A0A292IIU6 · A0A292IIU6_9MOLU
- Protein2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- GenegpmI
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids511 (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 | 14 | 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 | 155-156 | substrate | ||||
Sequence: RD | ||||||
Binding site | 186 | substrate | ||||
Sequence: R | ||||||
Binding site | 192 | substrate | ||||
Sequence: R | ||||||
Binding site | 261-264 | substrate | ||||
Sequence: RPDR | ||||||
Binding site | 335 | substrate | ||||
Sequence: K | ||||||
Binding site | 401 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 405 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 442 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 443 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 460 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Mycoplasmatota > Mollicutes > Mycoplasmataceae > Mycoplasma
Accessions
- Primary accessionA0A292IIU6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 7-496 | Metalloenzyme | ||||
Sequence: KVLLMILDGYGVCKEVKGNAVLNAKTPHLDRLQSAEFPHTLLAASGQAVGLPEGQIGNSEVGHLNIGAGRIIYTGLSLINKAISDHSFYENLALNQAVAHTKKHDSKLHVMGLVSHGGVHSLLNHIVATLKLAHQASVRTVLHIFGDGRDVPPESLLHDLEQLLPTLKELNVTIGMISGRYYAMDRDQRWERIDLAYDALLHGAQITFNDPIQYIKESYAKNESDEFIKPATNAVTDLQTITLQDHDAVVFANFRPDRARQLSHYIYGSNYYQVQPKMRRDGLFFVTMMQYEGIVPSAVAFPPETFKNTLGEVIANAGLKQLRISETEKYAHVTFFFDGGKEVDYPKETKNLIPSNRSVPTYDLVPQMSCKEITDALLPTLGKYELTVLNYANPDMVGHTGKYLPTVQALEMLDVQIGRVIDACIQNNVTLFFTADHGNAEVMLDDKNEPVTKHSTNPVPFTCTDKNIKLLDGGKLANVAPTILDYMEIE | ||||||
Domain | 85-298 | BPG-independent PGAM N-terminal | ||||
Sequence: INKAISDHSFYENLALNQAVAHTKKHDSKLHVMGLVSHGGVHSLLNHIVATLKLAHQASVRTVLHIFGDGRDVPPESLLHDLEQLLPTLKELNVTIGMISGRYYAMDRDQRWERIDLAYDALLHGAQITFNDPIQYIKESYAKNESDEFIKPATNAVTDLQTITLQDHDAVVFANFRPDRARQLSHYIYGSNYYQVQPKMRRDGLFFVTMMQYE |
Sequence similarities
Belongs to the BPG-independent phosphoglycerate mutase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length511
- Mass (Da)56,840
- Last updated2017-12-20 v1
- ChecksumD683E6C6367A7B1B
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
HG937516 EMBL· GenBank· DDBJ | CDN40482.1 EMBL· GenBank· DDBJ | Genomic DNA |