A0A202E7M9 · A0A202E7M9_9EURY
- Protein(S)-8-amino-7-oxononanoate synthase BioU
- GenebioU
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids355 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
A 'suicide' enzyme that participates in biotin synthesis. Catalyzes the formation of (S)-8-amino-7-oxononanoate (DAN-carbamic acid) from (7R,8S)-8-amino-7-(carboxyamino)nonanoate (DAN), a function equivalent to the cannonical BioA reaction and the first half-reaction of BioD. The cellular requirement for biotin is thought be low enough that this single turnover enzyme supplies a sufficient amount of the cofactor. Overall it catalyzes three reactions: formation of a covalent linkage with 8-amino-7-oxononanoate to yield a BioU-DAN conjugate at the epsilon-amino group of Lys124 of BioU using NAD(P)H, carboxylation of the conjugate to form BioU-DAN-carbamic acid, and release of DAN-carbamic acid using NAD(P)+.
Miscellaneous
In cannonical biotin synthesis a pimeloyl-conjugate is transformed into biotin by the subsequent action of BioF, BioA, BioD and BioB. This enzyme replaces BioA and performs the first half-reaction of BioD.
Catalytic activity
- (8S)-8-amino-7-oxononanoate + L-lysyl-[protein] + CO2 = (S)-2-amino-6-oxohexanoyl-[protein] + (7R,8S)-8-amino-7-(carboxyamino)nonanoate + 2 H+
- (8S)-8-amino-7-oxononanoate + L-lysyl-[protein] + NADH + H+ = N6-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysyl-[protein] + NAD+ + H2O
- (8S)-8-amino-7-oxononanoate + L-lysyl-[protein] + NADPH + H+ = N6-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysyl-[protein] + NADP+ + H2O
- N6-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysyl-[protein] + CO2 + NAD+ + H2O = (S)-2-amino-6-oxohexanoyl-[protein] + (7R,8S)-8-amino-7-(carboxyamino)nonanoate + NADH + 3 H+
- N6-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysyl-[protein] + CO2 + NADP+ + H2O = (S)-2-amino-6-oxohexanoyl-[protein] + (7R,8S)-8-amino-7-(carboxyamino)nonanoate + NADPH + 3 H+
Pathway
Cofactor biosynthesis; biotin biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 10-14 | NAD+ (UniProtKB | ChEBI) | |||
Active site | 149 | Nucleophile | |||
Binding site | 216-217 | NAD+ (UniProtKB | ChEBI) | |||
Active site | 220 | Proton acceptor | |||
Active site | 224 | Proton donor and proton acceptor | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | NAD binding | |
Molecular Function | NADP binding | |
Molecular Function | transaminase activity | |
Biological Process | biotin biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name(S)-8-amino-7-oxononanoate synthase BioU
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Natrialbaceae > Natronolimnobius
Accessions
- Primary accessionA0A202E7M9
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 149 | Allysine | |||
Interaction
Subunit
Monomer.
Structure
Sequence
- Sequence statusComplete
- Length355
- Mass (Da)37,376
- Last updated2017-09-27 v1
- MD5 Checksum0A4E783C7648C2535A05903CC5EF92AF
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 72-86 | Polar residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
MWPH01000002 EMBL· GenBank· DDBJ | OVE84271.1 EMBL· GenBank· DDBJ | Genomic DNA |