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Database: UniProt
Entry: T1I489_RHOPR
LinkDB: T1I489_RHOPR
Original site: T1I489_RHOPR 
ID   T1I489_RHOPR            Unreviewed;       147 AA.
AC   T1I489;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|ARBA:ARBA00012310, ECO:0000256|RuleBase:RU000499};
DE   Flags: Fragment;
OS   Rhodnius prolixus (Triatomid bug).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC   Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX   NCBI_TaxID=13249 {ECO:0000313|EnsemblMetazoa:RPRC011108-PA, ECO:0000313|Proteomes:UP000015103};
RN   [1] {ECO:0000313|Proteomes:UP000015103}
RP   NUCLEOTIDE SEQUENCE.
RA   Wilson R.K., Warren W., Dotson E., Oliveira P.L.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:RPRC011108-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-2015) to UniProtKB.
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:0000256|ARBA:ARBA00000217};
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR   EMBL; ACPB03020437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACPB03020438; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; T1I489; -.
DR   STRING; 13249.T1I489; -.
DR   EnsemblMetazoa; RPRC011108-RA; RPRC011108-PA; RPRC011108.
DR   VEuPathDB; VectorBase:RPRC011108; -.
DR   eggNOG; KOG1651; Eukaryota.
DR   HOGENOM; CLU_029507_2_0_1; -.
DR   InParanoid; T1I489; -.
DR   OMA; KWNWEKF; -.
DR   OrthoDB; 67394at2759; -.
DR   Proteomes; UP000015103; Unassembled WGS sequence.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR   PANTHER; PTHR11592:SF88; 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; 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:UP000015103}.
SQ   SEQUENCE   147 AA;  16973 MW;  04FEABC10CE2B3B9 CRC64;
     GFTPHYFGLN ALKEKYGEKI EILGVPCNQF GMQEPGKNFS EIMNGIKYVR PGNGFIPCFP
     LTEKIDVNGE NEHPMFTYLK KYCPSTRDGF SNKHELFYAP FKNWDVRWNF EKFLVDAKGY
     PYLRYDPSTE PISGITSDIE AIIHSEN
//
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