A0A1Q7F628 · A0A1Q7F628_9ARCH
- ProteinBiotin synthase
- GenebioB
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids323 (go to sequence)
- Protein existenceInferred from homology
- 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 | 66 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 70 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 73 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 110 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 202 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 272 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: K |
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
- Taxonomic lineageArchaea > Nitrososphaerota
Accessions
- Primary accessionA0A1Q7F628
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 51-277 | Radical SAM core | ||||
Sequence: YTVDVEALINAKSGRCPEDCSFCAQSSFYDTGITKYPLLPKDVLVENAKKAKESGATSFCLVCAYREPPEKDFQQICETIAEIRSRVDIEVNVSLGFMTPARARRLKEYGVKRYNHNLETSESYFPKICKTHDFADRVNTARIVKEAGLELCSGGIIGMGEGKNERLELAFSLASLSPDEVPINILIGREGTPMAAFEPIDPLEAIKTIAVWRFIMPKTILKIAGGR |
Sequence similarities
Belongs to the radical SAM superfamily. Biotin synthase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length323
- Mass (Da)35,225
- Last updated2017-04-12 v1
- ChecksumD26AB757AE903665