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Peroxidase N (EC 1.11.1.7) (Neutral peroxidase)

 PERN_ARMRU              Reviewed;         327 AA.
Q42517;
06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
30-AUG-2017, entry version 92.
RecName: Full=Peroxidase N;
EC=1.11.1.7;
AltName: Full=Neutral peroxidase;
Flags: Precursor;
Name=HRPN;
Armoracia rusticana (Horseradish) (Armoracia laphatifolia).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Cardamineae;
Armoracia.
NCBI_TaxID=3704;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Root;
PubMed=2001399;
Bartonek-Roxa E., Eriksson H., Mattiasson B.;
"The cDNA sequence of a neutral horseradish peroxidase.";
Biochim. Biophys. Acta 1088:245-250(1991).
-!- FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants,
biosynthesis and degradation of lignin, suberization, auxin
catabolism, response to environmental stresses such as wounding,
pathogen attack and oxidative stress. These functions might be
dependent on each isozyme/isoform in each plant tissue.
-!- CATALYTIC ACTIVITY: 2 phenolic donor + H(2)O(2) = 2 phenoxyl
radical of the donor + 2 H(2)O.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Note=Binds 2 calcium ions per subunit.;
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
subunit.;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-
ProRule:PRU00297}.
-!- SIMILARITY: Belongs to the peroxidase family. Classical plant
(class III) peroxidase subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
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EMBL; X57564; CAA40796.1; -; mRNA.
PIR; S14268; S14268.
ProteinModelPortal; Q42517; -.
SMR; Q42517; -.
PeroxiBase; 87; AruPrx06.
PRIDE; Q42517; -.
SABIO-RK; Q42517; -.
PRO; PR:Q42517; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
CDD; cd00693; secretory_peroxidase; 1.
InterPro; IPR010255; Haem_peroxidase.
InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
InterPro; IPR000823; Peroxidase_pln.
InterPro; IPR019794; Peroxidases_AS.
InterPro; IPR019793; Peroxidases_heam-ligand_BS.
InterPro; IPR033905; Secretory_peroxidase.
Pfam; PF00141; peroxidase; 1.
PRINTS; PR00458; PEROXIDASE.
PRINTS; PR00461; PLPEROXIDASE.
SUPFAM; SSF48113; SSF48113; 1.
PROSITE; PS00435; PEROXIDASE_1; 1.
PROSITE; PS00436; PEROXIDASE_2; 1.
PROSITE; PS50873; PEROXIDASE_4; 1.
2: Evidence at transcript level;
Calcium; Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron;
Metal-binding; Oxidoreductase; Peroxidase;
Pyrrolidone carboxylic acid; Secreted; Signal.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 327 Peroxidase N.
/FTId=PRO_0000023745.
ACT_SITE 70 70 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00297, ECO:0000255|PROSITE-
ProRule:PRU10012}.
METAL 71 71 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 74 74 Calcium 1; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
METAL 76 76 Calcium 1; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
METAL 78 78 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 80 80 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 193 193 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00297}.
METAL 194 194 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 245 245 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 248 248 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 253 253 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
BINDING 163 163 Substrate; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
SITE 66 66 Transition state stabilizer.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
MOD_RES 29 29 Pyrrolidone carboxylic acid.
{ECO:0000250|UniProtKB:Q42578}.
CARBOHYD 155 155 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 182 182 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 209 209 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 239 239 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 247 247 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 281 281 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 39 116 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 72 77 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 122 323 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 200 232 {ECO:0000255|PROSITE-ProRule:PRU00297}.
SEQUENCE 327 AA; 35126 MW; 5C427EBDD0A2CCDF CRC64;
MKTQTKVMGG HVLLTVFTLC MLCSAVRAQL SPDIYAKSCP NLLQIVRDQV KIALKAEIRM
AASLIRLHFH DCFVNGCDAS VLLDGTNSEK LAIPNVNSVR GFEVIDTIKA AVENACPGVV
SCADILTLAA RDSVYLSGGP QWRVALGRKD GLVANQSSAN NLPSPFEPLD AIIAKFAAVG
LNVTDVVALS GAHTFGQAKC DLFSNRLFNF TGAGTPDSTL ETTLLSDLQT VCPIGGNGNK
TAPLDRNSTD AFDNNYFKNL LEGKGLLSSD QILFSSDLAV NTTKRLVEAY SRSQYLFFRD
FTCSMIRMGS LVNGASGEVR TNCRVIN


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