PER59_ARATH
ID PER59_ARATH Reviewed; 328 AA.
AC Q39034;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Peroxidase 59;
DE Short=Atperox P59;
DE EC=1.11.1.7;
DE AltName: Full=ATPN;
DE AltName: Full=Peroxidase N;
DE Flags: Precursor;
GN Name=PER59; Synonyms=P59; OrderedLocusNames=At5g19890; ORFNames=F28I16.40;
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].
RC STRAIN=cv. Columbia;
RA Oestergaard L., Welinder K.G.;
RT "Sequence analysis and expression of two peroxidase encoding mRNAs from
RT Arabidopsis thaliana.";
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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 (1.9 ANGSTROMS) IN COMPLEX WITH CALCIUM AND HEME, AND
RP DISULFIDE BONDS.
RC STRAIN=cv. Columbia;
RX PubMed=10713531; DOI=10.1107/s0907444999016340;
RA Mirza O., Henriksen A., Oestergaard L., Welinder K.G., Gajhede M.;
RT "Arabidopsis thaliana peroxidase N: structure of a novel neutral
RT peroxidase.";
RL Acta Crystallogr. D 56:372-375(2000).
RN [8]
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 -!- 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=heme b; Xref=ChEBI:CHEBI:60344;
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 2 calcium ions per subunit.;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
CC -!- TISSUE SPECIFICITY: Slightly 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; X98453; CAA67092.1; -; mRNA.
DR EMBL; AF296836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92762.1; -; Genomic_DNA.
DR EMBL; AY123985; AAM74498.1; -; mRNA.
DR EMBL; BT000582; AAN18151.1; -; mRNA.
DR EMBL; AY088025; AAM65571.1; -; mRNA.
DR RefSeq; NP_568385.1; NM_121996.3.
DR PDB; 1QGJ; X-ray; 1.90 A; A/B=29-328.
DR PDBsum; 1QGJ; -.
DR AlphaFoldDB; Q39034; -.
DR SMR; Q39034; -.
DR BioGRID; 17387; 1.
DR STRING; 3702.AT5G19890.1; -.
DR PeroxiBase; 225; AtPrx59.
DR PaxDb; Q39034; -.
DR PRIDE; Q39034; -.
DR ProteomicsDB; 236403; -.
DR EnsemblPlants; AT5G19890.1; AT5G19890.1; AT5G19890.
DR GeneID; 832111; -.
DR Gramene; AT5G19890.1; AT5G19890.1; AT5G19890.
DR KEGG; ath:AT5G19890; -.
DR Araport; AT5G19890; -.
DR TAIR; locus:2147645; AT5G19890.
DR eggNOG; ENOG502QQQJ; Eukaryota.
DR HOGENOM; CLU_010543_0_3_1; -.
DR InParanoid; Q39034; -.
DR OMA; NGQRFSC; -.
DR OrthoDB; 902776at2759; -.
DR PhylomeDB; Q39034; -.
DR BioCyc; ARA:AT5G19890-MON; -.
DR EvolutionaryTrace; Q39034; -.
DR PRO; PR:Q39034; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q39034; baseline and differential.
DR Genevisible; Q39034; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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: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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..328
FT /note="Peroxidase 59"
FT /id="PRO_0000023724"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:10713531"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:10713531"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:10713531"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:10713531"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:10713531"
FT BINDING 163
FT /ligand="substrate"
FT BINDING 193
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 BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:10713531"
FT BINDING 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:10713531"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:10713531"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:10713531"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:10713531"
FT SITE 66
FT /note="Transition state stabilizer"
FT MOD_RES 29
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:Q42578,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:10713531"
FT DISULFID 72..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:10713531"
FT DISULFID 122..323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:10713531"
FT DISULFID 200..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:10713531"
FT CONFLICT 3
FT /note="T -> R (in Ref. 5; AAM65571)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="L -> A (in Ref. 1 and 5)"
FT /evidence="ECO:0000305"
FT TURN 32..38
FT /evidence="ECO:0007829|PDB:1QGJ"
FT HELIX 42..56
FT /evidence="ECO:0007829|PDB:1QGJ"
FT HELIX 60..72
FT /evidence="ECO:0007829|PDB:1QGJ"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:1QGJ"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:1QGJ"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:1QGJ"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1QGJ"
FT TURN 93..98
FT /evidence="ECO:0007829|PDB:1QGJ"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:1QGJ"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:1QGJ"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:1QGJ"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:1QGJ"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:1QGJ"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:1QGJ"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:1QGJ"
FT HELIX 183..190
FT /evidence="ECO:0007829|PDB:1QGJ"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:1QGJ"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:1QGJ"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:1QGJ"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:1QGJ"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:1QGJ"
FT HELIX 222..231
FT /evidence="ECO:0007829|PDB:1QGJ"
FT STRAND 241..247
FT /evidence="ECO:0007829|PDB:1QGJ"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:1QGJ"
FT HELIX 255..261
FT /evidence="ECO:0007829|PDB:1QGJ"
FT HELIX 268..275
FT /evidence="ECO:0007829|PDB:1QGJ"
FT TURN 277..283
FT /evidence="ECO:0007829|PDB:1QGJ"
FT HELIX 284..292
FT /evidence="ECO:0007829|PDB:1QGJ"
FT HELIX 294..308
FT /evidence="ECO:0007829|PDB:1QGJ"
SQ SEQUENCE 328 AA; 35023 MW; DABD3854FB2D3B12 CRC64;
MKTQTKVMGG HVLLTVFTLC MLCSGVRAQL SPDIYAKSCP NLVQIVRKQV AIALKAEIRM
AASLIRLHFH DCFVNGCDAS LLLDGADSEK LAIPNINSAR GFEVIDTIKA AVENACPGVV
SCADILTLAA RDSVVLSGGP GWRVALGRKD GLVANQNSAN NLPSPFEPLD AIIAKFVAVN
LNITDVVALS GAHTFGQAKC AVFSNRLFNF TGLGNPDATL ETSLLSNLQT VCPLGGNSNI
TAPLDRSTTD TFDNNYFKNL LEGKGLLSSD QILFSSDLAV NTTKKLVEAY SRSQSLFFRD
FTCAMIRMGN ISNGASGEVR TNCRVINN
