Q8X4S6 · ARGD_ECO57
- ProteinAcetylornithine/succinyldiaminopimelate aminotransferase
- GeneargD
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids406 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Involved in both the arginine and lysine biosynthetic pathways.
Miscellaneous
The reaction catalyzed by ACOAT is highly reversible. This enzyme may also transaminate ornithine (By similarity).
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 | 108-109 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: GT | ||||||
Binding site | 141 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 144 | N2-acetyl-L-ornithine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 226-229 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: DEVQ | ||||||
Binding site | 283 | N2-acetyl-L-ornithine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 284 | 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 | |
Molecular Function | succinyldiaminopimelate transaminase activity | |
Biological Process | arginine biosynthetic 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
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionQ8X4S6
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000112745 | 2-406 | Acetylornithine/succinyldiaminopimelate aminotransferase | |||
Sequence: AIEQTAITRATFDEVILPIYAPAEFIPVKGQGSRIWDQQGKEYVDFAGGIAVTALGHCHPALVNALKTQGETLWHISNVFTNEPALRLGRKLIEATFAERVVFMNSGTEANETAFKLARHYACVRHSPFKTKIIAFHNAFHGRSLFTVSVGGQPKYSDGFGPKPSDIIHVPFNDLHAVKAVMDDHTCAVVVEPIQGEGGVTAATPEFLQGLRELCDQHQALLVFDEVQCGMGRTGDLFAYMHYGVTPDILTSAKALGGGFPISAMLTTAEIASAFHPGSHGSTYGGNPLACAVAGAAFDIINTPEVLEGIQAKRQRFVDHLQKIDQQYDVFSDIRGMGLLIGAELKPQYKGQARDFLYAGAEAGVMVLNAGPDVMRFAPSLVVEDADIDEGMQRFAHAVAKVVGA | ||||||
Modified residue | 255 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Structure
Sequence
- Sequence statusComplete
- Length406
- Mass (Da)43,755
- Last updated2007-01-23 v3
- Checksum90C65E1438466979
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE005174 EMBL· GenBank· DDBJ | AAG58467.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BA000007 EMBL· GenBank· DDBJ | BAB37633.1 EMBL· GenBank· DDBJ | Genomic DNA |