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Protein

Biotin synthase

Gene

bioB

Organism
Clostridium botulinum (strain Alaska E43 / Type E3)
Status
Reviewed-Annotation score: -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 + 2 reduced [2Fe-2S] ferredoxin = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin.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: biotin biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes biotin from 7,8-diaminononanoate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. ATP-dependent dethiobiotin synthetase BioD (bioD)
  2. Biotin synthase (bioB)
This subpathway is part of the pathway biotin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes biotin from 7,8-diaminononanoate, the pathway biotin biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi62Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi66Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi69Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi106Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi138Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi198Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi268Iron-sulfur 2 (2Fe-2S)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processBiotin biosynthesis
Ligand2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciCBOT508767:G1GC0-661-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:CLH_0685
OrganismiClostridium botulinum (strain Alaska E43 / Type E3)
Taxonomic identifieri508767 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003813111 – 318Biotin synthaseAdd BLAST318

Proteomic databases

PRIDEiB2V167

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB2V167
SMRiB2V167
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000239958
KOiK01012
OMAiADRFCMG
OrthoDBiPOG091H01DF

Family and domain databases

Gene3Di3.20.20.70, 1 hit
HAMAPiMF_01694 BioB, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR010722 BATS_dom
IPR034416 BATS_domain_containing
IPR002684 Biotin_synth/BioAB
IPR024177 Biotin_synthase
IPR006638 Elp3/MiaB/NifB
IPR007197 rSAM
PANTHERiPTHR22976 PTHR22976, 1 hit
PfamiView protein in Pfam
PF06968 BATS, 1 hit
PF04055 Radical_SAM, 1 hit
PIRSFiPIRSF001619 Biotin_synth, 1 hit
SFLDiSFLDG01060 BATS_domain_containing, 1 hit
SFLDG01278 biotin_synthase_like, 1 hit
SFLDS00029 Radical_SAM, 1 hit
SMARTiView protein in SMART
SM00876 BATS, 1 hit
SM00729 Elp3, 1 hit
TIGRFAMsiTIGR00433 bioB, 1 hit

Sequencei

Sequence statusi: Complete.

B2V167-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIIDRFKEK ILSGELISKK EAIILSKENV DKLASAANDI RMSLCGKKFN
60 70 80 90 100
LCTIINGKSG RCGENCKYCA QSVYFKTDIE EYNLLDSESI ITSAISNYNS
110 120 130 140 150
GVHRFSVVTS GKKLTNKEID IVCKTYSEVQ EKCAIKLCAS HGLLNYEELV
160 170 180 190 200
KLKESGVIRY HNNLETSRRF FSNICTTHTF DEKINTIKNA LKAGLQVCSG
210 220 230 240 250
GIIGLGETME DRIDMAFTLR ELNVDSIPIN ILNPIKGTAL ENQEKLSYDE
260 270 280 290 300
ITKTFALFRF ILPEKQIRLA GGRALLNDKG ERLMKSGVNS AISGDMLTTS
310
GIKTFDDIKM IKELGFEV
Length:318
Mass (Da):35,486
Last modified:July 1, 2008 - v1
Checksum:i90ED5AD2D859FAFF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001078 Genomic DNA Translation: ACD51519.1
RefSeqiWP_012449859.1, NC_010723.1

Genome annotation databases

EnsemblBacteriaiACD51519; ACD51519; CLH_0685
KEGGicbt:CLH_0685

Similar proteinsi

Entry informationi

Entry nameiBIOB_CLOBA
AccessioniPrimary (citable) accession number: B2V167
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: July 1, 2008
Last modified: May 23, 2018
This is version 64 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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