ID A0A0D9VP85_9ORYZ Unreviewed; 320 AA.
AC A0A0D9VP85;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR03G02530.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR03G02530.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR03G02530.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR03G02530.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A0D9VP85; -.
DR STRING; 77586.A0A0D9VP85; -.
DR EnsemblPlants; LPERR03G02530.1; LPERR03G02530.1; LPERR03G02530.
DR Gramene; LPERR03G02530.1; LPERR03G02530.1; LPERR03G02530.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_5_5_1; -.
DR Proteomes; UP000032180; Chromosome 3.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
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; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43900; GLUTATHIONE S-TRANSFERASE RHO; 1.
DR PANTHER; PTHR43900:SF38; GLUTATHIONE S-TRANSFERASE, N-TERMINAL DOMAIN CONTAINING PROTEIN, EXPRESSED; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000032180}.
FT DOMAIN 4..85
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 93..270
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT REGION 157..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 182..209
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 278..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 320 AA; 35789 MW; 23FA03559FFF2A9D CRC64;
MAPASVKVFG SPTSAEVARV LMCLFEKDVE FQLVRVDAYR GPQRMPQYLK LQPRGEALTF
EDDNLTLSES RGILRHIAHK YARQGNPDLI GTGALERASI EQWLQTEAQS FDVPSAEMVY
SLAFLPPTMP KQNDNGNSNG NGRDVQVANA GSKRVVAGTA APEGTMNTAA SGGKQQKEEE
MRRLFEKSKK DLEKLLDIYE QRLEEAAYLA GDKFTIADLS HLPNADRLAS DPRSRRMFEA
RKNVSRWWNE ISKRESWEYV RSLQRPPSTV VDAAGEAHAN SNGQQQRGAS AGEQRGNDSS
NQQQGQQQHY RNDQVENYSN
//
