PRXQ_ARATH
ID PRXQ_ARATH Reviewed; 216 AA.
AC Q9LU86;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Peroxiredoxin Q, chloroplastic;
DE EC=1.11.1.24 {ECO:0000269|PubMed:21798375};
DE AltName: Full=Thioredoxin peroxidase;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin Q {ECO:0000305};
DE Flags: Precursor;
GN Name=PRXQ; OrderedLocusNames=At3g26060; ORFNames=MPE11_21;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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;
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 [4]
RP PROTEIN SEQUENCE OF 68-79, AND SUBCELLULAR LOCATION.
RX PubMed=16245054; DOI=10.1023/b:pres.0000006913.86689.f1;
RA Kieselbach T., Schroeder W.P.;
RT "The proteome of the chloroplast lumen of higher plants.";
RL Photosyn. Res. 78:249-264(2003).
RN [5]
RP FUNCTION, AND INTERACTION WITH CDSP32.
RX PubMed=12084836; DOI=10.1105/tpc.001644;
RA Broin M., Cuine S., Eymery F., Rey P.;
RT "The plastidic 2-cysteine peroxiredoxin is a target for a thioredoxin
RT involved in the protection of the photosynthetic apparatus against
RT oxidative damage.";
RL Plant Cell 14:1417-1432(2002).
RN [6]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX DOI=10.1016/S0981-9428(02)01396-7;
RA Horling F., Koenig J., Dietz K.-J.;
RT "Type II peroxiredoxin C, a member of the peroxiredoxin family of
RT Arabidopsis thaliana: its expression and activity in comparison with other
RT peroxiredoxins.";
RL Plant Physiol. Biochem. 40:491-499(2002).
RN [7]
RP INDUCTION.
RX PubMed=12529539; DOI=10.1104/pp.010017;
RA Horling F., Lamkemeyer P., Koenig J., Finkemeier I., Kandlbinder A.,
RA Baier M., Dietz K.-J.;
RT "Divergent light-, ascorbate-, and oxidative stress-dependent regulation of
RT expression of the peroxiredoxin gene family in Arabidopsis.";
RL Plant Physiol. 131:317-325(2003).
RN [8]
RP GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX PubMed=15890615; DOI=10.1016/j.freeradbiomed.2004.07.037;
RA Rouhier N., Jacquot J.-P.;
RT "The plant multigenic family of thiol peroxidases.";
RL Free Radic. Biol. Med. 38:1413-1421(2005).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=17054949; DOI=10.1016/j.febslet.2006.10.001;
RA Petersson U.A., Kieselbach T., Garcia-Cerdan J.G., Schroeder W.P.;
RT "The Prx Q protein of Arabidopsis thaliana is a member of the luminal
RT chloroplast proteome.";
RL FEBS Lett. 580:6055-6061(2006).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16507087; DOI=10.1111/j.1365-313x.2006.02665.x;
RA Lamkemeyer P., Laxa M., Collin V., Li W., Finkemeier I., Schoettler M.A.,
RA Holtkamp V., Tognetti V.B., Issakidis-Bourguet E., Kandlbinder A., Weis E.,
RA Miginiac-Maslow M., Dietz K.-J.;
RT "Peroxiredoxin Q of Arabidopsis thaliana is attached to the thylakoids and
RT functions in context of photosynthesis.";
RL Plant J. 45:968-981(2006).
RN [11]
RP FUNCTION, 3D-STRUCTURE MODELING, SUBUNIT, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21798375; DOI=10.1016/j.bbapap.2011.07.011;
RA Aden J., Wallgren M., Storm P., Weise C.F., Christiansen A., Schroder W.P.,
RA Funk C., Wolf-Watz M.;
RT "Extraordinary mus-ms backbone dynamics in Arabidopsis thaliana
RT peroxiredoxin Q.";
RL Biochim. Biophys. Acta 1814:1880-1890(2011).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides. Involved in the photosystem II protection
CC against hydrogen peroxide. {ECO:0000269|PubMed:12084836,
CC ECO:0000269|PubMed:16507087, ECO:0000269|PubMed:21798375}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24;
CC Evidence={ECO:0000269|PubMed:21798375};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=254 uM for H(2)O(2) {ECO:0000269|PubMed:21798375};
CC KM=1.09 uM for thioredoxin {ECO:0000269|PubMed:21798375};
CC Note=kcat is 4.5 sec(-1) for H(2)O(2). kcat is 2.75 sec(-1) for
CC thioredoxin.;
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:21798375};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:21798375};
CC -!- SUBUNIT: Monomer; Interacts with the plastidial thioredoxin CDSP32.
CC {ECO:0000269|PubMed:12084836, ECO:0000269|PubMed:21798375}.
CC -!- INTERACTION:
CC Q9LU86; P0AA25: trxA; Xeno; NbExp=2; IntAct=EBI-540311, EBI-368542;
CC Q9LU86; P07591; Xeno; NbExp=2; IntAct=EBI-540311, EBI-537449;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000269|PubMed:16507087}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LU86-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues at the exception of roots.
CC {ECO:0000269|PubMed:16507087, ECO:0000269|Ref.6}.
CC -!- INDUCTION: Highly induced by oxidative stress. Down-regulated by salt
CC stress and by ascorbate. {ECO:0000269|PubMed:12529539,
CC ECO:0000269|Ref.6}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In this atypical 2-Cys
CC peroxiredoxin, C(R) is present in the same subunit to form an
CC intramolecular disulfide. The disulfide is subsequently reduced by
CC thioredoxin. {ECO:0000250|UniProtKB:P0AE52}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
CC {ECO:0000305}.
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DR EMBL; AB023041; BAB01069.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77109.1; -; Genomic_DNA.
DR EMBL; AY048264; AAK82526.1; -; mRNA.
DR EMBL; AY072626; AAL62017.1; -; mRNA.
DR RefSeq; NP_189235.1; NM_113510.5. [Q9LU86-1]
DR AlphaFoldDB; Q9LU86; -.
DR SMR; Q9LU86; -.
DR BioGRID; 7534; 3.
DR IntAct; Q9LU86; 3.
DR STRING; 3702.AT3G26060.2; -.
DR PeroxiBase; 4015; AtPrxQ.
DR iPTMnet; Q9LU86; -.
DR PaxDb; Q9LU86; -.
DR PRIDE; Q9LU86; -.
DR ProteomicsDB; 226482; -. [Q9LU86-1]
DR EnsemblPlants; AT3G26060.1; AT3G26060.1; AT3G26060. [Q9LU86-1]
DR GeneID; 822203; -.
DR Gramene; AT3G26060.1; AT3G26060.1; AT3G26060. [Q9LU86-1]
DR KEGG; ath:AT3G26060; -.
DR Araport; AT3G26060; -.
DR eggNOG; KOG0855; Eukaryota.
DR InParanoid; Q9LU86; -.
DR PhylomeDB; Q9LU86; -.
DR BioCyc; ARA:AT3G26060-MON; -.
DR PRO; PR:Q9LU86; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LU86; baseline and differential.
DR Genevisible; Q9LU86; AT.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antioxidant; Chloroplast; Direct protein sequencing;
KW Disulfide bond; Oxidoreductase; Peroxidase; Plastid; Redox-active center;
KW Reference proteome; Thylakoid; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT ?..67
FT /note="Thylakoid"
FT /evidence="ECO:0000269|PubMed:16245054"
FT CHAIN 68..216
FT /note="Peroxiredoxin Q, chloroplastic"
FT /id="PRO_0000285109"
FT DOMAIN 69..216
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 111
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0AE52"
FT DISULFID 111..116
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P0AE52"
SQ SEQUENCE 216 AA; 23678 MW; 5DACF66AC059D10E CRC64;
MAASSSSFTL CNHTTLRTLP LRKTLVTKTQ FSVPTKSSES NFFGSTLTHS SYISPVSSSS
LKGLIFAKVN KGQAAPDFTL KDQNGKPVSL KKYKGKPVVL YFYPADETPG CTKQACAFRD
SYEKFKKAGA EVIGISGDDS ASHKAFASKY KLPYTLLSDE GNKVRKDWGV PGDLFGALPG
RQTYVLDKNG VVQLIYNNQF QPEKHIDETL KFLKAA
