ID   GSTF9_ARATH             Reviewed;         215 AA.
AC   O80852; A8MR26; C0Z2R9; O23626;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Glutathione S-transferase F9 {ECO:0000303|PubMed:12090627};
DE            Short=AtGSTF9 {ECO:0000303|PubMed:12090627};
DE            EC=2.5.1.18 {ECO:0000269|PubMed:12090627, ECO:0000269|PubMed:16538523};
DE   AltName: Full=AtGSTF7 {ECO:0000303|PubMed:12090627};
DE   AltName: Full=GST class-phi member 9 {ECO:0000303|PubMed:12090627, ECO:0000303|PubMed:29732642};
GN   Name=GSTF9 {ECO:0000303|PubMed:12090627};
GN   Synonyms=GLUTTR, GSTF7 {ECO:0000303|PubMed:12090627}, Phi9
GN   {ECO:0000303|PubMed:29732642};
GN   OrderedLocusNames=At2g30860 {ECO:0000312|Araport:AT2G30860};
GN   ORFNames=F7F1.7 {ECO:0000312|EMBL:AAC20720.1};
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] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RA   Jemth P., Jiang F., Mannervik B.;
RT   "Cloning, expression and characterisation of an Arabidopsis glutathione
RT   transferase gene.";
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
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 [LARGE SCALE MRNA] (ISOFORM 1).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, 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   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX   PubMed=16538523; DOI=10.1007/s00299-006-0146-1;
RA   Nutricati E., Miceli A., Blando F., De Bellis L.;
RT   "Characterization of two Arabidopsis thaliana glutathione S-transferases.";
RL   Plant Cell Rep. 25:997-1005(2006).
RN   [8]
RP   INDUCTION BY ZINC.
RX   PubMed=19880396; DOI=10.1093/pcp/pcp154;
RA   Fukao Y., Ferjani A., Fujiwara M., Nishimori Y., Ohtsu I.;
RT   "Identification of zinc-responsive proteins in the roots of Arabidopsis
RT   thaliana using a highly improved method of two-dimensional
RT   electrophoresis.";
RL   Plant Cell Physiol. 50:2234-2239(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE,
RP   ACTIVITY REGULATION, PTM, BIOPHYSICOCHEMICAL PROPERTIES, AND OXIDATION AT
RP   MET-35; MET-118; MET-123 AND MET-184.
RX   PubMed=29732642; DOI=10.1002/pro.3440;
RA   Tossounian M.-A., Wahni K., Van Molle I., Vertommen D., Astolfi Rosado L.,
RA   Messens J.;
RT   "Redox-regulated methionine oxidation of Arabidopsis thaliana glutathione
RT   transferase Phi9 induces H-site flexibility.";
RL   Protein Sci. 28:56-67(2019).
CC   -!- FUNCTION: In vitro, possesses glutathione S-transferase activity toward
CC       1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC),
CC       and glutathione peroxidase activity toward cumene hydroperoxide and
CC       linoleic acid-13-hydroperoxide. May be involved in the conjugation of
CC       reduced glutathione to a wide number of exogenous and endogenous
CC       hydrophobic electrophiles and have a detoxification role against
CC       certain herbicides. {ECO:0000269|PubMed:12090627,
CC       ECO:0000269|PubMed:16538523}.
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:0000269|PubMed:12090627, ECO:0000269|PubMed:16538523};
CC   -!- ACTIVITY REGULATION: Redox-regulated enzyme; in oxidative stress
CC       conditions methionine oxidation ensure a thermodynamic and structural
CC       compensatory mechanism to guarantee H(2)O(2) peroxidase activity
CC       despite transferase activity inhibition. {ECO:0000269|PubMed:29732642}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=71 uM for glutathione (in oxidative conditions)
CC         {ECO:0000269|PubMed:29732642};
CC         KM=131 uM for glutathione (in reductive conditions)
CC         {ECO:0000269|PubMed:29732642};
CC         KM=1.8 mM for 1-chloro-2,4-dinitrobenzene (in oxidative conditions)
CC         {ECO:0000269|PubMed:29732642};
CC         KM=1.3 mM for 1-chloro-2,4-dinitrobenzene (in reductive conditions)
CC         {ECO:0000269|PubMed:29732642};
CC         Note=kcat is 0.5 sec(-1) with glutathione as substrate (in oxidative
CC         conditions) (PubMed:29732642). kcat is 0.85 sec(-1) with glutathione
CC         as substrate (in reductive conditions) (PubMed:29732642). kcat is
CC         0.72 sec(-1) with 1-chloro-2,4-dinitrobenzene as substrate (in
CC         oxidative conditions) (PubMed:29732642). kcat is 0.98 sec(-1) with
CC         1-chloro-2,4-dinitrobenzene as substrate (in reductive conditions)
CC         (PubMed:29732642). {ECO:0000269|PubMed:29732642};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O80852-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O80852-2; Sequence=VSP_041938, VSP_041939;
CC   -!- INDUCTION: By zinc in roots and benoxacor.
CC       {ECO:0000269|PubMed:16538523, ECO:0000269|PubMed:19880396}.
CC   -!- PTM: Oxidated at Met-35, Met-118, Met-123 and Met-184 in oxidative
CC       stress conditions (e.g. hydrogen peroxide H(2)O(2)).
CC       {ECO:0000269|PubMed:29732642}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Phi family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAH56998.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; Y12295; CAA72973.1; -; mRNA.
DR   EMBL; AC004669; AAC20720.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08448.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08449.1; -; Genomic_DNA.
DR   EMBL; AF372905; AAK49621.1; -; mRNA.
DR   EMBL; BT002679; AAO11595.1; -; mRNA.
DR   EMBL; AK318883; BAH56998.1; ALT_FRAME; mRNA.
DR   PIR; E84713; E84713.
DR   RefSeq; NP_001077983.1; NM_001084514.1. [O80852-2]
DR   RefSeq; NP_180643.1; NM_128638.3. [O80852-1]
DR   PDB; 6EZY; X-ray; 2.35 A; A/B=1-215.
DR   PDB; 6F01; X-ray; 2.50 A; A/B=1-215.
DR   PDB; 6F05; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J=1-215.
DR   PDBsum; 6EZY; -.
DR   PDBsum; 6F01; -.
DR   PDBsum; 6F05; -.
DR   AlphaFoldDB; O80852; -.
DR   SMR; O80852; -.
DR   BioGRID; 2985; 1.
DR   IntAct; O80852; 1.
DR   STRING; 3702.O80852; -.
DR   iPTMnet; O80852; -.
DR   MetOSite; O80852; -.
DR   PaxDb; 3702-AT2G30860-1; -.
DR   ProteomicsDB; 247330; -. [O80852-1]
DR   EnsemblPlants; AT2G30860.1; AT2G30860.1; AT2G30860. [O80852-1]
DR   EnsemblPlants; AT2G30860.2; AT2G30860.2; AT2G30860. [O80852-2]
DR   GeneID; 817636; -.
DR   Gramene; AT2G30860.1; AT2G30860.1; AT2G30860. [O80852-1]
DR   Gramene; AT2G30860.2; AT2G30860.2; AT2G30860. [O80852-2]
DR   KEGG; ath:AT2G30860; -.
DR   Araport; AT2G30860; -.
DR   TAIR; AT2G30860; GSTF9.
DR   eggNOG; KOG0867; Eukaryota.
DR   HOGENOM; CLU_011226_5_1_1; -.
DR   InParanoid; O80852; -.
DR   OMA; FWSGEQW; -.
DR   OrthoDB; 639740at2759; -.
DR   PhylomeDB; O80852; -.
DR   SABIO-RK; O80852; -.
DR   PRO; PR:O80852; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O80852; baseline and differential.
DR   GO; GO:0048046; C:apoplast; HDA:TAIR.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0005737; C:cytoplasm; NAS:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR   GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR   GO; GO:0043295; F:glutathione binding; IDA:TAIR.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IDA:TAIR.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:TAIR.
DR   GO; GO:1901149; F:salicylic acid binding; HDA:TAIR.
DR   GO; GO:0006952; P:defense response; IEP:TAIR.
DR   GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
DR   GO; GO:0010043; P:response to zinc ion; 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:SF45; GLUTATHIONE S-TRANSFERASE F9; 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; O80852; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Detoxification; Oxidation;
KW   Oxidoreductase; Peroxidase; Phosphoprotein; Reference proteome;
KW   Stress response; Transferase.
FT   CHAIN           1..215
FT                   /note="Glutathione S-transferase F9"
FT                   /id="PRO_0000413544"
FT   DOMAIN          2..81
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          88..215
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:0000269|PubMed:29732642,
FT                   ECO:0007744|PDB:6EZY, ECO:0007744|PDB:6F01,
FT                   ECO:0007744|PDB:6F05"
FT   BINDING         39..40
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:29732642,
FT                   ECO:0007744|PDB:6EZY, ECO:0007744|PDB:6F01,
FT                   ECO:0007744|PDB:6F05"
FT   BINDING         52..53
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:29732642,
FT                   ECO:0007744|PDB:6EZY, ECO:0007744|PDB:6F01,
FT                   ECO:0007744|PDB:6F05"
FT   BINDING         65..66
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:29732642,
FT                   ECO:0007744|PDB:6EZY, ECO:0007744|PDB:6F01,
FT                   ECO:0007744|PDB:6F05"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
FT   MOD_RES         35
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000269|PubMed:29732642"
FT   MOD_RES         118
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000269|PubMed:29732642"
FT   MOD_RES         123
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000269|PubMed:29732642"
FT   MOD_RES         184
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000269|PubMed:29732642"
FT   VAR_SEQ         154..166
FT                   /note="KYLAGDFVSLADL -> NIHSQLKMCSSSW (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:19423640"
FT                   /id="VSP_041938"
FT   VAR_SEQ         167..215
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:19423640"
FT                   /id="VSP_041939"
FT   CONFLICT        87
FT                   /note="K -> E (in Ref. 5; BAH56998)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        147..151
FT                   /note="EAHLS -> KAQRA (in Ref. 1; CAA72973)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..6
FT                   /evidence="ECO:0007829|PDB:6F05"
FT   HELIX           11..23
FT                   /evidence="ECO:0007829|PDB:6F05"
FT   STRAND          27..30
FT                   /evidence="ECO:0007829|PDB:6F05"
FT   TURN            34..37
FT                   /evidence="ECO:0007829|PDB:6F05"
FT   HELIX           38..40
FT                   /evidence="ECO:0007829|PDB:6F05"
FT   HELIX           42..45
FT                   /evidence="ECO:0007829|PDB:6F05"
FT   STRAND          55..58
FT                   /evidence="ECO:0007829|PDB:6F05"
FT   STRAND          61..65
FT                   /evidence="ECO:0007829|PDB:6F05"
FT   HELIX           66..76
FT                   /evidence="ECO:0007829|PDB:6F05"
FT   TURN            77..79
FT                   /evidence="ECO:0007829|PDB:6F05"
FT   STRAND          80..82
FT                   /evidence="ECO:0007829|PDB:6F05"
FT   HELIX           89..104
FT                   /evidence="ECO:0007829|PDB:6F05"
FT   HELIX           107..116
FT                   /evidence="ECO:0007829|PDB:6F05"
FT   HELIX           120..123
FT                   /evidence="ECO:0007829|PDB:6EZY"
FT   HELIX           129..150
FT                   /evidence="ECO:0007829|PDB:6F05"
FT   STRAND          154..160
FT                   /evidence="ECO:0007829|PDB:6F05"
FT   HELIX           163..166
FT                   /evidence="ECO:0007829|PDB:6F05"
FT   HELIX           169..176
FT                   /evidence="ECO:0007829|PDB:6F05"
FT   TURN            177..179
FT                   /evidence="ECO:0007829|PDB:6F05"
FT   HELIX           183..186
FT                   /evidence="ECO:0007829|PDB:6F05"
FT   HELIX           189..198
FT                   /evidence="ECO:0007829|PDB:6F05"
FT   HELIX           202..211
FT                   /evidence="ECO:0007829|PDB:6F05"
SQ   SEQUENCE   215 AA;  24146 MW;  961996318A186F9C CRC64;
     MVLKVYGPHF ASPKRALVTL IEKGVAFETI PVDLMKGEHK QPAYLALQPF GTVPAVVDGD
     YKIFESRAVM RYVAEKYRSQ GPDLLGKTVE DRGQVEQWLD VEATTYHPPL LNLTLHIMFA
     SVMGFPSDEK LIKESEEKLA GVLDVYEAHL SKSKYLAGDF VSLADLAHLP FTDYLVGPIG
     KAYMIKDRKH VSAWWDDISS RPAWKETVAK YSFPA
//