ID R0IC62_9BRAS Unreviewed; 232 AA.
AC R0IC62;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU369102};
DE EC=2.5.1.18 {ECO:0000256|RuleBase:RU369102};
GN Name=GSTU11 {ECO:0000313|EMBL:AML27034.1};
GN ORFNames=CARUB_v10021750mg {ECO:0000313|EMBL:EOA34238.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA34238.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
RN [2] {ECO:0000313|EMBL:EOA34238.1}
RP NUCLEOTIDE SEQUENCE.
RA Schmutz J., Prochnik S., Nordborg M., Weigel D., Rokhsar D., Wright S.;
RT "Genome sequencing of Capsella rubella.";
RL Nat. Genet. 0:0-0(2013).
RN [3] {ECO:0000313|EMBL:AML27034.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Mixed rossette leaf {ECO:0000313|EMBL:AML27034.1};
RA Lan T.;
RT "Genome-wide analysis of the glutathione S-transferase gene family in
RT Capsella rubella: identification, expression and biochemical functions.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KT935206; AML27034.1; -; mRNA.
DR EMBL; KB870806; EOA34238.1; -; Genomic_DNA.
DR RefSeq; XP_006301340.1; XM_006301278.1.
DR AlphaFoldDB; R0IC62; -.
DR STRING; 81985.R0IC62; -.
DR GeneID; 17894185; -.
DR KEGG; crb:17894185; -.
DR eggNOG; KOG0406; Eukaryota.
DR OrthoDB; 767442at2759; -.
DR Proteomes; UP000029121; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-UniRule.
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; 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:SF791; GLUTATHIONE S-TRANSFERASE U10; 1.
DR PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 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 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|RuleBase:RU369102};
KW Detoxification {ECO:0000256|ARBA:ARBA00022575};
KW Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW Transferase {ECO:0000256|RuleBase:RU369102, ECO:0000313|EMBL:AML27034.1}.
FT DOMAIN 6..85
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 91..226
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 232 AA; 26936 MW; 3D7E9BBA6C05A9E5 CRC64;
MEDQSNKVTL HGMWISTYSK RVEIALKIKG ILYQYVEEDL QNKSESLIQL NPVHKKIPVL
VHNGKPVAES LVILEYIDET WKNSPHFFPE DPYERGQVRF WVSYINQQVF EVMGQVVFQE
GEAQAKSVEE ARKRIKVLEE GLKKHFSNKI IRENDDVGLL EIIIIATFGA HKVYREAIGV
EIIDPVNTPT LYNWIECLQD LPVMKEVEVP RDKLVNFLQS YRQKRLQQAA SA
//
