A0A0H3F429 · A0A0H3F429_RAHSY
- ProteinAcetylornithine/succinyldiaminopimelate aminotransferase
- GeneargD
- 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
- 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.
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 | 107-108 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 140 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 143 | N2-acetyl-L-ornithine (UniProtKB | ChEBI) | |||
Binding site | 225-228 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 282 | N2-acetyl-L-ornithine (UniProtKB | ChEBI) | |||
Binding site | 283 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
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 | 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 > Yersiniaceae > Rahnella
Accessions
- Primary accessionA0A0H3F429
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 254 | N6-(pyridoxal phosphate)lysine | |||
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length405
- Mass (Da)43,541
- Last updated2015-09-16 v1
- Checksum5B7F8E0085E3700F
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP002505 EMBL· GenBank· DDBJ | ADW71915.1 EMBL· GenBank· DDBJ | Genomic DNA |