http://purl.uniprot.org/enzyme/2.4.99.12 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/2.4.99.12 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.4.-.- |
http://purl.uniprot.org/enzyme/2.4.99.12 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.4.99.- |
http://purl.uniprot.org/enzyme/2.4.99.12 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.-.-.- |
http://purl.uniprot.org/enzyme/2.4.99.12 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/2.4.99.12 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzymes from Chlamydia transfer three or more 3-deoxy-D-manno-oct-2-ulosonate residues and generate genus-specific epitopes."xsd:string |
http://purl.uniprot.org/enzyme/2.4.99.12 | http://www.w3.org/2000/01/rdf-schema#comment | "The monofunctional enzymes from Bordetella pertusis, Aquifex aeolicus and Haemophilus influenzae catalyze the transfer of a single 3-D-manno-oct-2-ulosonate residue from CMP-3-D-manno-oct-2-ulosonate to lipid IVA."xsd:string |
http://purl.uniprot.org/enzyme/2.4.99.12 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme from Escherichia coli is bifunctional and transfers two 3-deoxy-D-manno-oct-2-ulosonate residues to lipid IVA (cf. EC 2.4.99.13)."xsd:string |
http://purl.uniprot.org/enzyme/2.4.99.12 | http://www.w3.org/2004/02/skos/core#prefLabel | "lipid IVA 3-deoxy-D-manno-octulosonic acid transferase"xsd:string |
http://purl.uniprot.org/enzyme/2.4.99.12 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/8748024 |
http://purl.uniprot.org/enzyme/2.4.99.12 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/19546212 |
http://purl.uniprot.org/enzyme/2.4.99.12 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/10198035 |
http://purl.uniprot.org/enzyme/2.4.99.12 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/1577828 |
http://purl.uniprot.org/enzyme/2.4.99.12 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9195966 |
http://purl.uniprot.org/enzyme/2.4.99.12 | http://www.w3.org/2004/02/skos/core#altLabel | "KDO transferase"xsd:string |
http://purl.uniprot.org/enzyme/2.4.99.12 | http://www.w3.org/2004/02/skos/core#altLabel | "3-deoxy-manno-octulosonic acid transferase"xsd:string |
http://purl.uniprot.org/enzyme/2.4.99.12 | http://www.w3.org/2004/02/skos/core#altLabel | "3-deoxy-D-manno-oct-2-ulosonic acid transferase"xsd:string |
http://purl.uniprot.org/enzyme/2.4.99.12 | http://www.w3.org/2004/02/skos/core#altLabel | "lipid IVA KDO transferase"xsd:string |
http://purl.uniprot.org/enzyme/2.4.99.12 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/2.4.99.12#SIP873EDB41A9F27EA9 |
http://purl.uniprot.org/enzyme/2.4.99.12 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/2.4.99.12#SIP7024EB6ADE0CA0C7 |
http://purl.uniprot.org/enzyme/2.4.99.12 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/2.4.99.- |
http://purl.uniprot.org/uniprot/A0AA45EV56 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.4.99.12 |
http://purl.uniprot.org/uniprot/A0A2C5SHI4 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.4.99.12 |
http://purl.uniprot.org/uniprot/A0A963IJ07 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.4.99.12 |
http://purl.uniprot.org/uniprot/A0AA42SXY3 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/2.4.99.12 |