ID Q9FQF0_SOYBN Unreviewed; 225 AA.
AC Q9FQF0;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
GN Name=GSTU30 {ECO:0000313|EMBL:AJE59666.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:AAG34798.1};
RN [1] {ECO:0000313|EMBL:AAG34798.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11080288; DOI=10.1104/pp.124.3.1105;
RA McGonigle B., Keeler S.J., Lau S.M., Koeppe M.K., O'Keefe D.P.;
RT "A genomics approach to the comprehensive analysis of the glutathione S-
RT transferase gene family in soybean and maize.";
RL Plant Physiol. 124:1105-1120(2000).
RN [2] {ECO:0000313|EMBL:AJE59666.1}
RP NUCLEOTIDE SEQUENCE.
RA Liu H.-J.;
RT "Evolutionary and functional dynamics of recent duplicate genes created by
RT whole genome duplication.";
RL Submitted (SEP-2014) 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.
CC {ECO:0000256|RuleBase:RU003494}.
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; AF243363; AAG34798.1; -; mRNA.
DR EMBL; KM818447; AJE59666.1; -; mRNA.
DR AlphaFoldDB; Q9FQF0; -.
DR SMR; Q9FQF0; -.
DR ProMEX; Q9FQF0; -.
DR ExpressionAtlas; Q9FQF0; baseline and differential.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0042221; P:response to chemical; 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; IPR004046; GST_C.
DR InterPro; IPR045074; GST_C_Tau.
DR InterPro; IPR045073; Omega/Tau-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1.
DR PANTHER; PTHR11260:SF719; GLUTATHIONE TRANSFERASE; 1.
DR Pfam; PF00043; GST_C; 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 Transferase {ECO:0000313|EMBL:AAG34798.1}.
FT DOMAIN 6..85
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 90..213
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 225 AA; 25852 MW; EE998FE94F7BA345 CRC64;
MASSQEEVTL LGATGSPFVC RVHIALKLKG VQYKYVEENL RNKSELLLKS NPVHKKVPVF
IHNEKPIAES LVIVEYIDET WKNNPILPSD PYQRALARFW SKFIDDKVFG AAWKSVFTAD
EKEREKNVEE AIEALQFLEN EIKDKKFFGG EEIGLVDIAA VYIAFWVPMV QEIAGLELFT
SEKFPKLHNW SQEFLNHPIV KESLPPRDPV FSFFKGLYES LFGSK
//
