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P53557

- BIOB_BACSU

UniProt

P53557 - BIOB_BACSU

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Protein
Biotin synthase
Gene
bioB, BSU30200
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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 By similarity.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

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.

Pathwayi

Sites

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

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 synthase (EC:2.8.1.6)
Gene namesi
Name:bioB
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 synthaseUniRule annotation
PRO_0000185546Add
BLAST

Proteomic databases

PaxDbiP53557.

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP53557.
SMRiP53557. Positions 15-323.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
OMAiRIMMPAS.
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

MNQWMELADR VLAGAEVTDE EALSILHCPD EDILLLMHGA FHIRKHFYGK    50
KVKLNMIMNA KSGLCPENCG YCSQSAISKA PIESYRMVNK ETLLEGAKRA 100
HDLNIGTYCI VASGRGPSNR EVDQVVDAVQ EIKETYGLKI CACLGLLKPE 150
QAKRLKDAGV DRYNHNLNTS QRNHSNITTS HTYDDRVNTV EIAKESGLSP 200
CSGAIIGMKE TKQDVIDIAK SLKALDADSI PVNFLHAIDG TPLEGVNELN 250
PLYCLKVLAL FRFINPSKEI RISGGREVNL RTLQPLGLYA ANSIFVGDYL 300
TTAGQEETED HKMLSDLGFE VESVEEMKAS LSAKS 335
Length:335
Mass (Da):36,927
Last modified:October 1, 1996 - v1
Checksum:iD4B2E1A53271ED26
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_CM000487.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U51868 Genomic DNA. Translation: AAB17461.1 .
AF008220 Genomic DNA. Translation: AAC00265.1 .
AL009126 Genomic DNA. Translation: CAB14998.1 .
PIRi D69594.
RefSeqi NP_390898.1. NC_000964.3.
WP_004398967.1. NZ_CM000487.1.

3D structure databases

ProteinModelPortali P53557.
SMRi P53557. Positions 15-323.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P53557. 1 interaction.
MINTi MINT-8366647.
STRINGi 224308.BSU30200.

Proteomic databases

PaxDbi P53557.

Protocols and materials databases

DNASUi 938180.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB14998 ; CAB14998 ; BSU30200 .
GeneIDi 938180.
KEGGi bsu:BSU30200.
PATRICi 18977942. VBIBacSub10457_3159.

Organism-specific databases

GenoListi BSU30200. [Micado ]

Phylogenomic databases

eggNOGi COG0502.
HOGENOMi HOG000239958.
KOi K01012.
OMAi RIMMPAS.
OrthoDBi EOG622PMP.
PhylomeDBi P53557.

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00162 .
BioCyci BSUB:BSU30200-MONOMER.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01694. BioB.
InterProi IPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR002684. Biotin_synth/BioAB.
IPR024177. Biotin_synthase.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
[Graphical view ]
Pfami PF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view ]
PIRSFi PIRSF001619. Biotin_synth. 1 hit.
SMARTi SM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00433. bioB. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 117 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

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