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Protein

Biotin synthase

Gene

bioB

Organism
Escherichia coli O45:K1 (strain S88 / ExPEC)
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 (ynfK), 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 bindingi53Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi57Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi60Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi97Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi128Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi188Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi260Iron-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:ECS88_0792
OrganismiEscherichia coli O45:K1 (strain S88 / ExPEC)
Taxonomic identifieri585035 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003813571 – 346Biotin synthaseAdd BLAST346

Proteomic databases

PRIDEiB7MGN3

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB7MGN3
SMRiB7MGN3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000239957
KOiK01012
OMAiADRFCMG

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.

B7MGN3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHRPRWTLS QVTELFEKPL LDLLFEAQQV HRQHFDPRQV QVSTLLSIKT
60 70 80 90 100
GACPEDCKYC PQSSRYKTGL EAERLMEVEQ VLESARKAKA AGSTRFCMGA
110 120 130 140 150
AWKNPHERDM PYLEQMVQGV KAMGLEACMT LGTLSESQAQ RLANAGLDYY
160 170 180 190 200
NHNLDTSPEF YGNIITTRTY QERLDTLEKV REAGIKVCSG GIVGLGETVK
210 220 230 240 250
DRAGLLLQLA NLPTPPESVP INMLVKVKGT PLADNDDVDA FDFIRTIAVA
260 270 280 290 300
RIMMPTSYVR LSAGREQMNE QTQAMCFMAG ANSIFYGCKL LTTPNPEEDK
310 320 330 340
DLQLFRKLGL NPQQTAVLAG DNEQQQRLEQ ALMTPDTDEY YNAAAL
Length:346
Mass (Da):38,662
Last modified:February 10, 2009 - v1
Checksum:i401F79C8E7303E8C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928161 Genomic DNA Translation: CAR02131.1
RefSeqiWP_000951218.1, NC_011742.1

Genome annotation databases

EnsemblBacteriaiCAR02131; CAR02131; ECS88_0792
KEGGiecz:ECS88_0792

Similar proteinsi

Entry informationi

Entry nameiBIOB_ECO45
AccessioniPrimary (citable) accession number: B7MGN3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: May 23, 2018
This is version 63 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

Documents

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

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