GSTF9_ARATH
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 03-AUG-2022, entry version 152.
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},
GN Phi9 {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 1-
CC 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.AT2G30860.1; -.
DR iPTMnet; O80852; -.
DR MetOSite; O80852; -.
DR PaxDb; O80852; -.
DR PRIDE; O80852; -.
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; locus:2052811; AT2G30860.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_5_1_1; -.
DR InParanoid; O80852; -.
DR OMA; QKVVWCA; -.
DR PhylomeDB; O80852; -.
DR PRO; PR:O80852; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80852; baseline and differential.
DR Genevisible; O80852; AT.
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; IBA:GO_Central.
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:0006749; P:glutathione metabolic process; IEA:InterPro.
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 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 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
