B0JLN5 · GPMI_MICAN
- Protein2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- GenegpmI
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids532 (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 | 15 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 65 | Phosphoserine intermediate | ||||
Sequence: S | ||||||
Binding site | 65 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 126 | substrate | ||||
Sequence: H | ||||||
Binding site | 156-157 | substrate | ||||
Sequence: RD | ||||||
Binding site | 188 | substrate | ||||
Sequence: R | ||||||
Binding site | 194 | substrate | ||||
Sequence: R | ||||||
Binding site | 258-261 | substrate | ||||
Sequence: RPDR | ||||||
Binding site | 331 | substrate | ||||
Sequence: K | ||||||
Binding site | 398 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 402 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 439 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 440 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 457 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H |
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
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Oscillatoriophycideae > Chroococcales > Microcystaceae > Microcystis
Accessions
- Primary accessionB0JLN5
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000084308 | 1-532 | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase | |||
Sequence: MTHAPISPVVLVILDGWGYRPQRSDNAIAMAKTPIMDSLWEVYPHTLIRTSAKDVGLPEGQMGNSEVGHLNIGAGRVVPQELVRISDAIEDGSIQQNQALLKLCAEIRPKKSKLHLIGLCSEGGVHSHLDHLLGLLDLAKVQGISDVCIHVITDGRDTNVTDGMPAIKRIQEHINKIKLGRMVTLSGRYYAMDRDRRWDRVEKAYNVMTSDQGIDGRSITEVLQAFYDQNITDEFIPPTRIAPGAIEAGDGVIFYNFRPDRARQLCYALTMPDFEDFDRDLISPLSFVTFTQYDPKLPVDVAFAPQNLNNILGQVIAQQGLKQFRCAETEKYPHVTYFFNGGLEKPFEGEVRELIPSPKVATYDQAPAMSAAAVTTSVCGAIEQGIYSLVVVNYANPDMVGHTGILDAAMKAVETVDLCLAKLLSSVNKLGGTVLITADHGNAETMVDESGNPWTAHTTNPVPLILIEGEGRKIPGHGGDVQLRDDGRLADIAPTILEILSIPVPVEMTGRSLIKPAEVEIKASRTPVRISL |
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length532
- Mass (Da)58,183
- Last updated2008-03-18 v1
- Checksum5121786BBEB39017
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP009552 EMBL· GenBank· DDBJ | BAG03059.1 EMBL· GenBank· DDBJ | Genomic DNA |