PER53_ARATH
ID PER53_ARATH Reviewed; 335 AA.
AC Q42578;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Peroxidase 53;
DE Short=Atperox P53;
DE EC=1.11.1.7;
DE AltName: Full=ATPA2;
DE Flags: Precursor;
GN Name=PER53; Synonyms=P53; OrderedLocusNames=At5g06720; ORFNames=MPH15.8;
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], AND PYROGLUTAMATE FORMATION AT GLN-31.
RC STRAIN=cv. Columbia;
RX PubMed=8977116; DOI=10.1016/s0014-5793(96)01244-6;
RA Oestergaard L., Abelskov A.K., Mattsson O., Welinder K.G.;
RT "Structure and organ specificity of an anionic peroxidase from Arabidopsis
RT thaliana cell suspension culture.";
RL FEBS Lett. 398:243-247(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
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].
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP CHARACTERIZATION.
RC STRAIN=cv. Columbia;
RX PubMed=9738941; DOI=10.1016/s0014-5793(98)00849-7;
RA Oestergaard L., Pedersen A.G., Jespersen H.M., Brunak S., Welinder K.G.;
RT "Computational analyses and annotations of the Arabidopsis peroxidase gene
RT family.";
RL FEBS Lett. 433:98-102(1998).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
RC STRAIN=cv. Columbia;
RX PubMed=11117266; DOI=10.1023/a:1006442618860;
RA Oestergaard L., Teilum K., Mirza O., Mattsson O., Petersen M.,
RA Welinder K.G., Mundy J., Gajhede M., Henriksen A.;
RT "Arabidopsis ATP A2 peroxidase. Expression and high-resolution structure of
RT a plant peroxidase with implications for lignification.";
RL Plant Mol. Biol. 44:231-243(2000).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
RC STRAIN=cv. Columbia;
RX PubMed=11551197; DOI=10.1021/bi010661o;
RA Nielsen K.L., Indiani C., Henriksen A., Feis A., Becucci M., Gajhede M.,
RA Smulevich G., Welinder K.G.;
RT "Differential activity and structure of highly similar peroxidases.
RT Spectroscopic, crystallographic, and enzymatic analyses of lignifying
RT Arabidopsis thaliana peroxidase A2 and horseradish peroxidase A2.";
RL Biochemistry 40:11013-11021(2001).
RN [9]
RP GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=12034502; DOI=10.1016/s0378-1119(02)00465-1;
RA Tognolli M., Penel C., Greppin H., Simon P.;
RT "Analysis and expression of the class III peroxidase large gene family in
RT Arabidopsis thaliana.";
RL Gene 288:129-138(2002).
CC -!- FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants,
CC biosynthesis and degradation of lignin, suberization, auxin catabolism,
CC response to environmental stresses such as wounding, pathogen attack
CC and oxidative stress. These functions might be dependent on each
CC isozyme/isoform in each plant tissue.
CC -!- FUNCTION: Closely linked to lignin formation by showing monolignol
CC substrate specificity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 2 calcium ions per subunit.;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in roots.
CC -!- MISCELLANEOUS: There are 73 peroxidase genes in A.thaliana.
CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class
CC III) peroxidase subfamily. {ECO:0000255|PROSITE-ProRule:PRU00297}.
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DR EMBL; X99952; CAA68212.1; -; mRNA.
DR EMBL; AP002032; BAB09806.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91055.1; -; Genomic_DNA.
DR EMBL; AY056186; AAL07035.1; -; mRNA.
DR EMBL; AY096713; AAM20347.1; -; mRNA.
DR EMBL; AY087674; AAM65211.1; -; mRNA.
DR RefSeq; NP_196290.1; NM_120755.3.
DR PDB; 1PA2; X-ray; 1.45 A; A=31-335.
DR PDB; 1QO4; X-ray; 3.00 A; A=31-335.
DR PDBsum; 1PA2; -.
DR PDBsum; 1QO4; -.
DR AlphaFoldDB; Q42578; -.
DR SMR; Q42578; -.
DR STRING; 3702.AT5G06720.1; -.
DR PeroxiBase; 219; AtPrx53.
DR PaxDb; Q42578; -.
DR PRIDE; Q42578; -.
DR ProteomicsDB; 236784; -.
DR EnsemblPlants; AT5G06720.1; AT5G06720.1; AT5G06720.
DR GeneID; 830561; -.
DR Gramene; AT5G06720.1; AT5G06720.1; AT5G06720.
DR KEGG; ath:AT5G06720; -.
DR Araport; AT5G06720; -.
DR TAIR; locus:2170204; AT5G06720.
DR eggNOG; ENOG502QVXS; Eukaryota.
DR HOGENOM; CLU_010543_0_1_1; -.
DR InParanoid; Q42578; -.
DR OMA; ENECSAT; -.
DR OrthoDB; 819626at2759; -.
DR PhylomeDB; Q42578; -.
DR BioCyc; ARA:AT5G06720-MON; -.
DR EvolutionaryTrace; Q42578; -.
DR PRO; PR:Q42578; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q42578; baseline and differential.
DR Genevisible; Q42578; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0002215; P:defense response to nematode; IMP:TAIR.
DR GO; GO:0009908; P:flower development; IMP:TAIR.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00693; secretory_peroxidase; 1.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR000823; Peroxidase_pln.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR InterPro; IPR033905; Secretory_peroxidase.
DR PANTHER; PTHR31388; PTHR31388; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00458; PEROXIDASE.
DR PRINTS; PR00461; PLPEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Disulfide bond; Glycoprotein; Heme;
KW Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..335
FT /note="Peroxidase 53"
FT /id="PRO_0000023718"
FT ACT_SITE 72
FT /note="Proton acceptor"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 169
FT /ligand="substrate"
FT BINDING 199
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT SITE 68
FT /note="Transition state stabilizer"
FT MOD_RES 31
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:8977116"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 74..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 127..329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 206..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CONFLICT 21
FT /note="V -> L (in Ref. 5; AAM65211)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="I -> V (in Ref. 5; AAM65211)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="F -> S (in Ref. 5; AAM65211)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="D -> N (in Ref. 5; AAM65211)"
FT /evidence="ECO:0000305"
FT TURN 34..40
FT /evidence="ECO:0007829|PDB:1PA2"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:1PA2"
FT HELIX 62..74
FT /evidence="ECO:0007829|PDB:1PA2"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:1PA2"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1PA2"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:1PA2"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1PA2"
FT TURN 98..103
FT /evidence="ECO:0007829|PDB:1PA2"
FT HELIX 107..120
FT /evidence="ECO:0007829|PDB:1PA2"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:1PA2"
FT HELIX 127..141
FT /evidence="ECO:0007829|PDB:1PA2"
FT HELIX 161..167
FT /evidence="ECO:0007829|PDB:1PA2"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:1PA2"
FT HELIX 189..196
FT /evidence="ECO:0007829|PDB:1PA2"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:1PA2"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:1PA2"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:1PA2"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:1PA2"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:1PA2"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:1PA2"
FT HELIX 228..237
FT /evidence="ECO:0007829|PDB:1PA2"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:1PA2"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:1PA2"
FT HELIX 261..267
FT /evidence="ECO:0007829|PDB:1PA2"
FT HELIX 274..281
FT /evidence="ECO:0007829|PDB:1PA2"
FT HELIX 287..296
FT /evidence="ECO:0007829|PDB:1PA2"
FT HELIX 298..313
FT /evidence="ECO:0007829|PDB:1PA2"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:1PA2"
SQ SEQUENCE 335 AA; 34989 MW; 57E375B212F1BC6B CRC64;
MAVTNLPTCD GLFIISLIVI VSSIFGTSSA QLNATFYSGT CPNASAIVRS TIQQALQSDT
RIGASLIRLH FHDCFVNGCD ASILLDDTGS IQSEKNAGPN VNSARGFNVV DNIKTALENA
CPGVVSCSDV LALASEASVS LAGGPSWTVL LGRRDSLTAN LAGANSSIPS PIESLSNITF
KFSAVGLNTN DLVALSGAHT FGRARCGVFN NRLFNFSGTG NPDPTLNSTL LSTLQQLCPQ
NGSASTITNL DLSTPDAFDN NYFANLQSND GLLQSDQELF STTGSSTIAI VTSFASNQTL
FFQAFAQSMI NMGNISPLTG SNGEIRLDCK KVNGS
