PER1A_ARMRU
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 03-AUG-2022, entry version 144.
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 (EC
RT 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 PeroxiBase; 90; AruPrx01-1.
DR GlyConnect; 491; 7 N-Linked glycans.
DR iPTMnet; P00433; -.
DR CPTAC; CPTAC-1477; -.
DR PRIDE; P00433; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; 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 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; PTHR31388; 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 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
