A0A0G0YC35 · A0A0G0YC35_9BACT
- Protein2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- GenegpmI
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids515 (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 | 3 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Active site | 53 | Phosphoserine intermediate | |||
Binding site | 53 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 114 | substrate | |||
Binding site | 177 | substrate | |||
Binding site | 183 | substrate | |||
Binding site | 326 | substrate | |||
Binding site | 391 | Mn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 395 | Mn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 432 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 433 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 451 | Mn2+ 1 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
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
- Taxonomic lineageBacteria
Accessions
- Primary accessionA0A0G0YC35
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 2-502 | Metalloenzyme | |||
Domain | 73-290 | BPG-independent PGAM N-terminal | |||
Sequence similarities
Belongs to the BPG-independent phosphoglycerate mutase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length515
- Mass (Da)57,422
- Last updated2015-07-22 v1
- MD5 ChecksumA467536531B50660C1CBD144BFA0CAC7
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LCCQ01000006 EMBL· GenBank· DDBJ | KKS34295.1 EMBL· GenBank· DDBJ | Genomic DNA |