ID   MGST_DICDI              Reviewed;         149 AA.
AC   Q54GA9;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Probable microsomal glutathione S-transferase;
DE            EC=2.5.1.18;
GN   Name=mgst; ORFNames=DDB_G0290291;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: May perform the conjugation of reduced glutathione to
CC       electrophiles. {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the MAPEG family. {ECO:0000305}.
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DR   EMBL; AAFI02000162; EAL62272.1; -; Genomic_DNA.
DR   RefSeq; XP_635774.1; XM_630682.1.
DR   AlphaFoldDB; Q54GA9; -.
DR   SMR; Q54GA9; -.
DR   STRING; 44689.DDB0231516; -.
DR   PaxDb; Q54GA9; -.
DR   EnsemblProtists; EAL62272; EAL62272; DDB_G0290291.
DR   GeneID; 8627578; -.
DR   KEGG; ddi:DDB_G0290291; -.
DR   dictyBase; DDB_G0290291; -.
DR   eggNOG; ENOG502RHV2; Eukaryota.
DR   HOGENOM; CLU_110291_3_1_1; -.
DR   InParanoid; Q54GA9; -.
DR   OMA; EYQNTSE; -.
DR   PhylomeDB; Q54GA9; -.
DR   Reactome; R-DDI-156590; Glutathione conjugation.
DR   Reactome; R-DDI-2142688; Synthesis of 5-eicosatetraenoic acids.
DR   Reactome; R-DDI-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR   Reactome; R-DDI-2142700; Synthesis of Lipoxins (LX).
DR   Reactome; R-DDI-5423646; Aflatoxin activation and detoxification.
DR   Reactome; R-DDI-9026762; Biosynthesis of maresin conjugates in tissue regeneration (MCTR).
DR   Reactome; R-DDI-9026766; Biosynthesis of protectin and resolvin conjugates in tissue regeneration (PCTR and RCTR).
DR   PRO; PR:Q54GA9; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IBA:GO_Central.
DR   GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR   Gene3D; 1.20.120.550; -; 1.
DR   InterPro; IPR023352; MAPEG-like_dom_sf.
DR   SUPFAM; SSF161084; SSF161084; 1.
PE   3: Inferred from homology;
KW   Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..149
FT                   /note="Probable microsomal glutathione S-transferase"
FT                   /id="PRO_0000331235"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   149 AA;  16626 MW;  FB822FF2A2C7818A CRC64;
     MPFDTKSIFP DFIVFPSAIS TIAIGLWSVQ AYKLGEARKR YNVKAPHVQG DPEFERIAHE
     YQNTSEALGA IIPATFMFSY YISPKCSLLL GGTWLVSKML NCCSYCCKKE KENDCAKNVH
     TCLSHISFFA LLGGSAFGIG SSLYNRYKL