ID A0A067EHR5_CITSI Unreviewed; 155 AA.
AC A0A067EHR5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU369102};
DE EC=2.5.1.18 {ECO:0000256|RuleBase:RU369102};
GN ORFNames=CISIN_1g040899mg {ECO:0000313|EMBL:KDO50481.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO50481.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO50481.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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. Tau family.
CC {ECO:0000256|ARBA:ARBA00025743}.
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DR EMBL; KK785078; KDO50481.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067EHR5; -.
DR Proteomes; UP000027120; 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:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0009407; P:toxin catabolic process; 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:SF781; GLUTATHIONE S-TRANSFERASE U22; 1.
DR PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1.
DR Pfam; PF13410; GST_C_2; 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 Cytoplasm {ECO:0000256|RuleBase:RU369102};
KW Detoxification {ECO:0000256|ARBA:ARBA00022575};
KW Reference proteome {ECO:0000313|Proteomes:UP000027120};
KW Transferase {ECO:0000256|RuleBase:RU369102}.
FT DOMAIN 1..66
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 12..152
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 155 AA; 18144 MW; B49A5E128BAD084A CRC64;
MRVRIALAEK GIEYEYREQN LLNKGPMLLQ MNRVHKKVPV LIHNGKPICE STNIVQYIDE
IHTDGREMRA VKLERQEEMT KEFIAILKTL EEELGDKPHF EGENFGFVDV SLIPLYCWLE
TECPKIIAWA KRCTQRKSVS KSLKDEKKVL GFVQR
//
