GSTA2_DICDI
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 03-AUG-2022, entry version 99.
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 (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=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.DDB0231432; -.
DR PaxDb; Q556G3; -.
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; AKPKLWY; -.
DR PhylomeDB; Q556G3; -.
DR Reactome; R-DDI-156590; Glutathione conjugation.
DR Reactome; R-DDI-189483; Heme degradation.
DR Reactome; R-DDI-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-9748787; Azathioprine ADME.
DR Reactome; R-DDI-9753281; Paracetamol ADME.
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:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:1904643; P:response to curcumin; IDA:dictyBase.
DR GO; GO:0031153; P:slug development involved in sorocarp development; IMP:dictyBase.
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 Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 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
