ID GSTA3_DICDI Reviewed; 204 AA.
AC Q54VI4;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Putative glutathione S-transferase alpha-3;
DE EC=2.5.1.18;
DE AltName: Full=GST class-alpha 3;
GN Name=gsta3; ORFNames=DDB_G0280317;
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).
RN [2]
RP PROTEIN SEQUENCE OF 2-10; 37-80; 114-123; 128-135 AND 174-188, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V., Patel H., Brunton V.G., Frame M.C.;
RL Submitted (APR-2008) to UniProtKB.
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 Evidence={ECO:0000250|UniProtKB:Q16772};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC Evidence={ECO:0000250|UniProtKB:Q16772};
CC -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000035; EAL67385.1; -; Genomic_DNA.
DR RefSeq; XP_641371.1; XM_636279.1.
DR AlphaFoldDB; Q54VI4; -.
DR SMR; Q54VI4; -.
DR STRING; 44689.Q54VI4; -.
DR PaxDb; 44689-DDB0231429; -.
DR EnsemblProtists; EAL67385; EAL67385; DDB_G0280317.
DR GeneID; 8622505; -.
DR KEGG; ddi:DDB_G0280317; -.
DR dictyBase; DDB_G0280317; -.
DR eggNOG; KOG1695; Eukaryota.
DR HOGENOM; CLU_039475_1_0_1; -.
DR InParanoid; Q54VI4; -.
DR OMA; EMIMQLP; -.
DR PhylomeDB; Q54VI4; -.
DR Reactome; R-DDI-156590; Glutathione conjugation.
DR Reactome; R-DDI-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR PRO; PR:Q54VI4; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:1904643; P:response to curcumin; IDA: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:SF258; GLUTATHIONE S-TRANSFERASE ALPHA-3-RELATED; 1.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 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.2"
FT CHAIN 2..204
FT /note="Putative glutathione S-transferase alpha-3"
FT /id="PRO_0000350740"
FT DOMAIN 2..79
FT /note="GST N-terminal"
FT DOMAIN 81..202
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 49..50
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P30711"
FT BINDING 63..64
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P13745"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000269|Ref.2"
SQ SEQUENCE 204 AA; 23606 MW; 16D7B61EDC21DCDA CRC64;
MTKPQLSYFK VRALGQFPRV LLSYLSIDYD NNYIDKIDEN IIDDLKYGQL PLYTDSNGFK
LVQSMAISKY IASQHDFVGK TPEEKALVDE TLAAVNIDVF TFIIRVFRGV EEKEKIQEII
IPRFFAKWNQ ILGEKKYLAG GNSYTLADLY VYVAYEYIGY VLPFAADLLY NGKFPHLDSL
KEHFESNKGV AEYLKNRPIT ERKI
//
