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Protein

Biotin synthase

Gene

bioB

Organism
Bacillus cereus (strain G9842)
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 + 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 bindingi71Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi75Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi78Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi115Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi147Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi207Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi277Iron-sulfur 2 (2Fe-2S)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

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

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:BCG9842_B1012
OrganismiBacillus cereus (strain G9842)
Taxonomic identifieri405531 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000006744 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003812201 – 332Biotin synthaseAdd BLAST332

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB7IWM8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000239958.
KOiK01012.
OMAiPFDFIRM.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01694. BioB. 1 hit.
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.

B7IWM8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQVQTKRDW KKLAYDVVEE KMITKEDAIA ILEADDTEVL EIMNAAYIIR
60 70 80 90 100
HHHFGKKVKL NMIINTKSGL CPEDCGYCSQ SIISEAPIDK YAWLTQEKIV
110 120 130 140 150
EGAHEAIRRK AGTYCIVASG RRPTDKEVNH VIGAVKEIRE TTDLKICCCL
160 170 180 190 200
GFLNEDQAGR LAEAGVHRYN HNLNTHANNY DSICSTHTYD DRVDTVQKAK
210 220 230 240 250
QAGISPCSGA IFGMGETIEE RAEIAFELQR IDADSIPCNF LVAVKGTPLE
260 270 280 290 300
GQKELTPVEC LKVLAMMRFV NPTKEIRISG GREINLRSVQ PIGLFAANSI
310 320 330
FVGDYLTTAG QEPTADWGMI ADLGFEIEEC AL
Length:332
Mass (Da):36,898
Last modified:February 10, 2009 - v1
Checksum:iA3545D884E726B80
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001186 Genomic DNA. Translation: ACK94805.1.
RefSeqiWP_000815856.1. NC_011772.1.

Genome annotation databases

EnsemblBacteriaiACK94805; ACK94805; BCG9842_B1012.
KEGGibcg:BCG9842_B1012.
PATRICi18903981. VBIBacCer50903_4142.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001186 Genomic DNA. Translation: ACK94805.1.
RefSeqiWP_000815856.1. NC_011772.1.

3D structure databases

ProteinModelPortaliB7IWM8.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACK94805; ACK94805; BCG9842_B1012.
KEGGibcg:BCG9842_B1012.
PATRICi18903981. VBIBacCer50903_4142.

Phylogenomic databases

HOGENOMiHOG000239958.
KOiK01012.
OMAiPFDFIRM.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01694. BioB. 1 hit.
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...

Entry informationi

Entry nameiBIOB_BACC2
AccessioniPrimary (citable) accession number: B7IWM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: November 2, 2016
This is version 50 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.