Q3SZ62 (PGAM1_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 57.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Phosphoglycerate mutase 1 EC=3.1.3.13 EC=5.4.2.1 EC=5.4.2.4 Alternative name(s): BPG-dependent PGAM 1 Phosphoglycerate mutase isozyme B Short name=PGAM-B | ||
| Gene names |
| ||
| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 254 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 | Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity By similarity. |
| Catalytic activity | 2-phospho-D-glycerate = 3-phospho-D-glycerate. 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-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 |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | glycolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | bisphosphoglycerate 2-phosphatase 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 – 254 | 253 | Phosphoglycerate mutase 1 | PRO_0000246079 | |||||
Regions | |||||||||
| Compositional bias | 122 – 131 | 10 | Pro-rich | ||||||
Sites | |||||||||
| Active site | 11 | 1 | Tele-phosphohistidine intermediate By similarity | ||||||
| Active site | 186 | 1 | By similarity | ||||||
| Site | 62 | 1 | Interaction with carboxyl group of phosphoglycerates By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||
| Modified residue | 14 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 26 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 31 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 92 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 118 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Heart ventricle. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC103115 mRNA. Translation: AAI03116.1. |
| IPI | IPI00698589. |
| RefSeq | NP_001029226.1. NM_001034054.1. |
| UniGene | Bt.15319. |
3D structure databases | |
| ProteinModelPortal | Q3SZ62. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q3SZ62. |
Proteomic databases | |
| PRIDE | Q3SZ62. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAT00000032937; ENSBTAP00000032864; ENSBTAG00000012697. |
| GeneID | 404148. |
| KEGG | bta:404148. |
Organism-specific databases | |
| CTD | 5223. |
Phylogenomic databases | |
| eggNOG | maNOG12725. |
| GeneTree | ENSGT00390000016700. |
| HOVERGEN | HBG027528. |
| InParanoid | Q3SZ62. |
| OMA | EWNALNL. |
| OrthoDB | EOG4MCX10. |
| PhylomeDB | Q3SZ62. |
Family and domain databases | |
| InterPro | IPR013078. His_Pase_superF_clade-1. IPR001345. PG/BPGM_mutase_AS. IPR005952. Phosphogly_mut1. [Graphical view] |
| KO | K01834. |
| PANTHER | PTHR11931. Phosphogly_mut1. 1 hit. |
| Pfam | PF00300. His_Phos_1. 1 hit. [Graphical view] |
| SMART | SM00855. 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 | PGAM1_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q3SZ62 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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