ID A0A158PP78_ANISI Unreviewed; 237 AA.
AC A0A158PP78;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 03-MAY-2023, entry version 27.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|ARBA:ARBA00012310, ECO:0000256|RuleBase:RU000499};
GN ORFNames=ASIM_LOCUS13287 {ECO:0000313|EMBL:VDK49354.1};
OS Anisakis simplex (Herring worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC Anisakis simplex complex.
OX NCBI_TaxID=6269 {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0001385901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ASIM_0001385901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK49354.1, ECO:0000313|Proteomes:UP000267096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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; UYRR01031355; VDK49354.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158PP78; -.
DR WBParaSite; ASIM_0001385901-mRNA-1; ASIM_0001385901-mRNA-1; ASIM_0001385901.
DR Proteomes; UP000036680; Unplaced.
DR Proteomes; UP000267096; Unassembled WGS sequence.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC.
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; IPR029760; GPX_CS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR PANTHER; PTHR11592:SF88; GLUTATHIONE PEROXIDASE-RELATED; 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; 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:UP000267096};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..237
FT /note="Glutathione peroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035112093"
FT ACT_SITE 85
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 237 AA; 27134 MW; 2F58442E28D0C64F CRC64;
MTIGHSATAS AGILLLVAVS IVQQGHHVNA TPGPAVVDET SRWTQCRLSN QSIYDFQVQQ
LDGKFTDLSK YRGQVLLIIN VATFCAFTQQ YLDFNPLIEQ NKRTTFKILA FPCNQFALQE
PSENHELLNG IRYVRPGNGW KPHSNLHIFG KLQVNGENNH PLYEFVKDQC PQTVNRIGKR
DELMYDPIRP SDITWNFEKF LVDRQGKVRF RFHPTAWSHG DVVQPFIQQL ANERARA
//