ID   GSTA5_DICDI             Reviewed;         198 AA.
AC   Q54QV7;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   RecName: Full=Putative glutathione S-transferase alpha-5;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-alpha 5;
GN   Name=gsta5; ORFNames=DDB_G0283575;
OS   Dictyostelium discoideum (Social amoeba).
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: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic 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   -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000055; EAL65665.1; -; Genomic_DNA.
DR   RefSeq; XP_639027.1; XM_633935.1.
DR   AlphaFoldDB; Q54QV7; -.
DR   SMR; Q54QV7; -.
DR   STRING; 44689.Q54QV7; -.
DR   PaxDb; 44689-DDB0231408; -.
DR   EnsemblProtists; EAL65665; EAL65665; DDB_G0283575.
DR   GeneID; 8624155; -.
DR   KEGG; ddi:DDB_G0283575; -.
DR   dictyBase; DDB_G0283575; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   HOGENOM; CLU_039475_1_0_1; -.
DR   InParanoid; Q54QV7; -.
DR   OMA; RVLQMYY; -.
DR   PhylomeDB; Q54QV7; -.
DR   Reactome; R-DDI-156590; Glutathione conjugation.
DR   Reactome; R-DDI-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR   PRO; PR:Q54QV7; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03192; GST_C_Sigma_like; 1.
DR   CDD; cd03039; GST_N_Sigma_like; 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; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR11571:SF258; GLUTATHIONE S-TRANSFERASE ALPHA-3-RELATED; 1.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDG00363; AMPS_(cytGST):_Alpha-__Mu-__Pi; 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; Transferase.
FT   CHAIN           1..198
FT                   /note="Putative glutathione S-transferase alpha-5"
FT                   /id="PRO_0000350742"
FT   DOMAIN          2..78
FT                   /note="GST N-terminal"
FT   DOMAIN          80..198
FT                   /note="GST C-terminal"
FT   BINDING         8
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P13745"
FT   BINDING         42
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08263"
FT   BINDING         49..50
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P30711"
FT   BINDING         62..63
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P13745"
SQ   SEQUENCE   198 AA;  23298 MW;  A5B154C82270C654 CRC64;
     MTKPTLTYFP VRGRVQFPRC LLEYLGEEYN FNEVKTISDD LRKQLLFKQL PLYQEGDFKI
     VQTPAIIDYI SEKHDFRGKT KEERARAHQC LAGIMEVLDH CLGYSFKMDK QQQEKFRNES
     PIKKFFEGFE MVLSQNKYLA SGEKETYVDL MAFVMVDYVT NLGLMPSGDY PKLISLKKHY
     ESSPQLKKYL ESRPQSNF
//