A0A0H2YX35 · A0A0H2YX35_ECOK1
- ProteinAdenosylmethionine-8-amino-7-oxononanoate aminotransferase
- GenebioA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids429 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor.
Catalytic activity
- (8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine = S-adenosyl-4-methylsulfanyl-2-oxobutanoate + (7R,8S)-7,8-diammoniononanoate
Cofactor
Pathway
Cofactor biosynthesis; biotin biosynthesis; 7,8-diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1.
Features
Showing features for site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Site | 17 | Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM | |||
Binding site | 52 | substrate | |||
Binding site | 112-113 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 144 | substrate | |||
Binding site | 245 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 274 | substrate | |||
Binding site | 307 | substrate | |||
Binding site | 308-309 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 391 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity | |
Molecular Function | pyridoxal phosphate binding | |
Biological Process | biotin biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdenosylmethionine-8-amino-7-oxononanoate aminotransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionA0A0H2YX35
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 274 | N6-(pyridoxal phosphate)lysine | |||
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length429
- Mass (Da)47,229
- Last updated2015-09-16 v1
- Checksum0E6C7784C13AC22E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000468 EMBL· GenBank· DDBJ | ABJ00156.1 EMBL· GenBank· DDBJ | Genomic DNA |