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P53557 (BIOB_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 114. 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:BSU30200
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length335 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 – 335335Biotin synthase HAMAP-Rule MF_01694
PRO_0000185546

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
P53557 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: D4B2E1A53271ED26

FASTA33536,927
        10         20         30         40         50         60 
MNQWMELADR VLAGAEVTDE EALSILHCPD EDILLLMHGA FHIRKHFYGK KVKLNMIMNA 

        70         80         90        100        110        120 
KSGLCPENCG YCSQSAISKA PIESYRMVNK ETLLEGAKRA HDLNIGTYCI VASGRGPSNR 

       130        140        150        160        170        180 
EVDQVVDAVQ EIKETYGLKI CACLGLLKPE QAKRLKDAGV DRYNHNLNTS QRNHSNITTS 

       190        200        210        220        230        240 
HTYDDRVNTV EIAKESGLSP CSGAIIGMKE TKQDVIDIAK SLKALDADSI PVNFLHAIDG 

       250        260        270        280        290        300 
TPLEGVNELN PLYCLKVLAL FRFINPSKEI RISGGREVNL RTLQPLGLYA ANSIFVGDYL 

       310        320        330 
TTAGQEETED HKMLSDLGFE VESVEEMKAS LSAKS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequencing, and characterization of the Bacillus subtilis biotin biosynthetic operon."
Bower S., Perkins J.B., Yocum R.R., Howitt C.L., Rahaim P., Pero J.
J. Bacteriol. 178:4122-4130(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region."
Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
Microbiology 143:3431-3441(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U51868 Genomic DNA. Translation: AAB17461.1.
AF008220 Genomic DNA. Translation: AAC00265.1.
AL009126 Genomic DNA. Translation: CAB14998.1.
PIRD69594.
RefSeqNP_390898.1. NC_000964.3.

3D structure databases

ProteinModelPortalP53557.
SMRP53557. Positions 15-323.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP53557. 1 interaction.
MINTMINT-8366647.
STRING224308.BSU30200.

Proteomic databases

PaxDbP53557.

Protocols and materials databases

DNASU938180.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14998; CAB14998; BSU30200.
GeneID938180.
KEGGbsu:BSU30200.
PATRIC18977942. VBIBacSub10457_3159.

Organism-specific databases

GenoListBSU30200. [Micado]

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBSUB:BSU30200-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_BACSU
AccessionPrimary (citable) accession number: P53557
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 19, 2014
This is version 114 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

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList