PER70_MAIZE
ID PER70_MAIZE Reviewed; 321 AA.
AC A5H452;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Peroxidase 70;
DE EC=1.11.1.7;
DE AltName: Full=Plasma membrane-bound peroxidase 2b;
DE Short=pmPOX2b;
DE Flags: Precursor;
GN Name=PER70; Synonyms=POX2B, PRX70;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Wisconsin 22;
RX PubMed=18603027; DOI=10.1016/j.jprot.2008.06.006;
RA Mika A., Buck F., Luethje S.;
RT "Membrane-bound class III peroxidases: identification, biochemical
RT properties and sequence analysis of isoenzymes purified from maize (Zea
RT mays L.) roots.";
RL J. Proteomics 71:412-424(2008).
RN [2]
RP FUNCTION.
RX PubMed=12857829; DOI=10.1104/pp.103.020396;
RA Mika A., Luethje S.;
RT "Properties of guaiacol peroxidase activities isolated from corn root
RT plasma membranes.";
RL Plant Physiol. 132:1489-1498(2003).
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. {ECO:0000255|PROSITE-
CC ProRule:PRU00297, ECO:0000269|PubMed:12857829}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=6.9 umol/min/mg enzyme with guaiacol as substrate
CC {ECO:0000269|PubMed:18603027};
CC Note=In the presence of H(2)O(2).;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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; EF059717; ABN48843.1; -; mRNA.
DR RefSeq; NP_001106040.1; NM_001112570.1.
DR AlphaFoldDB; A5H452; -.
DR SMR; A5H452; -.
DR STRING; 4577.GRMZM2G025441_P01; -.
DR PeroxiBase; 780; ZmPrx70.
DR PaxDb; A5H452; -.
DR PRIDE; A5H452; -.
DR GeneID; 100125639; -.
DR KEGG; zma:100125639; -.
DR eggNOG; ENOG502R50Y; Eukaryota.
DR OrthoDB; 902776at2759; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; A5H452; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 Calcium; Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..321
FT /note="Peroxidase 70"
FT /id="PRO_0000359406"
FT ACT_SITE 67
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
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 BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 194
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 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT SITE 63
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT MOD_RES 26
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 69..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 122..317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 201..226
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ SEQUENCE 321 AA; 33481 MW; 3862FA378D19383B CRC64;
MASSSFTSLS VMVLLCLAAA AVASAQLSPT FYSRSCPRAL ATIKAAVTAA VAQEARMGAS
LLRLHFHDCF VQGCDGSVLL NDTATFTGEQ TANPNVGSIR GFGVVDNIKA QVEAVCPGVV
SCADILAVAA RDSVVALGGP SWRVLLGRRD STTASLALAN SDLPAPSLDL ANLTAAFAKK
RLSRTDLVAL SGAHTIGLAQ CKNFRAHIYN DTNVNAAFAT LRRANCPAAA GNGDGNLAPL
DTATPTAFDN AYYTNLLAQR GLLHSDQQLF NGGATDGLVR TYASTPRRFS RDFAAAMIRM
GNISPLTGTQ GQIRRACSRV N
