ID H2G081_OCESG Unreviewed; 179 AA.
AC H2G081;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN OrderedLocusNames=GU3_01610 {ECO:0000313|EMBL:AEY00079.1};
OS Oceanimonas sp. (strain GK1 / IBRC-M 10197).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Oceanimonas.
OX NCBI_TaxID=511062 {ECO:0000313|EMBL:AEY00079.1, ECO:0000313|Proteomes:UP000007742};
RN [1] {ECO:0000313|EMBL:AEY00079.1, ECO:0000313|Proteomes:UP000007742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GK1 {ECO:0000313|EMBL:AEY00079.1,
RC ECO:0000313|Proteomes:UP000007742};
RX PubMed=22461556; DOI=10.1128/JB.00023-12;
RA Parsa Yeganeh L., Azarbaijani R., Sarikhan S., Mousavi H., Ramezani M.,
RA Amoozegar M.A., Shahzadeh Fazeli A., Salekdeh G.H.;
RT "Complete genome sequence of Oceanimonas sp. GK1, a halotolerant bacterium
RT from Gavkhouni Wetland in Iran.";
RL J. Bacteriol. 194:2123-2124(2012).
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR EMBL; CP003171; AEY00079.1; -; Genomic_DNA.
DR RefSeq; WP_014290815.1; NC_016745.1.
DR AlphaFoldDB; H2G081; -.
DR STRING; 511062.GU3_01610; -.
DR KEGG; oce:GU3_01610; -.
DR eggNOG; COG0386; Bacteria.
DR HOGENOM; CLU_029507_1_3_6; -.
DR OrthoDB; 9785502at2; -.
DR Proteomes; UP000007742; 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; IPR029759; GPX_AS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR PANTHER; PTHR11592:SF44; 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; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 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:UP000007742};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..179
FT /note="Glutathione peroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003561806"
FT DOMAIN 11..179
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 60
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 179 AA; 19903 MW; D67BD96DE856BD13 CRC64;
MKKLFSGLCG LLLWQTASAT EPNTAALFEH QLPRLHSDTT LDMRQLAGQP LLVVNTASHC
GFTGQFEGLE ALHQQYKDQG LRVVGFPSND FNQEAKSEEE AAQVCFQNFG VTFDMAAPIS
VKGDQAHPIF KEITRQSGKQ PRWNFYKFVI DRNGRVTEVF SSITGPESGR LKAAIEQVL
//