GenomeNet

Database: UniProt
Entry: D7KFC3_ARALL
LinkDB: D7KFC3_ARALL
Original site: D7KFC3_ARALL 
ID   D7KFC3_ARALL            Unreviewed;       218 AA.
AC   D7KFC3;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU369102};
DE            EC=2.5.1.18 {ECO:0000256|RuleBase:RU369102};
GN   ORFNames=ARALYDRAFT_471920 {ECO:0000313|EMBL:EFH66466.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
CC   -!- FUNCTION: Is involved in the conjugation of reduced glutathione to a
CC       wide number of exogenous and endogenous hydrophobic electrophiles.
CC       {ECO:0000256|RuleBase:RU369102}.
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         ECO:0000256|RuleBase:RU369102};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|RuleBase:RU369102}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Tau family.
CC       {ECO:0000256|ARBA:ARBA00025743}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GL348713; EFH66466.1; -; Genomic_DNA.
DR   RefSeq; XP_002890207.1; XM_002890161.1.
DR   AlphaFoldDB; D7KFC3; -.
DR   STRING; 81972.D7KFC3; -.
DR   EnsemblPlants; fgenesh2_kg.1__1874__AT1G17170.1; fgenesh2_kg.1__1874__AT1G17170.1; fgenesh2_kg.1__1874__AT1G17170.1.
DR   Gramene; fgenesh2_kg.1__1874__AT1G17170.1; fgenesh2_kg.1__1874__AT1G17170.1; fgenesh2_kg.1__1874__AT1G17170.1.
DR   eggNOG; KOG0406; Eukaryota.
DR   HOGENOM; CLU_011226_18_2_1; -.
DR   OrthoDB; 767442at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0043295; F:glutathione binding; IEA:EnsemblPlants.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046256; P:2,4,6-trinitrotoluene catabolic process; IEA:EnsemblPlants.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   GO; GO:0009407; P:toxin catabolic process; IEA:UniProt.
DR   CDD; cd03185; GST_C_Tau; 1.
DR   CDD; cd03058; GST_N_Tau; 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; IPR045074; GST_C_Tau.
DR   InterPro; IPR045073; Omega/Tau-like.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11260:SF549; GLUTATHIONE S-TRANSFERASE U24; 1.
DR   PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1.
DR   Pfam; PF13410; GST_C_2; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 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   Cytoplasm {ECO:0000256|RuleBase:RU369102};
KW   Detoxification {ECO:0000256|ARBA:ARBA00022575};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW   Transferase {ECO:0000256|RuleBase:RU369102}.
FT   DOMAIN          3..82
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          88..207
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   218 AA;  25395 MW;  2B8A9AEE542B1A28 CRC64;
     MAEEVILLDF WASMFGMRIR IALSEKRVKY DYREEDLWDK SSLLLEMNPV HKKIPVLIHN
     GKPVCESLIQ IEYIDETWPD KNPLLPSDPY KRAHAKFWAD FIDKKVNVTA RRIWAAKGEE
     QEAAKEFIEI LKTLESELGD KKYFGDETFG YVDIALIGFY SWFGVYEKFG NISIESECSK
     LIAWAKRCLE RESVAKALPE SEKVTTFVSD RRKKLGLE
//
DBGET integrated database retrieval system