BTUE_ECOLI
ID BTUE_ECOLI Reviewed; 183 AA.
AC P06610;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Thioredoxin/glutathione peroxidase BtuE {ECO:0000255|HAMAP-Rule:MF_02061, ECO:0000305};
DE EC=1.11.1.24 {ECO:0000255|HAMAP-Rule:MF_02061, ECO:0000269|PubMed:20621065};
DE EC=1.11.1.9 {ECO:0000255|HAMAP-Rule:MF_02061, ECO:0000269|PubMed:20621065};
GN Name=btuE {ECO:0000255|HAMAP-Rule:MF_02061};
GN OrderedLocusNames=b1710, JW1700;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=3528129; DOI=10.1128/jb.167.3.928-934.1986;
RA Friedrich M.J., Deveaux L.C., Kadner R.J.;
RT "Nucleotide sequence of the btuCED genes involved in vitamin B12 transport
RT in Escherichia coli and homology with components of periplasmic-binding-
RT protein-dependent transport systems.";
RL J. Bacteriol. 167:928-934(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=2671656; DOI=10.1007/bf02464897;
RA Rioux C.R., Kadner R.J.;
RT "Vitamin B12 transport in Escherichia coli K12 does not require the btuE
RT gene of the btuCED operon.";
RL Mol. Gen. Genet. 217:301-308(1989).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=20621065; DOI=10.1016/j.bbrc.2010.07.002;
RA Arenas F.A., Diaz W.A., Leal C.A., Perez-Donoso J.M., Imlay J.A.,
RA Vasquez C.C.;
RT "The Escherichia coli btuE gene, encodes a glutathione peroxidase that is
RT induced under oxidative stress conditions.";
RL Biochem. Biophys. Res. Commun. 398:690-694(2010).
CC -!- FUNCTION: Non-specific peroxidase that can use thioredoxin or
CC glutathione as a reducing agent. In vitro, utilizes preferentially
CC thioredoxin A to decompose hydrogen peroxide as well as cumene-, tert-
CC butyl-, and linoleic acid hydroperoxides, suggesting that it may have
CC one or more organic hydroperoxide as its physiological substrate.
CC {ECO:0000269|PubMed:20621065}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O;
CC Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02061,
CC ECO:0000269|PubMed:20621065};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02061, ECO:0000269|PubMed:20621065};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:3528129}.
CC Note=Appears to have a periplasmic location. It has the mean hydropathy
CC of a soluble protein but lacks an obvious signal sequence.
CC {ECO:0000305|PubMed:3528129}.
CC -!- INDUCTION: Induced by oxidative stress conditions.
CC {ECO:0000269|PubMed:20621065}.
CC -!- DISRUPTION PHENOTYPE: Deletion has no significant effect on the
CC binding, transport or utilization of vitamin B12 or other cobalamins.
CC {ECO:0000269|PubMed:2671656}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family. BtuE
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_02061}.
CC -!- CAUTION: Part of the btuCED operon, and was originally thought to
CC participate in the transport of vitamin B12, but it was shown later
CC that it plays no essential role in vitamin B12 transport.
CC {ECO:0000305|PubMed:2671656, ECO:0000305|PubMed:3528129}.
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DR EMBL; M14031; AAA23527.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74780.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15478.1; -; Genomic_DNA.
DR PIR; F64929; QRECBE.
DR RefSeq; NP_416225.1; NC_000913.3.
DR RefSeq; WP_001154168.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P06610; -.
DR SMR; P06610; -.
DR BioGRID; 4260286; 32.
DR IntAct; P06610; 17.
DR STRING; 511145.b1710; -.
DR PeroxiBase; 3987; EcoGPx01.
DR jPOST; P06610; -.
DR PaxDb; P06610; -.
DR PRIDE; P06610; -.
DR EnsemblBacteria; AAC74780; AAC74780; b1710.
DR EnsemblBacteria; BAA15478; BAA15478; BAA15478.
DR GeneID; 945915; -.
DR KEGG; ecj:JW1700; -.
DR KEGG; eco:b1710; -.
DR PATRIC; fig|1411691.4.peg.547; -.
DR EchoBASE; EB0127; -.
DR eggNOG; COG0386; Bacteria.
DR HOGENOM; CLU_029507_1_2_6; -.
DR InParanoid; P06610; -.
DR OMA; LAPFKGQ; -.
DR PhylomeDB; P06610; -.
DR BioCyc; EcoCyc:BTUE-MON; -.
DR BioCyc; MetaCyc:BTUE-MON; -.
DR PRO; PR:P06610; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IDA:EcoliWiki.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:EcoCyc.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:EcoCyc.
DR GO; GO:0033194; P:response to hydroperoxide; IEP:EcoCyc.
DR GO; GO:0000302; P:response to reactive oxygen species; IMP:EcoCyc.
DR CDD; cd00340; GSH_Peroxidase; 1.
DR HAMAP; MF_02061; Thiored_glutath_peroxid; 1.
DR InterPro; IPR033674; BtuE.
DR InterPro; IPR000889; Glutathione_peroxidase.
DR InterPro; IPR029759; GPX_AS.
DR InterPro; IPR029760; GPX_CS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11592; PTHR11592; 1.
DR Pfam; PF00255; GSHPx; 1.
DR PIRSF; PIRSF000303; Glutathion_perox; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE 1: Evidence at protein level;
KW Oxidoreductase; Periplasm; Peroxidase; Reference proteome; Stress response.
FT CHAIN 1..183
FT /note="Thioredoxin/glutathione peroxidase BtuE"
FT /id="PRO_0000066664"
FT ACT_SITE 37
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02061"
SQ SEQUENCE 183 AA; 20470 MW; C8DB671963A7F235 CRC64;
MQDSILTTVV KDIDGEVTTL EKFAGNVLLI VNVASKCGLT PQYEQLENIQ KAWVDRGFMV
LGFPCNQFLE QEPGSDEEIK TYCTTTWGVT FPMFSKIEVN GEGRHPLYQK LIAAAPTAVA
PEESGFYARM VSKGRAPLYP DDILWNFEKF LVGRDGKVIQ RFSPDMTPED PIVMESIKLA
LAK
