ID   GSTL2_ARATH             Reviewed;         292 AA.
AC   Q9M2W2; Q8GXL1;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=Glutathione S-transferase L2, chloroplastic;
DE            Short=AtGSTL2;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-lambda member 2;
DE   Flags: Precursor;
GN   Name=GSTL2; OrderedLocusNames=At3g55040; ORFNames=T15C9.60;
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 [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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-292.
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [5]
RP   FUNCTION.
RX   PubMed=12077129; DOI=10.1074/jbc.m202919200;
RA   Dixon D.P., Davis B.G., Edwards R.;
RT   "Functional divergence in the glutathione transferase superfamily in
RT   plants. Identification of two classes with putative functions in redox
RT   homeostasis in Arabidopsis thaliana.";
RL   J. Biol. Chem. 277:30859-30869(2002).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19174456; DOI=10.1093/jxb/ern365;
RA   Dixon D.P., Hawkins T., Hussey P.J., Edwards R.;
RT   "Enzyme activities and subcellular localization of members of the
RT   Arabidopsis glutathione transferase superfamily.";
RL   J. Exp. Bot. 60:1207-1218(2009).
RN   [7]
RP   FUNCTION.
RX   PubMed=20841361; DOI=10.1074/jbc.m110.164806;
RA   Dixon D.P., Edwards R.;
RT   "Roles for stress-inducible lambda glutathione transferases in flavonoid
RT   metabolism in plants as identified by ligand fishing.";
RL   J. Biol. Chem. 285:36322-36329(2010).
CC   -!- FUNCTION: Catalyzes the glutathione-dependent reduction of S-
CC       glutathionylquercetin to quercetin. In vitro, possesses glutathione-
CC       dependent thiol transferase activity toward 2-hydroxyethyl disulfide
CC       (HED). {ECO:0000269|PubMed:12077129, ECO:0000269|PubMed:20841361}.
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: Plastid, chloroplast
CC       {ECO:0000269|PubMed:19174456}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Lambda family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC42803.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL132970; CAB82699.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79331.1; -; Genomic_DNA.
DR   EMBL; BT030006; ABN04744.1; -; mRNA.
DR   EMBL; AK118180; BAC42803.1; ALT_INIT; mRNA.
DR   PIR; T47643; T47643.
DR   RefSeq; NP_191064.1; NM_115362.2.
DR   AlphaFoldDB; Q9M2W2; -.
DR   SMR; Q9M2W2; -.
DR   STRING; 3702.Q9M2W2; -.
DR   PaxDb; 3702-AT3G55040-1; -.
DR   ProteomicsDB; 247335; -.
DR   EnsemblPlants; AT3G55040.1; AT3G55040.1; AT3G55040.
DR   GeneID; 824670; -.
DR   Gramene; AT3G55040.1; AT3G55040.1; AT3G55040.
DR   KEGG; ath:AT3G55040; -.
DR   Araport; AT3G55040; -.
DR   TAIR; AT3G55040; GSTL2.
DR   eggNOG; KOG0406; Eukaryota.
DR   HOGENOM; CLU_072699_0_0_1; -.
DR   InParanoid; Q9M2W2; -.
DR   OMA; LEHNNRV; -.
DR   OrthoDB; 5491187at2759; -.
DR   PhylomeDB; Q9M2W2; -.
DR   PRO; PR:Q9M2W2; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M2W2; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:TAIR.
DR   GO; GO:0010731; P:protein glutathionylation; IDA:TAIR.
DR   GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR   CDD; cd03203; GST_C_Lambda; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR044629; GSTL1/2/3.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR44328; GLUTATHIONE S-TRANSFERASE L1; 1.
DR   PANTHER; PTHR44328:SF11; GLUTATHIONE S-TRANSFERASE L2, CHLOROPLASTIC; 1.
DR   Pfam; PF13410; GST_C_2; 1.
DR   Pfam; PF13417; GST_N_3; 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; Q9M2W2; AT.
PE   2: Evidence at transcript level;
KW   Chloroplast; Detoxification; Plastid; Reference proteome; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..56
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           57..292
FT                   /note="Glutathione S-transferase L2, chloroplastic"
FT                   /id="PRO_0000413578"
FT   DOMAIN          79..160
FT                   /note="GST N-terminal"
FT   DOMAIN          130..286
FT                   /note="GST C-terminal"
FT   BINDING         89..90
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         117..118
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         131..132
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         144..145
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   292 AA;  33058 MW;  0EAFE884E843D39F CRC64;
     MSVGLKVSAF LHPTLALSSR DVSLSSSSSS LYLDRKILRP GSGRRWCKSR RTEPILAVVE
     SSRVPELDSS SEPVQVFDGS TRLYISYTCP FAQRAWIARN YKGLQNKIEL VPIDLKNRPA
     WYKEKVYSAN KVPALEHNNR VLGESLDLIK YIDTNFEGPS LTPDGLEKQV VADELLSYTD
     SFSKAVRSTL NGTDTNAADV AFDYIEQALS KFNEGPFFLG QFSLVDVAYA PFIERFRLIL
     SDVMNVDITS GRPNLALWIQ EMNKIEAYTE TRQDPQELVE RYKRRVQAEA RL
//