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Q65MK9 (BIOB_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 82. 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:BLi00770, BL00956
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length333 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 – 333333Biotin synthase HAMAP-Rule MF_01694
PRO_0000381231

Sites

Metal binding651Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding691Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding721Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1091Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1411Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2011Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2711Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65MK9 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 5E4DD05AB72CE58C

FASTA33336,820
        10         20         30         40         50         60 
MNQWMELAER VLDGGEVTEK EALSILECPD DDVLLLMHAA FQIRKRYYGK KVKLNMIMNA 

        70         80         90        100        110        120 
KSGLCPENCG YCSQSSISKA PIDSYRMVDK TTLLEGAKRA HDLNIGTYCI VASGRGPSNR 

       130        140        150        160        170        180 
EVDQVVDAVK EIKETYGLKI CACLGLLKPG QAERLKEAGV DRYNHNINTS KTNHSNITTS 

       190        200        210        220        230        240 
HTYDDRVNTV ETAKKSGMSP CSGVIVGMKE TKQDVVDMAK SLKALDADSI PVNFLHAIDG 

       250        260        270        280        290        300 
TPLEGVNELN PLYCLKVLAL FRFINPTKEI RISGGREVNL RSLQPLGLYA ANSIFVGDYL 

       310        320        330 
TTAGQNETED HKMLHDLGFE VESVEEMKAS LQR 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000002 Genomic DNA. Translation: AAU22356.1.
AE017333 Genomic DNA. Translation: AAU39705.1.
RefSeqYP_006712176.1. NC_006322.1.
YP_077994.1. NC_006270.3.

3D structure databases

ProteinModelPortalQ65MK9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279010.BL00956.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU22356; AAU22356; BL00956.
AAU39705; AAU39705; BLi00770.
GeneID3029555.
3100183.
KEGGbld:BLi00770.
bli:BL00956.
PATRIC18947073. VBIBacLic203714_0761.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239958.
KOK01012.
OMAADRFCMG.
OrthoDBEOG622PMP.
ProtClustDBPRK06256.

Enzyme and pathway databases

BioCycBLIC279010:GJ2P-764-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_BACLD
AccessionPrimary (citable) accession number: Q65MK9
Secondary accession number(s): Q62Y02
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: October 25, 2004
Last modified: February 19, 2014
This is version 82 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