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P0A507 (BIOB_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. 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:Mb1615
OrganismMycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]
Taxonomic identifier233413 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length349 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 – 349349Biotin synthase HAMAP-Rule MF_01694
PRO_0000185558

Sites

Metal binding851Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding891Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding921Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1281Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1611Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2201Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2901Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A507 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: F3B0A5821B3F14A2

FASTA34937,550
        10         20         30         40         50         60 
MTQAATRPTN DAGQDGGNNS DILVVARQQV LQRGEGLNQD QVLAVLQLPD DRLEELLALA 

        70         80         90        100        110        120 
HEVRMRWCGP EVEVEGIISL KTGGCPEDCH FCSQSGLFAS PVRSAWLDIP SLVEAAKQTA 

       130        140        150        160        170        180 
KSGATEFCIV AAVRGPDERL MAQVAAGIEA IRNEVEINIA CSLGMLTAEQ VDQLAARGVH 

       190        200        210        220        230        240 
RYNHNLETAR SFFANVVTTH TWEERWQTLS MVRDAGMEVC CGGILGMGET LQQRAEFAAE 

       250        260        270        280        290        300 
LAELGPDEVP LNFLNPRPGT PFADLEVMPV GDALKAVAAF RLALPRTMLR FAGGREITLG 

       310        320        330        340 
DLGAKRGILG GINAVIVGNY LTTLGRPAEA DLELLDELQM PLKALNASL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequencing, and identification of Mycobacterium bovis BCG biotin biosynthetic genes by complementing two Mycobacterium smegmatis biotin mutants."
Yu S., Jacobs W.R. Jr.
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BCG / Pasteur.
[2]"The complete genome sequence of Mycobacterium bovis."
Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. expand/collapse author list , Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.
Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-935 / AF2122/97.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF041819 Genomic DNA. Translation: AAB96962.1.
BX248339 Genomic DNA. Translation: CAD96283.1.
RefSeqNP_855268.1. NC_002945.3.

3D structure databases

ProteinModelPortalP0A507.
SMRP0A507. Positions 45-340.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING233413.Mb1615.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD96283; CAD96283; Mb1615.
GeneID1092504.
KEGGmbo:Mb1615.
PATRIC18005233. VBIMycBov88188_1764.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

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_MYCBO
AccessionPrimary (citable) accession number: P0A507
Secondary accession number(s): O06601
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: February 19, 2014
This is version 68 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