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Database: UniProt
Entry: A0A2K6GSM4_PROCO
LinkDB: A0A2K6GSM4_PROCO
Original site: A0A2K6GSM4_PROCO 
ID   A0A2K6GSM4_PROCO        Unreviewed;       222 AA.
AC   A0A2K6GSM4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU003494};
DE            EC=2.5.1.18 {ECO:0000256|RuleBase:RU003494};
OS   Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS   coquereli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Indriidae; Propithecus.
OX   NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000029241.1, ECO:0000313|Proteomes:UP000233160};
RN   [1] {ECO:0000313|Ensembl:ENSPCOP00000029241.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:0000256|RuleBase:RU003494};
CC   -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC       {ECO:0000256|ARBA:ARBA00011055, ECO:0000256|RuleBase:RU003494}.
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DR   RefSeq; XP_012504047.1; XM_012648593.1.
DR   AlphaFoldDB; A0A2K6GSM4; -.
DR   STRING; 379532.ENSPCOP00000029241; -.
DR   Ensembl; ENSPCOT00000040177.1; ENSPCOP00000029241.1; ENSPCOG00000027305.1.
DR   GeneID; 105813799; -.
DR   KEGG; pcoq:105813799; -.
DR   GeneTree; ENSGT00940000154526; -.
DR   OMA; FTEMIMN; -.
DR   OrthoDB; 3412208at2759; -.
DR   Proteomes; UP000233160; Unplaced.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03208; GST_C_Alpha; 1.
DR   CDD; cd03077; GST_N_Alpha; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 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; IPR003080; GST_alpha.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR11571:SF107; GLUTATHIONE S-TRANSFERASE A2; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01266; GSTRNSFRASEA.
DR   SFLD; SFLDG01205; AMPS.1; 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 {ECO:0000313|Proteomes:UP000233160};
KW   Transferase {ECO:0000256|RuleBase:RU003494}.
FT   DOMAIN          3..83
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          85..208
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   222 AA;  25410 MW;  AC2820E969147D2E CRC64;
     MAGKPKLHYF NARGRMESIR WLLAAAGVEF EEKFIASPED LDKLRNDGRL MFQQVPMVEI
     DGMELAQTRA ILNYIASKHN LYGKDLKERA LIDMYIEGMA DLNEMIIMFP MHPPAEKDAK
     LAFIKEKTTN RYFPAFEKVL KSHGQDYLVG NRLSRADIHL VELIYNVEEL DPSLTANFPL
     LKALKTRISN LPTVKKFLQP GSQRKPPVTA EAIEAARKVF KF
//
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