ID Q0BTC1_GRABC Unreviewed; 159 AA.
AC Q0BTC1;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN OrderedLocusNames=GbCGDNIH1_1033 {ECO:0000313|EMBL:ABI61931.1};
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165 {ECO:0000313|EMBL:ABI61931.1, ECO:0000313|Proteomes:UP000001963};
RN [1] {ECO:0000313|EMBL:ABI61931.1, ECO:0000313|Proteomes:UP000001963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1260 / CGDNIH1 {ECO:0000313|Proteomes:UP000001963};
RX PubMed=17827295; DOI=10.1128/JB.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA Kupko J.J.III., Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(2007).
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR EMBL; CP000394; ABI61931.1; -; Genomic_DNA.
DR RefSeq; WP_011631740.1; NC_008343.2.
DR AlphaFoldDB; Q0BTC1; -.
DR STRING; 391165.GbCGDNIH1_1033; -.
DR KEGG; gbe:GbCGDNIH1_1033; -.
DR eggNOG; COG0386; Bacteria.
DR HOGENOM; CLU_029507_2_2_5; -.
DR OrthoDB; 9785502at2; -.
DR Proteomes; UP000001963; Chromosome.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00340; GSH_Peroxidase; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000889; Glutathione_peroxidase.
DR InterPro; IPR029760; GPX_CS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR PANTHER; PTHR11592:SF78; PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE; 1.
DR Pfam; PF00255; GSHPx; 1.
DR PIRSF; PIRSF000303; Glutathion_perox; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000499};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000499};
KW Reference proteome {ECO:0000313|Proteomes:UP000001963}.
FT ACT_SITE 36
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 159 AA; 18018 MW; 1319DC5887BDA1FD CRC64;
MTSLYDFQAT MLDGQVVPLS RWRGQVALVV NTASRCGFTP QYQGLEALYQ RFAASGFVVL
GFPCNQFGAQ EPGSSEEIRT FCDTRYSVSF PMFARVEVNG TNAHPLFDYL TRQRRGLLGT
RRIKWNFTKF LIGRDGVPVA RYAPSCKPEK LEKAVYRLL
//
