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B2V167 (BIOB_CLOBA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:CLH_0685
OrganismClostridium botulinum (strain Alaska E43 / Type E3) [Complete proteome] [HAMAP]
Taxonomic identifier508767 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length318 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 – 318318Biotin synthase HAMAP-Rule MF_01694
PRO_0000381311

Sites

Metal binding621Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding661Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding691Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1061Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1381Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1981Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2681Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
B2V167 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 90ED5AD2D859FAFF

FASTA31835,486
        10         20         30         40         50         60 
MNIIDRFKEK ILSGELISKK EAIILSKENV DKLASAANDI RMSLCGKKFN LCTIINGKSG 

        70         80         90        100        110        120 
RCGENCKYCA QSVYFKTDIE EYNLLDSESI ITSAISNYNS GVHRFSVVTS GKKLTNKEID 

       130        140        150        160        170        180 
IVCKTYSEVQ EKCAIKLCAS HGLLNYEELV KLKESGVIRY HNNLETSRRF FSNICTTHTF 

       190        200        210        220        230        240 
DEKINTIKNA LKAGLQVCSG GIIGLGETME DRIDMAFTLR ELNVDSIPIN ILNPIKGTAL 

       250        260        270        280        290        300 
ENQEKLSYDE ITKTFALFRF ILPEKQIRLA GGRALLNDKG ERLMKSGVNS AISGDMLTTS 

       310 
GIKTFDDIKM IKELGFEV 

« Hide

References

[1]"Complete genome sequence of Clostridium botulinum E3 str. Alaska E43."
Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Alaska E43 / Type E3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001078 Genomic DNA. Translation: ACD51519.1.
RefSeqYP_001920080.1. NC_010723.1.

3D structure databases

ProteinModelPortalB2V167.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING508767.CLH_0685.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD51519; ACD51519; CLH_0685.
GeneID6319955.
KEGGcbt:CLH_0685.
PATRIC19417632. VBICloBot115804_0614.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239958.
KOK01012.
OMANCRFCAQ.
OrthoDBEOG622PMP.
ProtClustDBCLSK972180.

Enzyme and pathway databases

BioCycCBOT508767:GHKO-680-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_CLOBA
AccessionPrimary (citable) accession number: B2V167
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: July 1, 2008
Last modified: February 19, 2014
This is version 43 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