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http://purl.uniprot.org/enzyme/2.6.1.52http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/2.6.1.52http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.6.1.-
http://purl.uniprot.org/enzyme/2.6.1.52http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.-.-.-
http://purl.uniprot.org/enzyme/2.6.1.52http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.6.-.-
http://purl.uniprot.org/enzyme/2.6.1.52http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/2.6.1.52http://www.w3.org/2000/01/rdf-schema#comment"A pyridoxal 5'-phosphate protein."xsd:string
http://purl.uniprot.org/enzyme/2.6.1.52http://www.w3.org/2000/01/rdf-schema#comment"Pyridoxal 5'-phosphate is the cofactor for both activities and therefore seems to be involved in its own biosynthesis."xsd:string
http://purl.uniprot.org/enzyme/2.6.1.52http://www.w3.org/2000/01/rdf-schema#comment"This enzyme catalyzes the second step in the phosphorylated pathway of serine biosynthesis and the third step in pyridoxal 5'-phosphate biosynthesis in the bacterium Escherichia coli."xsd:string
http://purl.uniprot.org/enzyme/2.6.1.52http://www.w3.org/2000/01/rdf-schema#comment"The archaeal enzyme has a relaxed specificity and can act on L-cysteate and L-alanine as alternative substrates to O-phospho-L-serine."xsd:string
http://purl.uniprot.org/enzyme/2.6.1.52http://www.w3.org/2000/01/rdf-schema#comment"Non-phosphorylated forms of serine and threonine are not substrates."xsd:string
http://purl.uniprot.org/enzyme/2.6.1.52http://www.w3.org/2004/02/skos/core#prefLabel"phosphoserine transaminase"xsd:string
http://purl.uniprot.org/enzyme/2.6.1.52http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8595869
http://purl.uniprot.org/enzyme/2.6.1.52http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/14086727
http://purl.uniprot.org/enzyme/2.6.1.52http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8550422
http://purl.uniprot.org/enzyme/2.6.1.52http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8706854
http://purl.uniprot.org/enzyme/2.6.1.52http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/6022873
http://purl.uniprot.org/enzyme/2.6.1.52http://www.w3.org/2004/02/skos/core#altLabel"phosphoserine aminotransferase"xsd:string
http://purl.uniprot.org/enzyme/2.6.1.52http://www.w3.org/2004/02/skos/core#altLabel"3-phosphoserine aminotransferase"xsd:string
http://purl.uniprot.org/enzyme/2.6.1.52http://www.w3.org/2004/02/skos/core#altLabel"PSAT"xsd:string
http://purl.uniprot.org/enzyme/2.6.1.52http://www.w3.org/2004/02/skos/core#altLabel"3PHP transaminase"xsd:string
http://purl.uniprot.org/enzyme/2.6.1.52http://www.w3.org/2004/02/skos/core#altLabel"L-phosphoserine aminotransferase"xsd:string
http://purl.uniprot.org/enzyme/2.6.1.52http://www.w3.org/2004/02/skos/core#altLabel"hydroxypyruvic phosphate--glutamic transaminase"xsd:string
http://purl.uniprot.org/enzyme/2.6.1.52http://www.w3.org/2004/02/skos/core#altLabel"phosphohydroxypyruvate transaminase"xsd:string
http://purl.uniprot.org/enzyme/2.6.1.52http://www.w3.org/2004/02/skos/core#altLabel"phosphohydroxypyruvic--glutamic transaminase"xsd:string
http://purl.uniprot.org/enzyme/2.6.1.52http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/2.6.1.52#SIPD17D8E7538A76774