http://purl.uniprot.org/enzyme/1.1.1.261 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/1.1.1.261 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.1.-.- |
http://purl.uniprot.org/enzyme/1.1.1.261 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.1.1.- |
http://purl.uniprot.org/enzyme/1.1.1.261 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.-.-.- |
http://purl.uniprot.org/enzyme/1.1.1.261 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/1.1.1.261 | http://www.w3.org/2000/01/rdf-schema#comment | "It is the enantiomer of sn-glycerol 3-phosphate, the form of glycerophosphate found in bacteria and eukaryotes."xsd:string |
http://purl.uniprot.org/enzyme/1.1.1.261 | http://www.w3.org/2000/01/rdf-schema#comment | "Activity of the enzyme is stimulated by K(+)."xsd:string |
http://purl.uniprot.org/enzyme/1.1.1.261 | http://www.w3.org/2000/01/rdf-schema#comment | "Responsible for the formation of archaea-specific sn-glycerol-1-phosphate, the first step in the biosynthesis of polar lipids in archaea."xsd:string |
http://purl.uniprot.org/enzyme/1.1.1.261 | http://www.w3.org/2000/01/rdf-schema#comment | "The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine."xsd:string |
http://purl.uniprot.org/enzyme/1.1.1.261 | http://www.w3.org/2000/01/rdf-schema#comment | "The other enzymes involved in the biosynthesis of polar lipids in archaea are EC 2.5.1.41 and EC 2.5.1.42, which together alkylate the hydroxy groups of glycerol 1-phosphate to give unsaturated archaetidic acid, which is acted upon by EC 2.7.7.67 to form CDP-unsaturated archaeol."xsd:string |
http://purl.uniprot.org/enzyme/1.1.1.261 | http://www.w3.org/2004/02/skos/core#prefLabel | "sn-glycerol-1-phosphate dehydrogenase"xsd:string |
http://purl.uniprot.org/enzyme/1.1.1.261 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9348086 |
http://purl.uniprot.org/enzyme/1.1.1.261 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9419225 |
http://purl.uniprot.org/enzyme/1.1.1.261 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/15876564 |
http://purl.uniprot.org/enzyme/1.1.1.261 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/18558723 |
http://purl.uniprot.org/enzyme/1.1.1.261 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/10960477 |
http://purl.uniprot.org/enzyme/1.1.1.261 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/8586635 |
http://purl.uniprot.org/enzyme/1.1.1.261 | http://www.w3.org/2004/02/skos/core#altLabel | "Gro1PDH"xsd:string |
http://purl.uniprot.org/enzyme/1.1.1.261 | http://www.w3.org/2004/02/skos/core#altLabel | "glycerol-1-phosphate dehydrogenase [NAD(P)(+)]"xsd:string |
http://purl.uniprot.org/enzyme/1.1.1.261 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/1.1.1.261#SIP222F8AF396079DF3 |
http://purl.uniprot.org/enzyme/1.1.1.261 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/1.1.1.261#SIPC7187C110EAA280F |
http://purl.uniprot.org/enzyme/1.1.1.261 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/1.1.1.- |
http://purl.uniprot.org/uniprot/A0A843DBF4 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.1.1.261 |
http://purl.uniprot.org/uniprot/A0A8T4XMY1 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.1.1.261 |
http://purl.uniprot.org/uniprot/A0A0K2AS00 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.1.1.261 |