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http://purl.uniprot.org/enzyme/2.3.1.292http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/2.3.1.292http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.3.-.-
http://purl.uniprot.org/enzyme/2.3.1.292http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.3.1.-
http://purl.uniprot.org/enzyme/2.3.1.292http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.-.-.-
http://purl.uniprot.org/enzyme/2.3.1.292http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/2.3.1.292http://www.w3.org/2000/01/rdf-schema#comment"The incorporation of the methylmalonyl units results in formation of two branched methyl groups in the elongated product."xsd:string
http://purl.uniprot.org/enzyme/2.3.1.292http://www.w3.org/2000/01/rdf-schema#comment"The enzyme, which is a complex of five polyketide synthase proteins, is involved in the synthesis of the lipid core common to phthiocerols and phenolphthiocerols."xsd:string
http://purl.uniprot.org/enzyme/2.3.1.292http://www.w3.org/2000/01/rdf-schema#comment"The substrates must first be adenylated by EC 6.2.1.59, which also loads them onto PpsA."xsd:string
http://purl.uniprot.org/enzyme/2.3.1.292http://www.w3.org/2000/01/rdf-schema#comment"The first protein, PpsA, can accept either a C18 or C20 long-chain fatty acyl, or a (4-hydroxyphenyl)-C17 or C19 fatty acyl."xsd:string
http://purl.uniprot.org/enzyme/2.3.1.292http://www.w3.org/2000/01/rdf-schema#comment"The enzyme does not contain a thioesterase domain, and release of the products requires the tesA-encoded type II thioesterase."xsd:string
http://purl.uniprot.org/enzyme/2.3.1.292http://www.w3.org/2000/01/rdf-schema#comment"PpsC adds a third malonyl unit (releasing a water molecule due to its dehydratase domain), PpsD adds an (R)-methylmalonyl unit, releasing a water molecule, and PpsE adds a second (R)-methylmalonyl unit, without releasing a water molecule."xsd:string
http://purl.uniprot.org/enzyme/2.3.1.292http://www.w3.org/2000/01/rdf-schema#comment"PpsA then extends them using a malonyl-CoA extender unit."xsd:string
http://purl.uniprot.org/enzyme/2.3.1.292http://www.w3.org/2000/01/rdf-schema#comment"The absence of a dehydratase and an enoyl reductase domains in the PpsA and PpsB modules results in the formation of the diol portion of the phthiocerol moiety."xsd:string
http://purl.uniprot.org/enzyme/2.3.1.292http://www.w3.org/2000/01/rdf-schema#comment"The PpsB protein adds the next malonyl-CoA extender unit."xsd:string
http://purl.uniprot.org/enzyme/2.3.1.292http://www.w3.org/2004/02/skos/core#prefLabel"(phenol)carboxyphthiodiolenone synthase"xsd:string
http://purl.uniprot.org/enzyme/2.3.1.292http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/15749014
http://purl.uniprot.org/enzyme/2.3.1.292http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/15668773
http://purl.uniprot.org/enzyme/2.3.1.292http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/2.3.1.292#SIPE15CFC82AF94C735
http://purl.uniprot.org/enzyme/2.3.1.292http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/2.3.1.292#SIP11A2399A6951C3AE
http://purl.uniprot.org/enzyme/2.3.1.292http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/2.3.1.292#SIP5BAC118E9C32BA6E
http://purl.uniprot.org/enzyme/2.3.1.292http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/2.3.1.292#SIP8114B73CF2E94A2A
http://purl.uniprot.org/enzyme/2.3.1.292http://www.w3.org/2004/02/skos/core#broaderTransitivehttp://purl.uniprot.org/enzyme/2.3.1.-
http://purl.uniprot.org/uniprot/Q7TXM0http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.3.1.292
http://purl.uniprot.org/uniprot/P9WQE2http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.3.1.292
http://purl.uniprot.org/uniprot/P9WQE3http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/2.3.1.292