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B9IWX7 (BIOB_BACCQ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 38. 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:BCQ_3904
OrganismBacillus cereus (strain Q1) [Complete proteome] [HAMAP]
Taxonomic identifier361100 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length332 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 – 332332Biotin synthase HAMAP-Rule MF_01694
PRO_0000381224

Sites

Metal binding711Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding751Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding781Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1151Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1471Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2071Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2771Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
B9IWX7 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 434960BB38A893C3

FASTA33236,952
        10         20         30         40         50         60 
MKQVQTKRDW KKLAYDVVEE KVITKEDAIA ILEADDTEIL EIMNAAYIIR HHHFGKKVKL 

        70         80         90        100        110        120 
NMIINTKSGL CPEDCGYCSQ SIISEAPIDK YAWLTQEKIV EGAHEAIRRK AGTYCIVASG 

       130        140        150        160        170        180 
RRPTDKEVNH VIGAVKEIRE TTDLKICCCL GFLNEDQAGR LAEAGVHRYN HNLNTHANNY 

       190        200        210        220        230        240 
ESICSTHTYD DRVDTVQKAK QAGISPCSGA IFGMGETIEE RAEIAFELQR IDADSIPCNF 

       250        260        270        280        290        300 
LVAVKGTPLE GQKELTPVEC LKVLAMMRFV NPTKEIRISG GREINLRSVQ PIGLFAANSI 

       310        320        330 
FVGDYLTTAG QEPTADWGMI EDLGFEIEEC AL 

« Hide

References

[1]"Complete genome sequence of the extremophilic Bacillus cereus strain Q1 with industrial applications."
Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X., Xue Y., Zhu Y., Jin Q.
J. Bacteriol. 191:1120-1121(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Q1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000227 Genomic DNA. Translation: ACM14332.1.
RefSeqYP_002531621.1. NC_011969.1.

3D structure databases

ProteinModelPortalB9IWX7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING361100.BCQ_3904.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM14332; ACM14332; BCQ_3904.
GeneID7376676.
KEGGbcq:BCQ_3904.
PATRIC18915550. VBIBacCer120424_3943.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239958.
KOK01012.
OMADETQALC.
OrthoDBEOG622PMP.

Enzyme and pathway databases

BioCycBCER361100:GJ7M-3892-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_BACCQ
AccessionPrimary (citable) accession number: B9IWX7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 38 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