GSTU6_ARATH
ID GSTU6_ARATH Reviewed; 223 AA.
AC Q9ZW26;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Glutathione S-transferase U6;
DE Short=AtGSTU6;
DE EC=2.5.1.18;
DE AltName: Full=GST class-tau member 6;
DE AltName: Full=Glutathione S-transferase 24;
GN Name=GSTU6; Synonyms=GST24; OrderedLocusNames=At2g29440; ORFNames=F16P2.18;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=12090627; DOI=10.1023/a:1015557300450;
RA Wagner U., Edwards R., Dixon D.P., Mauch F.;
RT "Probing the diversity of the Arabidopsis glutathione S-transferase gene
RT family.";
RL Plant Mol. Biol. 49:515-532(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in the conjugation of reduced glutathione to
CC a wide number of exogenous and endogenous hydrophobic electrophiles and
CC have a detoxification role against certain herbicides. {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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Tau family. {ECO:0000305}.
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; AF288187; AAG30136.1; -; mRNA.
DR EMBL; AC004561; AAC95194.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08254.1; -; Genomic_DNA.
DR EMBL; BT024843; ABD60726.1; -; mRNA.
DR EMBL; AK229012; BAF00899.1; -; mRNA.
DR PIR; D84696; D84696.
DR RefSeq; NP_180505.1; NM_128498.5.
DR AlphaFoldDB; Q9ZW26; -.
DR SMR; Q9ZW26; -.
DR STRING; 3702.AT2G29440.1; -.
DR PaxDb; Q9ZW26; -.
DR PRIDE; Q9ZW26; -.
DR ProteomicsDB; 247191; -.
DR EnsemblPlants; AT2G29440.1; AT2G29440.1; AT2G29440.
DR GeneID; 817493; -.
DR Gramene; AT2G29440.1; AT2G29440.1; AT2G29440.
DR KEGG; ath:AT2G29440; -.
DR Araport; AT2G29440; -.
DR TAIR; locus:2043057; AT2G29440.
DR eggNOG; KOG0406; Eukaryota.
DR HOGENOM; CLU_011226_18_1_1; -.
DR InParanoid; Q9ZW26; -.
DR OMA; PFCLERA; -.
DR OrthoDB; 1225872at2759; -.
DR PhylomeDB; Q9ZW26; -.
DR BioCyc; ARA:AT2G29440-MON; -.
DR PRO; PR:Q9ZW26; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZW26; baseline and differential.
DR Genevisible; Q9ZW26; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
DR CDD; cd03185; GST_C_Tau; 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; PTHR11260; 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; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Detoxification; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..223
FT /note="Glutathione S-transferase U6"
FT /id="PRO_0000413552"
FT DOMAIN 5..84
FT /note="GST N-terminal"
FT DOMAIN 89..216
FT /note="GST C-terminal"
FT BINDING 15..16
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 41..42
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 55..56
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 68..69
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT MOD_RES 150
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ZW27"
SQ SEQUENCE 223 AA; 25618 MW; AD15D4CD0C91B95F CRC64;
MGKNEEVKLL GIWASPFSRR IEMALKLKGV PYEYLEEDLE NKSSLLLALS PIHKKIPVLV
HNGKTIIESH VILEYIDETW KHNPILPQDP FQRSKARVLA KLVDEKIVNV GFASLAKTEK
GREVLIEQTR ELIMCLEKEL AGKDYFGGKT VGFLDFVAGS MIPFCLERAW EGMGVEMITE
KKFPEYNKWV KKLKEVEIVV DCIPLREKHI EHMNNMAEKI RSA