PERN1_TOBAC
ID PERN1_TOBAC Reviewed; 330 AA.
AC Q9XIV8; P81512; P81513; Q4A3Y7; Q50LI2;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Peroxidase N1;
DE EC=1.11.1.7;
DE AltName: Full=Peroxidase B2;
DE AltName: Full=Peroxidase B3;
DE Flags: Precursor;
GN Name=poxN1 {ECO:0000312|EMBL:CAH17984.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA82307.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Samsun NN; TISSUE=Leaf {ECO:0000312|EMBL:BAA82307.1};
RA Hiraga S., Ito H., Matsui H., Honma M., Ohashi Y.;
RT "cDNA sequences for two novel tobacco peroxidase isoenzymes (Accession Nos.
RT AB027752 and AB027753). (PGR99-109).";
RL (er) Plant Gene Register PGR99-109(1999).
RN [2] {ECO:0000312|EMBL:BAD97808.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Samsun; TISSUE=Callus {ECO:0000312|EMBL:BAD97808.1};
RA Kondo S.;
RT "cDNA sequence encoding a peroxidase highly expressed in paraquat-tolerant
RT tobacco callus.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:CAH17984.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-327.
RC TISSUE=Leaf {ECO:0000312|EMBL:CAH17984.1};
RX PubMed=15988562; DOI=10.1007/s11103-005-1426-9;
RA McInnis S.M., Costa L.M., Gutierrez-Marcos J.F., Henderson C.A.,
RA Hiscock S.J.;
RT "Isolation and characterization of a polymorphic stigma-specific class III
RT peroxidase gene from Senecio squalidus L. (Asteraceae).";
RL Plant Mol. Biol. 57:659-677(2005).
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 44-130 AND 270-330, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND VARIANTS GLN-77; ARG-101; LYS-111 AND
RP LYS-281.
RC STRAIN=cv. Bright Yellow 2 {ECO:0000269|PubMed:10364388};
RX PubMed=10364388; DOI=10.1104/pp.120.2.371;
RA de Marco A., Guzzardi P., Jamet E.;
RT "Isolation of tobacco isoperoxidases accumulated in cell-suspension culture
RT medium and characterization of activities related to cell wall
RT metabolism.";
RL Plant Physiol. 120:371-382(1999).
RN [5] {ECO:0000305}
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=10795310; DOI=10.1093/pcp/41.2.165;
RA Hiraga S., Ito H., Sasaki K., Yamakawa H., Mitsuhara I., Toshima H.,
RA Matsui H., Honma M., Ohashi Y.;
RT "Wound-induced expression of a tobacco peroxidase is not enhanced by
RT ethephon and suppressed by methyl jasmonate and coronatine.";
RL Plant Cell Physiol. 41:165-170(2000).
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. Can use NADH, NADPH and
CC monolignols as substrates. {ECO:0000255|PROSITE-ProRule:PRU00297,
CC ECO:0000269|PubMed:10364388, ECO:0000305}.
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:10364388};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q39034,
CC ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:Q39034,
CC ECO:0000255|PROSITE-ProRule:PRU00297};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:Q39034,
CC ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000250|UniProtKB:Q39034, ECO:0000255|PROSITE-ProRule:PRU00297};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.7. {ECO:0000269|PubMed:10364388};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P84516,
CC ECO:0000255|PROSITE-ProRule:PRU00297}.
CC -!- TISSUE SPECIFICITY: Expressed at a high level in roots and at a trace
CC level in lower leaves. Not expressed in upper leaves, stems, flowers,
CC seeds and shoot apices. {ECO:0000269|PubMed:10795310}.
CC -!- INDUCTION: Induced rapidly in leaves after wounding, mRNA is detectable
CC 30 minutes after wounding, reaches maximum levels after 4 hours, and
CC decreases slightly after 8 hours. When lower leaves are wounded, mRNA
CC also accumulates in upper, unwounded, leaves. Wound-induced expression
CC is enhanced by spermine, and suppressed by methyl jasmonite and
CC coronatine. Salicylic acid and ethephon have no effect on wound-induced
CC expression. Induced by infection with TMV.
CC {ECO:0000269|PubMed:10795310}.
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; AB027753; BAA82307.1; -; mRNA.
DR EMBL; AB044153; BAD97807.1; -; mRNA.
DR EMBL; AB044154; BAD97808.1; -; mRNA.
DR EMBL; AJ810538; CAH17984.1; -; Genomic_DNA.
DR RefSeq; NP_001312082.1; NM_001325153.1.
DR RefSeq; NP_001312671.1; NM_001325742.1.
DR AlphaFoldDB; Q9XIV8; -.
DR SMR; Q9XIV8; -.
DR STRING; 4097.Q9XIV8; -.
DR PeroxiBase; 3815; NtPrx10-1B.
DR PeroxiBase; 52; NtPrx10-1A.
DR PRIDE; Q9XIV8; -.
DR GeneID; 107773042; -.
DR GeneID; 107803841; -.
DR KEGG; nta:107773042; -.
DR KEGG; nta:107803841; -.
DR Proteomes; UP000084051; Unplaced.
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; Direct protein sequencing; Disulfide bond; Glycoprotein; Heme;
KW Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:10364388"
FT CHAIN 30..330
FT /note="Peroxidase N1"
FT /evidence="ECO:0000269|PubMed:10364388"
FT /id="PRO_0000312842"
FT ACT_SITE 72
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q39034,
FT ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000255|PROSITE-
FT ProRule:PRU10012"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q39034,
FT 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:0000250|UniProtKB:Q39034,
FT 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:0000250|UniProtKB:Q39034,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q39034,
FT 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:0000250|UniProtKB:Q39034,
FT 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:0000250|UniProtKB:Q39034,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q39034,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q39034,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT SITE 68
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q39034,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT MOD_RES 30
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..117
FT /evidence="ECO:0000250|UniProtKB:Q39034,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 74..79
FT /evidence="ECO:0000250|UniProtKB:Q39034,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 123..326
FT /evidence="ECO:0000250|UniProtKB:Q39034,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 201..233
FT /evidence="ECO:0000250|UniProtKB:Q39034,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT VARIANT 77
FT /note="L -> Q"
FT /evidence="ECO:0000269|PubMed:10364388"
FT VARIANT 101
FT /note="K -> R"
FT /evidence="ECO:0000269|PubMed:10364388"
FT VARIANT 111
FT /note="T -> K"
FT /evidence="ECO:0000269|PubMed:10364388"
FT VARIANT 281
FT /note="Q -> K"
FT /evidence="ECO:0000269|PubMed:10364388"
FT CONFLICT 86..88
FT /note="EGS -> DGT (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="R -> S (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="L -> V (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="D -> N (in Ref. 2; BAD97807)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="I -> V (in Ref. 2; BAD97807)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="R -> Q (in Ref. 2; BAD97807)"
FT /evidence="ECO:0000305"
FT CONFLICT 178..179
FT /note="LT -> TA (in Ref. 2; BAD97807)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="D -> G (in Ref. 2; BAD97807)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="R -> Q (in Ref. 2; BAD97807)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="S -> A (in Ref. 2; BAD97807)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="G -> A (in Ref. 2; BAD97807)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="V -> A (in Ref. 2; BAD97807)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="R -> G (in Ref. 3; CAH17984)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 35732 MW; 2034ACB6376B6180 CRC64;
MEYYHHSINK MAMFMVILVL AIDVTMVLGQ GTRVGFYSST CPRAESIVQS TVRAHFQSDP
TVAPGILRMH FHDCFVLGCD GSILIEGSDA ERTAIPNRNL KGFDVIEDAK TQIEAICPGV
VSCADILALA ARDSVVATRG LTWSVPTGRR DGRVSRAADA GDLPAFFDSV DIQKRKFLTK
GLNTQDLVAL TGAHTIGTAG CAVIRDRLFN FNSTGGPDPS IDATFLPQLR ALCPQNGDAS
RRVGLDTGSV NNFDTSYFSN LRNGRGVLES DQKLWTDAST QVFVQRFLGI RGLLGLTFGV
EFGRSMVKMS NIEVKTGTNG EIRKVCSAIN
