A0A955S3P8 · A0A955S3P8_UNCOM
- ProteinMultifunctional fusion protein
- GenebioA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids667 (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 + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 H+ + phosphate
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 | 11-16 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DVGKTI | ||||||
Binding site | 15 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Active site | 36 | |||||
Sequence: K | ||||||
Binding site | 44 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 44 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 105 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 105-108 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EGAG | ||||||
Binding site | 165-166 | ATP (UniProtKB | ChEBI) | ||||
Sequence: SE | ||||||
Site | 243 | Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM | ||||
Sequence: F | ||||||
Binding site | 340-341 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: GS | ||||||
Binding site | 373 | substrate | ||||
Sequence: Y | ||||||
Binding site | 472 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 501 | substrate | ||||
Sequence: K | ||||||
Binding site | 536 | substrate | ||||
Sequence: G | ||||||
Binding site | 537-538 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: HT | ||||||
Binding site | 631 | substrate | ||||
Sequence: R |
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
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
- Strain
- Taxonomic lineageBacteria > Candidatus Omnitrophota
Accessions
- Primary accessionA0A955S3P8
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 501 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length667
- Mass (Da)74,919
- Last updated2023-02-22 v1
- ChecksumF27856AA2D6103A8