PER1_ZINVI
ID PER1_ZINVI Reviewed; 321 AA.
AC Q4W1I8; P84332; P84333;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Basic peroxidase;
DE EC=1.11.1.7;
DE AltName: Full=ZePrx33.44;
DE AltName: Full=ZePrx34.70;
DE Flags: Precursor;
GN Name=POD1;
GN and
GN Name=POD2;
OS Zinnia violacea (Garden zinnia) (Zinnia elegans).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Zinnia.
OX NCBI_TaxID=34245;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-43; 133-146; 186-201 AND
RP 297-313, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, PYROGLUTAMATE FORMATION AT GLN-31, AND MASS SPECTROMETRY.
RC STRAIN=cv. Envy; TISSUE=Callus;
RX PubMed=16258008; DOI=10.1104/pp.105.069674;
RA Gabaldon C., Lopez-Serrano M., Pedreno M.A., Barcelo A.R.;
RT "Cloning and molecular characterization of the basic peroxidase isoenzyme
RT from Zinnia elegans, an enzyme involved in lignin biosynthesis.";
RL Plant Physiol. 139:1138-1154(2005).
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. Involved in the synthesis of
CC highly polymerized lignins.
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 Evidence={ECO:0000269|PubMed:16258008};
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 KM=241 uM for p-coumaryl alcohol (in the presence of 10.2 uM H2O2,
CC for a partially glycosylated enzyme) {ECO:0000269|PubMed:16258008};
CC KM=432 uM for p-coumaryl alcohol (in the presence of 10.2 uM H2O2,
CC for a fully glycosylated enzyme) {ECO:0000269|PubMed:16258008};
CC KM=83 uM for coniferyl alcohol (in the presence of 10.2 uM H2O2, for
CC a partially glycosylated enzyme) {ECO:0000269|PubMed:16258008};
CC KM=124 uM for coniferyl alcohol (in the presence of 10.2 uM H2O2, for
CC a fully glycosylated enzyme) {ECO:0000269|PubMed:16258008};
CC KM=15 uM for sinapyl alcohol (in the presence of 10.2 uM H2O2, for a
CC partially glycosylated enzyme) {ECO:0000269|PubMed:16258008};
CC KM=13 uM for sinapyl alcohol (in the presence of 10.2 uM H2O2, for a
CC fully glycosylated enzyme) {ECO:0000269|PubMed:16258008};
CC Note=The full glycosylation reduces the affinity of the enzyme for
CC both p-coumaryl and coniferyl, but not sinapyl, alcohol.;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
CC -!- TISSUE SPECIFICITY: Expressed in tracheary elements, roots, young and
CC old hypocotyls, and stems in the partially glycosylated form and in
CC roots and young hypocotyls in the fully glycosylated form. None of the
CC isoforms is significantly expressed in leaves or cotyledons.
CC {ECO:0000269|PubMed:16258008}.
CC -!- PTM: N-glycosylated.
CC -!- MASS SPECTROMETRY: Mass=31460; Method=MALDI; Note=Deglycosylated form.;
CC Evidence={ECO:0000269|PubMed:16258008};
CC -!- MASS SPECTROMETRY: Mass=33440; Method=MALDI; Note=Partially
CC glycosylated form.; Evidence={ECO:0000269|PubMed:16258008};
CC -!- MASS SPECTROMETRY: Mass=34700; Method=MALDI; Note=Fully glycosylated
CC form.; Evidence={ECO:0000269|PubMed:16258008};
CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class
CC III) peroxidase subfamily. {ECO:0000255|PROSITE-ProRule:PRU00297}.
CC -!- CAUTION: Four genes are encoding the same mature protein that may have
CC different glycosylation degree. The two precursors produced differ by
CC only one amino acid located in the signal peptide. {ECO:0000305}.
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DR EMBL; AJ880395; CAI54302.1; -; mRNA.
DR EMBL; AJ880393; CAI54300.1; -; mRNA.
DR AlphaFoldDB; Q4W1I8; -.
DR SMR; Q4W1I8; -.
DR PeroxiBase; 2626; ZePrx15.
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; Direct protein sequencing; Disulfide bond; Glycoprotein; Heme;
KW Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Pyrrolidone carboxylic acid; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:16258008"
FT CHAIN 31..321
FT /note="Basic peroxidase"
FT /id="PRO_0000042696"
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 /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 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 195
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 196
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 68
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT MOD_RES 31
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000269|PubMed:16258008"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 74..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 123..317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 202..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ SEQUENCE 321 AA; 34245 MW; A52326F2F189FB0A CRC64;
MSYHKSSGTI LMVPLFMLLI SVNYFMSCNA QLSTTFYDTT CPTALSTIRT SIRSSVSSNR
RNAALVIRLL FHDCFVQGCD ASLLLSGAGS ERASPANDGV LGYEVIDAAK AAVERVCPGV
VSCADILAVA ARDASVAVGG PSWTVRLGRR DSTTSNAAQA ATDLPRGNMV LSQLISNFAN
KGLNTREMVA LSGSHTLGQA RCIRFRGRIY NSTLRIEPNF NRSLSQACPP TGNDATLRPL
DLVTPNSFDN NYYRNLVTSR GLLISDQVLF NADSTDSIVT EYVNNPATFA ADFAAAMVKM
SEIGVVTGTS GIVRTLCGNP S
