http://purl.uniprot.org/enzyme/1.14.18.6 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/1.14.18.6 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.-.-.- |
http://purl.uniprot.org/enzyme/1.14.18.6 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.14.-.- |
http://purl.uniprot.org/enzyme/1.14.18.6 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.14.18.- |
http://purl.uniprot.org/enzyme/1.14.18.6 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/1.14.18.6 | http://www.w3.org/2000/01/rdf-schema#comment | "The newly introduced 2-hydroxyl group has R-configuration. cf. EC 1.14.18.7."xsd:string |
http://purl.uniprot.org/enzyme/1.14.18.6 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzymes from yeast and from mammals contain an N-terminal cytochrome b5 domain that acts as the direct electron donor to the desaturase active site."xsd:string |
http://purl.uniprot.org/enzyme/1.14.18.6 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme, characterized from yeast and mammals, catalyzes the hydroxylation of carbon 2 of long- or very-long-chain fatty acids attached to (4R)-4-hydroxysphinganine during de novo ceramide synthesis."xsd:string |
http://purl.uniprot.org/enzyme/1.14.18.6 | http://www.w3.org/2004/02/skos/core#prefLabel | "4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase"xsd:string |
http://purl.uniprot.org/enzyme/1.14.18.6 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9353282 |
http://purl.uniprot.org/enzyme/1.14.18.6 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9559540 |
http://purl.uniprot.org/enzyme/1.14.18.6 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/15337768 |
http://purl.uniprot.org/enzyme/1.14.18.6 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/15658937 |
http://purl.uniprot.org/enzyme/1.14.18.6 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/22517924 |
http://purl.uniprot.org/enzyme/1.14.18.6 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/1.14.18.6#SIP1F44BB3238989B7D |
http://purl.uniprot.org/enzyme/1.14.18.6 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/1.14.18.6#SIP1EDF6F31B82BE741 |
http://purl.uniprot.org/enzyme/1.14.18.6 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/1.14.18.- |
http://purl.uniprot.org/uniprot/A0A8S3RS94 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.14.18.6 |
http://purl.uniprot.org/uniprot/A0A8S3RP84 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.14.18.6 |
http://purl.uniprot.org/uniprot/A0AA43QKY0 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.14.18.6 |
http://purl.uniprot.org/uniprot/Q03529 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.14.18.6 |
http://purl.uniprot.org/uniprot/Q03529#SIP10F47A1CEB896275 | http://purl.uniprot.org/core/enzymeClass | http://purl.uniprot.org/enzyme/1.14.18.6 |
http://purl.uniprot.org/uniprot/#_kb.Q03529_up.enzyme_F1C853411032FF23 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/enzyme/1.14.18.6 |
http://purl.uniprot.org/uniprot/#_kb.A0AA43QKY0_up.enzyme_F1C853411032FF23 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/enzyme/1.14.18.6 |
http://purl.uniprot.org/uniprot/#_kb.A0A8S3RP84_up.enzyme_F1C853411032FF23 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/enzyme/1.14.18.6 |