V4XPU8 · V4XPU8_9ARCH
- Protein2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- GenegpmI
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids504 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic activity
- (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Cofactor
Note: Binds 2 manganese ions per subunit.
Pathway
Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 9 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Active site | 59 | Phosphoserine intermediate | |||
Binding site | 59 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 120 | substrate | |||
Binding site | 149-150 | substrate | |||
Binding site | 181 | substrate | |||
Binding site | 187 | substrate | |||
Binding site | 253-256 | substrate | |||
Binding site | 326 | substrate | |||
Binding site | 393 | Mn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 397 | Mn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 434 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 435 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 451 | Mn2+ 1 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity | |
Molecular Function | manganese ion binding | |
Biological Process | glucose catabolic process | |
Biological Process | glycolytic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- EC number
- Short namesBPG-independent PGAM ; Phosphoglyceromutase ; iPGM
Gene names
Organism names
- Organism
- Taxonomic lineageArchaea > environmental samples
Accessions
- Primary accessionV4XPU8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 1-489 | Metalloenzyme | |||
Domain | 79-289 | BPG-independent PGAM N-terminal | |||
Sequence similarities
Belongs to the BPG-independent phosphoglycerate mutase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length504
- Mass (Da)54,639
- Last updated2014-01-22 v1
- MD5 Checksum35A869F1D80F1DFED5883C32605D0E4C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KI543234 EMBL· GenBank· DDBJ | ESS10519.1 EMBL· GenBank· DDBJ | Genomic DNA |