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P0A506 (BIOB_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:Rv1589, MT1624
ORF Names:MTCY336.15c
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [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 + 2 S-adenosyl-L-methionine = biotin + 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.

Miscellaneous

Was identified as a high-confidence drug target. 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_0000185560

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
P0A506 [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

[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
Raman K., Yeturu K., Chandra N.
BMC Syst. Biol. 2:109-109(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX842577 Genomic DNA. Translation: CAB09080.1.
AE000516 Genomic DNA. Translation: AAK45892.1.
AL123456 Genomic DNA. Translation: CCP44353.1.
PIRG70542.
RefSeqNP_216105.1. NC_000962.3.
NP_336078.1. NC_002755.2.
YP_006514978.1. NC_018143.1.

3D structure databases

ProteinModelPortalP0A506.
SMRP0A506. Positions 45-340.
ModBaseSearch...

Protein-protein interaction databases

STRING83332.Rv1589.

Proteomic databases

PRIDEP0A506.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK45892; AAK45892; MT1624.
GeneID13316367.
886301.
924306.
KEGGmtc:MT1624.
mtu:Rv1589.
mtv:RVBD_1589.
PATRIC18125338. VBIMycTub22151_1784.

Organism-specific databases

TubercuListRv1589.

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239958.
KOK01012.
OMARIMMPAS.
ProtClustDBPRK06256.

Enzyme and pathway databases

UniPathwayUPA00078; UER00162.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01694. BioB.
InterProIPR013785. Aldolase_TIM.
IPR010722. Biotin/thiamin_synth-assoc.
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_MYCTU
AccessionPrimary (citable) accession number: P0A506
Secondary accession number(s): L0TA21, O06601
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: May 1, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families