GPX1_SCHMA
ID GPX1_SCHMA Reviewed; 169 AA.
AC Q00277;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Glutathione peroxidase;
DE Short=GPX;
DE EC=1.11.1.9;
GN Name=GPX1;
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Puerto Rican;
RX PubMed=1625700; DOI=10.1016/0166-6851(92)90042-i;
RA Williams D.L., Pierce R.J., Cookson E., Capron A.;
RT "Molecular cloning and sequencing of glutathione peroxidase from
RT Schistosoma mansoni.";
RL Mol. Biochem. Parasitol. 52:127-130(1992).
RN [2]
RP SEQUENCE REVISION TO 43.
RA Williams D.L., Pierce R.J., Cookson E., Capron A.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NMRI;
RX PubMed=7895842; DOI=10.1006/expr.1995.1038;
RA Mei H., Loverde P.T.;
RT "Schistosoma mansoni: cloning the gene encoding glutathione peroxidase.";
RL Exp. Parasitol. 80:319-322(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Puerto Rican;
RX PubMed=8125294; DOI=10.1016/0378-1119(94)90798-6;
RA Roche C., Williams D.L., Khalife J., Lepresle T., Capron A., Pierce R.J.;
RT "Cloning and characterization of the gene encoding Schistosoma mansoni
RT glutathione peroxidase.";
RL Gene 138:149-152(1994).
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 -!- INDUCTION: Activity increases significantly as worms mature in their
CC host and is positively correlated to the resistance to antioxidants.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
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DR EMBL; M86510; AAA29885.2; -; mRNA.
DR EMBL; L37762; AAC14468.2; -; Genomic_DNA.
DR EMBL; L14328; AAB08485.2; -; Genomic_DNA.
DR RefSeq; XP_018645850.1; XM_018790830.1.
DR PDB; 2V1M; X-ray; 1.00 A; A=1-169.
DR PDB; 2WGR; X-ray; 1.70 A; A=1-169.
DR PDBsum; 2V1M; -.
DR PDBsum; 2WGR; -.
DR SMR; Q00277; -.
DR STRING; 6183.Smp_058690.1; -.
DR PeroxiBase; 3745; SmamGPx01.
DR GeneID; 8352588; -.
DR KEGG; smm:Smp_058690; -.
DR CTD; 8352588; -.
DR eggNOG; KOG1651; Eukaryota.
DR HOGENOM; CLU_029507_0_1_1; -.
DR OMA; NGEDCHE; -.
DR OrthoDB; 1483113at2759; -.
DR BRENDA; 1.11.1.9; 5608.
DR EvolutionaryTrace; Q00277; -.
DR Proteomes; UP000008854; 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 InterPro; IPR000889; Glutathione_peroxidase.
DR InterPro; IPR029759; GPX_AS.
DR InterPro; IPR029760; GPX_CS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11592; PTHR11592; 1.
DR Pfam; PF00255; GSHPx; 1.
DR PIRSF; PIRSF000303; Glutathion_perox; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Oxidoreductase; Peroxidase; Reference proteome;
KW Selenocysteine.
FT CHAIN 1..169
FT /note="Glutathione peroxidase"
FT /id="PRO_0000066645"
FT ACT_SITE 43
FT /evidence="ECO:0000250"
FT NON_STD 43
FT /note="Selenocysteine"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:2V1M"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:2V1M"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:2V1M"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:2V1M"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:2V1M"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2V1M"
FT HELIX 46..60
FT /evidence="ECO:0007829|PDB:2V1M"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:2V1M"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:2V1M"
FT TURN 74..77
FT /evidence="ECO:0007829|PDB:2WGR"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:2V1M"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:2V1M"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:2V1M"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:2V1M"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:2V1M"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:2V1M"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:2V1M"
FT HELIX 159..167
FT /evidence="ECO:0007829|PDB:2V1M"
SQ SEQUENCE 169 AA; 19471 MW; 4B787788913F84B0 CRC64;
MSSSHKSWNS IYEFTVKDIN GVDVSLEKYR GHVCLIVNVA CKUGATDKNY RQLQEMHTRL
VGKGLRILAF PCNQFGGQEP WAEAEIKKFV TEKYGVQFDM FSKIKVNGSD ADDLYKFLKS
RQHGTLTNNI KWNFSKFLVD RQGQPVKRYS PTTAPYDIEG DIMELLEKK
