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Peroxidase C1C (EC 1.11.1.7) (Fragment)

 PER1C_ARMRU             Reviewed;         332 AA.
P15233;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
10-MAY-2017, entry version 99.
RecName: Full=Peroxidase C1C;
EC=1.11.1.7;
Flags: Precursor; Fragment;
Name=PRXC1C; Synonyms=HRPC3;
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 [GENOMIC DNA].
PubMed=3371352; DOI=10.1111/j.1432-1033.1988.tb14052.x;
Fujiyama K., Takemura H., Shibayama S., Kobayashi K., Choi J.K.,
Shinmyo A., Takano M., Yamada Y., Okada H.;
"Structure of the horseradish peroxidase isozyme C genes.";
Eur. J. Biochem. 173:681-687(1988).
-!- 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:0000305}. Vacuole
{ECO:0000305}. Note=Carboxy-terminal extension appears to target
the protein to vacuoles.
-!- SIMILARITY: Belongs to the peroxidase family. Classical plant
(class III) peroxidase subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
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EMBL; M60729; AAA33379.1; -; Genomic_DNA.
PIR; S00627; S00627.
ProteinModelPortal; P15233; -.
SMR; P15233; -.
PeroxiBase; 88; AruPrx01-3.
SABIO-RK; P15233; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005773; C:vacuole; 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.
3: Inferred from homology;
Calcium; Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron;
Metal-binding; Oxidoreductase; Peroxidase;
Pyrrolidone carboxylic acid; Secreted; Signal; Vacuole.
SIGNAL <1 9
CHAIN 10 332 Peroxidase C1C.
/FTId=PRO_0000023742.
ACT_SITE 51 51 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00297, ECO:0000255|PROSITE-
ProRule:PRU10012}.
METAL 52 52 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 55 55 Calcium 1; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
METAL 57 57 Calcium 1; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
METAL 59 59 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 61 61 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 179 179 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00297}.
METAL 180 180 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 231 231 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 234 234 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
METAL 239 239 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU00297}.
BINDING 148 148 Substrate; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
SITE 47 47 Transition state stabilizer.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
MOD_RES 10 10 Pyrrolidone carboxylic acid.
{ECO:0000250|UniProtKB:Q42578,
ECO:0000255|PROSITE-ProRule:PRU00297}.
CARBOHYD 22 22 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 66 66 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 195 195 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 207 207 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 223 223 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 264 264 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 20 100 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 53 58 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 106 310 {ECO:0000255|PROSITE-ProRule:PRU00297}.
DISULFID 186 218 {ECO:0000255|PROSITE-ProRule:PRU00297}.
NON_TER 1 1
SEQUENCE 332 AA; 36548 MW; 1938A450D595DFBE CRC64;
MLHASFSNAQ LTPTFYDNSC PNVSNIVRDI IINELRSDPS IAASILRLHF HDCFVNGCDA
SILLDNTTSF RTEKDAFGNA NSARGFPVVD RIKAAVERAC PRTVSCADVL TIAAQQSVNL
AGGPSWRVPL GRRDSRQAFL DLANANLPAP SFTLPELKAA FANVGLNRPS DLVALSGGHT
FGKNQCRFIM DRLYNFSNTG LPDPTLNTTY LQTLRQQCPR NGNQSVLVDF DLRTPTVFDN
KYYVNLKEQK GLIQSDQELF SSPNATDTIP LVRSYADGTQ TFFNAFVEAM NRMGNITPLT
GTQGEIRLNC RVVNSNSLLH DIVEVVDFVS SM


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