GSTF3_ARATH
ID GSTF3_ARATH Reviewed; 212 AA.
AC Q9SLM6; Q0WP56; Q1WWI5;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Glutathione S-transferase F3;
DE Short=AtGSTF3;
DE EC=2.5.1.18;
DE AltName: Full=GST class-phi member 3;
DE AltName: Full=Glutathione S-transferase 16;
GN Name=GSTF3; Synonyms=GST16; OrderedLocusNames=At2g02930;
GN ORFNames=T17M13.10;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=12090627; DOI=10.1023/a:1015557300450;
RA Wagner U., Edwards R., Dixon D.P., Mauch F.;
RT "Probing the diversity of the Arabidopsis glutathione S-transferase gene
RT family.";
RL Plant Mol. Biol. 49:515-532(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds a series of heterocyclic compounds, including
CC lumichrome, harmane, norharmane and indole-3-aldehyde. May be involved
CC in the conjugation of reduced glutathione to a wide number of exogenous
CC and endogenous hydrophobic electrophiles and have a detoxification role
CC against certain herbicides.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Phi family. {ECO:0000305}.
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DR EMBL; AF288181; AAG30130.1; -; mRNA.
DR EMBL; AC004138; AAC32912.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05642.1; -; Genomic_DNA.
DR EMBL; BT024921; ABD94077.1; -; mRNA.
DR EMBL; AK229226; BAF01093.1; -; mRNA.
DR PIR; D84442; D84442.
DR RefSeq; NP_178394.1; NM_126346.3.
DR AlphaFoldDB; Q9SLM6; -.
DR SMR; Q9SLM6; -.
DR STRING; 3702.AT2G02930.1; -.
DR MetOSite; Q9SLM6; -.
DR PaxDb; Q9SLM6; -.
DR PRIDE; Q9SLM6; -.
DR ProteomicsDB; 248516; -.
DR EnsemblPlants; AT2G02930.1; AT2G02930.1; AT2G02930.
DR GeneID; 814822; -.
DR Gramene; AT2G02930.1; AT2G02930.1; AT2G02930.
DR KEGG; ath:AT2G02930; -.
DR Araport; AT2G02930; -.
DR TAIR; locus:2056685; AT2G02930.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_5_1_1; -.
DR InParanoid; Q9SLM6; -.
DR OMA; AVIFYDY; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; Q9SLM6; -.
DR BioCyc; ARA:AT2G02930-MON; -.
DR PRO; PR:Q9SLM6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SLM6; baseline and differential.
DR Genevisible; Q9SLM6; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0043295; F:glutathione binding; IBA:GO_Central.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0002239; P:response to oomycetes; IEP:TAIR.
DR GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
DR CDD; cd03187; GST_C_Phi; 1.
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 Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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 Cytoplasm; Detoxification; Reference proteome; Transferase.
FT CHAIN 1..212
FT /note="Glutathione S-transferase F3"
FT /id="PRO_0000185853"
FT DOMAIN 2..83
FT /note="GST N-terminal"
FT DOMAIN 93..212
FT /note="GST C-terminal"
FT BINDING 12..13
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 41..42
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 54..55
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 67..68
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT CONFLICT 96
FT /note="Q -> R (in Ref. 5; BAF01093)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 212 AA; 24121 MW; 73818A85E6D05A59 CRC64;
MAGIKVFGHP ASTSTRRVLI ALHEKNLDFE LVHVELKDGE HKKEPFLSRN PFGQVPAFED
GDLKLFESRA ITQYIAHRYE NQGTNLLPAD SKNIAQYAIM SIGIQVEAHQ FDPVASKLAW
EQVFKFNYGL NTDQAVVAEE EAKLAKVLDV YEARLKEFKY LAGETFTLTD LHHIPVIQYL
LGTPTKKLFT ERPRVNEWVA EITKRPASEK VL
