A0A0K1P8D3 · A0A0K1P8D3_9BACT
- ProteinAcetylornithine aminotransferase
- GeneargD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids398 (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
- N2-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
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 | 106-107 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: GA | ||||||
Binding site | 138 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 141 | N2-acetyl-L-ornithine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 223-226 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: DEVQ | ||||||
Binding site | 280 | N2-acetyl-L-ornithine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 281 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | identical protein binding | |
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 > Myxococcota > Myxococcia > Myxococcales > Cystobacterineae > Vulgatibacteraceae > Vulgatibacter
Accessions
- Primary accessionA0A0K1P8D3
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 252 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Structure
Sequence
- Sequence statusComplete
- Length398
- Mass (Da)42,912
- Last updated2015-11-11 v1
- ChecksumE11768BA2B12A3FF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP012332 EMBL· GenBank· DDBJ | AKU89775.1 EMBL· GenBank· DDBJ | Genomic DNA |