A0A517XUC4 · A0A517XUC4_9BACT
- ProteinMultifunctional fusion protein
- GenebioA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids641 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
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
- (7R,8S)-7,8-diammoniononanoate + CO2 + ATP = (4R,5S)-dethiobiotin + ADP + phosphate + 3 H+
Cofactor
Protein has several cofactor binding sites:
Pathway
Cofactor biosynthesis; biotin biosynthesis; 7,8-diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1.
Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 16 | Mg2+ (UniProtKB | ChEBI) | |||
Active site | 34 | ||||
Binding site | 38 | substrate | |||
Binding site | 42 | ATP (UniProtKB | ChEBI) | |||
Binding site | 42 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 99 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 99-102 | ATP (UniProtKB | ChEBI) | |||
Site | 237 | Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM | |||
Binding site | 272 | substrate | |||
Binding site | 333-334 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 366 | substrate | |||
Binding site | 454 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 483 | substrate | |||
Binding site | 517 | substrate | |||
Binding site | 518-519 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 606 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity | |
Molecular Function | ATP binding | |
Molecular Function | dethiobiotin synthase activity | |
Molecular Function | magnesium ion binding | |
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 nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameAdenosylmethionine-8-amino-7-oxononanoate aminotransferase
- EC number
- Alternative names
- Recommended nameATP-dependent dethiobiotin synthetase BioD
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Planctomycetota > Planctomycetia > Gemmatales > Gemmataceae > Urbifossiella
Accessions
- Primary accessionA0A517XUC4
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 483 | N6-(pyridoxal phosphate)lysine | |||
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length641
- Mass (Da)68,127
- Last updated2019-10-16 v1
- ChecksumAACDB330964E960D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP036273 EMBL· GenBank· DDBJ | QDU21100.1 EMBL· GenBank· DDBJ | Genomic DNA |