ID B9R999_RICCO Unreviewed; 231 AA.
AC B9R999;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU369102};
DE EC=2.5.1.18 {ECO:0000256|RuleBase:RU369102};
GN ORFNames=RCOM_1515070 {ECO:0000313|EMBL:EEF52176.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
CC -!- FUNCTION: Is involved in the conjugation of reduced glutathione to a
CC wide number of exogenous and endogenous hydrophobic electrophiles.
CC {ECO:0000256|RuleBase:RU369102}.
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 ECO:0000256|RuleBase:RU369102};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|RuleBase:RU369102}.
CC -!- SIMILARITY: Belongs to the GST superfamily.
CC {ECO:0000256|RuleBase:RU369102}.
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DR EMBL; EQ973773; EEF52176.1; -; Genomic_DNA.
DR RefSeq; XP_002511574.1; XM_002511528.2.
DR AlphaFoldDB; B9R999; -.
DR STRING; 3988.B9R999; -.
DR GeneID; 8277424; -.
DR KEGG; rcu:8277424; -.
DR eggNOG; KOG0406; Eukaryota.
DR InParanoid; B9R999; -.
DR OrthoDB; 767442at2759; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
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; IPR045074; GST_C_Tau.
DR InterPro; IPR045073; Omega/Tau-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11260:SF711; GLUTATHIONE S-TRANSFERASE U9; 1.
DR PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 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 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU369102};
KW Lyase {ECO:0000313|EMBL:EEF52176.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW Transferase {ECO:0000256|RuleBase:RU369102, ECO:0000313|EMBL:EEF52176.1}.
FT DOMAIN 5..84
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 90..231
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 231 AA; 26297 MW; EDABE15DA0618D0A CRC64;
MGEENKVTLH GTWGSPFTKR VELALKLKGI TFNYVEEDLR NKSQLLLHYN PVHKKVPVLV
HNGRPIAESF VIIEYIDETW KSGPKLLPED PYGRAKVRFW ANYIQQKLFD TMFLVITTNG
EAQDKAGKEV MENLKVLENG MKDFLQDGIP TINSENVGLV DIIMCSLFSP HKAQEEVLGV
KIIDPDKTPL IFSWITSINE LPAVKEITPP HEKLVELLQF LRQKYGQPST A
//