A0AAC9IF71 · A0AAC9IF71_9BACI
- ProteinAcetylornithine aminotransferase
- GeneargD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids383 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Miscellaneous
May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis.
Catalytic activity
- 2-oxoglutarate + N2-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde
Cofactor
Note: Binds 1 pyridoxal phosphate per subunit.
Pathway
Amino-acid biosynthesis; L-arginine biosynthesis; N2-acetyl-L-ornithine from L-glutamate: step 4/4.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 95-96 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: GA | ||||||
Binding site | 122 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 125 | N2-acetyl-L-ornithine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 207-210 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: DEIQ | ||||||
Binding site | 264 | N2-acetyl-L-ornithine (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 265 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity | |
Molecular Function | pyridoxal phosphate binding | |
Biological Process | arginine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAcetylornithine aminotransferase
- EC number
- Short namesACOAT
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionA0AAC9IF71
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 236 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length383
- Mass (Da)40,935
- Last updated2024-05-29 v1
- Checksum50679F7C5971CEC5
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP017786 EMBL· GenBank· DDBJ | AOZ87701.1 EMBL· GenBank· DDBJ | Genomic DNA |