B7MI93 · ARGE_ECO45
- ProteinAcetylornithine deacetylase
- GeneargE
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids383 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the hydrolysis of the amide bond of N2-acetylated L-amino acids. Cleaves the acetyl group from N-acetyl-L-ornithine to form L-ornithine, an intermediate in L-arginine biosynthesis pathway, and a branchpoint in the synthesis of polyamines.
Catalytic activity
- N2-acetyl-L-ornithine + H2O = L-ornithine + acetate
Cofactor
Protein has several cofactor binding sites:
Co2+ (UniProtKB | Rhea| CHEBI:48828 )
Note: Binds 2 Zn2+ or Co2+ ions per subunit.
Pathway
Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine from N2-acetyl-L-ornithine (linear): step 1/1.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 80 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Active site | 82 | ||||
Binding site | 112 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 112 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Active site | 144 | ||||
Binding site | 145 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 169 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 355 | Zn2+ 2 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | acetylornithine deacetylase activity | |
Molecular Function | zinc ion binding | |
Biological Process | arginine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAcetylornithine deacetylase
- EC number
- Short namesAO ; Acetylornithinase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionB7MI93
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_1000137061 | 1-383 | Acetylornithine deacetylase | ||
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length383
- Mass (Da)42,266
- Last updated2009-02-10 v1
- MD5 Checksum38E24125F7267E16FEF3F44402F8D42B
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CU928161 EMBL· GenBank· DDBJ | CAR05591.1 EMBL· GenBank· DDBJ | Genomic DNA |