| http://purl.uniprot.org/enzyme/5.4.2.12 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/5.4.2.12 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/5.4.2.- |
| http://purl.uniprot.org/enzyme/5.4.2.12 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/5.-.-.- |
| http://purl.uniprot.org/enzyme/5.4.2.12 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/5.4.-.- |
| http://purl.uniprot.org/enzyme/5.4.2.12 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/5.4.2.12 | http://www.w3.org/2000/01/rdf-schema#comment | "The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position."xsd:string |
| http://purl.uniprot.org/enzyme/5.4.2.12 | http://www.w3.org/2000/01/rdf-schema#comment | "Both metal ions are involved in the reaction."xsd:string |
| http://purl.uniprot.org/enzyme/5.4.2.12 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzymes from higher plants, algae, some fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. cf. EC 5.4.2.11."xsd:string |
| http://purl.uniprot.org/enzyme/5.4.2.12 | http://www.w3.org/2004/02/skos/core#prefLabel | "phosphoglycerate mutase (2,3-diphosphoglycerate-independent)"xsd:string |
| http://purl.uniprot.org/enzyme/5.4.2.12 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/22458781 |
| http://purl.uniprot.org/enzyme/5.4.2.12 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/10764795 |
| http://purl.uniprot.org/enzyme/5.4.2.12 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/12729763 |
| http://purl.uniprot.org/enzyme/5.4.2.12 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/17085493 |
| http://purl.uniprot.org/enzyme/5.4.2.12 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/15234973 |
| http://purl.uniprot.org/enzyme/5.4.2.12 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/19781556 |
| http://purl.uniprot.org/enzyme/5.4.2.12 | http://www.w3.org/2004/02/skos/core#altLabel | "phosphoglyceromutase"xsd:string |
| http://purl.uniprot.org/enzyme/5.4.2.12 | http://www.w3.org/2004/02/skos/core#altLabel | "2,3-diphosphoglycerate-independent phosphoglycerate mutase"xsd:string |
| http://purl.uniprot.org/enzyme/5.4.2.12 | http://www.w3.org/2004/02/skos/core#altLabel | "cofactor independent phosphoglycerate mutase"xsd:string |
| http://purl.uniprot.org/enzyme/5.4.2.12 | http://www.w3.org/2004/02/skos/core#altLabel | "phosphoglycerate phosphomutase"xsd:string |
| http://purl.uniprot.org/enzyme/5.4.2.12 | http://purl.uniprot.org/core/replaces | http://purl.uniprot.org/enzyme/5.4.2.1 |
| http://purl.uniprot.org/enzyme/5.4.2.12 | http://purl.uniprot.org/core/replaces | http://purl.uniprot.org/enzyme/2.7.5.3 |
| http://purl.uniprot.org/enzyme/5.4.2.12 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/5.4.2.12#SIP0266882B831B162C |
| http://purl.uniprot.org/enzyme/5.4.2.12 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/5.4.2.- |
| http://purl.uniprot.org/uniprot/A0AA38L1R8 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/5.4.2.12 |
| http://purl.uniprot.org/uniprot/A0AA47EIV9 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/5.4.2.12 |