ID A0A183A6F6_9TREM Unreviewed; 219 AA.
AC A0A183A6F6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
GN ORFNames=ECPE_LOCUS2541 {ECO:0000313|EMBL:VDP66748.1};
OS Echinostoma caproni.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Echinostomatidae;
OC Echinostoma.
OX NCBI_TaxID=27848 {ECO:0000313|Proteomes:UP000050740, ECO:0000313|WBParaSite:ECPE_0000254101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ECPE_0000254101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP66748.1, ECO:0000313|Proteomes:UP000272942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Egypt {ECO:0000313|EMBL:VDP66748.1,
RC ECO:0000313|Proteomes:UP000272942};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
CC {ECO:0000256|ARBA:ARBA00003701}.
CC -!- FUNCTION: GST isoenzymes appear to play a central role in the parasite
CC detoxification system. Other functions are also suspected including a
CC role in increasing the solubility of haematin in the parasite gut.
CC {ECO:0000256|ARBA:ARBA00002446}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000256|ARBA:ARBA00000710};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family.
CC {ECO:0000256|ARBA:ARBA00005861}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; UZAN01039683; VDP66748.1; -; Genomic_DNA.
DR WBParaSite; ECPE_0000254101-mRNA-1; ECPE_0000254101-mRNA-1; ECPE_0000254101.
DR Proteomes; UP000050740; Unplaced.
DR Proteomes; UP000272942; Unassembled WGS sequence.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IEA:UniProt.
DR CDD; cd03209; GST_C_Mu; 1.
DR CDD; cd03075; GST_N_Mu; 1.
DR Gene3D; 1.20.1050.130; -; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR003081; GST_mu.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR PANTHER; PTHR11571:SF222; GLUTATHIONE S-TRANSFERASE 2-RELATED; 1.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01267; GSTRNSFRASEM.
DR SFLD; SFLDG01205; AMPS.1; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000272942};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..83
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 85..204
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 219 AA; 25247 MW; F7B7241F4DD0682E CRC64;
MAAKLGYWKL RGLGQPIRLL LEFVGDHYEE VQYSEGDREK WQSEKFNLGL DLPNLPYYID
GHVKLTQSLA ILRYIAEKHG MTGSTPEERA RISXMIEGAA LDLRIGLARI AYNPQFEQLK
QDYVKNLPTV LKMWSNFLGE RKYLMGDSVT HVDFLLYEAL DVNKHLEPHC LDHFSNLIQF
MQHIENLPKI KAYMASNRFI KWPLHGWAAH FGGGHAPPS
//
