Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q731I2 (BIOB_BACC1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 77. 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:BCE_4184
OrganismBacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]
Taxonomic identifier222523 [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_0000381219

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
Q731I2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 4357805DB937F2A4

FASTA33236,980
        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 HNLNTHVNNY 

       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]"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10987.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017194 Genomic DNA. Translation: AAS43085.1.
RefSeqNP_980477.1. NC_003909.8.

3D structure databases

ProteinModelPortalQ731I2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING222523.BCE_4184.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS43085; AAS43085; BCE_4184.
GeneID2748937.
KEGGbca:BCE_4184.
PATRIC18857017. VBIBacCer118379_4007.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239958.
KOK01012.
OMATCENTLR.
OrthoDBEOG622PMP.

Enzyme and pathway databases

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_BACC1
AccessionPrimary (citable) accession number: Q731I2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 77 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