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Database: UniProt
Entry: A0A2G5DTY7_AQUCA
LinkDB: A0A2G5DTY7_AQUCA
Original site: A0A2G5DTY7_AQUCA 
ID   A0A2G5DTY7_AQUCA        Unreviewed;       244 AA.
AC   A0A2G5DTY7;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   13-SEP-2023, entry version 19.
DE   RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE            EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
GN   ORFNames=AQUCO_01400012v1 {ECO:0000313|EMBL:PIA46994.1};
OS   Aquilegia coerulea (Rocky mountain columbine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC   Aquilegia.
OX   NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA46994.1, ECO:0000313|Proteomes:UP000230069};
RN   [1] {ECO:0000313|EMBL:PIA46994.1, ECO:0000313|Proteomes:UP000230069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA   Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA   Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT   "WGS assembly of Aquilegia coerulea Goldsmith.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000710};
CC   -!- SIMILARITY: Belongs to the GST superfamily. Zeta family.
CC       {ECO:0000256|ARBA:ARBA00010007}.
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DR   EMBL; KZ305031; PIA46994.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5DTY7; -.
DR   Proteomes; UP000230069; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009072; P:aromatic amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR   CDD; cd03191; GST_C_Zeta; 1.
DR   CDD; cd03042; GST_N_Zeta; 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; IPR004046; GST_C.
DR   InterPro; IPR005955; GST_Zeta.
DR   InterPro; IPR034330; GST_Zeta_C.
DR   InterPro; IPR034333; GST_Zeta_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR01262; maiA; 1.
DR   PANTHER; PTHR42673; MALEYLACETOACETATE ISOMERASE; 1.
DR   PANTHER; PTHR42673:SF4; MALEYLACETOACETATE ISOMERASE; 1.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 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:UP000230069}.
FT   DOMAIN          30..113
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          118..244
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   244 AA;  27494 MW;  1B43F11B45D77DE8 CRC64;
     MEKKIKDNDT SGGCSGGELV VVTEEDDSKL KLKLYSYYRS SCSWRVRIAL NLKGLKYEYK
     AVNLLKGDQF SQEFTKLNPI GYVPVLTDDE QDIVISDSFA ILLYLEDKYP QHPLLPQDLQ
     KKAINLQAAN IVSSSIQPLQ NLAVLKYIEE KVSSAEKLTW VQYHIGKGFA ALEKLLEGCC
     GKYATGNEVF LADLFLAPQI DAAITRFSLD MTQYPLLSRL HNAYMELPAF QAAVPERQPD
     YVKP
//
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