A0A7Z2K699 · A0A7Z2K699_9BACI
- ProteinPyrroline-5-carboxylate reductase
- GeneproC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids278 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic activity
- L-proline + NAD+ = 1-pyrroline-5-carboxylate + 2 H+ + NADH
Pathway
Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | pyrroline-5-carboxylate reductase activity | |
Biological Process | L-proline biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyrroline-5-carboxylate reductase
- EC number
- Short namesP5C reductase ; P5CR
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionA0A7Z2K699
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-97 | Pyrroline-5-carboxylate reductase catalytic N-terminal | ||||
Sequence: KIGVIGTGNMGTILVSSFIDSCAVIPSHLTIVNRSSEKASKLKQQYPSLNVVKSADEVVKKSDMIFICVKPHEYFPLFKKIRSNLKQQQLIVSITS | ||||||
Domain | 162-262 | Pyrroline-5-carboxylate reductase dimerisation | ||||
Sequence: TRVSSDIVSCGPAFLSYLIQQFIEGAVTETNISNEQATILATEMLIGMGKLLEKDYFSLETLQRKVTVKGGVTGEGLKVLEAETGEMFHHLIQSTHRKFKE |
Sequence similarities
Belongs to the pyrroline-5-carboxylate reductase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length278
- Mass (Da)30,757
- Last updated2021-06-02 v1
- Checksum52B77D20B140DD0E