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http://purl.uniprot.org/enzyme/1.1.1.261http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.1.1.261http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.1.-.-
http://purl.uniprot.org/enzyme/1.1.1.261http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.1.1.-
http://purl.uniprot.org/enzyme/1.1.1.261http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.-.-.-
http://purl.uniprot.org/enzyme/1.1.1.261http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.1.1.261http://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/1.1.1.261http://www.w3.org/2000/01/rdf-schema#comment"Activity of the enzyme is stimulated by K(+)."xsd:string
http://purl.uniprot.org/enzyme/1.1.1.261http://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/1.1.1.261http://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/1.1.1.261http://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/1.1.1.261http://www.w3.org/2004/02/skos/core#prefLabel"sn-glycerol-1-phosphate dehydrogenase"xsd:string
http://purl.uniprot.org/enzyme/1.1.1.261http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9348086
http://purl.uniprot.org/enzyme/1.1.1.261http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9419225
http://purl.uniprot.org/enzyme/1.1.1.261http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/15876564
http://purl.uniprot.org/enzyme/1.1.1.261http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/18558723
http://purl.uniprot.org/enzyme/1.1.1.261http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10960477
http://purl.uniprot.org/enzyme/1.1.1.261http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8586635
http://purl.uniprot.org/enzyme/1.1.1.261http://www.w3.org/2004/02/skos/core#altLabel"Gro1PDH"xsd:string
http://purl.uniprot.org/enzyme/1.1.1.261http://www.w3.org/2004/02/skos/core#altLabel"glycerol-1-phosphate dehydrogenase [NAD(P)(+)]"xsd:string
http://purl.uniprot.org/enzyme/1.1.1.261http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/1.1.1.261#SIP222F8AF396079DF3
http://purl.uniprot.org/enzyme/1.1.1.261http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/1.1.1.261#SIPC7187C110EAA280F
http://purl.uniprot.org/enzyme/1.1.1.261http://www.w3.org/2004/02/skos/core#broaderTransitivehttp://purl.uniprot.org/enzyme/1.1.1.-
http://purl.uniprot.org/uniprot/A0A843DBF4http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/1.1.1.261
http://purl.uniprot.org/uniprot/A0A8T4XMY1http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/1.1.1.261
http://purl.uniprot.org/uniprot/A0A0K2AS00http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/1.1.1.261