ID   GSTA2_DICDI             Reviewed;         198 AA.
AC   Q556G3; Q86AN9;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=Putative glutathione S-transferase alpha-2;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-alpha 2;
GN   Name=gsta2-1; ORFNames=DDB_G0272632;
GN   and
GN   Name=gsta2-2; ORFNames=DDB_G0274081;
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=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
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).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-15; 23-71; 116-127; 155-172; 178-188 AND 192-198,
RP   CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RA   Bienvenut W.V., Patel H., Brunton V.G., Frame M.C.;
RL   Submitted (APR-2008) to UniProtKB.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=AX2;
RX   PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA   Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA   Soldati T.;
RT   "Proteomics fingerprinting of phagosome maturation and evidence for the
RT   role of a Galpha during uptake.";
RL   Mol. Cell. Proteomics 5:2228-2243(2006).
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}.
CC   -!- CAUTION: The gene for this protein is duplicated in strains AX3 and
CC       AX4. These strains contain a duplication of a segment of 750 kb of
CC       chromosome 2 compared to the corresponding sequence in strain AX2.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000011; EAL70474.1; -; Genomic_DNA.
DR   EMBL; AAFI02000009; EAL70953.1; -; Genomic_DNA.
DR   RefSeq; XP_644399.1; XM_639307.1.
DR   RefSeq; XP_645014.1; XM_639922.1.
DR   AlphaFoldDB; Q556G3; -.
DR   SMR; Q556G3; -.
DR   STRING; 44689.Q556G3; -.
DR   PaxDb; 44689-DDB0231432; -.
DR   EnsemblProtists; EAL70474; EAL70474; DDB_G0274081.
DR   EnsemblProtists; EAL70953; EAL70953; DDB_G0272632.
DR   GeneID; 8618691; -.
DR   GeneID; 8619285; -.
DR   KEGG; ddi:DDB_G0272632; -.
DR   KEGG; ddi:DDB_G0274081; -.
DR   dictyBase; DDB_G0272632; gstA2-1.
DR   dictyBase; DDB_G0274081; gstA2-2.
DR   eggNOG; KOG1695; Eukaryota.
DR   HOGENOM; CLU_039475_1_0_1; -.
DR   InParanoid; Q556G3; -.
DR   OMA; EHYVETV; -.
DR   PhylomeDB; Q556G3; -.
DR   Reactome; R-DDI-156590; Glutathione conjugation.
DR   Reactome; R-DDI-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR   PRO; PR:Q556G3; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:dictyBase.
DR   GO; GO:1904643; P:response to curcumin; IDA:dictyBase.
DR   GO; GO:0031153; P:slug development involved in sorocarp development; IMP:dictyBase.
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:SF224; HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE; 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   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.3"
FT   CHAIN           2..198
FT                   /note="Putative glutathione S-transferase alpha-2"
FT                   /id="PRO_0000350739"
FT   DOMAIN          5..81
FT                   /note="GST N-terminal"
FT   DOMAIN          83..198
FT                   /note="GST C-terminal"
FT   BINDING         11
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P13745"
FT   BINDING         45
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08263"
FT   BINDING         52..53
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P30711"
FT   BINDING         65..66
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P13745"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|Ref.3"
SQ   SEQUENCE   198 AA;  22538 MW;  36104DBFD83CA2D1 CRC64;
     MSTSSVPSLT YFQGRGLGQF SRVLLSYLGI PYENITVTEI SDALRATLPY GQLPIYRDGD
     FVLTQSSTIA RYIAKKHNFM GKNLEEEFLV DQIVTAIHAD IFPAFNNPVP EKLQKLYEKY
     FGSFEKKLQE TGFLVGSSVT LADLYVYVGF DYIRFRGEAA LSSELSDEKY PKIAELKKFF
     ESNEGVAKYI KERPETKF
//