (ECO:0000256). The current entry does not specify the inner/plasma membrane; no direct localization assay or proton-pumping role is inferred.

membrane
GO:0016020
  • UniProtKB:G3XD60

    Source assertion: The entry annotates Membrane and Multi-pass membrane protein with ECO:0000256 ARBA00004141. Its GO cross-reference is GO:0016020 membrane, with IEA:UniProtKB-SubCell; this does not specify the inner/plasma membrane.

    Source locationJSON pointer /comments/0; /uniProtKBCrossReferences/18
  • GO:0016020

    Source assertion: The issuing active GO cellular-component term is membrane, defined as a lipid bilayer with embedded or attached proteins and complexes. This generic term does not assert plasma-membrane specificity.

    Source locationSemantic SQL statements: subject=GO:0016020; rdfs:label, IAO:0000115, oio:hasOBONamespace
Cytochrome c-551
UniProtKB:P00099
located_in

Current entry localization; inferred/rule-based scope remains as in the cited source. Membrane role does not itself demonstrate proton pumping.

periplasmic space
GO:0042597
  • UniProtKB:P00099

    Source assertion: The subcellular-location annotation places the protein in the periplasm.

    Source locationJSON pointer /comments/2

References

Curation history