ID E3MAZ2_CAERE Unreviewed; 223 AA.
AC E3MAZ2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|ARBA:ARBA00012310, ECO:0000256|RuleBase:RU000499};
GN ORFNames=CRE_16659 {ECO:0000313|EMBL:EFO97434.1}, FL81_01324
GN {ECO:0000313|EMBL:POM50555.1}, GCK72_023325
GN {ECO:0000313|EMBL:KAF1746867.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EFO97434.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|EMBL:EFO97434.1};
RG The Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:POM50555.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX356 {ECO:0000313|EMBL:POM50555.1};
RX PubMed=26114425; DOI=10.1371/journal.pgen.1005323;
RA Fierst J.L., Willis J.H., Thomas C.G., Wang W., Reynolds R.M.,
RA Ahearne T.E., Cutter A.D., Phillips P.C.;
RT "Reproductive Mode and the Evolution of Genome Size and Structure in
RT Caenorhabditis Nematodes.";
RL PLoS Genet. 11:e1005323-e1005323(2015).
RN [4] {ECO:0000313|EMBL:POM50555.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX356 {ECO:0000313|EMBL:POM50555.1};
RX PubMed=26394399; DOI=10.1371/journal.pgen.1005497;
RA Fierst J.L., Willis J.H., Thomas C.G., Wang W., Reynolds R.M.,
RA Ahearne T.E., Cutter A.D., Phillips P.C.;
RT "Correction: Reproductive Mode and the Evolution of Genome Size and
RT Structure in Caenorhabditis Nematodes.";
RL PLoS Genet. 11:e1005497-e1005497(2015).
RN [5] {ECO:0000313|EMBL:POM50555.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PX356 {ECO:0000313|EMBL:POM50555.1};
RA Banno H., Chua N.-H.;
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:KAF1746867.1, ECO:0000313|Proteomes:UP000483820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX506 {ECO:0000313|EMBL:KAF1746867.1,
RC ECO:0000313|Proteomes:UP000483820};
RC TISSUE=Whole organism {ECO:0000313|EMBL:KAF1746867.1};
RA Teterina A.A., Willis J.H., Phillips P.C.;
RT "Chromosome-level assembly of the Caenorhabditis remanei genome.";
RL Submitted (DEC-2019) 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; DS268432; EFO97434.1; -; Genomic_DNA.
DR EMBL; WUAV01000006; KAF1746867.1; -; Genomic_DNA.
DR EMBL; LFJK02000005; POM50555.1; -; Genomic_DNA.
DR RefSeq; XP_003106828.1; XM_003106780.1.
DR AlphaFoldDB; E3MAZ2; -.
DR STRING; 31234.E3MAZ2; -.
DR EnsemblMetazoa; CRE16659.1; CRE16659.1; WBGene00081886.
DR GeneID; 9809194; -.
DR KEGG; crq:GCK72_023325; -.
DR CTD; 9809194; -.
DR eggNOG; KOG1651; Eukaryota.
DR HOGENOM; CLU_029507_2_1_1; -.
DR OMA; HELMNGI; -.
DR OrthoDB; 67394at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR Proteomes; UP000483820; Chromosome x.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0000302; P:response to reactive oxygen species; IEA:EnsemblMetazoa.
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 InterPro; IPR013766; Thioredoxin_domain.
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.
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:UP000008281};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..223
FT /note="Glutathione peroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015089682"
FT DOMAIN 34..219
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 72
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 223 AA; 25838 MW; 23CEDD1F08DC34DC CRC64;
MALWQLTLAA LFALAAAQPG PKMVDETTRW SQCRDTNQSI YDFQVETLQG EYTDLSQYRG
QVLLMVNVAT FCAYTQQYTD FNPLIEKYQS QGFTLIAFPC NQFYLQEPAE NHELMNGIMY
VRPGNGWKPH QNLHIYGKLE TNGENHHPIY EFVKESCPQT VDKIGKTDEL MYNPIRASDI
TWNFEKFLID RNGQPRFRFH PTAWSHGDVV TPFIEQLLAE QAN
//