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Q818X3 (BIOB_BACCR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 81. 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:BC_4114
OrganismBacillus cereus (strain ATCC 14579 / DSM 31) [Reference proteome] [HAMAP]
Taxonomic identifier226900 [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_0000381225

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
Q818X3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: CF38BD68407C8FCE

FASTA33236,899
        10         20         30         40         50         60 
MKQVQTKRDW KKLAYDVVEE KMITKEDAIA ILEADDTEVL 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 HNLDTHANNY 

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

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

       310        320        330 
FVGDYLTTAG QEPTADWGMI ADLGFEIEEC AL 

« Hide

References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016877 Genomic DNA. Translation: AAP11033.1.
RefSeqNP_833832.1. NC_004722.1.

3D structure databases

ProteinModelPortalQ818X3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226900.BC4114.

Proteomic databases

PRIDEQ818X3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP11033; AAP11033; BC_4114.
GeneID1206459.
KEGGbce:BC4114.
PATRIC32604294. VBIBacCer54481_4250.

Phylogenomic databases

eggNOGCOG0502.
KOK01012.
OMACKEDCIF.
OrthoDBEOG622PMP.

Enzyme and pathway databases

BioCycBCER226900:GJEU-4110-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_BACCR
AccessionPrimary (citable) accession number: Q818X3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 81 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