GPX7_ARATH
ID GPX7_ARATH Reviewed; 233 AA.
AC Q9SZ54;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Putative glutathione peroxidase 7, chloroplastic;
DE EC=1.11.1.9;
DE Flags: Precursor;
GN Name=GPX7; OrderedLocusNames=At4g31870; ORFNames=F11C18.70;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=14617062; DOI=10.1046/j.1365-313x.2003.01901.x;
RA Rodriguez Milla M.A., Maurer A., Rodriguez Huete A., Gustafson J.P.;
RT "Glutathione peroxidase genes in Arabidopsis are ubiquitous and regulated
RT by abiotic stresses through diverse signaling pathways.";
RL Plant J. 36:602-615(2003).
CC -!- FUNCTION: May constitute a glutathione peroxidase-like protective
CC system against oxidative stresses. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O;
CC Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB40757.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79905.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL049607; CAB40757.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161579; CAB79905.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85970.1; -; Genomic_DNA.
DR PIR; T06309; T06309.
DR RefSeq; NP_194915.2; NM_119337.3.
DR AlphaFoldDB; Q9SZ54; -.
DR SMR; Q9SZ54; -.
DR STRING; 3702.AT4G31870.1; -.
DR PeroxiBase; 2250; AtGPx07.
DR PaxDb; Q9SZ54; -.
DR PRIDE; Q9SZ54; -.
DR ProteomicsDB; 222290; -.
DR EnsemblPlants; AT4G31870.1; AT4G31870.1; AT4G31870.
DR GeneID; 829316; -.
DR Gramene; AT4G31870.1; AT4G31870.1; AT4G31870.
DR KEGG; ath:AT4G31870; -.
DR Araport; AT4G31870; -.
DR TAIR; locus:2116782; AT4G31870.
DR eggNOG; KOG1651; Eukaryota.
DR HOGENOM; CLU_029507_0_0_1; -.
DR InParanoid; Q9SZ54; -.
DR OMA; THPLWKF; -.
DR OrthoDB; 1483113at2759; -.
DR BioCyc; ARA:AT4G31870-MON; -.
DR PRO; PR:Q9SZ54; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZ54; baseline and differential.
DR Genevisible; Q9SZ54; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:1900367; P:positive regulation of defense response to insect; IMP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00340; GSH_Peroxidase; 1.
DR InterPro; IPR000889; Glutathione_peroxidase.
DR InterPro; IPR029759; GPX_AS.
DR InterPro; IPR029760; GPX_CS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR11592; PTHR11592; 1.
DR Pfam; PF00255; GSHPx; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE 3: Inferred from homology;
KW Chloroplast; Oxidoreductase; Peroxidase; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..69
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 70..233
FT /note="Putative glutathione peroxidase 7, chloroplastic"
FT /id="PRO_0000045459"
FT ACT_SITE 108
FT /evidence="ECO:0000250"
SQ SEQUENCE 233 AA; 25774 MW; 269C745F1B52AC14 CRC64;
MAFSYASFST PFNGFAANPS PITSAFLGPS LRFSTRTSKT RNPSNGVSVK SSNSHRFLVK
SKNFSVYARA AAEKSVHDFT VKDIDGNDVS LDKFKGKPLL IVNVASRCGL TSSNYSELSQ
LYEKYKNQGF EILAFPCNQF GGQEPGSNPE IKQFACTRFK AEFPIFDKVD VNGPSTAPIY
KFLKSNAGGF LGDIIKWNFE KFLVDKKGKV VERYPPTTSP FQIEKDIQKL LAA
