P18335 · ARGD_ECOLI
- ProteinAcetylornithine/succinyldiaminopimelate aminotransferase
- GeneargD
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids406 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
Catalytic activity
- 2-oxoglutarate + N2-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde
Cofactor
Note: Binds 1 pyridoxal phosphate per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.15 mM | N-acetylornithine | |||||
0.075 mM | N-succinyldiaminopimelate |
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 | 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 via ornithine | |
Biological Process | lysine biosynthetic process via diaminopimelate and N-succinyl-2-amino-6-ketopimelate |
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 accessionP18335
- Secondary accessions
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_0000112743 | 2-406 | Acetylornithine/succinyldiaminopimelate aminotransferase | |||
Sequence: AIEQTAITRATFDEVILPIYAPAEFIPVKGQGSRIWDQQGKEYVDFAGGIAVTALGHCHPALVNALKTQGETLWHISNVFTNEPALRLGRKLIEATFAERVVFMNSGTEANETAFKLARHYACVRHSPFKTKIIAFHNAFHGRSLFTVSVGGQPKYSDGFGPKPADIIHVPFNDLHAVKAVMDDHTCAVVVEPIQGEGGVTAATPEFLQGLRELCDQHQALLVFDEVQCGMGRTGDLFAYMHYGVTPDILTSAKALGGGFPISAMLTTAEIASAFHPGSHGSTYGGNPLACAVAGAAFDIINTPEVLEGIQAKRQRFVDHLQKIDQQYDVFSDIRGMGLLIGAELKPQYKGRARDFLYAGAEAGVMVLNAGPDVMRFAPSLVVEDADIDEGMQRFAHAVAKVVGA | ||||||
Modified residue | 255 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Proteomic databases
Structure
Sequence
- Sequence statusComplete
- Length406
- Mass (Da)43,767
- Last updated2007-01-23 v4
- Checksum645AA1EBCA442214
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 245-247 | in Ref. 1; AAA23480 | ||||
Sequence: GVT → ALA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M32796 EMBL· GenBank· DDBJ | AAA23480.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U18997 EMBL· GenBank· DDBJ | AAA58156.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC76384.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE77931.1 EMBL· GenBank· DDBJ | Genomic DNA |