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Protein

Thioredoxin/glutathione peroxidase BtuE

Gene

btuE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Non-specific peroxidase that can use thioredoxin or glutathione as a reducing agent. In vitro, utilizes preferentially thioredoxin A to decompose hydrogen peroxide as well as cumene-, tert-butyl-, and linoleic acid hydroperoxides, suggesting that it may have one or more organic hydroperoxide as its physiological substrate.1 Publication

Catalytic activityi

2 glutathione + H2O2 = glutathione disulfide + 2 H2O.UniRule annotation1 Publication
2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.UniRule annotation1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei37 – 371UniRule annotation

GO - Molecular functioni

  • glutathione peroxidase activity Source: EcoCyc
  • thioredoxin peroxidase activity Source: EcoCyc

GO - Biological processi

  • response to hydroperoxide Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BioCyciEcoCyc:BTUE-MONOMER.
ECOL316407:JW1700-MONOMER.
MetaCyc:BTUE-MONOMER.
RETL1328306-WGS:GSTH-1617-MONOMER.

Protein family/group databases

PeroxiBasei3987. EcoGPx01.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin/glutathione peroxidase BtuEUniRule annotationCurated (EC:1.11.1.15UniRule annotation1 Publication, EC:1.11.1.9UniRule annotation1 Publication)
Gene namesi
Name:btuEUniRule annotation
Ordered Locus Names:b1710, JW1700
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10129. btuE.

Subcellular locationi

  • Periplasm 1 Publication

  • Note: Appears to have a periplasmic location. It has the mean hydropathy of a soluble protein but lacks an obvious signal sequence.1 Publication

GO - Cellular componenti

  • periplasmic space Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Disruption phenotypei

Deletion has no significant effect on the binding, transport or utilization of vitamin B12 or other cobalamins.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 183183Thioredoxin/glutathione peroxidase BtuEPRO_0000066664Add
BLAST

Proteomic databases

EPDiP06610.
PaxDbiP06610.
PRIDEiP06610.

Expressioni

Inductioni

Induced by oxidative stress conditions.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi4260286. 10 interactions.
IntActiP06610. 17 interactions.
STRINGi511145.b1710.

Structurei

3D structure databases

ProteinModelPortaliP06610.
SMRiP06610. Positions 15-163.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutathione peroxidase family. BtuE subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108V06. Bacteria.
COG0386. LUCA.
HOGENOMiHOG000277053.
InParanoidiP06610.
KOiK00432.
OMAiDEIKTFC.
OrthoDBiEOG66QM2H.
PhylomeDBiP06610.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
HAMAPiMF_02061. Thiored_glutath_peroxid.
InterProiIPR000889. Glutathione_peroxidase.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR11592. PTHR11592. 1 hit.
PfamiPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFiPIRSF000303. Glutathion_perox. 1 hit.
PRINTSiPR01011. GLUTPROXDASE.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P06610-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQDSILTTVV KDIDGEVTTL EKFAGNVLLI VNVASKCGLT PQYEQLENIQ
60 70 80 90 100
KAWVDRGFMV LGFPCNQFLE QEPGSDEEIK TYCTTTWGVT FPMFSKIEVN
110 120 130 140 150
GEGRHPLYQK LIAAAPTAVA PEESGFYARM VSKGRAPLYP DDILWNFEKF
160 170 180
LVGRDGKVIQ RFSPDMTPED PIVMESIKLA LAK
Length:183
Mass (Da):20,470
Last modified:January 1, 1988 - v1
Checksum:iC8DB671963A7F235
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14031 Genomic DNA. Translation: AAA23527.1.
U00096 Genomic DNA. Translation: AAC74780.1.
AP009048 Genomic DNA. Translation: BAA15478.1.
PIRiF64929. QRECBE.
RefSeqiNP_416225.1. NC_000913.3.
WP_001154168.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74780; AAC74780; b1710.
BAA15478; BAA15478; BAA15478.
GeneIDi945915.
KEGGiecj:JW1700.
eco:b1710.
PATRICi32118726. VBIEscCol129921_1781.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14031 Genomic DNA. Translation: AAA23527.1.
U00096 Genomic DNA. Translation: AAC74780.1.
AP009048 Genomic DNA. Translation: BAA15478.1.
PIRiF64929. QRECBE.
RefSeqiNP_416225.1. NC_000913.3.
WP_001154168.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP06610.
SMRiP06610. Positions 15-163.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260286. 10 interactions.
IntActiP06610. 17 interactions.
STRINGi511145.b1710.

Protein family/group databases

PeroxiBasei3987. EcoGPx01.

Proteomic databases

EPDiP06610.
PaxDbiP06610.
PRIDEiP06610.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74780; AAC74780; b1710.
BAA15478; BAA15478; BAA15478.
GeneIDi945915.
KEGGiecj:JW1700.
eco:b1710.
PATRICi32118726. VBIEscCol129921_1781.

Organism-specific databases

EchoBASEiEB0127.
EcoGeneiEG10129. btuE.

Phylogenomic databases

eggNOGiENOG4108V06. Bacteria.
COG0386. LUCA.
HOGENOMiHOG000277053.
InParanoidiP06610.
KOiK00432.
OMAiDEIKTFC.
OrthoDBiEOG66QM2H.
PhylomeDBiP06610.

Enzyme and pathway databases

BioCyciEcoCyc:BTUE-MONOMER.
ECOL316407:JW1700-MONOMER.
MetaCyc:BTUE-MONOMER.
RETL1328306-WGS:GSTH-1617-MONOMER.

Miscellaneous databases

PROiP06610.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
HAMAPiMF_02061. Thiored_glutath_peroxid.
InterProiIPR000889. Glutathione_peroxidase.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR11592. PTHR11592. 1 hit.
PfamiPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFiPIRSF000303. Glutathion_perox. 1 hit.
PRINTSiPR01011. GLUTPROXDASE.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the btuCED genes involved in vitamin B12 transport in Escherichia coli and homology with components of periplasmic-binding-protein-dependent transport systems."
    Friedrich M.J., Deveaux L.C., Kadner R.J.
    J. Bacteriol. 167:928-934(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Vitamin B12 transport in Escherichia coli K12 does not require the btuE gene of the btuCED operon."
    Rioux C.R., Kadner R.J.
    Mol. Gen. Genet. 217:301-308(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
    Strain: K12.
  6. "The Escherichia coli btuE gene, encodes a glutathione peroxidase that is induced under oxidative stress conditions."
    Arenas F.A., Diaz W.A., Leal C.A., Perez-Donoso J.M., Imlay J.A., Vasquez C.C.
    Biochem. Biophys. Res. Commun. 398:690-694(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INDUCTION.

Entry informationi

Entry nameiBTUE_ECOLI
AccessioniPrimary (citable) accession number: P06610
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: July 6, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Part of the btuCED operon, and was originally thought to participate in the transport of vitamin B12, but it was shown later that it plays no essential role in vitamin B12 transport.2 Publications

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  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.