A0A218Q112 · A0A218Q112_9CYAN
- Protein(S)-8-amino-7-oxononanoate synthase BioU
- GenebioU
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids334 (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 | 16-20 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 61 | NAD+ (UniProtKB | ChEBI) | |||
Active site | 127 | Nucleophile | |||
Binding site | 193-194 | NAD+ (UniProtKB | ChEBI) | |||
Active site | 197 | Proton acceptor | |||
Active site | 201 | Proton donor and proton acceptor | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | NAD binding | |
Molecular Function | NADP binding | |
Molecular Function | oxidoreductase activity | |
Molecular Function | transaminase activity | |
Biological Process | amino acid metabolic process | |
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 lineageBacteria > Cyanobacteriota > Cyanophyceae > Nostocales > Aphanizomenonaceae > Nodularia
Accessions
- Primary accessionA0A218Q112
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 127 | Allysine | |||
Interaction
Subunit
Monomer.
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length334
- Mass (Da)35,750
- Last updated2017-09-27 v1
- Checksum95579AC9DC9BF0E9
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BDUB01000001 EMBL· GenBank· DDBJ | GAX35562.1 EMBL· GenBank· DDBJ | Genomic DNA |