pyochelin biosynthetic process

GO:0042864

The complete eleven-object MetaCyc PWY-6408 thiotemplate pathway is represented from supplied salicylate and two L-cysteines through pyochelin release. The PAO1 implementation uses PchD, PchE, PchF and PchG; it does not include upstream PchA/PchB salicylate synthesis. The shared cysteine-adenylation reaction turns twice per formal product. Carrier-class coefficients count reactive sites, not whole polypeptides: PchE has distinct aryl and peptidyl carrier domains on one chain. The three-ATP total is a stoichiometric derivation, not a measured yield. Native CPD-9992 specifies the pyochelin I monoanion, one member of the experimentally observed interconverting I/II products. Its use preserves a source-defined I projection; it does not assert exclusive I production, identity with the neutral I/II class, or a separate experimentally resolved release stereoselectivity. Native carrier names do not specify every stereocenter. PchE epimerization occurs after amide formation; its coupled cyclization step retains that scope without adding an unsupported separate reaction. Direct 2022 PAO1 structural work observes a PchE homodimer and bound magnesium; functional enables edges do not assert monomer sufficiency or a stable PchDEFG heterotetramer. The 1999 deposited PchD/E/F sequences are from PA14 and differ from current PAO1; the older PAO1 PchF submission also differs at six residues. Later PAO1 source and construct evidence is distinguished from exact engineered-sequence identity. Current PchD and some PchE/F mechanistic annotations retain similarity or curator inference. PchG is an unreviewed current entry, supported separately by PAO1 genetics and biochemical work; free-analogue measurements are not full carrier-substrate kinetics. PchC editing, transport, iron loading and regulation are outside this native assembly boundary.

Pathway type
pyochelin biosynthesis
Organism scope

Read the source YAML

Pathway network

42 nodes · 91 asserted directed edges

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

Pathway network: pyochelin biosynthetic process 42 nodes · 91 asserted directed edges. Every arrow links to its evidence table row; nodes link to their component details. Isolated declared components are retained. CHEBI:15378 — consumes → MetaCyc:RXN-11113; Evidence: MetaCyc:RXN-11113, MetaCyc:PROTON, CHEBI:15378consumes CHEBI:30762 — consumes → MetaCyc:RXN-11113; Evidence: MetaCyc:RXN-11113, MetaCyc:CPD-110, CHEBI:30762consumes CHEBI:30616 — consumes → MetaCyc:RXN-11113; Evidence: MetaCyc:RXN-11113, MetaCyc:ATP, CHEBI:30616consumes MetaCyc:RXN-11113 — produces → CHEBI:86458; Evidence: MetaCyc:RXN-11113, MetaCyc:CPD-12084, CHEBI:86458produces MetaCyc:RXN-11113 — produces → CHEBI:33019; Evidence: MetaCyc:RXN-11113, MetaCyc:PPI, CHEBI:33019produces CHEBI:35235 — consumes → MetaCyc:RXN-11115; Evidence: MetaCyc:RXN-11115, MetaCyc:CYS, CHEBI:35235consumes CHEBI:30616 — consumes → MetaCyc:RXN-11115; Evidence: MetaCyc:RXN-11115, MetaCyc:ATP, CHEBI:30616consumes CHEBI:15378 — consumes → MetaCyc:RXN-11115; Evidence: MetaCyc:RXN-11115, MetaCyc:PROTON, CHEBI:15378consumes MetaCyc:RXN-11115 — produces → CHEBI:144924; Evidence: MetaCyc:RXN-11115, MetaCyc:CPD-12085, CHEBI:144924produces MetaCyc:RXN-11115 — produces → CHEBI:33019; Evidence: MetaCyc:RXN-11115, MetaCyc:PPI, CHEBI:33019produces CHEBI:144924 — consumes → MetaCyc:RXN-11117; Evidence: MetaCyc:RXN-11117, MetaCyc:CPD-12085, CHEBI:144924consumes MetaCyc:PchF — consumes → MetaCyc:RXN-11117; Native PchF reactive-domain state; coefficient is not an enzyme assembly count.; Evidence: MetaCyc:RXN-11117, MetaCyc:PchF, DOI:10.1038/s41467-022-28284-xconsumes MetaCyc:RXN-11117 — produces → MetaCyc:L-cysteinyl-PchF; Native PchF reactive-domain state; coefficient is not an enzyme assembly count.; Evidence: MetaCyc:RXN-11117, MetaCyc:L-cysteinyl-PchF, DOI:10.1038/s41467-022-28284-xproduces MetaCyc:RXN-11117 — produces → CHEBI:456215; Evidence: MetaCyc:RXN-11117, MetaCyc:AMP, CHEBI:456215produces MetaCyc:RXN-11117 — produces → CHEBI:15378; Evidence: MetaCyc:RXN-11117, MetaCyc:PROTON, CHEBI:15378produces MetaCyc:Salicyl-L-cysteinyl-PchE — consumes → MetaCyc:RXN-11118; Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.; Evidence: MetaCyc:RXN-11118, MetaCyc:Salicyl-L-cysteinyl-PchE, DOI:10.1038/s41467-022-28284-xconsumes MetaCyc:RXN-11118 — produces → MetaCyc:hydroxyphenyl-thiazolinyl-PchE; Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.; Evidence: MetaCyc:RXN-11118, MetaCyc:hydroxyphenyl-thiazolinyl-PchE, DOI:10.1038/s41467-022-28284-xproduces MetaCyc:RXN-11118 — produces → CHEBI:15377; Evidence: MetaCyc:RXN-11118, MetaCyc:WATER, CHEBI:15377produces MetaCyc:L-cysteinyl-PchF — consumes → MetaCyc:RXN-11120; Native PchF reactive-domain state; coefficient is not an enzyme assembly count.; Evidence: MetaCyc:RXN-11120, MetaCyc:L-cysteinyl-PchF, DOI:10.1038/s41467-022-28284-xconsumes MetaCyc:hydroxyphenyl-thiazolinyl-PchE — consumes → MetaCyc:RXN-11120; Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.; Evidence: MetaCyc:RXN-11120, MetaCyc:hydroxyphenyl-thiazolinyl-PchE, DOI:10.1038/s41467-022-28284-xconsumes MetaCyc:RXN-11120 — produces → MetaCyc:Hydroxyphenyl-bis-thiazolinyl-PchF; Native PchF reactive-domain state; coefficient is not an enzyme assembly count.; Evidence: MetaCyc:RXN-11120, MetaCyc:Hydroxyphenyl-bis-thiazolinyl-PchF, DOI:10.1038/s41467-022-28284-xproduces MetaCyc:RXN-11120 — produces → CHEBI:15377; Evidence: MetaCyc:RXN-11120, MetaCyc:WATER, CHEBI:15377produces MetaCyc:RXN-11120 — produces → MetaCyc:PchE; Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.; Evidence: MetaCyc:RXN-11120, MetaCyc:PchE, DOI:10.1038/s41467-022-28284-xproduces MetaCyc:RXN-11120 — produces → CHEBI:15378; Evidence: MetaCyc:RXN-11120, MetaCyc:PROTON, CHEBI:15378produces MetaCyc:Hydroxyphenyl-bis-thiazolinyl-PchF — consumes → MetaCyc:RXN-11121; Native PchF reactive-domain state; coefficient is not an enzyme assembly count.; Evidence: MetaCyc:RXN-11121, MetaCyc:Hydroxyphenyl-bis-thiazolinyl-PchF, DOI:10.1038/s41467-022-28284-xconsumes CHEBI:57783 — consumes → MetaCyc:RXN-11121; Evidence: MetaCyc:RXN-11121, MetaCyc:NADPH, CHEBI:57783consumes CHEBI:15378 — consumes → MetaCyc:RXN-11121; Evidence: MetaCyc:RXN-11121, MetaCyc:PROTON, CHEBI:15378consumes MetaCyc:RXN-11121 — produces → MetaCyc:N-desmethyl-pyochelin-PchF; Native PchF reactive-domain state; coefficient is not an enzyme assembly count.; Evidence: MetaCyc:RXN-11121, MetaCyc:N-desmethyl-pyochelin-PchF, DOI:10.1038/s41467-022-28284-xproduces MetaCyc:RXN-11121 — produces → CHEBI:58349; Evidence: MetaCyc:RXN-11121, MetaCyc:NADP, CHEBI:58349produces CHEBI:59789 — consumes → MetaCyc:RXN-11122; Evidence: MetaCyc:RXN-11122, MetaCyc:S-ADENOSYLMETHIONINE, CHEBI:59789consumes MetaCyc:N-desmethyl-pyochelin-PchF — consumes → MetaCyc:RXN-11122; Native PchF reactive-domain state; coefficient is not an enzyme assembly count.; Evidence: MetaCyc:RXN-11122, MetaCyc:N-desmethyl-pyochelin-PchF, DOI:10.1038/s41467-022-28284-xconsumes MetaCyc:RXN-11122 — produces → MetaCyc:Pyochelinyl-PchF; Native PchF reactive-domain state; coefficient is not an enzyme assembly count.; Evidence: MetaCyc:RXN-11122, MetaCyc:Pyochelinyl-PchF, DOI:10.1038/s41467-022-28284-xproduces MetaCyc:RXN-11122 — produces → CHEBI:57856; Evidence: MetaCyc:RXN-11122, MetaCyc:ADENOSYL-HOMO-CYS, CHEBI:57856produces MetaCyc:RXN-11122 — produces → CHEBI:15378; Evidence: MetaCyc:RXN-11122, MetaCyc:PROTON, CHEBI:15378produces MetaCyc:Pyochelinyl-PchF — consumes → MetaCyc:RXN-11123; Native PchF reactive-domain state; coefficient is not an enzyme assembly count.; Evidence: MetaCyc:RXN-11123, MetaCyc:Pyochelinyl-PchF, DOI:10.1038/s41467-022-28284-xconsumes CHEBI:15377 — consumes → MetaCyc:RXN-11123; Evidence: MetaCyc:RXN-11123, MetaCyc:WATER, CHEBI:15377consumes MetaCyc:RXN-11123 — produces → MetaCyc:CPD-9992; Formal native pyochelin I monoanion endpoint; no exclusive-I physiological product or I-selective release claim.; Evidence: MetaCyc:RXN-11123, MetaCyc:CPD-9992, CHEBI:67183, PMID:17938167produces MetaCyc:RXN-11123 — produces → MetaCyc:PchF; Native PchF reactive-domain state; coefficient is not an enzyme assembly count.; Evidence: MetaCyc:RXN-11123, MetaCyc:PchF, DOI:10.1038/s41467-022-28284-xproduces MetaCyc:RXN-11123 — produces → CHEBI:15378; Evidence: MetaCyc:RXN-11123, MetaCyc:PROTON, CHEBI:15378produces CHEBI:144924 — consumes → MetaCyc:RXN-11125; Evidence: MetaCyc:RXN-11125, MetaCyc:CPD-12085, CHEBI:144924consumes MetaCyc:PchE — consumes → MetaCyc:RXN-11125; Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.; Evidence: MetaCyc:RXN-11125, MetaCyc:PchE, DOI:10.1038/s41467-022-28284-xconsumes MetaCyc:RXN-11125 — produces → MetaCyc:L-cysteinyl-PchE; Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.; Evidence: MetaCyc:RXN-11125, MetaCyc:L-cysteinyl-PchE, DOI:10.1038/s41467-022-28284-xproduces MetaCyc:RXN-11125 — produces → CHEBI:456215; Evidence: MetaCyc:RXN-11125, MetaCyc:AMP, CHEBI:456215produces MetaCyc:RXN-11125 — produces → CHEBI:15378; Evidence: MetaCyc:RXN-11125, MetaCyc:PROTON, CHEBI:15378produces CHEBI:86458 — consumes → MetaCyc:RXN-19466; Evidence: MetaCyc:RXN-19466, MetaCyc:CPD-12084, CHEBI:86458consumes MetaCyc:PchE — consumes → MetaCyc:RXN-19466; Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.; Evidence: MetaCyc:RXN-19466, MetaCyc:PchE, DOI:10.1038/s41467-022-28284-xconsumes MetaCyc:RXN-19466 — produces → MetaCyc:Salicyl-PchE; Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.; Evidence: MetaCyc:RXN-19466, MetaCyc:Salicyl-PchE, DOI:10.1038/s41467-022-28284-xproduces MetaCyc:RXN-19466 — produces → CHEBI:456215; Evidence: MetaCyc:RXN-19466, MetaCyc:AMP, CHEBI:456215produces MetaCyc:RXN-19466 — produces → CHEBI:15378; Evidence: MetaCyc:RXN-19466, MetaCyc:PROTON, CHEBI:15378produces MetaCyc:Salicyl-PchE — consumes → MetaCyc:RXN-19469; Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.; Evidence: MetaCyc:RXN-19469, MetaCyc:Salicyl-PchE, DOI:10.1038/s41467-022-28284-xconsumes MetaCyc:L-cysteinyl-PchE — consumes → MetaCyc:RXN-19469; Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.; Evidence: MetaCyc:RXN-19469, MetaCyc:L-cysteinyl-PchE, DOI:10.1038/s41467-022-28284-xconsumes MetaCyc:RXN-19469 — produces → MetaCyc:Salicyl-L-cysteinyl-PchE; Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.; Evidence: MetaCyc:RXN-19469, MetaCyc:Salicyl-L-cysteinyl-PchE, DOI:10.1038/s41467-022-28284-xproduces MetaCyc:RXN-19469 — produces → MetaCyc:PchE; Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.; Evidence: MetaCyc:RXN-19469, MetaCyc:PchE, DOI:10.1038/s41467-022-28284-xproduces MetaCyc:RXN-19469 — produces → CHEBI:15378; Evidence: MetaCyc:RXN-19469, MetaCyc:PROTON, CHEBI:15378produces UniProtKB:Q9HWG3 — enables → MetaCyc:RXN-11113; PchD adenylates salicylate before transfer to the PchE aryl carrier site. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.; Evidence: UniProtKB:Q9HWG3, PMID:35105906enables UniProtKB:G3XCV2 — enables → MetaCyc:RXN-11115; The PchE and PchF adenylation domains each activate a cysteine; one native reaction object is reused twice. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.; Evidence: UniProtKB:G3XCV2, PMID:35105906enables UniProtKB:Q9HWG4 — enables → MetaCyc:RXN-11115; The PchE and PchF adenylation domains each activate a cysteine; one native reaction object is reused twice. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.; Evidence: UniProtKB:Q9HWG4, PMID:30525512, PMID:11467965enables UniProtKB:Q9HWG4 — enables → MetaCyc:RXN-11117; PchF loads its activated cysteine onto its carrier site. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.; Evidence: UniProtKB:Q9HWG4, PMID:30525512, PMID:11467965enables UniProtKB:G3XCV2 — enables → MetaCyc:RXN-11118; PchE performs first-ring cyclization with epimerization after amide formation. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.; Evidence: UniProtKB:G3XCV2, PMID:35105906, PMID:12950179enables UniProtKB:Q9HWG4 — enables → MetaCyc:RXN-11120; PchF accepts the PchE-bound intermediate, condenses the second cysteine and forms the second thiazoline. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.; Evidence: UniProtKB:Q9HWG4, PMID:30525512, PMID:11467965enables UniProtKB:Q9HWG5 — enables → MetaCyc:RXN-11121; PchG reduces the PchF-tethered terminal thiazoline using NADPH. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.; Evidence: UniProtKB:Q9HWG5, PMID:11467965, PMID:11208777, PMID:27601130enables UniProtKB:Q9HWG4 — enables → MetaCyc:RXN-11122; PchF methylates the reduced terminal nitrogen with SAM. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.; Evidence: UniProtKB:Q9HWG4, PMID:30525512, PMID:11467965enables UniProtKB:Q9HWG4 — enables → MetaCyc:RXN-11123; PchF releases pyochelin by thioester hydrolysis; the native I structure is a formal projection of the observed I/II products. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.; Evidence: UniProtKB:Q9HWG4, PMID:30525512, PMID:11467965enables UniProtKB:G3XCV2 — enables → MetaCyc:RXN-11125; PchE loads cysteine onto its peptidyl carrier site. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.; Evidence: UniProtKB:G3XCV2, PMID:35105906enables UniProtKB:Q9HWG3 — enables → MetaCyc:RXN-19466; PchD transfers activated salicylate to the PchE aryl carrier site. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.; Evidence: UniProtKB:Q9HWG3, PMID:35105906enables UniProtKB:G3XCV2 — enables → MetaCyc:RXN-19469; PchE condenses its aryl-site salicyl group with its peptidyl-site cysteinyl group. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.; Evidence: UniProtKB:G3XCV2, PMID:35105906enables UniProtKB:G3XCV2 — has_cofactor → CHEBI:47942; Covalently attached carrier-arm moiety; no free-cofactor consumption or inferred whole-protein count.; Evidence: UniProtKB:G3XCV2has cofactor UniProtKB:Q9HWG4 — has_cofactor → CHEBI:47942; Covalently attached carrier-arm moiety; no free-cofactor consumption or inferred whole-protein count.; Evidence: UniProtKB:Q9HWG4has cofactor UniProtKB:G3XCV2 — has_cofactor → CHEBI:18420; Direct bound-metal observation in the PAO1 PchE construct; no transfer of an MgATP assay condition to other proteins.; Evidence: PMID:35105906has cofactor MetaCyc:RXN-11113 — part_of → GO:0042864; Evidence: MetaCyc:PWY-6408, GO:0042864part of MetaCyc:RXN-11115 — part_of → GO:0042864; Evidence: MetaCyc:PWY-6408, GO:0042864part of MetaCyc:RXN-11117 — part_of → GO:0042864; Evidence: MetaCyc:PWY-6408, GO:0042864part of MetaCyc:RXN-11118 — part_of → GO:0042864; Evidence: MetaCyc:PWY-6408, GO:0042864part of MetaCyc:RXN-11120 — part_of → GO:0042864; Evidence: MetaCyc:PWY-6408, GO:0042864part of MetaCyc:RXN-11121 — part_of → GO:0042864; Evidence: MetaCyc:PWY-6408, GO:0042864part of MetaCyc:RXN-11122 — part_of → GO:0042864; Evidence: MetaCyc:PWY-6408, GO:0042864part of MetaCyc:RXN-11123 — part_of → GO:0042864; Evidence: MetaCyc:PWY-6408, GO:0042864part of MetaCyc:RXN-11125 — part_of → GO:0042864; Evidence: MetaCyc:PWY-6408, GO:0042864part of MetaCyc:RXN-19466 — part_of → GO:0042864; Evidence: MetaCyc:PWY-6408, GO:0042864part of MetaCyc:RXN-19469 — part_of → GO:0042864; Evidence: MetaCyc:PWY-6408, GO:0042864part of MetaCyc:RXN-11113 — provides_input_for → MetaCyc:RXN-19466; Evidence: MetaCyc:RXN-11113, MetaCyc:RXN-19466provides input for MetaCyc:RXN-11115 — provides_input_for → MetaCyc:RXN-11125; Evidence: MetaCyc:RXN-11115, MetaCyc:RXN-11125provides input for MetaCyc:RXN-11115 — provides_input_for → MetaCyc:RXN-11117; Evidence: MetaCyc:RXN-11115, MetaCyc:RXN-11117provides input for MetaCyc:RXN-19466 — provides_input_for → MetaCyc:RXN-19469; Evidence: MetaCyc:RXN-19466, MetaCyc:RXN-19469provides input for MetaCyc:RXN-11125 — provides_input_for → MetaCyc:RXN-19469; Evidence: MetaCyc:RXN-11125, MetaCyc:RXN-19469provides input for MetaCyc:RXN-19469 — provides_input_for → MetaCyc:RXN-11118; Evidence: MetaCyc:RXN-19469, MetaCyc:RXN-11118provides input for MetaCyc:RXN-11118 — provides_input_for → MetaCyc:RXN-11120; Evidence: MetaCyc:RXN-11118, MetaCyc:RXN-11120provides input for MetaCyc:RXN-11117 — provides_input_for → MetaCyc:RXN-11120; Evidence: MetaCyc:RXN-11117, MetaCyc:RXN-11120provides input for MetaCyc:RXN-11120 — provides_input_for → MetaCyc:RXN-11121; Evidence: MetaCyc:RXN-11120, MetaCyc:RXN-11121provides input for MetaCyc:RXN-11121 — provides_input_for → MetaCyc:RXN-11122; Evidence: MetaCyc:RXN-11121, MetaCyc:RXN-11122provides input for MetaCyc:RXN-11122 — provides_input_for → MetaCyc:RXN-11123; Evidence: MetaCyc:RXN-11122, MetaCyc:RXN-11123provides input for S-adenosyl-L-homocysteine zwitterion; CHEBI:57856; Declared type: small_molecule small molecule S-adenosyl-L-homocysteine zwitterion adenosine 5'-monophosphate(2-); CHEBI:456215; Declared type: small_molecule small molecule adenosine 5'-monophosphate(2-) ATP(4-); CHEBI:30616; Declared type: small_molecule small molecule ATP(4-) salicylate; CHEBI:30762; Declared type: small_molecule small molecule salicylate 2-hydroxybenzoyl-AMP(1-); CHEBI:86458; Declared type: small_molecule small molecule 2-hydroxybenzoyl-AMP(1-) L-cysteinyl-AMP zwitterion; CHEBI:144924; Declared type: small_molecule small molecule L-cysteinyl-AMP zwitterion pyochelin; MetaCyc:CPD-9992; Declared type: small_molecule small molecule pyochelin L-cysteine zwitterion; CHEBI:35235; Declared type: small_molecule small molecule L-cysteine zwitterion hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase]; MetaCyc:Hydroxyphenyl-bis-thiazolinyl-PchF; Declared type: chemical_entity chemical entity hydroxyphenyl-4,2-bis- thiazolinyl-[PchF non- ribosomal peptide synthase] an L-cysteinyl-[PchE non-ribosomal peptide synthase]; MetaCyc:L-cysteinyl-PchE; Declared type: chemical_entity chemical entity an L-cysteinyl-[PchE non- ribosomal peptide synthase] an L-cysteinyl-[PchF non-ribosomal peptide synthase]; MetaCyc:L-cysteinyl-PchF; Declared type: chemical_entity chemical entity an L-cysteinyl-[PchF non- ribosomal peptide synthase] N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase]; MetaCyc:N-desmethyl-pyochelin-PchF; Declared type: chemical_entity chemical entity N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] NADP(3-); CHEBI:58349; Declared type: small_molecule small molecule NADP(3-) NADPH(4-); CHEBI:57783; Declared type: small_molecule small molecule NADPH(4-) diphosphate(3-); CHEBI:33019; Declared type: small_molecule small molecule diphosphate(3-) hydron; CHEBI:15378; Declared type: small_molecule small molecule hydron a [PchE non-ribosomal peptide synthase]; MetaCyc:PchE; Declared type: chemical_entity chemical entity a [PchE non-ribosomal peptide synthase] a [PchF non-ribosomal peptide synthase protein]; MetaCyc:PchF; Declared type: chemical_entity chemical entity a [PchF non-ribosomal peptide synthase protein] pyochelinyl-[PchF non-ribosomal peptide synthase]; MetaCyc:Pyochelinyl-PchF; Declared type: chemical_entity chemical entity pyochelinyl-[PchF non- ribosomal peptide synthase] S-adenosyl-L-methionine zwitterion; CHEBI:59789; Declared type: small_molecule small molecule S-adenosyl-L-methionine zwitterion salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas]; MetaCyc:Salicyl-L-cysteinyl-PchE; Declared type: chemical_entity chemical entity salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] a salicyl-[PchE non-ribosomal peptide synthase]; MetaCyc:Salicyl-PchE; Declared type: chemical_entity chemical entity a salicyl-[PchE non- ribosomal peptide synthase] water; CHEBI:15377; Declared type: small_molecule small molecule water hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase]; MetaCyc:hydroxyphenyl-thiazolinyl-PchE; Declared type: chemical_entity chemical entity hydroxyphenyl- thiazolinyl-[PchE non- ribosomal peptide synthase] Pyochelin synthase PchD; UniProtKB:Q9HWG3; Declared type: protein protein Pyochelin synthase PchD Pyochelin synthetase PchE; UniProtKB:G3XCV2; Declared type: protein protein Pyochelin synthetase PchE Pyochelin synthetase PchF; UniProtKB:Q9HWG4; Declared type: protein protein Pyochelin synthetase PchF Pyochelin biosynthetic protein PchG; UniProtKB:Q9HWG5; Declared type: protein protein Pyochelin biosynthetic protein PchG magnesium(2+); CHEBI:18420; Declared type: cofactor cofactor magnesium(2+) pantetheine 4'-phosphate(2-); CHEBI:47942; Declared type: cofactor cofactor pantetheine 4'-phosphate(2-) salicylate + ATP + H+ -> (salicyl)adenylate + diphosphate; MetaCyc:RXN-11113; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity salicylate + ATP + H+ -> (salicyl)adenylate + diphosphate L-cysteine + ATP + H+ -> (L-cysteinyl)adenylate + diphosphate; MetaCyc:RXN-11115; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity L-cysteine + ATP + H+ -> (L-cysteinyl)adenylate + diphosphate (L-cysteinyl)adenylate + a [PchF non-ribosomal peptide synthase] -> an L-cysteinyl-[PchF non-ribosomal peptide synthase] + AMP + H+; MetaCyc:RXN-11117; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity (L-cysteinyl)adenylate + a [PchF non-ribosomal peptide synthase] -> an L-cysteinyl-[PchF non- ribosomal peptide synthase] + AMP + H+ salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] -> hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase] + H2O; MetaCyc:RXN-11118; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] -> hydroxyphenyl- thiazolinyl-[PchE non- ribosomal peptide synthase] + H2O an L-cysteinyl-[PchF non-ribosomal peptide synthase] + hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase] -> hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + a [PchE non-ribosomal peptide synthase] + H2O + H+; MetaCyc:RXN-11120; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity an L-cysteinyl-[PchF non- ribosomal peptide synthase] + hydroxyphenyl- thiazolinyl-[PchE non- ribosomal peptide synthase] -> hydroxyphenyl-4,2-bis- thiazolinyl-[PchF non- ribosomal peptide synthase] + a [PchE non-ribosomal peptide synthase] + H2O + H+ hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + NADPH + H+ -> N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] + NADP+; MetaCyc:RXN-11121; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity hydroxyphenyl-4,2-bis- thiazolinyl-[PchF non- ribosomal peptide synthase] + NADPH + H+ -> N-desmethyl- pyochelin-[PchF non- ribosomal peptide synthase] + NADP+ S-adenosyl-L-methionine + N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] -> pyochelinyl-[PchF non-ribosomal peptide synthase] + S-adenosyl-L-homocysteine + H+; MetaCyc:RXN-11122; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity S-adenosyl-L-methionine + N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] -> pyochelinyl-[PchF non- ribosomal peptide synthase] + S-adenosyl-L-homocysteine + H+ pyochelinyl-[PchF non-ribosomal peptide synthase] + H2O -> pyochelin + a [PchF non-ribosomal peptide synthase] + H+; MetaCyc:RXN-11123; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity pyochelinyl-[PchF non- ribosomal peptide synthase] + H2O -> pyochelin + a [PchF non-ribosomal peptide synthase] + H+ (L-cysteinyl)adenylate + a [PchE non-ribosomal peptide synthase] -> an L-cysteinyl-[PchE non-ribosomal peptide synthase] + AMP + H+; MetaCyc:RXN-11125; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity (L-cysteinyl)adenylate + a [PchE non-ribosomal peptide synthase] -> an L-cysteinyl-[PchE non- ribosomal peptide synthase] + AMP + H+ (salicyl)adenylate + a [PchE non-ribosomal peptide synthase] -> a salicyl-[PchE non-ribosomal peptide synthase] + AMP + H+; MetaCyc:RXN-19466; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity (salicyl)adenylate + a [PchE non-ribosomal peptide synthase] -> a salicyl-[PchE non-ribosomal peptide synthase] + AMP + H+ a salicyl-[PchE non-ribosomal peptide synthase] + an L-cysteinyl-[PchE non-ribosomal peptide synthase] -> salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] + a [PchE non-ribosomal peptide synthase] + H+; MetaCyc:RXN-19469; Declared type: molecular_activity; Source reaction direction: left_to_right molecular activity a salicyl-[PchE non- ribosomal peptide synthase] + an L-cysteinyl-[PchE non- ribosomal peptide synthase] -> salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] + a [PchE non- ribosomal peptide synthase] + H+ pyochelin biosynthetic process; GO:0042864; Declared type: pathway pathway pyochelin biosynthetic process

Components and activities

Declared biological components and source reaction directions
NodeKind or roleSource direction
Pseudomonas aeruginosa PAO1
NCBITaxon:208964
taxon
S-adenosyl-L-homocysteine zwitterion
CHEBI:57856
small molecule
adenosine 5'-monophosphate(2-)
CHEBI:456215
small molecule
ATP(4-)
CHEBI:30616
small molecule
salicylate
CHEBI:30762
small molecule
2-hydroxybenzoyl-AMP(1-)
CHEBI:86458
small molecule
L-cysteinyl-AMP zwitterion
CHEBI:144924
small molecule
pyochelin
MetaCyc:CPD-9992
small molecule
L-cysteine zwitterion
CHEBI:35235
small molecule
hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase]
MetaCyc:Hydroxyphenyl-bis-thiazolinyl-PchF
chemical entity
an L-cysteinyl-[PchE non-ribosomal peptide synthase]
MetaCyc:L-cysteinyl-PchE
chemical entity
an L-cysteinyl-[PchF non-ribosomal peptide synthase]
MetaCyc:L-cysteinyl-PchF
chemical entity
N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase]
MetaCyc:N-desmethyl-pyochelin-PchF
chemical entity
NADP(3-)
CHEBI:58349
small molecule
NADPH(4-)
CHEBI:57783
small molecule
diphosphate(3-)
CHEBI:33019
small molecule
hydron
CHEBI:15378
small molecule
a [PchE non-ribosomal peptide synthase]
MetaCyc:PchE
chemical entity
a [PchF non-ribosomal peptide synthase protein]
MetaCyc:PchF
chemical entity
pyochelinyl-[PchF non-ribosomal peptide synthase]
MetaCyc:Pyochelinyl-PchF
chemical entity
S-adenosyl-L-methionine zwitterion
CHEBI:59789
small molecule
salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas]
MetaCyc:Salicyl-L-cysteinyl-PchE
chemical entity
a salicyl-[PchE non-ribosomal peptide synthase]
MetaCyc:Salicyl-PchE
chemical entity
water
CHEBI:15377
small molecule
hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase]
MetaCyc:hydroxyphenyl-thiazolinyl-PchE
chemical entity
Pyochelin synthase PchD
UniProtKB:Q9HWG3
protein
Pyochelin synthetase PchE
UniProtKB:G3XCV2
protein
Pyochelin synthetase PchF
UniProtKB:Q9HWG4
protein
Pyochelin biosynthetic protein PchG
UniProtKB:Q9HWG5
protein
magnesium(2+)
CHEBI:18420
cofactor
pantetheine 4'-phosphate(2-)
CHEBI:47942
cofactor
salicylate + ATP + H+ -> (salicyl)adenylate + diphosphate
MetaCyc:RXN-11113
molecular activityleft to right
L-cysteine + ATP + H+ -> (L-cysteinyl)adenylate + diphosphate
MetaCyc:RXN-11115
molecular activityleft to right
(L-cysteinyl)adenylate + a [PchF non-ribosomal peptide synthase] -> an L-cysteinyl-[PchF non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-11117
molecular activityleft to right
salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] -> hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase] + H2O
MetaCyc:RXN-11118
molecular activityleft to right
an L-cysteinyl-[PchF non-ribosomal peptide synthase] + hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase] -> hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + a [PchE non-ribosomal peptide synthase] + H2O + H+
MetaCyc:RXN-11120
molecular activityleft to right
hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + NADPH + H+ -> N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] + NADP+
MetaCyc:RXN-11121
molecular activityleft to right
S-adenosyl-L-methionine + N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] -> pyochelinyl-[PchF non-ribosomal peptide synthase] + S-adenosyl-L-homocysteine + H+
MetaCyc:RXN-11122
molecular activityleft to right
pyochelinyl-[PchF non-ribosomal peptide synthase] + H2O -> pyochelin + a [PchF non-ribosomal peptide synthase] + H+
MetaCyc:RXN-11123
molecular activityleft to right
(L-cysteinyl)adenylate + a [PchE non-ribosomal peptide synthase] -> an L-cysteinyl-[PchE non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-11125
molecular activityleft to right
(salicyl)adenylate + a [PchE non-ribosomal peptide synthase] -> a salicyl-[PchE non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-19466
molecular activityleft to right
a salicyl-[PchE non-ribosomal peptide synthase] + an L-cysteinyl-[PchE non-ribosomal peptide synthase] -> salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] + a [PchE non-ribosomal peptide synthase] + H+
MetaCyc:RXN-19469
molecular activityleft to right

Mechanistic edges

Mechanistic edges and their cited evidence
SubjectPredicate and descriptionObjectEvidence
hydron
CHEBI:15378
consumes

salicylate + ATP + H+ -> (salicyl)adenylate + diphosphate
MetaCyc:RXN-11113
  • MetaCyc:RXN-11113

    Source assertion: The native left side explicitly contains PROTON with coefficient 1; direction is LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11113"]/left[*/@frameid="PROTON"]; reaction-direction
  • MetaCyc:PROTON

    Source assertion: The original PROTON structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:15378.

    Source locationptools-xml/Compound[@frameid="PROTON"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:15378

    Source assertion: CHEBI:15378 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:15378; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
salicylate
CHEBI:30762
consumes

salicylate + ATP + H+ -> (salicyl)adenylate + diphosphate
MetaCyc:RXN-11113
  • MetaCyc:RXN-11113

    Source assertion: The native left side explicitly contains CPD-110 with coefficient 1; direction is LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11113"]/left[*/@frameid="CPD-110"]; reaction-direction
  • MetaCyc:CPD-110

    Source assertion: The original CPD-110 structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:30762.

    Source locationptools-xml/Compound[@frameid="CPD-110"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:30762

    Source assertion: CHEBI:30762 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:30762; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
ATP(4-)
CHEBI:30616
consumes

salicylate + ATP + H+ -> (salicyl)adenylate + diphosphate
MetaCyc:RXN-11113
  • MetaCyc:RXN-11113

    Source assertion: The native left side explicitly contains ATP with coefficient 1; direction is LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11113"]/left[*/@frameid="ATP"]; reaction-direction
  • MetaCyc:ATP

    Source assertion: The original ATP structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:30616.

    Source locationptools-xml/Compound[@frameid="ATP"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:30616

    Source assertion: CHEBI:30616 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:30616; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
salicylate + ATP + H+ -> (salicyl)adenylate + diphosphate
MetaCyc:RXN-11113
produces

2-hydroxybenzoyl-AMP(1-)
CHEBI:86458
  • MetaCyc:RXN-11113

    Source assertion: The native right side explicitly contains CPD-12084 with coefficient 1; direction is LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11113"]/right[*/@frameid="CPD-12084"]; reaction-direction
  • MetaCyc:CPD-12084

    Source assertion: The original CPD-12084 structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:86458.

    Source locationptools-xml/Compound[@frameid="CPD-12084"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:86458

    Source assertion: CHEBI:86458 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:86458; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
salicylate + ATP + H+ -> (salicyl)adenylate + diphosphate
MetaCyc:RXN-11113
produces

diphosphate(3-)
CHEBI:33019
  • MetaCyc:RXN-11113

    Source assertion: The native right side explicitly contains PPI with coefficient 1; direction is LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11113"]/right[*/@frameid="PPI"]; reaction-direction
  • MetaCyc:PPI

    Source assertion: The original PPI structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:33019.

    Source locationptools-xml/Compound[@frameid="PPI"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:33019

    Source assertion: CHEBI:33019 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:33019; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
L-cysteine zwitterion
CHEBI:35235
consumes

L-cysteine + ATP + H+ -> (L-cysteinyl)adenylate + diphosphate
MetaCyc:RXN-11115
  • MetaCyc:RXN-11115

    Source assertion: The native left side explicitly contains CYS with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11115"]/left[*/@frameid="CYS"]; reaction-direction
  • MetaCyc:CYS

    Source assertion: The original CYS structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:35235.

    Source locationptools-xml/Compound[@frameid="CYS"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:35235

    Source assertion: CHEBI:35235 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:35235; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
ATP(4-)
CHEBI:30616
consumes

L-cysteine + ATP + H+ -> (L-cysteinyl)adenylate + diphosphate
MetaCyc:RXN-11115
  • MetaCyc:RXN-11115

    Source assertion: The native left side explicitly contains ATP with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11115"]/left[*/@frameid="ATP"]; reaction-direction
  • MetaCyc:ATP

    Source assertion: The original ATP structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:30616.

    Source locationptools-xml/Compound[@frameid="ATP"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:30616

    Source assertion: CHEBI:30616 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:30616; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
hydron
CHEBI:15378
consumes

L-cysteine + ATP + H+ -> (L-cysteinyl)adenylate + diphosphate
MetaCyc:RXN-11115
  • MetaCyc:RXN-11115

    Source assertion: The native left side explicitly contains PROTON with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11115"]/left[*/@frameid="PROTON"]; reaction-direction
  • MetaCyc:PROTON

    Source assertion: The original PROTON structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:15378.

    Source locationptools-xml/Compound[@frameid="PROTON"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:15378

    Source assertion: CHEBI:15378 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:15378; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
L-cysteine + ATP + H+ -> (L-cysteinyl)adenylate + diphosphate
MetaCyc:RXN-11115
produces

L-cysteinyl-AMP zwitterion
CHEBI:144924
  • MetaCyc:RXN-11115

    Source assertion: The native right side explicitly contains CPD-12085 with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11115"]/right[*/@frameid="CPD-12085"]; reaction-direction
  • MetaCyc:CPD-12085

    Source assertion: The original CPD-12085 structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:144924.

    Source locationptools-xml/Compound[@frameid="CPD-12085"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:144924

    Source assertion: CHEBI:144924 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:144924; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
L-cysteine + ATP + H+ -> (L-cysteinyl)adenylate + diphosphate
MetaCyc:RXN-11115
produces

diphosphate(3-)
CHEBI:33019
  • MetaCyc:RXN-11115

    Source assertion: The native right side explicitly contains PPI with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11115"]/right[*/@frameid="PPI"]; reaction-direction
  • MetaCyc:PPI

    Source assertion: The original PPI structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:33019.

    Source locationptools-xml/Compound[@frameid="PPI"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:33019

    Source assertion: CHEBI:33019 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:33019; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
L-cysteinyl-AMP zwitterion
CHEBI:144924
consumes

(L-cysteinyl)adenylate + a [PchF non-ribosomal peptide synthase] -> an L-cysteinyl-[PchF non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-11117
  • MetaCyc:RXN-11117

    Source assertion: The native left side explicitly contains CPD-12085 with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11117"]/left[*/@frameid="CPD-12085"]; reaction-direction
  • MetaCyc:CPD-12085

    Source assertion: The original CPD-12085 structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:144924.

    Source locationptools-xml/Compound[@frameid="CPD-12085"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:144924

    Source assertion: CHEBI:144924 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:144924; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
a [PchF non-ribosomal peptide synthase protein]
MetaCyc:PchF
consumes

Native PchF reactive-domain state; coefficient is not an enzyme assembly count.

(L-cysteinyl)adenylate + a [PchF non-ribosomal peptide synthase] -> an L-cysteinyl-[PchF non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-11117
  • MetaCyc:RXN-11117

    Source assertion: The native left side explicitly contains PchF with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11117"]/left[*/@frameid="PchF"]; reaction-direction
  • MetaCyc:PchF

    Source assertion: The original frame explicitly declares a Protein class and names its carrier acyl state; it supplies no full protein sequence or atom-complete carrier structure.

    Source locationptools-xml/Protein[@frameid="PchF"]/common-name; @class
  • DOI:10.1038/s41467-022-28284-x

    Source assertion: The original assembly diagram distinguishes the PchE ArCP and PCP sites and the PchF carrier site with covalent phosphopantetheine-tethered intermediates. Reactive-site accounting must not be read as whole-polypeptide coefficients.

    Source locationOriginal supplement PDF page2, Supplementary Figure1c; page3, Supplementary Figure2
(L-cysteinyl)adenylate + a [PchF non-ribosomal peptide synthase] -> an L-cysteinyl-[PchF non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-11117
produces

Native PchF reactive-domain state; coefficient is not an enzyme assembly count.

an L-cysteinyl-[PchF non-ribosomal peptide synthase]
MetaCyc:L-cysteinyl-PchF
  • MetaCyc:RXN-11117

    Source assertion: The native right side explicitly contains L-cysteinyl-PchF with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11117"]/right[*/@frameid="L-cysteinyl-PchF"]; reaction-direction
  • MetaCyc:L-cysteinyl-PchF

    Source assertion: The original frame explicitly declares a Protein class and names its carrier acyl state; it supplies no full protein sequence or atom-complete carrier structure.

    Source locationptools-xml/Protein[@frameid="L-cysteinyl-PchF"]/common-name; @class
  • DOI:10.1038/s41467-022-28284-x

    Source assertion: The original assembly diagram distinguishes the PchE ArCP and PCP sites and the PchF carrier site with covalent phosphopantetheine-tethered intermediates. Reactive-site accounting must not be read as whole-polypeptide coefficients.

    Source locationOriginal supplement PDF page2, Supplementary Figure1c; page3, Supplementary Figure2
(L-cysteinyl)adenylate + a [PchF non-ribosomal peptide synthase] -> an L-cysteinyl-[PchF non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-11117
produces

adenosine 5'-monophosphate(2-)
CHEBI:456215
  • MetaCyc:RXN-11117

    Source assertion: The native right side explicitly contains AMP with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11117"]/right[*/@frameid="AMP"]; reaction-direction
  • MetaCyc:AMP

    Source assertion: The original AMP structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:456215.

    Source locationptools-xml/Compound[@frameid="AMP"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:456215

    Source assertion: CHEBI:456215 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:456215; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
(L-cysteinyl)adenylate + a [PchF non-ribosomal peptide synthase] -> an L-cysteinyl-[PchF non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-11117
produces

hydron
CHEBI:15378
  • MetaCyc:RXN-11117

    Source assertion: The native right side explicitly contains PROTON with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11117"]/right[*/@frameid="PROTON"]; reaction-direction
  • MetaCyc:PROTON

    Source assertion: The original PROTON structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:15378.

    Source locationptools-xml/Compound[@frameid="PROTON"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:15378

    Source assertion: CHEBI:15378 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:15378; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas]
MetaCyc:Salicyl-L-cysteinyl-PchE
consumes

Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.

salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] -> hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase] + H2O
MetaCyc:RXN-11118
  • MetaCyc:RXN-11118

    Source assertion: The native left side explicitly contains Salicyl-L-cysteinyl-PchE with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11118"]/left[*/@frameid="Salicyl-L-cysteinyl-PchE"]; reaction-direction
  • MetaCyc:Salicyl-L-cysteinyl-PchE

    Source assertion: The original frame explicitly declares a Protein class and names its carrier acyl state; it supplies no full protein sequence or atom-complete carrier structure.

    Source locationptools-xml/Protein[@frameid="Salicyl-L-cysteinyl-PchE"]/common-name; @class
  • DOI:10.1038/s41467-022-28284-x

    Source assertion: The original assembly diagram distinguishes the PchE ArCP and PCP sites and the PchF carrier site with covalent phosphopantetheine-tethered intermediates. Reactive-site accounting must not be read as whole-polypeptide coefficients.

    Source locationOriginal supplement PDF page2, Supplementary Figure1c; page3, Supplementary Figure2
salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] -> hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase] + H2O
MetaCyc:RXN-11118
produces

Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.

hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase]
MetaCyc:hydroxyphenyl-thiazolinyl-PchE
  • MetaCyc:RXN-11118

    Source assertion: The native right side explicitly contains hydroxyphenyl-thiazolinyl-PchE with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11118"]/right[*/@frameid="hydroxyphenyl-thiazolinyl-PchE"]; reaction-direction
  • MetaCyc:hydroxyphenyl-thiazolinyl-PchE

    Source assertion: The original frame explicitly declares a Protein class and names its carrier acyl state; it supplies no full protein sequence or atom-complete carrier structure.

    Source locationptools-xml/Protein[@frameid="hydroxyphenyl-thiazolinyl-PchE"]/common-name; @class
  • DOI:10.1038/s41467-022-28284-x

    Source assertion: The original assembly diagram distinguishes the PchE ArCP and PCP sites and the PchF carrier site with covalent phosphopantetheine-tethered intermediates. Reactive-site accounting must not be read as whole-polypeptide coefficients.

    Source locationOriginal supplement PDF page2, Supplementary Figure1c; page3, Supplementary Figure2
salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] -> hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase] + H2O
MetaCyc:RXN-11118
produces

water
CHEBI:15377
  • MetaCyc:RXN-11118

    Source assertion: The native right side explicitly contains WATER with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11118"]/right[*/@frameid="WATER"]; reaction-direction
  • MetaCyc:WATER

    Source assertion: The original WATER structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:15377.

    Source locationptools-xml/Compound[@frameid="WATER"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:15377

    Source assertion: CHEBI:15377 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:15377; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
an L-cysteinyl-[PchF non-ribosomal peptide synthase]
MetaCyc:L-cysteinyl-PchF
consumes

Native PchF reactive-domain state; coefficient is not an enzyme assembly count.

an L-cysteinyl-[PchF non-ribosomal peptide synthase] + hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase] -> hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + a [PchE non-ribosomal peptide synthase] + H2O + H+
MetaCyc:RXN-11120
  • MetaCyc:RXN-11120

    Source assertion: The native left side explicitly contains L-cysteinyl-PchF with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11120"]/left[*/@frameid="L-cysteinyl-PchF"]; reaction-direction
  • MetaCyc:L-cysteinyl-PchF

    Source assertion: The original frame explicitly declares a Protein class and names its carrier acyl state; it supplies no full protein sequence or atom-complete carrier structure.

    Source locationptools-xml/Protein[@frameid="L-cysteinyl-PchF"]/common-name; @class
  • DOI:10.1038/s41467-022-28284-x

    Source assertion: The original assembly diagram distinguishes the PchE ArCP and PCP sites and the PchF carrier site with covalent phosphopantetheine-tethered intermediates. Reactive-site accounting must not be read as whole-polypeptide coefficients.

    Source locationOriginal supplement PDF page2, Supplementary Figure1c; page3, Supplementary Figure2
hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase]
MetaCyc:hydroxyphenyl-thiazolinyl-PchE
consumes

Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.

an L-cysteinyl-[PchF non-ribosomal peptide synthase] + hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase] -> hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + a [PchE non-ribosomal peptide synthase] + H2O + H+
MetaCyc:RXN-11120
  • MetaCyc:RXN-11120

    Source assertion: The native left side explicitly contains hydroxyphenyl-thiazolinyl-PchE with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11120"]/left[*/@frameid="hydroxyphenyl-thiazolinyl-PchE"]; reaction-direction
  • MetaCyc:hydroxyphenyl-thiazolinyl-PchE

    Source assertion: The original frame explicitly declares a Protein class and names its carrier acyl state; it supplies no full protein sequence or atom-complete carrier structure.

    Source locationptools-xml/Protein[@frameid="hydroxyphenyl-thiazolinyl-PchE"]/common-name; @class
  • DOI:10.1038/s41467-022-28284-x

    Source assertion: The original assembly diagram distinguishes the PchE ArCP and PCP sites and the PchF carrier site with covalent phosphopantetheine-tethered intermediates. Reactive-site accounting must not be read as whole-polypeptide coefficients.

    Source locationOriginal supplement PDF page2, Supplementary Figure1c; page3, Supplementary Figure2
an L-cysteinyl-[PchF non-ribosomal peptide synthase] + hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase] -> hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + a [PchE non-ribosomal peptide synthase] + H2O + H+
MetaCyc:RXN-11120
produces

Native PchF reactive-domain state; coefficient is not an enzyme assembly count.

hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase]
MetaCyc:Hydroxyphenyl-bis-thiazolinyl-PchF
  • MetaCyc:RXN-11120

    Source assertion: The native right side explicitly contains Hydroxyphenyl-bis-thiazolinyl-PchF with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11120"]/right[*/@frameid="Hydroxyphenyl-bis-thiazolinyl-PchF"]; reaction-direction
  • MetaCyc:Hydroxyphenyl-bis-thiazolinyl-PchF

    Source assertion: The original frame explicitly declares a Protein class and names its carrier acyl state; it supplies no full protein sequence or atom-complete carrier structure.

    Source locationptools-xml/Protein[@frameid="Hydroxyphenyl-bis-thiazolinyl-PchF"]/common-name; @class
  • DOI:10.1038/s41467-022-28284-x

    Source assertion: The original assembly diagram distinguishes the PchE ArCP and PCP sites and the PchF carrier site with covalent phosphopantetheine-tethered intermediates. Reactive-site accounting must not be read as whole-polypeptide coefficients.

    Source locationOriginal supplement PDF page2, Supplementary Figure1c; page3, Supplementary Figure2
an L-cysteinyl-[PchF non-ribosomal peptide synthase] + hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase] -> hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + a [PchE non-ribosomal peptide synthase] + H2O + H+
MetaCyc:RXN-11120
produces

water
CHEBI:15377
  • MetaCyc:RXN-11120

    Source assertion: The native right side explicitly contains WATER with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11120"]/right[*/@frameid="WATER"]; reaction-direction
  • MetaCyc:WATER

    Source assertion: The original WATER structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:15377.

    Source locationptools-xml/Compound[@frameid="WATER"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:15377

    Source assertion: CHEBI:15377 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:15377; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
an L-cysteinyl-[PchF non-ribosomal peptide synthase] + hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase] -> hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + a [PchE non-ribosomal peptide synthase] + H2O + H+
MetaCyc:RXN-11120
produces

Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.

a [PchE non-ribosomal peptide synthase]
MetaCyc:PchE
  • MetaCyc:RXN-11120

    Source assertion: The native right side explicitly contains PchE with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11120"]/right[*/@frameid="PchE"]; reaction-direction
  • MetaCyc:PchE

    Source assertion: The original frame explicitly declares a Protein class and names its carrier acyl state; it supplies no full protein sequence or atom-complete carrier structure.

    Source locationptools-xml/Protein[@frameid="PchE"]/common-name; @class
  • DOI:10.1038/s41467-022-28284-x

    Source assertion: The original assembly diagram distinguishes the PchE ArCP and PCP sites and the PchF carrier site with covalent phosphopantetheine-tethered intermediates. Reactive-site accounting must not be read as whole-polypeptide coefficients.

    Source locationOriginal supplement PDF page2, Supplementary Figure1c; page3, Supplementary Figure2
an L-cysteinyl-[PchF non-ribosomal peptide synthase] + hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase] -> hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + a [PchE non-ribosomal peptide synthase] + H2O + H+
MetaCyc:RXN-11120
produces

hydron
CHEBI:15378
  • MetaCyc:RXN-11120

    Source assertion: The native right side explicitly contains PROTON with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11120"]/right[*/@frameid="PROTON"]; reaction-direction
  • MetaCyc:PROTON

    Source assertion: The original PROTON structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:15378.

    Source locationptools-xml/Compound[@frameid="PROTON"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:15378

    Source assertion: CHEBI:15378 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:15378; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase]
MetaCyc:Hydroxyphenyl-bis-thiazolinyl-PchF
consumes

Native PchF reactive-domain state; coefficient is not an enzyme assembly count.

hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + NADPH + H+ -> N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] + NADP+
MetaCyc:RXN-11121
  • MetaCyc:RXN-11121

    Source assertion: The native left side explicitly contains Hydroxyphenyl-bis-thiazolinyl-PchF with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11121"]/left[*/@frameid="Hydroxyphenyl-bis-thiazolinyl-PchF"]; reaction-direction
  • MetaCyc:Hydroxyphenyl-bis-thiazolinyl-PchF

    Source assertion: The original frame explicitly declares a Protein class and names its carrier acyl state; it supplies no full protein sequence or atom-complete carrier structure.

    Source locationptools-xml/Protein[@frameid="Hydroxyphenyl-bis-thiazolinyl-PchF"]/common-name; @class
  • DOI:10.1038/s41467-022-28284-x

    Source assertion: The original assembly diagram distinguishes the PchE ArCP and PCP sites and the PchF carrier site with covalent phosphopantetheine-tethered intermediates. Reactive-site accounting must not be read as whole-polypeptide coefficients.

    Source locationOriginal supplement PDF page2, Supplementary Figure1c; page3, Supplementary Figure2
NADPH(4-)
CHEBI:57783
consumes

hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + NADPH + H+ -> N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] + NADP+
MetaCyc:RXN-11121
  • MetaCyc:RXN-11121

    Source assertion: The native left side explicitly contains NADPH with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11121"]/left[*/@frameid="NADPH"]; reaction-direction
  • MetaCyc:NADPH

    Source assertion: The original NADPH structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:57783.

    Source locationptools-xml/Compound[@frameid="NADPH"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:57783

    Source assertion: CHEBI:57783 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:57783; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
hydron
CHEBI:15378
consumes

hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + NADPH + H+ -> N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] + NADP+
MetaCyc:RXN-11121
  • MetaCyc:RXN-11121

    Source assertion: The native left side explicitly contains PROTON with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11121"]/left[*/@frameid="PROTON"]; reaction-direction
  • MetaCyc:PROTON

    Source assertion: The original PROTON structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:15378.

    Source locationptools-xml/Compound[@frameid="PROTON"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:15378

    Source assertion: CHEBI:15378 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:15378; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + NADPH + H+ -> N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] + NADP+
MetaCyc:RXN-11121
produces

Native PchF reactive-domain state; coefficient is not an enzyme assembly count.

N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase]
MetaCyc:N-desmethyl-pyochelin-PchF
  • MetaCyc:RXN-11121

    Source assertion: The native right side explicitly contains N-desmethyl-pyochelin-PchF with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11121"]/right[*/@frameid="N-desmethyl-pyochelin-PchF"]; reaction-direction
  • MetaCyc:N-desmethyl-pyochelin-PchF

    Source assertion: The original frame explicitly declares a Protein class and names its carrier acyl state; it supplies no full protein sequence or atom-complete carrier structure.

    Source locationptools-xml/Protein[@frameid="N-desmethyl-pyochelin-PchF"]/common-name; @class
  • DOI:10.1038/s41467-022-28284-x

    Source assertion: The original assembly diagram distinguishes the PchE ArCP and PCP sites and the PchF carrier site with covalent phosphopantetheine-tethered intermediates. Reactive-site accounting must not be read as whole-polypeptide coefficients.

    Source locationOriginal supplement PDF page2, Supplementary Figure1c; page3, Supplementary Figure2
hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + NADPH + H+ -> N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] + NADP+
MetaCyc:RXN-11121
produces

NADP(3-)
CHEBI:58349
  • MetaCyc:RXN-11121

    Source assertion: The native right side explicitly contains NADP with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11121"]/right[*/@frameid="NADP"]; reaction-direction
  • MetaCyc:NADP

    Source assertion: The original NADP structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:58349.

    Source locationptools-xml/Compound[@frameid="NADP"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:58349

    Source assertion: CHEBI:58349 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:58349; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
S-adenosyl-L-methionine zwitterion
CHEBI:59789
consumes

S-adenosyl-L-methionine + N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] -> pyochelinyl-[PchF non-ribosomal peptide synthase] + S-adenosyl-L-homocysteine + H+
MetaCyc:RXN-11122
  • MetaCyc:RXN-11122

    Source assertion: The native left side explicitly contains S-ADENOSYLMETHIONINE with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11122"]/left[*/@frameid="S-ADENOSYLMETHIONINE"]; reaction-direction
  • MetaCyc:S-ADENOSYLMETHIONINE

    Source assertion: The original S-ADENOSYLMETHIONINE structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:59789.

    Source locationptools-xml/Compound[@frameid="S-ADENOSYLMETHIONINE"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:59789

    Source assertion: CHEBI:59789 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:59789; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase]
MetaCyc:N-desmethyl-pyochelin-PchF
consumes

Native PchF reactive-domain state; coefficient is not an enzyme assembly count.

S-adenosyl-L-methionine + N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] -> pyochelinyl-[PchF non-ribosomal peptide synthase] + S-adenosyl-L-homocysteine + H+
MetaCyc:RXN-11122
  • MetaCyc:RXN-11122

    Source assertion: The native left side explicitly contains N-desmethyl-pyochelin-PchF with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11122"]/left[*/@frameid="N-desmethyl-pyochelin-PchF"]; reaction-direction
  • MetaCyc:N-desmethyl-pyochelin-PchF

    Source assertion: The original frame explicitly declares a Protein class and names its carrier acyl state; it supplies no full protein sequence or atom-complete carrier structure.

    Source locationptools-xml/Protein[@frameid="N-desmethyl-pyochelin-PchF"]/common-name; @class
  • DOI:10.1038/s41467-022-28284-x

    Source assertion: The original assembly diagram distinguishes the PchE ArCP and PCP sites and the PchF carrier site with covalent phosphopantetheine-tethered intermediates. Reactive-site accounting must not be read as whole-polypeptide coefficients.

    Source locationOriginal supplement PDF page2, Supplementary Figure1c; page3, Supplementary Figure2
S-adenosyl-L-methionine + N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] -> pyochelinyl-[PchF non-ribosomal peptide synthase] + S-adenosyl-L-homocysteine + H+
MetaCyc:RXN-11122
produces

Native PchF reactive-domain state; coefficient is not an enzyme assembly count.

pyochelinyl-[PchF non-ribosomal peptide synthase]
MetaCyc:Pyochelinyl-PchF
  • MetaCyc:RXN-11122

    Source assertion: The native right side explicitly contains Pyochelinyl-PchF with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11122"]/right[*/@frameid="Pyochelinyl-PchF"]; reaction-direction
  • MetaCyc:Pyochelinyl-PchF

    Source assertion: The original frame explicitly declares a Protein class and names its carrier acyl state; it supplies no full protein sequence or atom-complete carrier structure.

    Source locationptools-xml/Protein[@frameid="Pyochelinyl-PchF"]/common-name; @class
  • DOI:10.1038/s41467-022-28284-x

    Source assertion: The original assembly diagram distinguishes the PchE ArCP and PCP sites and the PchF carrier site with covalent phosphopantetheine-tethered intermediates. Reactive-site accounting must not be read as whole-polypeptide coefficients.

    Source locationOriginal supplement PDF page2, Supplementary Figure1c; page3, Supplementary Figure2
S-adenosyl-L-methionine + N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] -> pyochelinyl-[PchF non-ribosomal peptide synthase] + S-adenosyl-L-homocysteine + H+
MetaCyc:RXN-11122
produces

S-adenosyl-L-homocysteine zwitterion
CHEBI:57856
  • MetaCyc:RXN-11122

    Source assertion: The native right side explicitly contains ADENOSYL-HOMO-CYS with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11122"]/right[*/@frameid="ADENOSYL-HOMO-CYS"]; reaction-direction
  • MetaCyc:ADENOSYL-HOMO-CYS

    Source assertion: The original ADENOSYL-HOMO-CYS structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:57856.

    Source locationptools-xml/Compound[@frameid="ADENOSYL-HOMO-CYS"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:57856

    Source assertion: CHEBI:57856 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:57856; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
S-adenosyl-L-methionine + N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] -> pyochelinyl-[PchF non-ribosomal peptide synthase] + S-adenosyl-L-homocysteine + H+
MetaCyc:RXN-11122
produces

hydron
CHEBI:15378
  • MetaCyc:RXN-11122

    Source assertion: The native right side explicitly contains PROTON with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11122"]/right[*/@frameid="PROTON"]; reaction-direction
  • MetaCyc:PROTON

    Source assertion: The original PROTON structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:15378.

    Source locationptools-xml/Compound[@frameid="PROTON"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:15378

    Source assertion: CHEBI:15378 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:15378; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
pyochelinyl-[PchF non-ribosomal peptide synthase]
MetaCyc:Pyochelinyl-PchF
consumes

Native PchF reactive-domain state; coefficient is not an enzyme assembly count.

pyochelinyl-[PchF non-ribosomal peptide synthase] + H2O -> pyochelin + a [PchF non-ribosomal peptide synthase] + H+
MetaCyc:RXN-11123
  • MetaCyc:RXN-11123

    Source assertion: The native left side explicitly contains Pyochelinyl-PchF with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11123"]/left[*/@frameid="Pyochelinyl-PchF"]; reaction-direction
  • MetaCyc:Pyochelinyl-PchF

    Source assertion: The original frame explicitly declares a Protein class and names its carrier acyl state; it supplies no full protein sequence or atom-complete carrier structure.

    Source locationptools-xml/Protein[@frameid="Pyochelinyl-PchF"]/common-name; @class
  • DOI:10.1038/s41467-022-28284-x

    Source assertion: The original assembly diagram distinguishes the PchE ArCP and PCP sites and the PchF carrier site with covalent phosphopantetheine-tethered intermediates. Reactive-site accounting must not be read as whole-polypeptide coefficients.

    Source locationOriginal supplement PDF page2, Supplementary Figure1c; page3, Supplementary Figure2
water
CHEBI:15377
consumes

pyochelinyl-[PchF non-ribosomal peptide synthase] + H2O -> pyochelin + a [PchF non-ribosomal peptide synthase] + H+
MetaCyc:RXN-11123
  • MetaCyc:RXN-11123

    Source assertion: The native left side explicitly contains WATER with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11123"]/left[*/@frameid="WATER"]; reaction-direction
  • MetaCyc:WATER

    Source assertion: The original WATER structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:15377.

    Source locationptools-xml/Compound[@frameid="WATER"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:15377

    Source assertion: CHEBI:15377 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:15377; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
pyochelinyl-[PchF non-ribosomal peptide synthase] + H2O -> pyochelin + a [PchF non-ribosomal peptide synthase] + H+
MetaCyc:RXN-11123
produces

Formal native pyochelin I monoanion endpoint; no exclusive-I physiological product or I-selective release claim.

pyochelin
MetaCyc:CPD-9992
  • MetaCyc:RXN-11123

    Source assertion: The native right side explicitly contains CPD-9992 with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11123"]/right[*/@frameid="CPD-9992"]; reaction-direction
  • MetaCyc:CPD-9992

    Source assertion: The issued CPD-9992 InChI has the monoanion layer /p-1 and the stereochemical layers /t9-,10+,13-/m1/s1. The structure alone does not establish physiological product ratios or enzyme release selectivity.

    Source locationptools-xml/Compound[@frameid="CPD-9992"]/inchi; /p-1 and /t9-,10+,13-/m1/s1
  • CHEBI:67183

    Source assertion: ChEBI names this neutral structure pyochelin I. Its connectivity and stereochemical InChI layers match native CPD-9992 after removing /p-1; this independently derived I assignment is protonation-normalized, not exact charge equivalence.

    Source location/name; /chemical_data/charge; /default_structure/standard_inchi; explicit comparison with CPD-9992 /inchi after removal of /p-1
  • PMID:17938167

    Source assertion: P. aeruginosa produces pyochelin I and II, differing at the interconverting thioaminal center; this does not establish I-selective release.

    Source locationresponseWrapper/resultList/result[id="17938167"]/abstractText
pyochelinyl-[PchF non-ribosomal peptide synthase] + H2O -> pyochelin + a [PchF non-ribosomal peptide synthase] + H+
MetaCyc:RXN-11123
produces

Native PchF reactive-domain state; coefficient is not an enzyme assembly count.

a [PchF non-ribosomal peptide synthase protein]
MetaCyc:PchF
  • MetaCyc:RXN-11123

    Source assertion: The native right side explicitly contains PchF with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11123"]/right[*/@frameid="PchF"]; reaction-direction
  • MetaCyc:PchF

    Source assertion: The original frame explicitly declares a Protein class and names its carrier acyl state; it supplies no full protein sequence or atom-complete carrier structure.

    Source locationptools-xml/Protein[@frameid="PchF"]/common-name; @class
  • DOI:10.1038/s41467-022-28284-x

    Source assertion: The original assembly diagram distinguishes the PchE ArCP and PCP sites and the PchF carrier site with covalent phosphopantetheine-tethered intermediates. Reactive-site accounting must not be read as whole-polypeptide coefficients.

    Source locationOriginal supplement PDF page2, Supplementary Figure1c; page3, Supplementary Figure2
pyochelinyl-[PchF non-ribosomal peptide synthase] + H2O -> pyochelin + a [PchF non-ribosomal peptide synthase] + H+
MetaCyc:RXN-11123
produces

hydron
CHEBI:15378
  • MetaCyc:RXN-11123

    Source assertion: The native right side explicitly contains PROTON with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11123"]/right[*/@frameid="PROTON"]; reaction-direction
  • MetaCyc:PROTON

    Source assertion: The original PROTON structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:15378.

    Source locationptools-xml/Compound[@frameid="PROTON"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:15378

    Source assertion: CHEBI:15378 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:15378; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
L-cysteinyl-AMP zwitterion
CHEBI:144924
consumes

(L-cysteinyl)adenylate + a [PchE non-ribosomal peptide synthase] -> an L-cysteinyl-[PchE non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-11125
  • MetaCyc:RXN-11125

    Source assertion: The native left side explicitly contains CPD-12085 with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11125"]/left[*/@frameid="CPD-12085"]; reaction-direction
  • MetaCyc:CPD-12085

    Source assertion: The original CPD-12085 structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:144924.

    Source locationptools-xml/Compound[@frameid="CPD-12085"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:144924

    Source assertion: CHEBI:144924 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:144924; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
a [PchE non-ribosomal peptide synthase]
MetaCyc:PchE
consumes

Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.

(L-cysteinyl)adenylate + a [PchE non-ribosomal peptide synthase] -> an L-cysteinyl-[PchE non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-11125
  • MetaCyc:RXN-11125

    Source assertion: The native left side explicitly contains PchE with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11125"]/left[*/@frameid="PchE"]; reaction-direction
  • MetaCyc:PchE

    Source assertion: The original frame explicitly declares a Protein class and names its carrier acyl state; it supplies no full protein sequence or atom-complete carrier structure.

    Source locationptools-xml/Protein[@frameid="PchE"]/common-name; @class
  • DOI:10.1038/s41467-022-28284-x

    Source assertion: The original assembly diagram distinguishes the PchE ArCP and PCP sites and the PchF carrier site with covalent phosphopantetheine-tethered intermediates. Reactive-site accounting must not be read as whole-polypeptide coefficients.

    Source locationOriginal supplement PDF page2, Supplementary Figure1c; page3, Supplementary Figure2
(L-cysteinyl)adenylate + a [PchE non-ribosomal peptide synthase] -> an L-cysteinyl-[PchE non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-11125
produces

Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.

an L-cysteinyl-[PchE non-ribosomal peptide synthase]
MetaCyc:L-cysteinyl-PchE
  • MetaCyc:RXN-11125

    Source assertion: The native right side explicitly contains L-cysteinyl-PchE with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11125"]/right[*/@frameid="L-cysteinyl-PchE"]; reaction-direction
  • MetaCyc:L-cysteinyl-PchE

    Source assertion: The original frame explicitly declares a Protein class and names its carrier acyl state; it supplies no full protein sequence or atom-complete carrier structure.

    Source locationptools-xml/Protein[@frameid="L-cysteinyl-PchE"]/common-name; @class
  • DOI:10.1038/s41467-022-28284-x

    Source assertion: The original assembly diagram distinguishes the PchE ArCP and PCP sites and the PchF carrier site with covalent phosphopantetheine-tethered intermediates. Reactive-site accounting must not be read as whole-polypeptide coefficients.

    Source locationOriginal supplement PDF page2, Supplementary Figure1c; page3, Supplementary Figure2
(L-cysteinyl)adenylate + a [PchE non-ribosomal peptide synthase] -> an L-cysteinyl-[PchE non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-11125
produces

adenosine 5'-monophosphate(2-)
CHEBI:456215
  • MetaCyc:RXN-11125

    Source assertion: The native right side explicitly contains AMP with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11125"]/right[*/@frameid="AMP"]; reaction-direction
  • MetaCyc:AMP

    Source assertion: The original AMP structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:456215.

    Source locationptools-xml/Compound[@frameid="AMP"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:456215

    Source assertion: CHEBI:456215 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:456215; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
(L-cysteinyl)adenylate + a [PchE non-ribosomal peptide synthase] -> an L-cysteinyl-[PchE non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-11125
produces

hydron
CHEBI:15378
  • MetaCyc:RXN-11125

    Source assertion: The native right side explicitly contains PROTON with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-11125"]/right[*/@frameid="PROTON"]; reaction-direction
  • MetaCyc:PROTON

    Source assertion: The original PROTON structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:15378.

    Source locationptools-xml/Compound[@frameid="PROTON"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:15378

    Source assertion: CHEBI:15378 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:15378; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
2-hydroxybenzoyl-AMP(1-)
CHEBI:86458
consumes

(salicyl)adenylate + a [PchE non-ribosomal peptide synthase] -> a salicyl-[PchE non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-19466
  • MetaCyc:RXN-19466

    Source assertion: The native left side explicitly contains CPD-12084 with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-19466"]/left[*/@frameid="CPD-12084"]; reaction-direction
  • MetaCyc:CPD-12084

    Source assertion: The original CPD-12084 structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:86458.

    Source locationptools-xml/Compound[@frameid="CPD-12084"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:86458

    Source assertion: CHEBI:86458 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:86458; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
a [PchE non-ribosomal peptide synthase]
MetaCyc:PchE
consumes

Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.

(salicyl)adenylate + a [PchE non-ribosomal peptide synthase] -> a salicyl-[PchE non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-19466
  • MetaCyc:RXN-19466

    Source assertion: The native left side explicitly contains PchE with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-19466"]/left[*/@frameid="PchE"]; reaction-direction
  • MetaCyc:PchE

    Source assertion: The original frame explicitly declares a Protein class and names its carrier acyl state; it supplies no full protein sequence or atom-complete carrier structure.

    Source locationptools-xml/Protein[@frameid="PchE"]/common-name; @class
  • DOI:10.1038/s41467-022-28284-x

    Source assertion: The original assembly diagram distinguishes the PchE ArCP and PCP sites and the PchF carrier site with covalent phosphopantetheine-tethered intermediates. Reactive-site accounting must not be read as whole-polypeptide coefficients.

    Source locationOriginal supplement PDF page2, Supplementary Figure1c; page3, Supplementary Figure2
(salicyl)adenylate + a [PchE non-ribosomal peptide synthase] -> a salicyl-[PchE non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-19466
produces

Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.

a salicyl-[PchE non-ribosomal peptide synthase]
MetaCyc:Salicyl-PchE
  • MetaCyc:RXN-19466

    Source assertion: The native right side explicitly contains Salicyl-PchE with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-19466"]/right[*/@frameid="Salicyl-PchE"]; reaction-direction
  • MetaCyc:Salicyl-PchE

    Source assertion: The original frame explicitly declares a Protein class and names its carrier acyl state; it supplies no full protein sequence or atom-complete carrier structure.

    Source locationptools-xml/Protein[@frameid="Salicyl-PchE"]/common-name; @class
  • DOI:10.1038/s41467-022-28284-x

    Source assertion: The original assembly diagram distinguishes the PchE ArCP and PCP sites and the PchF carrier site with covalent phosphopantetheine-tethered intermediates. Reactive-site accounting must not be read as whole-polypeptide coefficients.

    Source locationOriginal supplement PDF page2, Supplementary Figure1c; page3, Supplementary Figure2
(salicyl)adenylate + a [PchE non-ribosomal peptide synthase] -> a salicyl-[PchE non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-19466
produces

adenosine 5'-monophosphate(2-)
CHEBI:456215
  • MetaCyc:RXN-19466

    Source assertion: The native right side explicitly contains AMP with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-19466"]/right[*/@frameid="AMP"]; reaction-direction
  • MetaCyc:AMP

    Source assertion: The original AMP structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:456215.

    Source locationptools-xml/Compound[@frameid="AMP"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:456215

    Source assertion: CHEBI:456215 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:456215; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
(salicyl)adenylate + a [PchE non-ribosomal peptide synthase] -> a salicyl-[PchE non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-19466
produces

hydron
CHEBI:15378
  • MetaCyc:RXN-19466

    Source assertion: The native right side explicitly contains PROTON with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-19466"]/right[*/@frameid="PROTON"]; reaction-direction
  • MetaCyc:PROTON

    Source assertion: The original PROTON structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:15378.

    Source locationptools-xml/Compound[@frameid="PROTON"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:15378

    Source assertion: CHEBI:15378 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:15378; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
a salicyl-[PchE non-ribosomal peptide synthase]
MetaCyc:Salicyl-PchE
consumes

Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.

a salicyl-[PchE non-ribosomal peptide synthase] + an L-cysteinyl-[PchE non-ribosomal peptide synthase] -> salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] + a [PchE non-ribosomal peptide synthase] + H+
MetaCyc:RXN-19469
  • MetaCyc:RXN-19469

    Source assertion: The native left side explicitly contains Salicyl-PchE with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-19469"]/left[*/@frameid="Salicyl-PchE"]; reaction-direction
  • MetaCyc:Salicyl-PchE

    Source assertion: The original frame explicitly declares a Protein class and names its carrier acyl state; it supplies no full protein sequence or atom-complete carrier structure.

    Source locationptools-xml/Protein[@frameid="Salicyl-PchE"]/common-name; @class
  • DOI:10.1038/s41467-022-28284-x

    Source assertion: The original assembly diagram distinguishes the PchE ArCP and PCP sites and the PchF carrier site with covalent phosphopantetheine-tethered intermediates. Reactive-site accounting must not be read as whole-polypeptide coefficients.

    Source locationOriginal supplement PDF page2, Supplementary Figure1c; page3, Supplementary Figure2
an L-cysteinyl-[PchE non-ribosomal peptide synthase]
MetaCyc:L-cysteinyl-PchE
consumes

Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.

a salicyl-[PchE non-ribosomal peptide synthase] + an L-cysteinyl-[PchE non-ribosomal peptide synthase] -> salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] + a [PchE non-ribosomal peptide synthase] + H+
MetaCyc:RXN-19469
  • MetaCyc:RXN-19469

    Source assertion: The native left side explicitly contains L-cysteinyl-PchE with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-19469"]/left[*/@frameid="L-cysteinyl-PchE"]; reaction-direction
  • MetaCyc:L-cysteinyl-PchE

    Source assertion: The original frame explicitly declares a Protein class and names its carrier acyl state; it supplies no full protein sequence or atom-complete carrier structure.

    Source locationptools-xml/Protein[@frameid="L-cysteinyl-PchE"]/common-name; @class
  • DOI:10.1038/s41467-022-28284-x

    Source assertion: The original assembly diagram distinguishes the PchE ArCP and PCP sites and the PchF carrier site with covalent phosphopantetheine-tethered intermediates. Reactive-site accounting must not be read as whole-polypeptide coefficients.

    Source locationOriginal supplement PDF page2, Supplementary Figure1c; page3, Supplementary Figure2
a salicyl-[PchE non-ribosomal peptide synthase] + an L-cysteinyl-[PchE non-ribosomal peptide synthase] -> salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] + a [PchE non-ribosomal peptide synthase] + H+
MetaCyc:RXN-19469
produces

Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.

salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas]
MetaCyc:Salicyl-L-cysteinyl-PchE
  • MetaCyc:RXN-19469

    Source assertion: The native right side explicitly contains Salicyl-L-cysteinyl-PchE with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-19469"]/right[*/@frameid="Salicyl-L-cysteinyl-PchE"]; reaction-direction
  • MetaCyc:Salicyl-L-cysteinyl-PchE

    Source assertion: The original frame explicitly declares a Protein class and names its carrier acyl state; it supplies no full protein sequence or atom-complete carrier structure.

    Source locationptools-xml/Protein[@frameid="Salicyl-L-cysteinyl-PchE"]/common-name; @class
  • DOI:10.1038/s41467-022-28284-x

    Source assertion: The original assembly diagram distinguishes the PchE ArCP and PCP sites and the PchF carrier site with covalent phosphopantetheine-tethered intermediates. Reactive-site accounting must not be read as whole-polypeptide coefficients.

    Source locationOriginal supplement PDF page2, Supplementary Figure1c; page3, Supplementary Figure2
a salicyl-[PchE non-ribosomal peptide synthase] + an L-cysteinyl-[PchE non-ribosomal peptide synthase] -> salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] + a [PchE non-ribosomal peptide synthase] + H+
MetaCyc:RXN-19469
produces

Native reactive-domain class; PchE aryl and peptidyl sites are separate reaction sites on the same polypeptide.

a [PchE non-ribosomal peptide synthase]
MetaCyc:PchE
  • MetaCyc:RXN-19469

    Source assertion: The native right side explicitly contains PchE with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-19469"]/right[*/@frameid="PchE"]; reaction-direction
  • MetaCyc:PchE

    Source assertion: The original frame explicitly declares a Protein class and names its carrier acyl state; it supplies no full protein sequence or atom-complete carrier structure.

    Source locationptools-xml/Protein[@frameid="PchE"]/common-name; @class
  • DOI:10.1038/s41467-022-28284-x

    Source assertion: The original assembly diagram distinguishes the PchE ArCP and PCP sites and the PchF carrier site with covalent phosphopantetheine-tethered intermediates. Reactive-site accounting must not be read as whole-polypeptide coefficients.

    Source locationOriginal supplement PDF page2, Supplementary Figure1c; page3, Supplementary Figure2
a salicyl-[PchE non-ribosomal peptide synthase] + an L-cysteinyl-[PchE non-ribosomal peptide synthase] -> salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] + a [PchE non-ribosomal peptide synthase] + H+
MetaCyc:RXN-19469
produces

hydron
CHEBI:15378
  • MetaCyc:RXN-19469

    Source assertion: The native right side explicitly contains PROTON with coefficient 1; direction is PHYSIOL-LEFT-TO-RIGHT.

    Source locationptools-xml/Reaction[@frameid="RXN-19469"]/right[*/@frameid="PROTON"]; reaction-direction
  • MetaCyc:PROTON

    Source assertion: The original PROTON structure defines the chemical form selected for this side; its InChI and charged atoms were compared with CHEBI:15378.

    Source locationptools-xml/Compound[@frameid="PROTON"]/inchi; cml/molecule/atomArray/atom/@formalCharge
  • CHEBI:15378

    Source assertion: CHEBI:15378 supplies the matching structure, formula and charge. Zwitterionic forms preserve the native amino/carboxyl charges where present.

    Source locationSemantic SQL statements subject=CHEBI:15378; chemrof:inchi_string, chemrof:charge, chemrof:generalized_empirical_formula
Pyochelin synthase PchD
UniProtKB:Q9HWG3
enables

PchD adenylates salicylate before transfer to the PchE aryl carrier site. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.

salicylate + ATP + H+ -> (salicyl)adenylate + diphosphate
MetaCyc:RXN-11113
  • UniProtKB:Q9HWG3

    Source assertion: Current PAO1 identity and functional annotation support this gene-product role. Detailed PchD and PchE/F steps include ECO:0000250 or ECO:0000305 inference; this is not a claim of purified monomer sufficiency.

    Source location/results/3/primaryAccession; /results/3/organism/taxonId; /results/3/comments/0; /results/3/sequence/value
  • PMID:35105906

    Source assertion: PchD adenylates salicylate before transfer to the PchE aryl carrier site. The inspected work uses PAO1 genes and observes dimeric PchE; the functional relation does not assert a stable four-protein complex.

    Source locationarticle/body//sec[@id="Sec1"]; sec[@id="Sec4"] and sec[@id="Sec5"]; Methods article/body//sec[@id="Sec9"]
Pyochelin synthetase PchE
UniProtKB:G3XCV2
enables

The PchE and PchF adenylation domains each activate a cysteine; one native reaction object is reused twice. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.

L-cysteine + ATP + H+ -> (L-cysteinyl)adenylate + diphosphate
MetaCyc:RXN-11115
  • UniProtKB:G3XCV2

    Source assertion: Current PAO1 identity and functional annotation support this gene-product role. Detailed PchD and PchE/F steps include ECO:0000250 or ECO:0000305 inference; this is not a claim of purified monomer sufficiency.

    Source location/results/1/primaryAccession; /results/1/organism/taxonId; /results/1/comments/0; /results/1/sequence/value
  • PMID:35105906

    Source assertion: The PchE and PchF adenylation domains each activate a cysteine; one native reaction object is reused twice. The inspected work uses PAO1 genes and observes dimeric PchE; the functional relation does not assert a stable four-protein complex.

    Source locationarticle/body//sec[@id="Sec1"]; sec[@id="Sec4"] and sec[@id="Sec5"]; Methods article/body//sec[@id="Sec9"]
Pyochelin synthetase PchF
UniProtKB:Q9HWG4
enables

The PchE and PchF adenylation domains each activate a cysteine; one native reaction object is reused twice. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.

L-cysteine + ATP + H+ -> (L-cysteinyl)adenylate + diphosphate
MetaCyc:RXN-11115
  • UniProtKB:Q9HWG4

    Source assertion: Current PAO1 identity and functional annotation support this gene-product role. Detailed PchD and PchE/F steps include ECO:0000250 or ECO:0000305 inference; this is not a claim of purified monomer sufficiency.

    Source location/results/2/primaryAccession; /results/2/organism/taxonId; /results/2/comments/0; /results/2/sequence/value
  • PMID:30525512

    Source assertion: The PchE and PchF adenylation domains each activate a cysteine; one native reaction object is reused twice. The study names O85740 and uses PAO1 constructs; detailed methylation tests use analogues, not complete thiotemplate steady-state turnover.

    Source locationcollection/document/passage[offset="9139" or offset="9446" or offset="41012" or offset="53276" or offset="65484"]/text
  • PMID:11467965

    Source assertion: Four-protein reconstitution assigns terminal reduction to PchG and methylation/release to PchF. Only the original indexed abstract was retained; no fixed DEFG heterotetramer follows.

    Source locationresponseWrapper/resultList/result[id="11467965"]/abstractText
Pyochelin synthetase PchF
UniProtKB:Q9HWG4
enables

PchF loads its activated cysteine onto its carrier site. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.

(L-cysteinyl)adenylate + a [PchF non-ribosomal peptide synthase] -> an L-cysteinyl-[PchF non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-11117
  • UniProtKB:Q9HWG4

    Source assertion: Current PAO1 identity and functional annotation support this gene-product role. Detailed PchD and PchE/F steps include ECO:0000250 or ECO:0000305 inference; this is not a claim of purified monomer sufficiency.

    Source location/results/2/primaryAccession; /results/2/organism/taxonId; /results/2/comments/0; /results/2/sequence/value
  • PMID:30525512

    Source assertion: PchF loads its activated cysteine onto its carrier site. The study names O85740 and uses PAO1 constructs; detailed methylation tests use analogues, not complete thiotemplate steady-state turnover.

    Source locationcollection/document/passage[offset="9139" or offset="9446" or offset="41012" or offset="53276" or offset="65484"]/text
  • PMID:11467965

    Source assertion: Four-protein reconstitution assigns terminal reduction to PchG and methylation/release to PchF. Only the original indexed abstract was retained; no fixed DEFG heterotetramer follows.

    Source locationresponseWrapper/resultList/result[id="11467965"]/abstractText
Pyochelin synthetase PchE
UniProtKB:G3XCV2
enables

PchE performs first-ring cyclization with epimerization after amide formation. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.

salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] -> hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase] + H2O
MetaCyc:RXN-11118
  • UniProtKB:G3XCV2

    Source assertion: Current PAO1 identity and functional annotation support this gene-product role. Detailed PchD and PchE/F steps include ECO:0000250 or ECO:0000305 inference; this is not a claim of purified monomer sufficiency.

    Source location/results/1/primaryAccession; /results/1/organism/taxonId; /results/1/comments/0; /results/1/sequence/value
  • PMID:35105906

    Source assertion: PchE performs first-ring cyclization with epimerization after amide formation. The inspected work uses PAO1 genes and observes dimeric PchE; the functional relation does not assert a stable four-protein complex.

    Source locationarticle/body//sec[@id="Sec1"]; sec[@id="Sec4"] and sec[@id="Sec5"]; Methods article/body//sec[@id="Sec9"]
  • PMID:12950179

    Source assertion: Epimerization was detected after amide formation rather than on simple cysteinyl-S-PchE; the native ring-forming object compresses these coupled events.

    Source locationresponseWrapper/resultList/result[id="12950179"]/abstractText
Pyochelin synthetase PchF
UniProtKB:Q9HWG4
enables

PchF accepts the PchE-bound intermediate, condenses the second cysteine and forms the second thiazoline. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.

an L-cysteinyl-[PchF non-ribosomal peptide synthase] + hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase] -> hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + a [PchE non-ribosomal peptide synthase] + H2O + H+
MetaCyc:RXN-11120
  • UniProtKB:Q9HWG4

    Source assertion: Current PAO1 identity and functional annotation support this gene-product role. Detailed PchD and PchE/F steps include ECO:0000250 or ECO:0000305 inference; this is not a claim of purified monomer sufficiency.

    Source location/results/2/primaryAccession; /results/2/organism/taxonId; /results/2/comments/0; /results/2/sequence/value
  • PMID:30525512

    Source assertion: PchF accepts the PchE-bound intermediate, condenses the second cysteine and forms the second thiazoline. The study names O85740 and uses PAO1 constructs; detailed methylation tests use analogues, not complete thiotemplate steady-state turnover.

    Source locationcollection/document/passage[offset="9139" or offset="9446" or offset="41012" or offset="53276" or offset="65484"]/text
  • PMID:11467965

    Source assertion: Four-protein reconstitution assigns terminal reduction to PchG and methylation/release to PchF. Only the original indexed abstract was retained; no fixed DEFG heterotetramer follows.

    Source locationresponseWrapper/resultList/result[id="11467965"]/abstractText
Pyochelin biosynthetic protein PchG
UniProtKB:Q9HWG5
enables

PchG reduces the PchF-tethered terminal thiazoline using NADPH. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.

hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + NADPH + H+ -> N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] + NADP+
MetaCyc:RXN-11121
  • UniProtKB:Q9HWG5

    Source assertion: The current unreviewed PAO1 entry identifies PchG; the biochemical assignment is supported separately by original PAO1 evidence.

    Source location/results/5/primaryAccession; /results/5/organism/taxonId; /results/5/proteinDescription; /results/5/sequence/value
  • PMID:11467965

    Source assertion: Purified PchG reduces the hydroxyphenylbisthiazoline-S-PchF acyl enzyme with NADPH during complete reconstitution. Only the original indexed abstract was retained; historical construct scope is distinct from exact current PAO1 sequence identity.

    Source locationresponseWrapper/resultList/result[id="11467965"]/abstractText
  • PMID:11208777

    Source assertion: P. aeruginosa genetics and biochemical reconstitution establish the PchG requirement for pyochelin synthesis, separately from the current unreviewed sequence annotation.

    Source locationresponseWrapper/resultList/result[id="11208777"]/abstractText
  • PMID:27601130

    Source assertion: PAO1-derived PchG reduces an oxidized free analogue with NADPH; the authors caution that this is a poor model for full physiological carrier-substrate kinetics and stereochemistry.

    Source locationcollection/document/passage[offset="4948" or offset="34049"]/text; Results, Enzymatic Activity
Pyochelin synthetase PchF
UniProtKB:Q9HWG4
enables

PchF methylates the reduced terminal nitrogen with SAM. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.

S-adenosyl-L-methionine + N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] -> pyochelinyl-[PchF non-ribosomal peptide synthase] + S-adenosyl-L-homocysteine + H+
MetaCyc:RXN-11122
  • UniProtKB:Q9HWG4

    Source assertion: The current entry identifies Q9HWG4 as PAO1 PchF and supplies its sequence. This identity evidence does not independently assign methylation or mature-product hydrolysis; those roles are supported by separate primary evidence.

    Source location/results/2/primaryAccession; /results/2/genes/0/geneName/value; /results/2/organism/taxonId; /results/2/sequence/value
  • PMID:30525512

    Source assertion: PchF methylates the reduced terminal nitrogen with SAM. The study names O85740 and uses PAO1 constructs; detailed methylation tests use analogues, not complete thiotemplate steady-state turnover.

    Source locationcollection/document/passage[offset="9139" or offset="9446" or offset="41012" or offset="53276" or offset="65484"]/text
  • PMID:11467965

    Source assertion: Four-protein reconstitution assigns terminal reduction to PchG and methylation/release to PchF. Only the original indexed abstract was retained; no fixed DEFG heterotetramer follows.

    Source locationresponseWrapper/resultList/result[id="11467965"]/abstractText
Pyochelin synthetase PchF
UniProtKB:Q9HWG4
enables

PchF releases pyochelin by thioester hydrolysis; the native I structure is a formal projection of the observed I/II products. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.

pyochelinyl-[PchF non-ribosomal peptide synthase] + H2O -> pyochelin + a [PchF non-ribosomal peptide synthase] + H+
MetaCyc:RXN-11123
  • UniProtKB:Q9HWG4

    Source assertion: The current entry identifies Q9HWG4 as PAO1 PchF and supplies its sequence. This identity evidence does not independently assign methylation or mature-product hydrolysis; those roles are supported by separate primary evidence.

    Source location/results/2/primaryAccession; /results/2/genes/0/geneName/value; /results/2/organism/taxonId; /results/2/sequence/value
  • PMID:30525512

    Source assertion: PchF releases pyochelin by thioester hydrolysis. The study names O85740 and uses PAO1 constructs; detailed methylation tests use analogues, not complete thiotemplate steady-state turnover.

    Source locationcollection/document/passage[offset="9139" or offset="9446" or offset="41012" or offset="53276" or offset="65484"]/text
  • PMID:11467965

    Source assertion: Four-protein reconstitution assigns terminal reduction to PchG and methylation/release to PchF. Only the original indexed abstract was retained; no fixed DEFG heterotetramer follows.

    Source locationresponseWrapper/resultList/result[id="11467965"]/abstractText
Pyochelin synthetase PchE
UniProtKB:G3XCV2
enables

PchE loads cysteine onto its peptidyl carrier site. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.

(L-cysteinyl)adenylate + a [PchE non-ribosomal peptide synthase] -> an L-cysteinyl-[PchE non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-11125
  • UniProtKB:G3XCV2

    Source assertion: Current PAO1 identity and functional annotation support this gene-product role. Detailed PchD and PchE/F steps include ECO:0000250 or ECO:0000305 inference; this is not a claim of purified monomer sufficiency.

    Source location/results/1/primaryAccession; /results/1/organism/taxonId; /results/1/comments/0; /results/1/sequence/value
  • PMID:35105906

    Source assertion: PchE loads cysteine onto its peptidyl carrier site. The inspected work uses PAO1 genes and observes dimeric PchE; the functional relation does not assert a stable four-protein complex.

    Source locationarticle/body//sec[@id="Sec1"]; sec[@id="Sec4"] and sec[@id="Sec5"]; Methods article/body//sec[@id="Sec9"]
Pyochelin synthase PchD
UniProtKB:Q9HWG3
enables

PchD transfers activated salicylate to the PchE aryl carrier site. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.

(salicyl)adenylate + a [PchE non-ribosomal peptide synthase] -> a salicyl-[PchE non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-19466
  • UniProtKB:Q9HWG3

    Source assertion: Current PAO1 identity and functional annotation support this gene-product role. Detailed PchD and PchE/F steps include ECO:0000250 or ECO:0000305 inference; this is not a claim of purified monomer sufficiency.

    Source location/results/3/primaryAccession; /results/3/organism/taxonId; /results/3/comments/0; /results/3/sequence/value
  • PMID:35105906

    Source assertion: PchD transfers activated salicylate to the PchE aryl carrier site. The inspected work uses PAO1 genes and observes dimeric PchE; the functional relation does not assert a stable four-protein complex.

    Source locationarticle/body//sec[@id="Sec1"]; sec[@id="Sec4"] and sec[@id="Sec5"]; Methods article/body//sec[@id="Sec9"]
Pyochelin synthetase PchE
UniProtKB:G3XCV2
enables

PchE condenses its aryl-site salicyl group with its peptidyl-site cysteinyl group. Functional gene-product relation; no monomer sufficiency or stable PchDEFG assembly is asserted.

a salicyl-[PchE non-ribosomal peptide synthase] + an L-cysteinyl-[PchE non-ribosomal peptide synthase] -> salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] + a [PchE non-ribosomal peptide synthase] + H+
MetaCyc:RXN-19469
  • UniProtKB:G3XCV2

    Source assertion: Current PAO1 identity and functional annotation support this gene-product role. Detailed PchD and PchE/F steps include ECO:0000250 or ECO:0000305 inference; this is not a claim of purified monomer sufficiency.

    Source location/results/1/primaryAccession; /results/1/organism/taxonId; /results/1/comments/0; /results/1/sequence/value
  • PMID:35105906

    Source assertion: PchE condenses its aryl-site salicyl group with its peptidyl-site cysteinyl group. The inspected work uses PAO1 genes and observes dimeric PchE; the functional relation does not assert a stable four-protein complex.

    Source locationarticle/body//sec[@id="Sec1"]; sec[@id="Sec4"] and sec[@id="Sec5"]; Methods article/body//sec[@id="Sec9"]
Pyochelin synthetase PchE
UniProtKB:G3XCV2
has_cofactor

Covalently attached carrier-arm moiety; no free-cofactor consumption or inferred whole-protein count.

pantetheine 4'-phosphate(2-)
CHEBI:47942
  • UniProtKB:G3XCV2

    Source assertion: The entry assigns pantetheine 4'-phosphate as a cofactor with ECO:0000305. In this pathway its covalently attached arm carries intermediates; it is not a free stoichiometric substrate.

    Source location/results/1/comments/2/cofactors/0; cofactorCrossReference/id=CHEBI:47942
Pyochelin synthetase PchF
UniProtKB:Q9HWG4
has_cofactor

Covalently attached carrier-arm moiety; no free-cofactor consumption or inferred whole-protein count.

pantetheine 4'-phosphate(2-)
CHEBI:47942
  • UniProtKB:Q9HWG4

    Source assertion: The entry assigns pantetheine 4'-phosphate as a cofactor with ECO:0000305. In this pathway its covalently attached arm carries intermediates; it is not a free stoichiometric substrate.

    Source location/results/2/comments/2/cofactors/0; cofactorCrossReference/id=CHEBI:47942
Pyochelin synthetase PchE
UniProtKB:G3XCV2
has_cofactor

Direct bound-metal observation in the PAO1 PchE construct; no transfer of an MgATP assay condition to other proteins.

magnesium(2+)
CHEBI:18420
  • PMID:35105906

    Source assertion: Cryo-EM structures directly place Mg2+ with cysteinyl-AMP in the PchE A-domain pocket. This supports bound magnesium in the inspected PAO1 construct, without a universal metal-dependence or stoichiometric claim.

    Source locationarticle/body//sec[@id="Sec5"]/p describing cysteinyl-AMP and Mg2+; Figure 3b
salicylate + ATP + H+ -> (salicyl)adenylate + diphosphate
MetaCyc:RXN-11113
part_of

GO:0042864
  • MetaCyc:PWY-6408

    Source assertion: The complete native reaction-list contains RXN-11113; the selected scope begins at salicylate and retains all eleven listed reaction objects.

    Source locationptools-xml/Pathway[@frameid="PWY-6408"]/reaction-list/Reaction[@frameid="RXN-11113"]
  • GO:0042864

    Source assertion: The active GO process denotes chemical reactions and pathways forming pyochelin; this record describes the complete native salicylate-dependent implementation.

    Source location/results/0/id; /results/0/isObsolete; /results/0/definition/text
L-cysteine + ATP + H+ -> (L-cysteinyl)adenylate + diphosphate
MetaCyc:RXN-11115
part_of

GO:0042864
  • MetaCyc:PWY-6408

    Source assertion: The complete native reaction-list contains RXN-11115; the selected scope begins at salicylate and retains all eleven listed reaction objects.

    Source locationptools-xml/Pathway[@frameid="PWY-6408"]/reaction-list/Reaction[@frameid="RXN-11115"]
  • GO:0042864

    Source assertion: The active GO process denotes chemical reactions and pathways forming pyochelin; this record describes the complete native salicylate-dependent implementation.

    Source location/results/0/id; /results/0/isObsolete; /results/0/definition/text
(L-cysteinyl)adenylate + a [PchF non-ribosomal peptide synthase] -> an L-cysteinyl-[PchF non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-11117
part_of

GO:0042864
  • MetaCyc:PWY-6408

    Source assertion: The complete native reaction-list contains RXN-11117; the selected scope begins at salicylate and retains all eleven listed reaction objects.

    Source locationptools-xml/Pathway[@frameid="PWY-6408"]/reaction-list/Reaction[@frameid="RXN-11117"]
  • GO:0042864

    Source assertion: The active GO process denotes chemical reactions and pathways forming pyochelin; this record describes the complete native salicylate-dependent implementation.

    Source location/results/0/id; /results/0/isObsolete; /results/0/definition/text
salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] -> hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase] + H2O
MetaCyc:RXN-11118
part_of

GO:0042864
  • MetaCyc:PWY-6408

    Source assertion: The complete native reaction-list contains RXN-11118; the selected scope begins at salicylate and retains all eleven listed reaction objects.

    Source locationptools-xml/Pathway[@frameid="PWY-6408"]/reaction-list/Reaction[@frameid="RXN-11118"]
  • GO:0042864

    Source assertion: The active GO process denotes chemical reactions and pathways forming pyochelin; this record describes the complete native salicylate-dependent implementation.

    Source location/results/0/id; /results/0/isObsolete; /results/0/definition/text
an L-cysteinyl-[PchF non-ribosomal peptide synthase] + hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase] -> hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + a [PchE non-ribosomal peptide synthase] + H2O + H+
MetaCyc:RXN-11120
part_of

GO:0042864
  • MetaCyc:PWY-6408

    Source assertion: The complete native reaction-list contains RXN-11120; the selected scope begins at salicylate and retains all eleven listed reaction objects.

    Source locationptools-xml/Pathway[@frameid="PWY-6408"]/reaction-list/Reaction[@frameid="RXN-11120"]
  • GO:0042864

    Source assertion: The active GO process denotes chemical reactions and pathways forming pyochelin; this record describes the complete native salicylate-dependent implementation.

    Source location/results/0/id; /results/0/isObsolete; /results/0/definition/text
hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + NADPH + H+ -> N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] + NADP+
MetaCyc:RXN-11121
part_of

GO:0042864
  • MetaCyc:PWY-6408

    Source assertion: The complete native reaction-list contains RXN-11121; the selected scope begins at salicylate and retains all eleven listed reaction objects.

    Source locationptools-xml/Pathway[@frameid="PWY-6408"]/reaction-list/Reaction[@frameid="RXN-11121"]
  • GO:0042864

    Source assertion: The active GO process denotes chemical reactions and pathways forming pyochelin; this record describes the complete native salicylate-dependent implementation.

    Source location/results/0/id; /results/0/isObsolete; /results/0/definition/text
S-adenosyl-L-methionine + N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] -> pyochelinyl-[PchF non-ribosomal peptide synthase] + S-adenosyl-L-homocysteine + H+
MetaCyc:RXN-11122
part_of

GO:0042864
  • MetaCyc:PWY-6408

    Source assertion: The complete native reaction-list contains RXN-11122; the selected scope begins at salicylate and retains all eleven listed reaction objects.

    Source locationptools-xml/Pathway[@frameid="PWY-6408"]/reaction-list/Reaction[@frameid="RXN-11122"]
  • GO:0042864

    Source assertion: The active GO process denotes chemical reactions and pathways forming pyochelin; this record describes the complete native salicylate-dependent implementation.

    Source location/results/0/id; /results/0/isObsolete; /results/0/definition/text
pyochelinyl-[PchF non-ribosomal peptide synthase] + H2O -> pyochelin + a [PchF non-ribosomal peptide synthase] + H+
MetaCyc:RXN-11123
part_of

GO:0042864
  • MetaCyc:PWY-6408

    Source assertion: The complete native reaction-list contains RXN-11123; the selected scope begins at salicylate and retains all eleven listed reaction objects.

    Source locationptools-xml/Pathway[@frameid="PWY-6408"]/reaction-list/Reaction[@frameid="RXN-11123"]
  • GO:0042864

    Source assertion: The active GO process denotes chemical reactions and pathways forming pyochelin; this record describes the complete native salicylate-dependent implementation.

    Source location/results/0/id; /results/0/isObsolete; /results/0/definition/text
(L-cysteinyl)adenylate + a [PchE non-ribosomal peptide synthase] -> an L-cysteinyl-[PchE non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-11125
part_of

GO:0042864
  • MetaCyc:PWY-6408

    Source assertion: The complete native reaction-list contains RXN-11125; the selected scope begins at salicylate and retains all eleven listed reaction objects.

    Source locationptools-xml/Pathway[@frameid="PWY-6408"]/reaction-list/Reaction[@frameid="RXN-11125"]
  • GO:0042864

    Source assertion: The active GO process denotes chemical reactions and pathways forming pyochelin; this record describes the complete native salicylate-dependent implementation.

    Source location/results/0/id; /results/0/isObsolete; /results/0/definition/text
(salicyl)adenylate + a [PchE non-ribosomal peptide synthase] -> a salicyl-[PchE non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-19466
part_of

GO:0042864
  • MetaCyc:PWY-6408

    Source assertion: The complete native reaction-list contains RXN-19466; the selected scope begins at salicylate and retains all eleven listed reaction objects.

    Source locationptools-xml/Pathway[@frameid="PWY-6408"]/reaction-list/Reaction[@frameid="RXN-19466"]
  • GO:0042864

    Source assertion: The active GO process denotes chemical reactions and pathways forming pyochelin; this record describes the complete native salicylate-dependent implementation.

    Source location/results/0/id; /results/0/isObsolete; /results/0/definition/text
a salicyl-[PchE non-ribosomal peptide synthase] + an L-cysteinyl-[PchE non-ribosomal peptide synthase] -> salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] + a [PchE non-ribosomal peptide synthase] + H+
MetaCyc:RXN-19469
part_of

GO:0042864
  • MetaCyc:PWY-6408

    Source assertion: The complete native reaction-list contains RXN-19469; the selected scope begins at salicylate and retains all eleven listed reaction objects.

    Source locationptools-xml/Pathway[@frameid="PWY-6408"]/reaction-list/Reaction[@frameid="RXN-19469"]
  • GO:0042864

    Source assertion: The active GO process denotes chemical reactions and pathways forming pyochelin; this record describes the complete native salicylate-dependent implementation.

    Source location/results/0/id; /results/0/isObsolete; /results/0/definition/text
salicylate + ATP + H+ -> (salicyl)adenylate + diphosphate
MetaCyc:RXN-11113
provides_input_for

(salicyl)adenylate + a [PchE non-ribosomal peptide synthase] -> a salicyl-[PchE non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-19466
  • MetaCyc:RXN-11113

    Source assertion: The original product side contains CPD-12084; the subsequent reaction consumes that same source-native intermediate.

    Source locationptools-xml/Reaction[@frameid="RXN-11113"]/right[*/@frameid="CPD-12084"]
  • MetaCyc:RXN-19466

    Source assertion: The original substrate side contains CPD-12084; this supplies the second half of the intermediate bridge.

    Source locationptools-xml/Reaction[@frameid="RXN-19466"]/left[*/@frameid="CPD-12084"]
L-cysteine + ATP + H+ -> (L-cysteinyl)adenylate + diphosphate
MetaCyc:RXN-11115
provides_input_for

(L-cysteinyl)adenylate + a [PchE non-ribosomal peptide synthase] -> an L-cysteinyl-[PchE non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-11125
  • MetaCyc:RXN-11115

    Source assertion: The original product side contains CPD-12085; the subsequent reaction consumes that same source-native intermediate.

    Source locationptools-xml/Reaction[@frameid="RXN-11115"]/right[*/@frameid="CPD-12085"]
  • MetaCyc:RXN-11125

    Source assertion: The original substrate side contains CPD-12085; this supplies the second half of the intermediate bridge.

    Source locationptools-xml/Reaction[@frameid="RXN-11125"]/left[*/@frameid="CPD-12085"]
L-cysteine + ATP + H+ -> (L-cysteinyl)adenylate + diphosphate
MetaCyc:RXN-11115
provides_input_for

(L-cysteinyl)adenylate + a [PchF non-ribosomal peptide synthase] -> an L-cysteinyl-[PchF non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-11117
  • MetaCyc:RXN-11115

    Source assertion: The original product side contains CPD-12085; the subsequent reaction consumes that same source-native intermediate.

    Source locationptools-xml/Reaction[@frameid="RXN-11115"]/right[*/@frameid="CPD-12085"]
  • MetaCyc:RXN-11117

    Source assertion: The original substrate side contains CPD-12085; this supplies the second half of the intermediate bridge.

    Source locationptools-xml/Reaction[@frameid="RXN-11117"]/left[*/@frameid="CPD-12085"]
(salicyl)adenylate + a [PchE non-ribosomal peptide synthase] -> a salicyl-[PchE non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-19466
provides_input_for

a salicyl-[PchE non-ribosomal peptide synthase] + an L-cysteinyl-[PchE non-ribosomal peptide synthase] -> salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] + a [PchE non-ribosomal peptide synthase] + H+
MetaCyc:RXN-19469
  • MetaCyc:RXN-19466

    Source assertion: The original product side contains Salicyl-PchE; the subsequent reaction consumes that same source-native intermediate.

    Source locationptools-xml/Reaction[@frameid="RXN-19466"]/right[*/@frameid="Salicyl-PchE"]
  • MetaCyc:RXN-19469

    Source assertion: The original substrate side contains Salicyl-PchE; this supplies the second half of the intermediate bridge.

    Source locationptools-xml/Reaction[@frameid="RXN-19469"]/left[*/@frameid="Salicyl-PchE"]
(L-cysteinyl)adenylate + a [PchE non-ribosomal peptide synthase] -> an L-cysteinyl-[PchE non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-11125
provides_input_for

a salicyl-[PchE non-ribosomal peptide synthase] + an L-cysteinyl-[PchE non-ribosomal peptide synthase] -> salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] + a [PchE non-ribosomal peptide synthase] + H+
MetaCyc:RXN-19469
  • MetaCyc:RXN-11125

    Source assertion: The original product side contains L-cysteinyl-PchE; the subsequent reaction consumes that same source-native intermediate.

    Source locationptools-xml/Reaction[@frameid="RXN-11125"]/right[*/@frameid="L-cysteinyl-PchE"]
  • MetaCyc:RXN-19469

    Source assertion: The original substrate side contains L-cysteinyl-PchE; this supplies the second half of the intermediate bridge.

    Source locationptools-xml/Reaction[@frameid="RXN-19469"]/left[*/@frameid="L-cysteinyl-PchE"]
a salicyl-[PchE non-ribosomal peptide synthase] + an L-cysteinyl-[PchE non-ribosomal peptide synthase] -> salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] + a [PchE non-ribosomal peptide synthase] + H+
MetaCyc:RXN-19469
provides_input_for

salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] -> hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase] + H2O
MetaCyc:RXN-11118
  • MetaCyc:RXN-19469

    Source assertion: The original product side contains Salicyl-L-cysteinyl-PchE; the subsequent reaction consumes that same source-native intermediate.

    Source locationptools-xml/Reaction[@frameid="RXN-19469"]/right[*/@frameid="Salicyl-L-cysteinyl-PchE"]
  • MetaCyc:RXN-11118

    Source assertion: The original substrate side contains Salicyl-L-cysteinyl-PchE; this supplies the second half of the intermediate bridge.

    Source locationptools-xml/Reaction[@frameid="RXN-11118"]/left[*/@frameid="Salicyl-L-cysteinyl-PchE"]
salicyl-L-cysteinyl-[PchE non-ribosomal peptide synthas] -> hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase] + H2O
MetaCyc:RXN-11118
provides_input_for

an L-cysteinyl-[PchF non-ribosomal peptide synthase] + hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase] -> hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + a [PchE non-ribosomal peptide synthase] + H2O + H+
MetaCyc:RXN-11120
  • MetaCyc:RXN-11118

    Source assertion: The original product side contains hydroxyphenyl-thiazolinyl-PchE; the subsequent reaction consumes that same source-native intermediate.

    Source locationptools-xml/Reaction[@frameid="RXN-11118"]/right[*/@frameid="hydroxyphenyl-thiazolinyl-PchE"]
  • MetaCyc:RXN-11120

    Source assertion: The original substrate side contains hydroxyphenyl-thiazolinyl-PchE; this supplies the second half of the intermediate bridge.

    Source locationptools-xml/Reaction[@frameid="RXN-11120"]/left[*/@frameid="hydroxyphenyl-thiazolinyl-PchE"]
(L-cysteinyl)adenylate + a [PchF non-ribosomal peptide synthase] -> an L-cysteinyl-[PchF non-ribosomal peptide synthase] + AMP + H+
MetaCyc:RXN-11117
provides_input_for

an L-cysteinyl-[PchF non-ribosomal peptide synthase] + hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase] -> hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + a [PchE non-ribosomal peptide synthase] + H2O + H+
MetaCyc:RXN-11120
  • MetaCyc:RXN-11117

    Source assertion: The original product side contains L-cysteinyl-PchF; the subsequent reaction consumes that same source-native intermediate.

    Source locationptools-xml/Reaction[@frameid="RXN-11117"]/right[*/@frameid="L-cysteinyl-PchF"]
  • MetaCyc:RXN-11120

    Source assertion: The original substrate side contains L-cysteinyl-PchF; this supplies the second half of the intermediate bridge.

    Source locationptools-xml/Reaction[@frameid="RXN-11120"]/left[*/@frameid="L-cysteinyl-PchF"]
an L-cysteinyl-[PchF non-ribosomal peptide synthase] + hydroxyphenyl-thiazolinyl-[PchE non-ribosomal peptide synthase] -> hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + a [PchE non-ribosomal peptide synthase] + H2O + H+
MetaCyc:RXN-11120
provides_input_for

hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + NADPH + H+ -> N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] + NADP+
MetaCyc:RXN-11121
  • MetaCyc:RXN-11120

    Source assertion: The original product side contains Hydroxyphenyl-bis-thiazolinyl-PchF; the subsequent reaction consumes that same source-native intermediate.

    Source locationptools-xml/Reaction[@frameid="RXN-11120"]/right[*/@frameid="Hydroxyphenyl-bis-thiazolinyl-PchF"]
  • MetaCyc:RXN-11121

    Source assertion: The original substrate side contains Hydroxyphenyl-bis-thiazolinyl-PchF; this supplies the second half of the intermediate bridge.

    Source locationptools-xml/Reaction[@frameid="RXN-11121"]/left[*/@frameid="Hydroxyphenyl-bis-thiazolinyl-PchF"]
hydroxyphenyl-4,2-bis-thiazolinyl-[PchF non-ribosomal peptide synthase] + NADPH + H+ -> N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] + NADP+
MetaCyc:RXN-11121
provides_input_for

S-adenosyl-L-methionine + N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] -> pyochelinyl-[PchF non-ribosomal peptide synthase] + S-adenosyl-L-homocysteine + H+
MetaCyc:RXN-11122
  • MetaCyc:RXN-11121

    Source assertion: The original product side contains N-desmethyl-pyochelin-PchF; the subsequent reaction consumes that same source-native intermediate.

    Source locationptools-xml/Reaction[@frameid="RXN-11121"]/right[*/@frameid="N-desmethyl-pyochelin-PchF"]
  • MetaCyc:RXN-11122

    Source assertion: The original substrate side contains N-desmethyl-pyochelin-PchF; this supplies the second half of the intermediate bridge.

    Source locationptools-xml/Reaction[@frameid="RXN-11122"]/left[*/@frameid="N-desmethyl-pyochelin-PchF"]
S-adenosyl-L-methionine + N-desmethyl-pyochelin-[PchF non-ribosomal peptide synthase] -> pyochelinyl-[PchF non-ribosomal peptide synthase] + S-adenosyl-L-homocysteine + H+
MetaCyc:RXN-11122
provides_input_for

pyochelinyl-[PchF non-ribosomal peptide synthase] + H2O -> pyochelin + a [PchF non-ribosomal peptide synthase] + H+
MetaCyc:RXN-11123
  • MetaCyc:RXN-11122

    Source assertion: The original product side contains Pyochelinyl-PchF; the subsequent reaction consumes that same source-native intermediate.

    Source locationptools-xml/Reaction[@frameid="RXN-11122"]/right[*/@frameid="Pyochelinyl-PchF"]
  • MetaCyc:RXN-11123

    Source assertion: The original substrate side contains Pyochelinyl-PchF; this supplies the second half of the intermediate bridge.

    Source locationptools-xml/Reaction[@frameid="RXN-11123"]/left[*/@frameid="Pyochelinyl-PchF"]

References

Curation history