A0A161HS49 · A0A161HS49_9EUGL
- Proteinphosphoglycerate mutase (2,3-diphosphoglycerate-independent)
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids551 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score2/5
Function
Cofactor
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 | 22 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Active site | 73 | Phosphoserine intermediate | |||
Binding site | 73 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 134 | substrate | |||
Binding site | 164-165 | substrate | |||
Binding site | 201 | substrate | |||
Binding site | 208 | substrate | |||
Binding site | 281-284 | substrate | |||
Binding site | 356 | substrate | |||
Binding site | 424 | Mn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 428 | Mn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 465 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 466 | Mn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 495 | Mn2+ 1 (UniProtKB | ChEBI) | |||
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 namephosphoglycerate mutase (2,3-diphosphoglycerate-independent)
- EC number
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Discoba > Euglenozoa > Kinetoplastea > Prokinetoplastina > Ichthyobodonidae > Perkinsela
Accessions
- Primary accessionA0A161HS49
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 14-538 | Metalloenzyme | |||
Domain | 93-317 | BPG-independent PGAM N-terminal | |||
Sequence similarities
Belongs to the BPG-independent phosphoglycerate mutase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length551
- Mass (Da)60,811
- Last updated2016-07-06 v1
- ChecksumDECB96E363415B88
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KU609021 EMBL· GenBank· DDBJ | ANB27667.1 EMBL· GenBank· DDBJ | mRNA |