PRX2A_ARATH
ID PRX2A_ARATH Reviewed; 553 AA.
AC Q7G959;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Peroxiredoxin-2A;
DE EC=1.11.1.25 {ECO:0000250|UniProtKB:A9PCL4};
DE AltName: Full=Glutaredoxin-dependent peroxiredoxin {ECO:0000305};
DE AltName: Full=Peroxiredoxin IIA;
DE AltName: Full=Thioredoxin peroxidase 2A;
GN Name=PRXIIA; OrderedLocusNames=At1g65990; ORFNames=F12P19.16;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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).
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 (By similarity). May be involved in
CC intracellular redox signaling (Probable).
CC {ECO:0000250|UniProtKB:A9PCL4, ECO:0000305|PubMed:15890615}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[glutaredoxin]-dithiol + a hydroperoxide = [glutaredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62624, Rhea:RHEA-
CC COMP:10729, Rhea:RHEA-COMP:10730, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.25;
CC Evidence={ECO:0000250|UniProtKB:A9PCL4};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:A9PCL4}.
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 1-Cys
CC peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide
CC with a cysteine from another protein or with a small thiol molecule.
CC C(P) is reactivated by glutathionylation and subsequent reduction by
CC glutaredoxin (Grx), or by thioredoxin (Trx).
CC {ECO:0000250|UniProtKB:A9PCL4}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC {ECO:0000305}.
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DR EMBL; AC009513; AAF06060.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34450.1; -; Genomic_DNA.
DR EMBL; DQ056510; AAY78667.1; -; mRNA.
DR PIR; D96684; D96684.
DR RefSeq; NP_176774.1; NM_105271.1.
DR AlphaFoldDB; Q7G959; -.
DR SMR; Q7G959; -.
DR STRING; 3702.AT1G65990.1; -.
DR PeroxiBase; 4352; AtPrxII01.
DR PaxDb; Q7G959; -.
DR PRIDE; Q7G959; -.
DR EnsemblPlants; AT1G65990.1; AT1G65990.1; AT1G65990.
DR GeneID; 842912; -.
DR Gramene; AT1G65990.1; AT1G65990.1; AT1G65990.
DR KEGG; ath:AT1G65990; -.
DR Araport; AT1G65990; -.
DR TAIR; locus:2009734; AT1G65990.
DR eggNOG; KOG0541; Eukaryota.
DR HOGENOM; CLU_034692_0_0_1; -.
DR InParanoid; Q7G959; -.
DR OMA; VERNEYA; -.
DR OrthoDB; 1281610at2759; -.
DR PhylomeDB; Q7G959; -.
DR BioCyc; ARA:AT1G65990-MON; -.
DR PRO; PR:Q7G959; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q7G959; baseline and differential.
DR Genevisible; Q7G959; AT.
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 GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR CDD; cd03013; PRX5_like; 1.
DR InterPro; IPR006527; F-box-assoc_dom_typ1.
DR InterPro; IPR017451; F-box-assoc_interact_dom.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR037944; PRX5-like.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00646; F-box; 1.
DR Pfam; PF07734; FBA_1; 1.
DR Pfam; PF08534; Redoxin; 1.
DR SMART; SM00256; FBOX; 1.
DR SUPFAM; SSF50965; SSF50965; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR TIGRFAMs; TIGR01640; F_box_assoc_1; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 2: Evidence at transcript level;
KW Antioxidant; Oxidoreductase; Peroxidase; Redox-active center;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..553
FT /note="Peroxiredoxin-2A"
FT /id="PRO_0000282278"
FT DOMAIN 4..160
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 156..201
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT ACT_SITE 51
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:A9PCL4"
SQ SEQUENCE 553 AA; 62654 MW; 3F53BBC2D3184E16 CRC64;
MAPIDVGDFV PDGSISFFDD DDQLQTVSVH SLAAGKKVIL FGVPGAFPPT CSMNHVNGFI
EKAEELKSNG VDEIICLSGD DPFMITACSE NKHVKFVEDG SGEYIQLLGL ELEVKDKGLG
VRSRGFALLL DNLKVIVVNV GSGGDCSLFQ LMKMTTTTMS NLPTDLLEEI ISRVPRKYMR
AVRLTCKRWN GMFKSQSFTK MHIGKEEAAT RELRQTRMIV MMDYNVYLMG IAVNEIPSIE
TLGKLTCLDD SEQVKISQVF CCEGLLLCIL KDDDTKIVVW NPYLGQTRWI QTRLICCVSG
WKKYALGYGN NSENRSCRSP KILRVTDNFN IFSENIPLQY EIYDFDSDVW TTLDVSPHWF
IMSERGLSLK GNTYWGAKER HAYGSIDHII CFDFTRERFG PLLPLPFSAW GAQFASLSSV
REDKITALFQ NCRAYKLELW ITTKIDVNNA TWSKFFTMDT PYLHEILSLK TFFIDEENKI
VVVSNKERDT KGDLTHDSID IINGEARCLW KLGLGKPADK NCWPLVCPYV PSVVQIKQHK
GGKTKEQSDY KRH
