A0A0C1YDA6 · A0A0C1YDA6_9CYAN
- Protein(S)-8-amino-7-oxononanoate synthase BioU
- GenebioU
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids336 (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 + CO2 + L-lysyl-[protein] = (7R,8S)-8-amino-7-(carboxyamino)nonanoate + (S)-2-amino-6-oxohexanoyl-[protein] + 2 H+
- (8S)-8-amino-7-oxononanoate + H+ + L-lysyl-[protein] + NADH = H2O + N6-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysyl-[protein] + NAD+
- (8S)-8-amino-7-oxononanoate + H+ + L-lysyl-[protein] + NADPH = H2O + N6-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysyl-[protein] + NADP+
- CO2 + H2O + N6-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysyl-[protein] + NAD+ = (7R,8S)-8-amino-7-(carboxyamino)nonanoate + (S)-2-amino-6-oxohexanoyl-[protein] + 3 H+ + NADH
- CO2 + H2O + N6-[(2S,3R)-2-amino-8-carboxyoctan-3-yl]-L-lysyl-[protein] + NADP+ = (7R,8S)-8-amino-7-(carboxyamino)nonanoate + (S)-2-amino-6-oxohexanoyl-[protein] + 3 H+ + NADPH
Pathway
Cofactor biosynthesis; biotin biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 18-22 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GFGGL | ||||||
Binding site | 63 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Active site | 129 | Nucleophile | ||||
Sequence: K | ||||||
Binding site | 195-196 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: AT | ||||||
Active site | 199 | Proton acceptor | ||||
Sequence: E | ||||||
Active site | 203 | Proton donor and proton acceptor | ||||
Sequence: H |
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 > Oscillatoriophycideae > Oscillatoriales > Oscillatoriaceae > Lyngbya
Accessions
- Primary accessionA0A0C1YDA6
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 129 | Allysine | ||||
Sequence: K |
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 14-74 | Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase C-terminal | ||||
Sequence: VGVLGFGGLGQAATRVLMPKTEMQLVAAADKQGYVYDARGLEPQTCIEAYRDRGSVGYVES |
Sequence similarities
Belongs to the BioU family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length336
- Mass (Da)35,979
- Last updated2015-04-01 v1
- Checksum4E986C76B31D1543