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Protein

Biotin synthase

Gene

bioB

Organism
Ehrlichia ruminantium (strain Gardel)
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 bindingi55Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi59Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi62Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi99Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi130Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi190Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi262Iron-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

BioCyciERUM302409:G1GJ9-707-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:ERGA_CDS_06730
OrganismiEhrlichia ruminantium (strain Gardel)
Taxonomic identifieri302409 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeEhrlichia
Proteomesi
  • UP000000533 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003813761 – 322Biotin synthaseAdd BLAST322

Proteomic databases

PRIDEiQ5FFY2

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ5FFY2
SMRiQ5FFY2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000239957
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
SFLDiSFLDF00272 biotin_synthase, 1 hit
SFLDG01060 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.

Q5FFY2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCTSIRHDWQ LPEVLELFNI PFNDLILNAH LIHRKFFNSN EIQIAGLLNI
60 70 80 90 100
KTGGCPENCK YCSQSAHYKT QLKKEDLLNI ETIKEAIKKA KVNGIDRFCF
110 120 130 140 150
AAAWRQIRDR DIEYICNIIS LIKSENLESC ASLGMVTLEQ AKKLKTAGLD
160 170 180 190 200
FYNHNIDTSR DFYYNVTTTR SYDDRLSSLN NISEAEINIC SGGILGLGES
210 220 230 240 250
IEDRAKMLLT LANLKKHPKS VPINRLVPIK GTPFENNPKI SNIDFIRTIA
260 270 280 290 300
VARILMPESY VRLAAGRESM SHEMQALCLF AGANSLFYGE KLLTTPNADC
310 320
NDDKNLLSKL GVKTKQAVFF DS
Length:322
Mass (Da):36,318
Last modified:March 1, 2005 - v1
Checksum:i8E11CAB36A23F150
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR925677 Genomic DNA Translation: CAI28125.1
RefSeqiWP_011255762.1, NC_006831.1

Genome annotation databases

EnsemblBacteriaiCAI28125; CAI28125; ERGA_CDS_06730
KEGGierg:ERGA_CDS_06730

Similar proteinsi

Entry informationi

Entry nameiBIOB_EHRRG
AccessioniPrimary (citable) accession number: Q5FFY2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 1, 2005
Last modified: May 23, 2018
This is version 103 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, Reference proteome
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Main funding by: National Institutes of Health