ID PER1A_ARMRU Reviewed; 353 AA. AC P00433; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 2. DT 08-NOV-2023, entry version 148. DE RecName: Full=Peroxidase C1A; DE EC=1.11.1.7; DE Flags: Precursor; GN Name=PRXC1A; Synonyms=HPRC1; OS Armoracia rusticana (Horseradish) (Armoracia laphatifolia). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Cardamineae; Armoracia. OX NCBI_TaxID=3704; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3371352; DOI=10.1111/j.1432-1033.1988.tb14052.x; RA Fujiyama K., Takemura H., Shibayama S., Kobayashi K., Choi J.K., RA Shinmyo A., Takano M., Yamada Y., Okada H.; RT "Structure of the horseradish peroxidase isozyme C genes."; RL Eur. J. Biochem. 173:681-687(1988). RN [2] RP PROTEIN SEQUENCE OF 31-338, AND PYROGLUTAMATE FORMATION AT GLN-31. RX PubMed=1001465; DOI=10.1016/0014-5793(76)80804-6; RA Welinder K.G.; RT "Covalent structure of the glycoprotein horseradish peroxidase RT (EC 1.11.1.7)."; RL FEBS Lett. 72:19-23(1976). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS). RX PubMed=9406554; DOI=10.1038/nsb1297-1032; RA Gajhede M., Schuller D.J., Henriksen A., Smith A.T., Poulos T.L.; RT "Crystal structure of horseradish peroxidase C at 2.15-A resolution."; RL Nat. Struct. Biol. 4:1032-1038(1997). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=9609699; DOI=10.1021/bi980234j; RA Henriksen A., Schuller D.J., Meno K., Welinder K.G., Smith A.T., RA Gajhede M.; RT "Structural interactions between horseradish peroxidase C and the substrate RT benzhydroxamic acid determined by X-ray crystallography."; RL Biochemistry 37:8054-8060(1998). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RA Meno K., White C.G., Smith A.T., Gajhede M.; RL Submitted (DEC-1998) to the PDB data bank. 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. 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 -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Note=Binds 2 calcium ions per subunit.; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.; CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Vacuole {ECO:0000305}. CC Note=Carboxy-terminal extension appears to target the protein to CC vacuoles. CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class CC III) peroxidase subfamily. {ECO:0000255|PROSITE-ProRule:PRU00297}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M37156; AAA33377.1; -; Genomic_DNA. DR PIR; S00625; OPRHC. DR PDB; 1ATJ; X-ray; 2.15 A; A/B/C/D/E/F=31-336. DR PDB; 1GW2; X-ray; 2.15 A; A=31-338. DR PDB; 1GWO; X-ray; 2.07 A; A=31-338. DR PDB; 1GWT; X-ray; 1.70 A; A=31-338. DR PDB; 1GWU; X-ray; 1.31 A; A=31-338. DR PDB; 1GX2; X-ray; 2.20 A; A/B=31-338. DR PDB; 1H55; X-ray; 1.61 A; A=31-338. DR PDB; 1H57; X-ray; 1.60 A; A=31-338. DR PDB; 1H58; X-ray; 1.70 A; A=31-338. DR PDB; 1H5A; X-ray; 1.60 A; A=31-338. DR PDB; 1H5C; X-ray; 1.62 A; A=31-338. DR PDB; 1H5D; X-ray; 1.60 A; A=31-338. DR PDB; 1H5E; X-ray; 1.60 A; A=31-338. DR PDB; 1H5F; X-ray; 1.60 A; A=31-338. DR PDB; 1H5G; X-ray; 1.57 A; A=31-338. DR PDB; 1H5H; X-ray; 1.60 A; A=31-338. DR PDB; 1H5I; X-ray; 1.60 A; A=31-338. DR PDB; 1H5J; X-ray; 1.60 A; A=31-338. DR PDB; 1H5K; X-ray; 1.60 A; A=31-338. DR PDB; 1H5L; X-ray; 1.60 A; A=31-338. DR PDB; 1H5M; X-ray; 1.57 A; A=31-338. DR PDB; 1HCH; X-ray; 1.57 A; A=31-336. DR PDB; 1KZM; X-ray; 2.00 A; A=31-338. DR PDB; 1W4W; X-ray; 1.55 A; A=31-353. DR PDB; 1W4Y; X-ray; 1.60 A; A=31-353. DR PDB; 2ATJ; X-ray; 2.00 A; A/B=31-337. DR PDB; 2YLJ; X-ray; 1.69 A; A=31-336. DR PDB; 3ATJ; X-ray; 2.20 A; A/B=31-338. DR PDB; 4ATJ; X-ray; 2.50 A; A/B=31-338. DR PDB; 6ATJ; X-ray; 2.00 A; A=31-338. DR PDB; 7ATJ; X-ray; 1.47 A; A=31-338. DR PDBsum; 1ATJ; -. DR PDBsum; 1GW2; -. DR PDBsum; 1GWO; -. DR PDBsum; 1GWT; -. DR PDBsum; 1GWU; -. DR PDBsum; 1GX2; -. DR PDBsum; 1H55; -. DR PDBsum; 1H57; -. DR PDBsum; 1H58; -. DR PDBsum; 1H5A; -. DR PDBsum; 1H5C; -. DR PDBsum; 1H5D; -. DR PDBsum; 1H5E; -. DR PDBsum; 1H5F; -. DR PDBsum; 1H5G; -. DR PDBsum; 1H5H; -. DR PDBsum; 1H5I; -. DR PDBsum; 1H5J; -. DR PDBsum; 1H5K; -. DR PDBsum; 1H5L; -. DR PDBsum; 1H5M; -. DR PDBsum; 1HCH; -. DR PDBsum; 1KZM; -. DR PDBsum; 1W4W; -. DR PDBsum; 1W4Y; -. DR PDBsum; 2ATJ; -. DR PDBsum; 2YLJ; -. DR PDBsum; 3ATJ; -. DR PDBsum; 4ATJ; -. DR PDBsum; 6ATJ; -. DR PDBsum; 7ATJ; -. DR AlphaFoldDB; P00433; -. DR PCDDB; P00433; -. DR SMR; P00433; -. DR ChEMBL; CHEMBL5169106; -. DR PeroxiBase; 90; AruPrx01-1. DR GlyConnect; 491; 7 N-Linked glycans. DR GlyCosmos; P00433; 8 sites, 10 glycans. DR iPTMnet; P00433; -. DR CPTAC; CPTAC-1477; -. DR BRENDA; 1.11.1.7; 429. DR SABIO-RK; P00433; -. DR EvolutionaryTrace; P00433; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; 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 Gene3D; 1.10.520.10; -; 1. DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 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:SF141; PEROXIDASE 33-RELATED; 1. DR PANTHER; PTHR31388; PEROXIDASE 72-RELATED; 1. DR Pfam; PF00141; peroxidase; 1. DR PRINTS; PR00458; PEROXIDASE. DR PRINTS; PR00461; PLPEROXIDASE. DR SUPFAM; SSF48113; Heme-dependent peroxidases; 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 3D-structure; Calcium; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; KW Peroxidase; Pyrrolidone carboxylic acid; Secreted; Signal; Vacuole. FT SIGNAL 1..30 FT /evidence="ECO:0000269|PubMed:1001465" FT CHAIN 31..338 FT /note="Peroxidase C1A" FT /evidence="ECO:0000269|PubMed:1001465" FT /id="PRO_0000023739" FT PROPEP 339..353 FT /id="PRO_0000023740" 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 BINDING 76 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT BINDING 78 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT BINDING 80 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT BINDING 82 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT BINDING 94 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT BINDING 169 FT /ligand="substrate" FT BINDING 200 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 201 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT BINDING 252 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT BINDING 255 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT BINDING 260 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT SITE 68 FT /note="Transition state stabilizer" FT MOD_RES 31 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, FT ECO:0000269|PubMed:1001465" FT CARBOHYD 43 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:1001465" FT CARBOHYD 87 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:1001465" FT CARBOHYD 188 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 216 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 228 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 244 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 285 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 298 FT /note="N-linked (GlcNAc...) asparagine" FT DISULFID 41..121 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, FT ECO:0000269|PubMed:1001465" FT DISULFID 74..79 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297, FT ECO:0000269|PubMed:1001465" FT DISULFID 127..331 FT DISULFID 207..239 FT TURN 34..40 FT /evidence="ECO:0007829|PDB:1GWU" FT HELIX 44..58 FT /evidence="ECO:0007829|PDB:1GWU" FT HELIX 62..74 FT /evidence="ECO:0007829|PDB:1GWU" FT TURN 75..77 FT /evidence="ECO:0007829|PDB:1GWU" FT STRAND 78..81 FT /evidence="ECO:0007829|PDB:1GWU" FT HELIX 82..84 FT /evidence="ECO:0007829|PDB:1GWU" FT STRAND 89..91 FT /evidence="ECO:0007829|PDB:1GWU" FT HELIX 94..96 FT /evidence="ECO:0007829|PDB:1GWU" FT TURN 98..103 FT /evidence="ECO:0007829|PDB:1GWU" FT HELIX 107..120 FT /evidence="ECO:0007829|PDB:1GWU" FT TURN 122..124 FT /evidence="ECO:0007829|PDB:1GWU" FT HELIX 127..141 FT /evidence="ECO:0007829|PDB:1GWU" FT HELIX 161..167 FT /evidence="ECO:0007829|PDB:1GWU" FT HELIX 175..184 FT /evidence="ECO:0007829|PDB:1GWU" FT HELIX 190..197 FT /evidence="ECO:0007829|PDB:1GWU" FT HELIX 198..201 FT /evidence="ECO:0007829|PDB:1GWU" FT STRAND 204..206 FT /evidence="ECO:0007829|PDB:1GWU" FT HELIX 207..210 FT /evidence="ECO:0007829|PDB:1GWU" FT HELIX 211..215 FT /evidence="ECO:0007829|PDB:1GWU" FT HELIX 217..219 FT /evidence="ECO:0007829|PDB:1GWU" FT STRAND 220..222 FT /evidence="ECO:0007829|PDB:1GWU" FT HELIX 229..238 FT /evidence="ECO:0007829|PDB:1GWU" FT STRAND 248..251 FT /evidence="ECO:0007829|PDB:1GWU" FT STRAND 253..255 FT /evidence="ECO:0007829|PDB:1H5F" FT HELIX 262..268 FT /evidence="ECO:0007829|PDB:1GWU" FT HELIX 275..282 FT /evidence="ECO:0007829|PDB:1GWU" FT TURN 284..288 FT /evidence="ECO:0007829|PDB:1GWU" FT HELIX 289..298 FT /evidence="ECO:0007829|PDB:1GWU" FT HELIX 300..314 FT /evidence="ECO:0007829|PDB:1GWU" FT STRAND 324..326 FT /evidence="ECO:0007829|PDB:1GWU" SQ 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 //