Reviewed,
UniProtKB/Swiss-Prot Q4R6L7 (PMGE_MACFA)
Last modified
June 16, 2009.
Version 24.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Bisphosphoglycerate mutase Short name=BPGM EC=5.4.2.4 Alternative name(s): 2,3-bisphosphoglycerate mutase, erythrocyte 2,3-bisphosphoglycerate synthase EC=5.4.2.1 EC=3.1.3.13 BPG-dependent PGAM | ||||
| Gene names |
| ||||
| Organism | Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey) | ||||
| Taxonomic identifier | 9541 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca |
Protein attributes
| Sequence length | 259 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Plays a major role in regulating hemoglobin oxygen affinity as a consequence of controlling 2,3-BPG concentration. Can also catalyze the reaction of EC 5.4.2.1 (mutase) and EC 3.1.3.13 (phosphatase), but with a reduced activity By similarity. |
| Catalytic activity | 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate. 2-phospho-D-glycerate = 3-phospho-D-glycerate. 2,3-bisphospho-D-glycerate + H2O = 3-phospho-D-glycerate + phosphate. |
| Subunit structure | Homodimer By similarity. |
| Sequence similarities | Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Molecular function | Hydrolase Isomerase |
| Gene Ontology (GO) | |
| Biological process | glycolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 2,3-bisphospho-D-glycerate 2-phosphohydrolase activity Inferred from electronic annotation. Source: EC bisphosphoglycerate mutase activityInferred from electronic annotation. Source: EC phosphoglycerate mutase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 259 | 258 | Bisphosphoglycerate mutase | PRO_0000268184 | |||||
Sites | |||||||||
| Active site | 11 | 1 | Tele-phosphohistidine intermediate By similarity | ||||||
| Active site | 188 | 1 | By similarity | ||||||
| Site | 62 | 1 | Interaction with carboxyl group of phosphoglycerates By similarity | ||||||
Sequences
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References
| [1] | "DNA sequences of macaque genes expressed in brain or testis and its evolutionary implications." International consortium for macaque cDNA sequencing and analysis Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis. |
Cross-references
Sequence databases | |
|---|---|
| AB169166 mRNA. Translation: BAE01258.1. | |
3D structure databases | |
| SMR | Q4R6L7. Positions 2-256. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | Q4R6L7. |
Enzyme and pathway databases | |
| BRENDA | 3.1.3.13. 3438. 5.4.2.1. 3438. 5.4.2.4. 3438. |
Family and domain databases | |
| InterPro | IPR001345. PG/BPGM_mutase. IPR013078. PG_mutase. IPR005952. Phosphogly_mut1. [Graphical view] |
| PANTHER | PTHR11931. Phosphogly_mut1. 1 hit. |
| Pfam | PF00300. PGAM. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01258. pgm_1. 1 hit. |
| PROSITE | PS00175. PG_MUTASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PMGE_MACFA | ||||||||
| Accession | Primary (citable) accession number: Q4R6L7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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