ID A0A0D9VP86_9ORYZ Unreviewed; 647 AA.
AC A0A0D9VP86;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
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:LPERR03G02540.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR03G02540.1, 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:LPERR03G02540.1, 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:LPERR03G02540.1}
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. Phi family.
CC {ECO:0000256|ARBA:ARBA00010128}.
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DR AlphaFoldDB; A0A0D9VP86; -.
DR STRING; 77586.A0A0D9VP86; -.
DR EnsemblPlants; LPERR03G02540.1; LPERR03G02540.1; LPERR03G02540.
DR Gramene; LPERR03G02540.1; LPERR03G02540.1; LPERR03G02540.
DR eggNOG; KOG0867; Eukaryota.
DR Proteomes; UP000032180; Chromosome 3.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR CDD; cd03187; GST_C_Phi; 3.
DR CDD; cd03053; GST_N_Phi; 1.
DR Gene3D; 1.20.1050.10; -; 3.
DR Gene3D; 3.40.30.10; Glutaredoxin; 3.
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; IPR004046; GST_C.
DR InterPro; IPR034347; GST_Phi_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43900; GLUTATHIONE S-TRANSFERASE RHO; 1.
DR PANTHER; PTHR43900:SF88; GLUTATHIONE TRANSFERASE; 1.
DR Pfam; PF00043; GST_C; 3.
DR Pfam; PF02798; GST_N; 3.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 3.
DR SFLD; SFLDG01154; Main.5:_Phi-like; 3.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 3.
DR SUPFAM; SSF52833; Thioredoxin-like; 3.
DR PROSITE; PS50405; GST_CTER; 3.
DR PROSITE; PS50404; GST_NTER; 3.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000032180}.
FT DOMAIN 3..84
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 95..233
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 206..287
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 295..437
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 410..491
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 499..631
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 647 AA; 73686 MW; 5DA765E2953BC4DD CRC64;
MAAPVTVYGP MISPAVARVA ACLLEKDVPF QVEPVDMSKG EHKSPSFLKL QPFGQVPAFK
DSLTTVFESR AICRYICDQY ADSGNKTLMG RKEDGAVGRA AIEQWIESEG QSFNPPSLSM
AFQLAFAPFM GRATDMAVVE ENEAKLVKVL DVYEQWLGEN QYFAGDEFSL ADLVHMPNTD
LLVRKTNKAG LFTERKNLAR WWDEVSARPS WKKPASTDVA RVLTCLFEKD LEFELVRIDT
FKREHKLPEF IKLRDPNGQV TFKHGDKTLV DSRAICRYVC TQFPKEGNKT LYGTGSLERA
SIEQWLQAEA QNFSPPSSAL VFHLAFAPHL SIPQDNAVIA ENEKKLQQVL NVYDEILSKN
EYLAGDEFTL ADLSHLPNSH YIVSSERGRK LFTSRKNVAR WYDQISKRKT WEQVFGQPAS
TDVARVLTCL FEKNLEFELI RIDTFKKEHK LPEFIKLRDP TGQVTFKHGD KTLVDSRAIC
RYLCTQFPED GNRTIYGTGS LERASIEQWL QAESQSFDAP SSELVFHLAF APQLNIPADE
ARIAENERKL QQMLNVYDEI LAKNKYLAGD EFTLADLSHL PNSHYIVNAR SPRGKKLFTS
KKHVARWFEE ISSRPSWKQV VKMQSEHPGA FEQEHTTIFL LKPHQSQ
//
