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Protein

Biotin synthase

Gene

bioB

Organism
Clostridium botulinum (strain Loch Maree / Type A3)
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

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:CLK_1702
OrganismiClostridium botulinum (strain Loch Maree / Type A3)
Taxonomic identifieri498214 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000000722 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003813161 – 318Biotin synthaseAdd BLAST318

Proteomic databases

PRIDEiB1KW08

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB1KW08
SMRiB1KW08
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.

B1KW08-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNIIKYKKK ILNGDLLTKE EVEELLEEGI TDLAATANEI REFLCGNKFD
60 70 80 90 100
LCTIINGKSG RCQENCKYCA QSSYFDTDII EYNILHSDRI INSGISNYNK
110 120 130 140 150
GVHRFSVVTS GRALNNNEVD TLCKTYSKLK EICSIRLCAS HGLLKYEDLK
160 170 180 190 200
RLKDSGVTRY HNNLETSKSF FKNICTTHTY NDKIETIKNA KKAGLEICSG
210 220 230 240 250
GIIGLGETME DRIDMAFTLR ELSVESVPVN ILNPIKGTPL ENQEILSYEE
260 270 280 290 300
IIKTLALFRF ILPTVQIRLA GGRALLSDKG KKVLESGVNG AISGDMLTTL
310
GIETSEDIKM IKNLGFEV
Length:318
Mass (Da):35,485
Last modified:April 29, 2008 - v1
Checksum:i15E10CBC68E20AC4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000962 Genomic DNA Translation: ACA55752.1
RefSeqiWP_012343697.1, NC_010520.1

Genome annotation databases

EnsemblBacteriaiACA55752; ACA55752; CLK_1702
KEGGicbl:CLK_1702

Similar proteinsi

Entry informationi

Entry nameiBIOB_CLOBM
AccessioniPrimary (citable) accession number: B1KW08
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 29, 2008
Last modified: May 23, 2018
This is version 62 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

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