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B2TL73 (BIOB_CLOBB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. 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:CLL_A0721
OrganismClostridium botulinum (strain Eklund 17B / Type B) [Complete proteome] [HAMAP]
Taxonomic identifier508765 [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_0000381312

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
B2TL73 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 0F47A586ECE2BC74

FASTA31835,497
        10         20         30         40         50         60 
MNIVDKFKEK ILSGELISKK EAMILSKENI DELASAANDI RMSLCGKEFN LCTIINGKSG 

        70         80         90        100        110        120 
RCGENCKYCA QSVYFKTDIE EYNLLDSESI ITSAISNYNN GVHRFSVVTS GKKITNKEVH 

       130        140        150        160        170        180 
TVCKTYSELK DKCDIKLCAS HGLLNYEELV KLKESGVIRY HNNLETSRNF FSNICTTHTF 

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

       250        260        270        280        290        300 
ENQEKLSYDE ITKTFALFRF ILPKKQIRLA GGRALLNDKG ERLMKSGVNA AISGDMLTTS 

       310 
GIKTFDDIKM IKELGFEV 

« Hide

References

[1]"Complete sequence of Clostridium botulinum strain Eklund."
Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Eklund 17B / Type B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001056 Genomic DNA. Translation: ACD21960.1.
RefSeqYP_001884922.1. NC_010674.1.

3D structure databases

ProteinModelPortalB2TL73.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING508765.CLL_A0721.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD21960; ACD21960; CLL_A0721.
GeneID6293260.
KEGGcbk:CLL_A0721.
PATRIC19394287. VBICloBot123574_0655.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239958.
KOK01012.
OMAFEIANEC.
OrthoDBEOG622PMP.

Enzyme and pathway databases

BioCycCBOT508765:GJ4H-715-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_CLOBB
AccessionPrimary (citable) accession number: B2TL73
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: July 1, 2008
Last modified: May 14, 2014
This is version 42 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