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C0QVM0 (BIOB_BRAHW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Biotin synthase

EC=2.8.1.6
Gene names
Name:bioB
Ordered Locus Names:BHWA1_02062
OrganismBrachyspira hyodysenteriae (strain ATCC 49526 / WA1) [Complete proteome] [HAMAP]
Taxonomic identifier565034 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesBrachyspiraceaeBrachyspira

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism By similarity. HAMAP-Rule MF_01694

Catalytic activity

Dethiobiotin + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine. HAMAP-Rule MF_01694

Cofactor

Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.

Binds 1 2Fe-2S cluster. The cluster is coordinated with 3 cysteines and 1 arginine By similarity.

Pathway

Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2. HAMAP-Rule MF_01694

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01694

Sequence similarities

Belongs to the radical SAM superfamily. Biotin synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 333333Biotin synthase HAMAP-Rule MF_01694
PRO_0000381243

Sites

Metal binding721Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding761Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding791Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1161Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1481Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2081Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2781Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
C0QVM0 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: D8E04E7D9B4F64EA

FASTA33337,263
        10         20         30         40         50         60 
MSNIDLIIKK EISLDELREK IIKGYDITKE EAMQLVEAPL EDLCSVANEI RKYFCSNTFD 

        70         80         90        100        110        120 
MCSIINAKSG KCSENCKFCA QSSHYDTKCD EYDILDKEKI LEQGKSDFNK GVLRYSIVTS 

       130        140        150        160        170        180 
GRALYGKEID EVYDAIETLN KETDGYICAS LGLLDEEGFN KMKNAGLKRV HNNLEASRNF 

       190        200        210        220        230        240 
FSKVCTTHTY DDKINAIKAA QKAGMVVCSG GIMGMGETWE DRIDMAIELR ELGIMSIPVN 

       250        260        270        280        290        300 
MLNPIASTPF ENIEPLTEDD MRRIVAIYRF INPRAFIRLA GGRGLMKDKG KSCFLSGANA 

       310        320        330 
AITGDMLTTA GISIETDKKM VEELGYKIEL KED 

« Hide

References

[1]"Genome sequence of the pathogenic intestinal spirochete Brachyspira hyodysenteriae reveals adaptations to its lifestyle in the porcine large intestine."
Bellgard M.I., Wanchanthuek P., La T., Ryan K., Moolhuijzen P., Albertyn Z., Shaban B., Motro Y., Dunn D.S., Schibeci D., Hunter A., Barrero R., Phillips N.D., Hampson D.J.
PLoS ONE 4:E4641-E4641(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49526 / WA1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001357 Genomic DNA. Translation: ACN84521.1.
RefSeqYP_002722225.1. NC_012225.1.

3D structure databases

ProteinModelPortalC0QVM0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING565034.BHWA1_02062.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACN84521; ACN84521; BHWA1_02062.
GeneID7667153.
KEGGbhy:BHWA1_02062.
PATRIC21182176. VBIBraHyo62857_2008.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239958.
KOK01012.
OMANCRFCAQ.
OrthoDBEOG622PMP.
ProtClustDBCLSK2810438.

Enzyme and pathway databases

BioCycBHYO565034:GJI7-2049-MONOMER.
UniPathwayUPA00078; UER00162.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01694. BioB.
InterProIPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR002684. Biotin_synth/BioAB.
IPR024177. Biotin_synthase.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
[Graphical view]
PfamPF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFPIRSF001619. Biotin_synth. 1 hit.
SMARTSM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00433. bioB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBIOB_BRAHW
AccessionPrimary (citable) accession number: C0QVM0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 5, 2009
Last modified: February 19, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways