M0FPE1 · M0FPE1_9EURY
- ProteinBiotin synthase
- GenebioB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids352 (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 | 68 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 72 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 75 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 208 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 280 | [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 lineageArchaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Haloferacaceae > Haloferax
Accessions
- Primary accessionM0FPE1
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 50-276 | Radical SAM core | ||||
Sequence: RSDGTVDACSIVNAKAGDCAEDCGFCAQSAHFDTGIETHGFLGPEAVLDAARRAERDGAQRFGIVVAEKGVSKERRPDEWAEVLAAIRLVRDETSVEIDASLGLLTEEEARILSAEGVNHYNHNIETSPRYFDEVVGTHDFEDRLVTLRRAKDAGMDLCAGVILGMGETPADRVDAALELQKVGVESLPVNVLNPVPGTPLGDADHADITTTELVKTVAVYRLLHPD |
Sequence similarities
Belongs to the radical SAM superfamily. Biotin synthase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length352
- Mass (Da)37,836
- Last updated2013-04-03 v1
- ChecksumAE73DDD414282AE9
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AOLE01000035 EMBL· GenBank· DDBJ | ELZ61143.1 EMBL· GenBank· DDBJ | Genomic DNA |