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Protein

Biotin synthase

Gene

bioB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.UniRule annotation

Catalytic activityi

Dethiobiotin + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • [4Fe-4S] clusterUniRule annotationNote: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation
  • [2Fe-2S] clusterUniRule annotationNote: Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi65 – 651Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi69 – 691Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi72 – 721Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi109 – 1091Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi141 – 1411Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi201 – 2011Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi271 – 2711Iron-sulfur 2 (2Fe-2S)UniRule annotation

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  3. biotin synthase activity Source: UniProtKB-HAMAP
  4. iron ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. biotin biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Biotin biosynthesis

Keywords - Ligandi

2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciBSUB:BSU30200-MONOMER.
UniPathwayiUPA00078; UER00162.

Names & Taxonomyi

Protein namesi
Recommended name:
Biotin synthaseUniRule annotation (EC:2.8.1.6UniRule annotation)
Gene namesi
Name:bioBUniRule annotation
Ordered Locus Names:BSU30200
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU30200. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 335335Biotin synthasePRO_0000185546Add
BLAST

Proteomic databases

PaxDbiP53557.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

IntActiP53557. 1 interaction.
MINTiMINT-8366647.
STRINGi224308.BSU30200.

Structurei

3D structure databases

ProteinModelPortaliP53557.
SMRiP53557. Positions 15-323.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. Biotin synthase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
InParanoidiP53557.
KOiK01012.
OMAiCGYCPQS.
OrthoDBiEOG622PMP.
PhylomeDBiP53557.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01694. BioB.
InterProiIPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR002684. Biotin_synth/BioAB.
IPR024177. Biotin_synthase.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
[Graphical view]
PfamiPF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF001619. Biotin_synth. 1 hit.
SMARTiSM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00433. bioB. 1 hit.

Sequencei

Sequence statusi: Complete.

P53557-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNQWMELADR VLAGAEVTDE EALSILHCPD EDILLLMHGA FHIRKHFYGK
60 70 80 90 100
KVKLNMIMNA KSGLCPENCG YCSQSAISKA PIESYRMVNK ETLLEGAKRA
110 120 130 140 150
HDLNIGTYCI VASGRGPSNR EVDQVVDAVQ EIKETYGLKI CACLGLLKPE
160 170 180 190 200
QAKRLKDAGV DRYNHNLNTS QRNHSNITTS HTYDDRVNTV EIAKESGLSP
210 220 230 240 250
CSGAIIGMKE TKQDVIDIAK SLKALDADSI PVNFLHAIDG TPLEGVNELN
260 270 280 290 300
PLYCLKVLAL FRFINPSKEI RISGGREVNL RTLQPLGLYA ANSIFVGDYL
310 320 330
TTAGQEETED HKMLSDLGFE VESVEEMKAS LSAKS
Length:335
Mass (Da):36,927
Last modified:October 1, 1996 - v1
Checksum:iD4B2E1A53271ED26
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51868 Genomic DNA. Translation: AAB17461.1.
AF008220 Genomic DNA. Translation: AAC00265.1.
AL009126 Genomic DNA. Translation: CAB14998.1.
PIRiD69594.
RefSeqiNP_390898.1. NC_000964.3.
WP_004398967.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14998; CAB14998; BSU30200.
GeneIDi938180.
KEGGibsu:BSU30200.
PATRICi18977942. VBIBacSub10457_3159.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51868 Genomic DNA. Translation: AAB17461.1.
AF008220 Genomic DNA. Translation: AAC00265.1.
AL009126 Genomic DNA. Translation: CAB14998.1.
PIRiD69594.
RefSeqiNP_390898.1. NC_000964.3.
WP_004398967.1. NZ_JNCM01000036.1.

3D structure databases

ProteinModelPortaliP53557.
SMRiP53557. Positions 15-323.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP53557. 1 interaction.
MINTiMINT-8366647.
STRINGi224308.BSU30200.

Proteomic databases

PaxDbiP53557.

Protocols and materials databases

DNASUi938180.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14998; CAB14998; BSU30200.
GeneIDi938180.
KEGGibsu:BSU30200.
PATRICi18977942. VBIBacSub10457_3159.

Organism-specific databases

GenoListiBSU30200. [Micado]

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
InParanoidiP53557.
KOiK01012.
OMAiCGYCPQS.
OrthoDBiEOG622PMP.
PhylomeDBiP53557.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciBSUB:BSU30200-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01694. BioB.
InterProiIPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR002684. Biotin_synth/BioAB.
IPR024177. Biotin_synthase.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
[Graphical view]
PfamiPF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF001619. Biotin_synth. 1 hit.
SMARTiSM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00433. bioB. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiBIOB_BACSU
AccessioniPrimary (citable) accession number: P53557
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 7, 2015
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.