http://purl.uniprot.org/enzyme/4.1.2.25 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/4.1.2.25 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/4.1.2.- |
http://purl.uniprot.org/enzyme/4.1.2.25 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/4.1.-.- |
http://purl.uniprot.org/enzyme/4.1.2.25 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/4.-.-.- |
http://purl.uniprot.org/enzyme/4.1.2.25 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/4.1.2.25 | http://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/4.1.2.25 | http://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/4.1.2.25 | http://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/4.1.2.25 | http://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/4.1.2.25 | http://www.w3.org/2004/02/skos/core#prefLabel | "dihydroneopterin aldolase"xsd:string |
http://purl.uniprot.org/enzyme/4.1.2.25 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/24982305 |
http://purl.uniprot.org/enzyme/4.1.2.25 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/15169867 |
http://purl.uniprot.org/enzyme/4.1.2.25 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/15107504 |
http://purl.uniprot.org/enzyme/4.1.2.25 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/23150985 |
http://purl.uniprot.org/enzyme/4.1.2.25 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/25264482 |
http://purl.uniprot.org/enzyme/4.1.2.25 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9651328 |
http://purl.uniprot.org/enzyme/4.1.2.25 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/4912541 |
http://purl.uniprot.org/enzyme/4.1.2.25 | http://www.w3.org/2004/02/skos/core#altLabel | "7,8-dihydroneopterin aldolase"xsd:string |
http://purl.uniprot.org/enzyme/4.1.2.25 | http://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/4.1.2.25 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/4.1.2.25#SIP1C8A5E15A63326DA |
http://purl.uniprot.org/enzyme/4.1.2.25 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/4.1.2.- |
http://purl.uniprot.org/uniprot/A0A0K1RE64 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/4.1.2.25 |
http://purl.uniprot.org/uniprot/A0A9X1IHJ6 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/4.1.2.25 |
http://purl.uniprot.org/uniprot/A0A9X0JH63 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/4.1.2.25 |
http://purl.uniprot.org/uniprot/A0A086YR90 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/4.1.2.25 |