| http://purl.uniprot.org/enzyme/5.4.2.11 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/5.4.2.- |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/5.-.-.- |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/5.4.-.- |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme has no requirement for metal ions."xsd:string |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://www.w3.org/2000/01/rdf-schema#comment | "This phosphate can be transferred to the free OH of 2-phospho-D-glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine. cf. EC 5.4.2.12."xsd:string |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His(10) in man and Escherichia coli, His(8) in Saccharomyces cerevisiae)."xsd:string |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://www.w3.org/2000/01/rdf-schema#comment | "This enzyme also catalyze, slowly, the reactions of EC 5.4.2.4."xsd:string |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some fungi, yeast and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor."xsd:string |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://www.w3.org/2004/02/skos/core#prefLabel | "phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)"xsd:string |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11038361 |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/10064712 |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11827481 |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/12498792 |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/6255773 |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://www.w3.org/2004/02/skos/core#altLabel | "phosphoglyceromutase"xsd:string |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://www.w3.org/2004/02/skos/core#altLabel | "PGAM"xsd:string |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://www.w3.org/2004/02/skos/core#altLabel | "2,3-diphosphoglycerate dependent phosphoglycerate mutase"xsd:string |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://www.w3.org/2004/02/skos/core#altLabel | "cofactor dependent phosphoglycerate mutase"xsd:string |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://www.w3.org/2004/02/skos/core#altLabel | "phosphoglycerate phosphomutase"xsd:string |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://purl.uniprot.org/core/replaces | http://purl.uniprot.org/enzyme/5.4.2.1 |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://purl.uniprot.org/core/replaces | http://purl.uniprot.org/enzyme/2.7.5.3 |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/5.4.2.11#SIP0266882B831B162C |
| http://purl.uniprot.org/enzyme/5.4.2.11 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/5.4.2.- |