A5ZUL4 · A5ZUL4_9FIRM
- ProteinBiotin synthase
- GenebioB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids327 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Catalytic activity
- (4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
CHEBI:149473 + RHEA-COMP:14737 + 2 RHEA-COMP:10001 + 2 CHEBI:59789 = 2 CHEBI:17319 + RHEA-COMP:14739 + CHEBI:57586 + 2 CHEBI:57844 + 2 RHEA-COMP:10000
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.
Note: Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.
Note: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway
Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 62 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 62 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 66 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 66 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 68 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 69 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 69 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 74 | Fe3+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 106 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 138 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 163 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 165 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 198 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 233 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 268 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | biotin synthase activity | |
Molecular Function | iron ion binding | |
Biological Process | biotin biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBiotin synthase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Lachnospirales > Lachnospiraceae > Blautia
Accessions
- Primary accessionA5ZUL4
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 44-270 | Radical SAM core | ||||
Sequence: CIGDKVDLCSIINGRSGRCPEDCKYCAQSAHHHTSCEVYNFLPEEKILEACKMNESEGVDRFSIVTAGKALTGKEFDQAIHAYETMHRECKIDLCASMGFISAEQLHRLHEAGVTSYHHNIETSRRNFPNICTTHTYDMKIETLKKVKAEGMCACSGGIIGMGETWEDRLDMAISLAELGIDSIPINALMPIPGTPLEHLPELSEPDILRTIAFFRYINPEANIRLA |
Sequence similarities
Belongs to the radical SAM superfamily. Biotin synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length327
- Mass (Da)36,286
- Last updated2007-07-24 v1
- Checksum96AB0337ACCCD345
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAVO02000012 EMBL· GenBank· DDBJ | EDM86794.1 EMBL· GenBank· DDBJ | Genomic DNA |