ID   GSTFB_ARATH             Reviewed;         214 AA.
AC   Q96324;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   24-JAN-2024, entry version 166.
DE   RecName: Full=Glutathione S-transferase F11 {ECO:0000303|PubMed:12090627};
DE            Short=AtGSTF11 {ECO:0000303|PubMed:12090627};
DE            EC=2.5.1.18 {ECO:0000250|UniProtKB:O80852};
DE   AltName: Full=AtGSTF6 {ECO:0000303|PubMed:12090627};
DE   AltName: Full=GST class-phi {ECO:0000303|PubMed:12090627};
DE   AltName: Full=GST class-phi member 11 {ECO:0000303|PubMed:12090627};
GN   Name=GSTF11 {ECO:0000303|PubMed:12090627};
GN   Synonyms=GSTF6 {ECO:0000303|PubMed:12090627};
GN   OrderedLocusNames=At3g03190 {ECO:0000312|Araport:AT3G03190};
GN   ORFNames=T17B22.12 {ECO:0000312|EMBL:AAF26107.1};
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].
RC   STRAIN=cv. Columbia;
RX   PubMed=9668133; DOI=10.1105/tpc.10.7.1135;
RA   Alfenito M.R., Souer E., Goodman C.D., Buell R., Mol J., Koes R.,
RA   Walbot V.;
RT   "Functional complementation of anthocyanin sequestration in the vacuole by
RT   widely divergent glutathione S-transferases.";
RL   Plant Cell 10:1135-1149(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
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 [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
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).
CC   -!- FUNCTION: May be involved in the conjugation of reduced glutathione to
CC       a wide number of exogenous and endogenous hydrophobic electrophiles and
CC       have a detoxification role against certain herbicides.
CC       {ECO:0000250|UniProtKB:O80852}.
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:0000250|UniProtKB:O80852};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Phi family. {ECO:0000305}.
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DR   EMBL; U70672; AAB09584.1; -; mRNA.
DR   EMBL; AC012328; AAF26107.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE73911.1; -; Genomic_DNA.
DR   EMBL; AY099776; AAM20627.1; -; mRNA.
DR   EMBL; AY128877; AAM91277.1; -; mRNA.
DR   RefSeq; NP_186969.1; NM_111189.3.
DR   AlphaFoldDB; Q96324; -.
DR   SMR; Q96324; -.
DR   STRING; 3702.Q96324; -.
DR   PaxDb; 3702-AT3G03190-1; -.
DR   ProteomicsDB; 230163; -.
DR   EnsemblPlants; AT3G03190.1; AT3G03190.1; AT3G03190.
DR   GeneID; 821227; -.
DR   Gramene; AT3G03190.1; AT3G03190.1; AT3G03190.
DR   KEGG; ath:AT3G03190; -.
DR   Araport; AT3G03190; -.
DR   TAIR; AT3G03190; GSTF11.
DR   eggNOG; KOG0867; Eukaryota.
DR   HOGENOM; CLU_011226_5_1_1; -.
DR   InParanoid; Q96324; -.
DR   OMA; ANWCWVR; -.
DR   PhylomeDB; Q96324; -.
DR   BioCyc; ARA:AT3G03190-MONOMER; -.
DR   PRO; PR:Q96324; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q96324; differential.
DR   GO; GO:0005737; C:cytoplasm; NAS:TAIR.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR   GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
DR   CDD; cd03187; GST_C_Phi; 1.
DR   CDD; cd03053; GST_N_Phi; 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; 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:SF64; GLUTATHIONE S-TRANSFERASE F11; 1.
DR   PANTHER; PTHR43900; GLUTATHIONE S-TRANSFERASE RHO; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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.
DR   Genevisible; Q96324; AT.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Detoxification; Reference proteome; Transferase.
FT   CHAIN           1..214
FT                   /note="Glutathione S-transferase F11"
FT                   /id="PRO_0000185851"
FT   DOMAIN          2..82
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          89..214
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000255"
FT   BINDING         11..12
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O80852"
FT   BINDING         40..41
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O80852"
FT   BINDING         53..54
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O80852"
FT   BINDING         66..67
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O80852"
SQ   SEQUENCE   214 AA;  24637 MW;  24B58B67A5672E91 CRC64;
     MVVKVYGQIK AANPQRVLLC FLEKDIEFEV IHVDLDKLEQ KKPQHLLRQP FGQVPAIEDG
     YLKLFESRAI ARYYATKYAD QGTDLLGKTL EGRAIVDQWV EVENNYFYAV ALPLVMNVVF
     KPKSGKPCDV ALVEELKVKF DKVLDVYENR LATNRYLGGD EFTLADLSHM PGMRYIMNET
     SLSGLVTSRE NLNRWWNEIS ARPAWKKLME LAAY
//