GSTX6_SOYBN
ID GSTX6_SOYBN Reviewed; 225 AA.
AC P32110;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Probable glutathione S-transferase;
DE EC=2.5.1.18;
DE AltName: Full=G2-4;
DE AltName: Full=Heat shock protein 26A;
GN Name=HSP26-A;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2835661; DOI=10.1128/mcb.8.3.1113-1122.1988;
RA Czarnecka E., Nagao R.T., Key J.L., Gurley W.B.;
RT "Characterization of Gmhsp26-A, a stress gene encoding a divergent heat
RT shock protein of soybean: heavy-metal-induced inhibition of intron
RT processing.";
RL Mol. Cell. Biol. 8:1113-1122(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 86-225.
RX PubMed=3360788; DOI=10.1016/s0021-9258(18)68806-4;
RA Hagen G., Uhrhammer N., Guilfoyle T.J.;
RT "Regulation of expression of an auxin-induced soybean sequence by
RT cadmium.";
RL J. Biol. Chem. 263:6442-6446(1988).
CC -!- FUNCTION: May play a role in the cellular response to stress.
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 -!- INDUCTION: By heat shock and auxin; by heavy metals like cadmium,
CC silver and copper.
CC -!- SIMILARITY: Belongs to the GST superfamily. HSP26 family.
CC {ECO:0000305}.
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DR EMBL; M20363; AAA33973.1; -; Genomic_DNA.
DR EMBL; J03197; AAA33943.1; -; Genomic_DNA.
DR PIR; A33654; A33654.
DR RefSeq; NP_001238439.1; NM_001251510.1.
DR AlphaFoldDB; P32110; -.
DR SMR; P32110; -.
DR STRING; 3847.GLYMA07G16810.1; -.
DR PRIDE; P32110; -.
DR EnsemblPlants; KRH49213; KRH49213; GLYMA_07G139700.
DR GeneID; 100527851; -.
DR Gramene; KRH49213; KRH49213; GLYMA_07G139700.
DR KEGG; gmx:100527851; -.
DR eggNOG; KOG0406; Eukaryota.
DR HOGENOM; CLU_011226_18_1_1; -.
DR InParanoid; P32110; -.
DR OMA; FWIPASE; -.
DR OrthoDB; 1225872at2759; -.
DR SABIO-RK; P32110; -.
DR Proteomes; UP000008827; Chromosome 7.
DR Genevisible; P32110; GM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0009737; P:response to abscisic acid; TAS:AgBase.
DR GO; GO:0009733; P:response to auxin; TAS:AgBase.
DR GO; GO:0009735; P:response to cytokinin; TAS:AgBase.
DR GO; GO:0009739; P:response to gibberellin; TAS:AgBase.
DR GO; GO:0009408; P:response to heat; TAS:AgBase.
DR GO; GO:0010038; P:response to metal ion; TAS:AgBase.
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; 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; PTHR11260; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 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 Reference proteome; Stress response; Transferase.
FT CHAIN 1..225
FT /note="Probable glutathione S-transferase"
FT /id="PRO_0000185871"
FT DOMAIN 6..85
FT /note="GST N-terminal"
FT DOMAIN 90..214
FT /note="GST C-terminal"
FT BINDING 16
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 69..70
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT CONFLICT 216
FT /note="A -> E (in Ref. 2; AAA33943)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 225 AA; 26011 MW; 9E89AC46A312E240 CRC64;
MAATQEDVKL LGIVGSPFVC RVQIALKLKG VEYKFLEENL GNKSDLLLKY NPVHKKVPVF
VHNEQPIAES LVIVEYIDET WKNNPILPSD PYQRALARFW SKFIDDKIVG AVSKSVFTVD
EKEREKNVEE TYEALQFLEN ELKDKKFFGG EEFGLVDIAA VFIAFWIPIF QEIAGLQLFT
SEKFPILYKW SQEFLNHPFV HEVLPPRDPL FAYFKARYES LSASK
