PER60_ARATH
ID PER60_ARATH Reviewed; 331 AA.
AC Q9FMR0; Q96507;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Peroxidase 60;
DE Short=Atperox P60;
DE EC=1.11.1.7;
DE AltName: Full=ATP14a;
DE Flags: Precursor;
GN Name=PER60; Synonyms=P60; OrderedLocusNames=At5g22410; ORFNames=MWD9.21;
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Welinder K.G., Jespersen H.M., Kjaersgaard I.V.H., Justesen A.F.,
RA Oestergaard L., Abelskov A.K., Hansen L.N., Rasmussen S.K.;
RT "From expressed sequence tags to structure, function, evolution and
RT expression of 28 ER-targeted Arabidopsis peroxidases.";
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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 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 [5]
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 Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00297};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00297};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, slightly in leaves.
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; X98803; CAA67335.1; -; mRNA.
DR EMBL; AB007651; BAB08340.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93023.1; -; Genomic_DNA.
DR RefSeq; NP_197633.1; NM_122146.4.
DR AlphaFoldDB; Q9FMR0; -.
DR SMR; Q9FMR0; -.
DR BioGRID; 17577; 2.
DR STRING; 3702.AT5G22410.1; -.
DR PeroxiBase; 226; AtPrx60.
DR PaxDb; Q9FMR0; -.
DR PRIDE; Q9FMR0; -.
DR ProteomicsDB; 234826; -.
DR EnsemblPlants; AT5G22410.1; AT5G22410.1; AT5G22410.
DR GeneID; 832302; -.
DR Gramene; AT5G22410.1; AT5G22410.1; AT5G22410.
DR KEGG; ath:AT5G22410; -.
DR Araport; AT5G22410; -.
DR TAIR; locus:2176402; AT5G22410.
DR eggNOG; ENOG502QPI1; Eukaryota.
DR HOGENOM; CLU_010543_0_3_1; -.
DR InParanoid; Q9FMR0; -.
DR OMA; AMIRLYF; -.
DR OrthoDB; 902776at2759; -.
DR PhylomeDB; Q9FMR0; -.
DR BioCyc; ARA:AT5G22410-MON; -.
DR PRO; PR:Q9FMR0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMR0; baseline and differential.
DR Genevisible; Q9FMR0; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; IBA:GO_Central.
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; IBA:GO_Central.
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; PTHR31235; PTHR31235; 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 Calcium; Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..331
FT /note="Peroxidase 60"
FT /id="PRO_0000023725"
FT ACT_SITE 68
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
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 BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
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 BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 191
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 192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
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 BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT SITE 64
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 70..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 119..321
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 198..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CONFLICT 182
FT /note="N -> T (in Ref. 1; CAA67335)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="A -> G (in Ref. 1; CAA67335)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="S -> G (in Ref. 1; CAA67335)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="S -> N (in Ref. 1; CAA67335)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="I -> N (in Ref. 1; CAA67335)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="S -> R (in Ref. 1; CAA67335)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 36016 MW; A5138FDFAD17105A CRC64;
MAVKISTIEV LILSLALLSF GHGCYGQLRL GFYSQNCQNV ENIVSKVVGE AFIKDSSIAP
AMIRLYFHDC FSNGCDASLL LDGSNSEKKA SPNLSVRGYE VIDDIKSAVE KECDRVVSCA
DIIALATRDL VTLASGGKTR YEIPTGRLDG KISSALLVDL PSPKMTVAET AAKFDQRKLS
LNDMVLLLGG HTIGVTHCSF IMDRLYNFQN TQKPDPSMDP KLVEELSAKC PKSSSTDGII
SLDQNATSSN TMDVSFYKEI KVSRGVLHID QKLAIDDLTS KMVTDIANGN DFLVRFGQAM
VNLGSVRVIS KPKDGEIRRS CRSTCNNPLC V
