A0A6M3WBI8 · A0A6M3WBI8_COROI
- Protein2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- GenepgmA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids547 (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 | 25 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Active site | 75 | Phosphoserine intermediate | |||
Binding site | 75 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 136 | substrate | |||
Binding site | 166-167 | substrate | |||
Binding site | 198 | substrate | |||
Binding site | 204 | substrate | |||
Binding site | 271-274 | substrate | |||
Binding site | 344 | substrate | |||
Binding site | 411 | Mn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 415 | Mn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 452 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 453 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 470 | Mn2+ 1 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
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
Encoded on
- Chloroplast
Organism names
- Taxonomic lineageEukaryota > Rhodophyta > Florideophyceae > Corallinophycidae > Corallinales > Corallinaceae > Corallinoideae > Corallina
Accessions
- Primary accessionA0A6M3WBI8
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 17-516 | Metalloenzyme | |||
Domain | 95-307 | BPG-independent PGAM N-terminal | |||
Sequence similarities
Belongs to the BPG-independent phosphoglycerate mutase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length547
- Mass (Da)62,793
- Last updated2020-10-07 v1
- MD5 Checksum1FFD50155BCAF01A5C597C001C41C937
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
MT211884 EMBL· GenBank· DDBJ | QJF58242.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
MT211885 EMBL· GenBank· DDBJ | QJF58441.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
MT211886 EMBL· GenBank· DDBJ | QJF58640.1 EMBL· GenBank· DDBJ | Genomic DNA |