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Protein

Biotin synthase

Gene

bioB

Organism
Francisella tularensis subsp. tularensis (strain FSC 198)
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

Pathway:ibiotin 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi46 – 461Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi50 – 501Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi53 – 531Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi90 – 901Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi121 – 1211Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi181 – 1811Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi256 – 2561Iron-sulfur 2 (2Fe-2S)UniRule annotation

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

BioCyciFTUL393115:GJUT-955-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:FTF0937c
OrganismiFrancisella tularensis subsp. tularensis (strain FSC 198)
Taxonomic identifieri393115 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 313313Biotin synthasePRO_0000381391Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ14HR4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
OMAiADRFCMG.
OrthoDBiEOG622PMP.

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.

Q14HR4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLQQIKEIY SRPLTELILQ ALEIHNKNFG NDIELCSLKS IKTGTCPEDC
60 70 80 90 100
KYCPQSGHYN TSIEKHKLLD KDSILAEAKN AKDAGSKRFC MGAAWKHIPK
110 120 130 140 150
KDFDQVAEII TEVKNLGLET CVTLGSINAD EATKLKQAGL DYYNHNLDTS
160 170 180 190 200
REFYPEIITT RKFEERIETI RNVANADINV CCGGILGMGE SLDDRFNLLL
210 220 230 240 250
ELLQLPAAPK SIPINTLIPI KGTPLGDKYT NAQIDSFELV RFIATTRILF
260 270 280 290 300
PQARLRLSAG RENMSLETQT LCFLAGINSI FYGNKLLTEN NATVNSDNFL
310
LAKLGLKSNA ELC
Length:313
Mass (Da):34,895
Last modified:August 22, 2006 - v1
Checksum:iE964798853D01157
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM286280 Genomic DNA. Translation: CAL08953.1.
RefSeqiWP_003020978.1. NC_008245.1.

Genome annotation databases

EnsemblBacteriaiCAL08953; CAL08953; FTF0937c.
KEGGiftf:FTF0937c.
PATRICi17960811. VBIFraTul133500_1070.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM286280 Genomic DNA. Translation: CAL08953.1.
RefSeqiWP_003020978.1. NC_008245.1.

3D structure databases

ProteinModelPortaliQ14HR4.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAL08953; CAL08953; FTF0937c.
KEGGiftf:FTF0937c.
PATRICi17960811. VBIFraTul133500_1070.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
OMAiADRFCMG.
OrthoDBiEOG622PMP.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciFTUL393115:GJUT-955-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

  1. "Genome sequencing shows that European isolates of Francisella tularensis subspecies tularensis are almost identical to US laboratory strain Schu S4."
    Chaudhuri R.R., Ren C.-P., Desmond L., Vincent G.A., Silman N.J., Brehm J.K., Elmore M.J., Hudson M.J., Forsman M., Isherwood K.E., Gurycova D., Minton N.P., Titball R.W., Pallen M.J., Vipond R.
    PLoS ONE 2:E352-E352(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FSC 198.

Entry informationi

Entry nameiBIOB_FRAT1
AccessioniPrimary (citable) accession number: Q14HR4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: August 22, 2006
Last modified: July 22, 2015
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.