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A7GSD8 (BIOB_BACCN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. 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:Bcer98_2813
OrganismBacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]
Taxonomic identifier315749 [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_0000381223

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
A7GSD8 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 536B7078184395D7

FASTA33237,185
        10         20         30         40         50         60 
MKQIQTKVDW KKIAFEGIEG KRITKEDALA ILEADDTEVL EIMNAAYMIR HHYFGKKVKL 

        70         80         90        100        110        120 
NMIINTKSGL CPEDCGYCSQ SIVSEAPIDK YAWLTQEKIV EGAHEAVRRK AGTYCIVASG 

       130        140        150        160        170        180 
RRPTDKEVNH VIGAVKEIKE TTDLKICCCL GFLNEDQAKR LAEAGVHRYN HNLNTHANHY 

       190        200        210        220        230        240 
DNICSTHTYD DRVDTVEKVK QAGISPCSGA IFGMGETKEE RVEIAFELQR LDADSIPCNF 

       250        260        270        280        290        300 
LVSVKGTPFE GRKELTPVEC LKILAMMRFV NPSKEIRISG GRELNLRSVQ PLGLFAANSI 

       310        320        330 
FVGDYLTTVG QESTADWEMI QDLGFEIEEC AL 

« Hide

References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NVH 391-98.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000764 Genomic DNA. Translation: ABS23046.1.
RefSeqYP_001376041.1. NC_009674.1.

3D structure databases

ProteinModelPortalA7GSD8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING315749.Bcer98_2813.

Proteomic databases

PRIDEA7GSD8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS23046; ABS23046; Bcer98_2813.
GeneID5343487.
KEGGbcy:Bcer98_2813.
PATRIC18934240. VBIBacCyt128034_2964.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239958.
KOK01012.
OMANCRFCAQ.
OrthoDBEOG622PMP.
ProtClustDBPRK06256.

Enzyme and pathway databases

BioCycBCYT315749:GH2A-2921-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_BACCN
AccessionPrimary (citable) accession number: A7GSD8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: September 11, 2007
Last modified: February 19, 2014
This is version 48 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