I0BAC6 · I0BAC6_9BACL
- Protein2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- GenegpmI
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids514 (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 | 13 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 63 | Phosphoserine intermediate | ||||
Sequence: S | ||||||
Binding site | 63 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 124 | substrate | ||||
Sequence: H | ||||||
Binding site | 154-155 | substrate | ||||
Sequence: RD | ||||||
Binding site | 186 | substrate | ||||
Sequence: R | ||||||
Binding site | 192 | substrate | ||||
Sequence: R | ||||||
Binding site | 262-265 | substrate | ||||
Sequence: RPDR | ||||||
Binding site | 337 | substrate | ||||
Sequence: K | ||||||
Binding site | 404 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 408 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 445 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 446 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 463 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H |
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
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Paenibacillaceae > Paenibacillus
Accessions
- Primary accessionI0BAC6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-499 | Metalloenzyme | ||||
Sequence: KPVAVIILDGFGLRGDVQGNAVAQAKKPNYERYWNEFPHTTLTACGEAVGLPEGQMGNSEVGHLNIGAGRIVYQDLTRISKSIRDGEFYENETILGAIRHAKDNGKKLHLYGLLSDGGVHSHIEHLFALLDVCKKESFEEVYIHAFLDGRDVAPDSAAGYMERLLKKIADVGVGRIATVQGRYYAMDRDKRWERTEKSYRAMVYGDGPTFEDPMNAIQESYIRSVYDEFVMPTVIVKPDHTPVGLVESGDSVVFFNFRPDRAIQLSQVFTNSDFRGFDRGDKAPTDLYYVCLTLFSETVGGYVAYKPKNLDNTLGEVLAQNDLKQLRIAETEKYPHVTFFFSGGRDVELPGETRILIPSPKVATYDLQPEMSAYELAAAAVAEIEAERQDVIILNFANPDMVGHSGLLEPTIKAVEATDECLGKVVDAIIAKGGVALITADHGNADVVTNPDGSRNTAHTTNPVPFIVTDGRVTLRNDGILADIAPTVLDLLGVS | ||||||
Domain | 83-300 | BPG-independent PGAM N-terminal | ||||
Sequence: ISKSIRDGEFYENETILGAIRHAKDNGKKLHLYGLLSDGGVHSHIEHLFALLDVCKKESFEEVYIHAFLDGRDVAPDSAAGYMERLLKKIADVGVGRIATVQGRYYAMDRDKRWERTEKSYRAMVYGDGPTFEDPMNAIQESYIRSVYDEFVMPTVIVKPDHTPVGLVESGDSVVFFNFRPDRAIQLSQVFTNSDFRGFDRGDKAPTDLYYVCLTLFS |
Sequence similarities
Belongs to the BPG-independent phosphoglycerate mutase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length514
- Mass (Da)56,304
- Last updated2012-06-13 v1
- Checksum7E0E8A9BD4DF772E
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP003422 EMBL· GenBank· DDBJ | AFH59323.1 EMBL· GenBank· DDBJ | Genomic DNA |