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http://purl.uniprot.org/enzyme/4.1.2.25http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/4.1.2.25http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/4.1.2.-
http://purl.uniprot.org/enzyme/4.1.2.25http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/4.1.-.-
http://purl.uniprot.org/enzyme/4.1.2.25http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/4.-.-.-
http://purl.uniprot.org/enzyme/4.1.2.25http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/4.1.2.25http://www.w3.org/2000/01/rdf-schema#comment"The enzymes from the bacterium Escherichia coli and the plant Arabidopsis thaliana also catalyze the epimerisation of the 2' hydroxy-group (EC 5.1.99.8)."xsd:string
http://purl.uniprot.org/enzyme/4.1.2.25http://www.w3.org/2000/01/rdf-schema#comment"The enzyme from the yeast Saccharomyces cerevisiae also catalyzes the two subsequent steps in the folate biosynthesis pathway - EC 2.7.6.3 and EC 2.5.1.15."xsd:string
http://purl.uniprot.org/enzyme/4.1.2.25http://www.w3.org/2000/01/rdf-schema#comment"The enzyme from the bacterium Mycobacterium tuberculosis is trifunctional and also catalyzes EC 5.1.99.8 and EC 1.13.11.81."xsd:string
http://purl.uniprot.org/enzyme/4.1.2.25http://www.w3.org/2000/01/rdf-schema#comment"The enzyme participates in folate (in bacteria, plants and fungi) and methanopterin (in archaea) biosynthesis."xsd:string
http://purl.uniprot.org/enzyme/4.1.2.25http://www.w3.org/2004/02/skos/core#prefLabel"dihydroneopterin aldolase"xsd:string
http://purl.uniprot.org/enzyme/4.1.2.25http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/24982305
http://purl.uniprot.org/enzyme/4.1.2.25http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/15169867
http://purl.uniprot.org/enzyme/4.1.2.25http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/15107504
http://purl.uniprot.org/enzyme/4.1.2.25http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/23150985
http://purl.uniprot.org/enzyme/4.1.2.25http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/25264482
http://purl.uniprot.org/enzyme/4.1.2.25http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9651328
http://purl.uniprot.org/enzyme/4.1.2.25http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/4912541
http://purl.uniprot.org/enzyme/4.1.2.25http://www.w3.org/2004/02/skos/core#altLabel"7,8-dihydroneopterin aldolase"xsd:string
http://purl.uniprot.org/enzyme/4.1.2.25http://www.w3.org/2004/02/skos/core#altLabel"2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine glycolaldehyde-lyase"xsd:string
http://purl.uniprot.org/enzyme/4.1.2.25http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/4.1.2.25#SIP1C8A5E15A63326DA
http://purl.uniprot.org/enzyme/4.1.2.25http://www.w3.org/2004/02/skos/core#broaderTransitivehttp://purl.uniprot.org/enzyme/4.1.2.-
http://purl.uniprot.org/uniprot/A0A0K1RE64http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/4.1.2.25
http://purl.uniprot.org/uniprot/A0A9X1IHJ6http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/4.1.2.25
http://purl.uniprot.org/uniprot/A0A9X0JH63http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/4.1.2.25
http://purl.uniprot.org/uniprot/A0A086YR90http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/4.1.2.25