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Peroxidase C1A (EC 1.11.1.7)

 PER1A_ARMRU             Reviewed;         353 AA.
P00433;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 2.
10-MAY-2017, entry version 126.
RecName: Full=Peroxidase C1A;
EC=1.11.1.7;
Flags: Precursor;
Name=PRXC1A; Synonyms=HPRC1;
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).
[2]
PROTEIN SEQUENCE OF 31-338.
PubMed=1001465; DOI=10.1016/0014-5793(76)80804-6;
Welinder K.G.;
"Covalent structure of the glycoprotein horseradish peroxidase (EC
1.11.1.7).";
FEBS Lett. 72:19-23(1976).
[3]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
PubMed=9406554; DOI=10.1038/nsb1297-1032;
Gajhede M., Schuller D.J., Henriksen A., Smith A.T., Poulos T.L.;
"Crystal structure of horseradish peroxidase C at 2.15-A resolution.";
Nat. Struct. Biol. 4:1032-1038(1997).
[4]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=9609699; DOI=10.1021/bi980234j;
Henriksen A., Schuller D.J., Meno K., Welinder K.G., Smith A.T.,
Gajhede M.;
"Structural interactions between horseradish peroxidase C and the
substrate benzhydroxamic acid determined by X-ray crystallography.";
Biochemistry 37:8054-8060(1998).
[5]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Meno K., White C.G., Smith A.T., Gajhede M.;
Submitted (DEC-1998) to the PDB data bank.
-!- 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.;
-!- SUBUNIT: Monomer.
-!- 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; M37156; AAA33377.1; -; Genomic_DNA.
PIR; S00625; OPRHC.
PDB; 1ATJ; X-ray; 2.15 A; A/B/C/D/E/F=31-336.
PDB; 1GW2; X-ray; 2.15 A; A=31-338.
PDB; 1GWO; X-ray; 2.07 A; A=31-338.
PDB; 1GWT; X-ray; 1.70 A; A=31-338.
PDB; 1GWU; X-ray; 1.31 A; A=31-338.
PDB; 1GX2; X-ray; 2.20 A; A/B=31-338.
PDB; 1H55; X-ray; 1.61 A; A=31-338.
PDB; 1H57; X-ray; 1.60 A; A=31-338.
PDB; 1H58; X-ray; 1.70 A; A=31-338.
PDB; 1H5A; X-ray; 1.60 A; A=31-338.
PDB; 1H5C; X-ray; 1.62 A; A=31-338.
PDB; 1H5D; X-ray; 1.60 A; A=31-338.
PDB; 1H5E; X-ray; 1.60 A; A=31-338.
PDB; 1H5F; X-ray; 1.60 A; A=31-338.
PDB; 1H5G; X-ray; 1.57 A; A=31-338.
PDB; 1H5H; X-ray; 1.60 A; A=31-338.
PDB; 1H5I; X-ray; 1.60 A; A=31-338.
PDB; 1H5J; X-ray; 1.60 A; A=31-338.
PDB; 1H5K; X-ray; 1.60 A; A=31-338.
PDB; 1H5L; X-ray; 1.60 A; A=31-338.
PDB; 1H5M; X-ray; 1.57 A; A=31-338.
PDB; 1HCH; X-ray; 1.57 A; A=31-336.
PDB; 1KZM; X-ray; 2.00 A; A=31-338.
PDB; 1W4W; X-ray; 1.55 A; A=31-353.
PDB; 1W4Y; X-ray; 1.60 A; A=31-353.
PDB; 2ATJ; X-ray; 2.00 A; A/B=31-337.
PDB; 2YLJ; X-ray; 1.69 A; A=31-336.
PDB; 3ATJ; X-ray; 2.20 A; A/B=31-338.
PDB; 4ATJ; X-ray; 2.50 A; A/B=31-338.
PDB; 6ATJ; X-ray; 2.00 A; A=31-338.
PDB; 7ATJ; X-ray; 1.47 A; A=31-338.
PDBsum; 1ATJ; -.
PDBsum; 1GW2; -.
PDBsum; 1GWO; -.
PDBsum; 1GWT; -.
PDBsum; 1GWU; -.
PDBsum; 1GX2; -.
PDBsum; 1H55; -.
PDBsum; 1H57; -.
PDBsum; 1H58; -.
PDBsum; 1H5A; -.
PDBsum; 1H5C; -.
PDBsum; 1H5D; -.
PDBsum; 1H5E; -.
PDBsum; 1H5F; -.
PDBsum; 1H5G; -.
PDBsum; 1H5H; -.
PDBsum; 1H5I; -.
PDBsum; 1H5J; -.
PDBsum; 1H5K; -.
PDBsum; 1H5L; -.
PDBsum; 1H5M; -.
PDBsum; 1HCH; -.
PDBsum; 1KZM; -.
PDBsum; 1W4W; -.
PDBsum; 1W4Y; -.
PDBsum; 2ATJ; -.
PDBsum; 2YLJ; -.
PDBsum; 3ATJ; -.
PDBsum; 4ATJ; -.
PDBsum; 6ATJ; -.
PDBsum; 7ATJ; -.
ProteinModelPortal; P00433; -.
SMR; P00433; -.
PeroxiBase; 90; AruPrx01-1.
UniCarbKB; P00433; -.
BRENDA; 1.11.1.7; 429.
SABIO-RK; P00433; -.
EvolutionaryTrace; P00433; -.
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.
1: Evidence at protein level;
3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding;
Oxidoreductase; Peroxidase; Pyrrolidone carboxylic acid; Secreted;
Signal; Vacuole.
SIGNAL 1 30 {ECO:0000269|PubMed:1001465}.
CHAIN 31 338 Peroxidase C1A.
{ECO:0000269|PubMed:1001465}.
/FTId=PRO_0000023739.
PROPEP 339 353
/FTId=PRO_0000023740.
ACT_SITE 72 72 Proton acceptor.
METAL 73 73 Calcium 1.
METAL 76 76 Calcium 1; via carbonyl oxygen.
METAL 78 78 Calcium 1; via carbonyl oxygen.
METAL 80 80 Calcium 1.
METAL 82 82 Calcium 1.
METAL 94 94 Calcium 1.
METAL 200 200 Iron (heme axial ligand).
METAL 201 201 Calcium 2.
METAL 252 252 Calcium 2.
METAL 255 255 Calcium 2.
METAL 260 260 Calcium 2.
BINDING 169 169 Substrate; via carbonyl oxygen.
SITE 68 68 Transition state stabilizer.
MOD_RES 31 31 Pyrrolidone carboxylic acid.
{ECO:0000255|PROSITE-ProRule:PRU00297,
ECO:0000269|PubMed:1001465}.
CARBOHYD 43 43 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:1001465}.
CARBOHYD 87 87 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:1001465}.
CARBOHYD 188 188 N-linked (GlcNAc...) asparagine.
CARBOHYD 216 216 N-linked (GlcNAc...) asparagine.
CARBOHYD 228 228 N-linked (GlcNAc...) asparagine.
CARBOHYD 244 244 N-linked (GlcNAc...) asparagine.
CARBOHYD 285 285 N-linked (GlcNAc...) asparagine.
CARBOHYD 298 298 N-linked (GlcNAc...) asparagine.
DISULFID 41 121 {ECO:0000255|PROSITE-ProRule:PRU00297,
ECO:0000269|PubMed:1001465}.
DISULFID 74 79 {ECO:0000255|PROSITE-ProRule:PRU00297,
ECO:0000269|PubMed:1001465}.
DISULFID 127 331
DISULFID 207 239
TURN 34 40 {ECO:0000244|PDB:1GWU}.
HELIX 44 58 {ECO:0000244|PDB:1GWU}.
HELIX 62 74 {ECO:0000244|PDB:1GWU}.
TURN 75 77 {ECO:0000244|PDB:1GWU}.
STRAND 78 81 {ECO:0000244|PDB:1GWU}.
HELIX 82 84 {ECO:0000244|PDB:1GWU}.
STRAND 89 91 {ECO:0000244|PDB:1GWU}.
HELIX 94 96 {ECO:0000244|PDB:1GWU}.
TURN 98 103 {ECO:0000244|PDB:1GWU}.
HELIX 107 120 {ECO:0000244|PDB:1GWU}.
TURN 122 124 {ECO:0000244|PDB:1GWU}.
HELIX 127 141 {ECO:0000244|PDB:1GWU}.
HELIX 161 167 {ECO:0000244|PDB:1GWU}.
HELIX 175 184 {ECO:0000244|PDB:1GWU}.
HELIX 190 197 {ECO:0000244|PDB:1GWU}.
HELIX 198 201 {ECO:0000244|PDB:1GWU}.
STRAND 204 206 {ECO:0000244|PDB:1GWU}.
HELIX 207 210 {ECO:0000244|PDB:1GWU}.
HELIX 211 215 {ECO:0000244|PDB:1GWU}.
HELIX 217 219 {ECO:0000244|PDB:1GWU}.
STRAND 220 222 {ECO:0000244|PDB:1GWU}.
HELIX 229 238 {ECO:0000244|PDB:1GWU}.
STRAND 248 251 {ECO:0000244|PDB:1GWU}.
STRAND 253 255 {ECO:0000244|PDB:1H5F}.
HELIX 262 268 {ECO:0000244|PDB:1GWU}.
HELIX 275 282 {ECO:0000244|PDB:1GWU}.
TURN 284 288 {ECO:0000244|PDB:1GWU}.
HELIX 289 298 {ECO:0000244|PDB:1GWU}.
HELIX 300 314 {ECO:0000244|PDB:1GWU}.
STRAND 324 326 {ECO:0000244|PDB:1GWU}.
SEQUENCE 353 AA; 38825 MW; AC916C03C4A24D27 CRC64;
MHFSSSSTLF TCITLIPLVC LILHASLSDA QLTPTFYDNS CPNVSNIVRD TIVNELRSDP
RIAASILRLH FHDCFVNGCD ASILLDNTTS FRTEKDAFGN ANSARGFPVI DRMKAAVESA
CPRTVSCADL LTIAAQQSVT LAGGPSWRVP LGRRDSLQAF LDLANANLPA PFFTLPQLKD
SFRNVGLNRS SDLVALSGGH TFGKNQCRFI MDRLYNFSNT GLPDPTLNTT YLQTLRGLCP
LNGNLSALVD FDLRTPTIFD NKYYVNLEEQ KGLIQSDQEL FSSPNATDTI PLVRSFANST
QTFFNAFVEA MDRMGNITPL TGTQGQIRLN CRVVNSNSLL HDMVEVVDFV SSM


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