ID F4JBC9_ARATH Unreviewed; 217 AA.
AC F4JBC9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Peroxiredoxin Q, chloroplastic {ECO:0000256|ARBA:ARBA00039701};
DE EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
DE AltName: Full=Thioredoxin peroxidase {ECO:0000256|ARBA:ARBA00032824};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin Q {ECO:0000256|ARBA:ARBA00042163};
GN Name=PRXQ {ECO:0000313|EMBL:AEE77110.1, ECO:0000313|TAIR:AT3G26060};
GN Synonyms=ATPRX Q {ECO:0000313|EMBL:AEE77110.1}, peroxiredoxin Q
GN {ECO:0000313|EMBL:AEE77110.1};
GN OrderedLocusNames=At3g26060 {ECO:0000313|Araport:AT3G26060,
GN ECO:0000313|EMBL:AEE77110.1};
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 {ECO:0000313|EMBL:AEE77110.1, ECO:0000313|Proteomes:UP000006548};
RN [1] {ECO:0000313|EMBL:AEE77110.1, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=11130713; DOI=10.1038/35048706;
RG European Union Chromosome 3 Arabidopsis Sequencing Consortium;
RG Institute for Genomic Research;
RG Kazusa DNA Research Institute;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Blocker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M.,
RA Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N.,
RA Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L.,
RA Weissenbach J., Saurin W., Quetier F., Schafer M., Muller-Auer S.,
RA Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N.,
RA Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P.,
RA Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S.,
RA Simionati B., Conrad A., Hornischer K., Kauer G., Lohnert T.H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schon O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwalder 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., Kaul S.,
RA 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] {ECO:0000313|Proteomes:UP000006548}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
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).
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:0000256|ARBA:ARBA00000280};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000256|ARBA:ARBA00004456}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
CC {ECO:0000256|ARBA:ARBA00038489}.
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DR EMBL; CP002686; AEE77110.1; -; Genomic_DNA.
DR RefSeq; NP_001189979.1; NM_001203050.1.
DR AlphaFoldDB; F4JBC9; -.
DR SMR; F4JBC9; -.
DR ProteomicsDB; 212115; -.
DR EnsemblPlants; AT3G26060.2; AT3G26060.2; AT3G26060.
DR GeneID; 822203; -.
DR Gramene; AT3G26060.2; AT3G26060.2; AT3G26060.
DR Araport; AT3G26060; -.
DR TAIR; AT3G26060; PRXQ.
DR HOGENOM; CLU_042529_14_2_1; -.
DR OrthoDB; 9011at2759; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4JBC9; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009533; C:chloroplast stromal thylakoid; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0010287; C:plastoglobule; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0051920; F:peroxiredoxin activity; IDA:TAIR.
DR GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; IEA:UniProtKB-EC.
DR CDD; cd03017; PRX_BCP; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR42801:SF4; AHPC_TSA FAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR42801; THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Proteomics identification {ECO:0007829|PeptideAtlas:F4JBC9,
KW ECO:0007829|ProteomicsDB:F4JBC9};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078}.
FT DOMAIN 70..217
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 217 AA; 23806 MW; C5ABD283F3AEDF7C CRC64;
MAASSSSFTL CNHTTLRTLP LRKTLVTKTQ FSVPTKSSES NFFGSTLTHS SYISPVSSSS
LKGLIFAKQV NKGQAAPDFT LKDQNGKPVS LKKYKGKPVV LYFYPADETP GCTKQACAFR
DSYEKFKKAG AEVIGISGDD SASHKAFASK YKLPYTLLSD EGNKVRKDWG VPGDLFGALP
GRQTYVLDKN GVVQLIYNNQ FQPEKHIDET LKFLKAA
//
