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Protein

Biotin synthase

Gene

bioB

Organism
Leptospira borgpetersenii serovar Hardjo-bovis (strain L550)
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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi70 – 701Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi74 – 741Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi77 – 771Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi114 – 1141Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi146 – 1461Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi206 – 2061Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi276 – 2761Iron-sulfur 2 (2Fe-2S)UniRule annotation

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

BioCyciLBOR355276:GHUQ-1402-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:LBL_1414
OrganismiLeptospira borgpetersenii serovar Hardjo-bovis (strain L550)
Taxonomic identifieri355276 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira
ProteomesiUP000000655 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 358358Biotin synthasePRO_0000381444Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi355276.LBL_1414.

Structurei

3D structure databases

ProteinModelPortaliQ051U2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
OMAiYNINIQV.
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.

Q051U2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEKMYATLK TAEKIFSEIS SVITKQEGLE ILNGSIPLTT CLDKAFQERN
60 70 80 90 100
RYFYNKVRIH ILDNIKNGYC PEDCGYCAQR KNANSGIKEY PMKSEAEIYE
110 120 130 140 150
DAVQAKKNGA YRFCMVTSGT GPNRLTTERL ASTIRRITNE LGMKVCLSAG
160 170 180 190 200
LLDEEKAQVL KSAGLDRYNH NLNTSENHYP EICDTHTYAQ RTQTLDSVSK
210 220 230 240 250
AGIGMCSGVI VGMGESFQDI VDMAFELKSF RVISIPVNFF IPVKGHAIKN
260 270 280 290 300
PGILTPELCV RILCLFRLVN PDSEIRIAAG REGHLRSLSA MALFAANSLF
310 320 330 340 350
SSGYLNVKGS EIIETVTMIR DAGFVPELVD GGILPEESGT EMLYSEKNFP

ELYKFKKS
Length:358
Mass (Da):39,844
Last modified:November 13, 2006 - v1
Checksum:i77B9930EF3CF4746
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000348 Genomic DNA. Translation: ABJ78903.1.
RefSeqiWP_011670109.1. NC_008508.1.
YP_797836.1. NC_008508.1.

Genome annotation databases

EnsemblBacteriaiABJ78903; ABJ78903; LBL_1414.
KEGGilbl:LBL_1414.
PATRICi22366650. VBILepBor75619_1784.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000348 Genomic DNA. Translation: ABJ78903.1.
RefSeqiWP_011670109.1. NC_008508.1.
YP_797836.1. NC_008508.1.

3D structure databases

ProteinModelPortaliQ051U2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi355276.LBL_1414.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABJ78903; ABJ78903; LBL_1414.
KEGGilbl:LBL_1414.
PATRICi22366650. VBILepBor75619_1784.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
OMAiYNINIQV.
OrthoDBiEOG622PMP.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciLBOR355276:GHUQ-1402-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: L550.

Entry informationi

Entry nameiBIOB_LEPBL
AccessioniPrimary (citable) accession number: Q051U2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 27, 2009
Last sequence update: November 13, 2006
Last modified: March 31, 2015
This is version 61 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

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.