A0A506VFH7 · A0A506VFH7_9GAMM
- ProteinAcetylornithine/succinyldiaminopimelate aminotransferase
- GeneastC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids405 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Involved in both the arginine and lysine biosynthetic pathways.
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.
Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 2/3.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 105-106 | 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: T | ||||||
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 | |
Molecular Function | succinyldiaminopimelate transaminase activity | |
Biological Process | arginine biosynthetic process | |
Biological Process | arginine catabolic process | |
Biological Process | lysine biosynthetic process via diaminopimelate |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAcetylornithine/succinyldiaminopimelate aminotransferase
- EC number
- Short namesACOAT ; DapATase ; Succinyldiaminopimelate transferase
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Erwiniaceae > Mixta
Accessions
- Primary accessionA0A506VFH7
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
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length405
- Mass (Da)43,228
- Last updated2019-09-18 v1
- ChecksumE4E0A67FBD3997B0