PERA2_ARMRU
ID PERA2_ARMRU Reviewed; 305 AA.
AC P80679;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Peroxidase A2;
DE EC=1.11.1.7;
GN Name=HRPA2;
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 PROTEIN SEQUENCE.
RA Rasmussen C.B., Stoffer B., Welinder K.G.;
RL Submitted (AUG-1996) to UniProtKB.
RN [2]
RP CHARACTERIZATION.
RX PubMed=11551197; DOI=10.1021/bi010661o;
RA Nielsen K.L., Indiani C., Henriksen A., Feis A., Becucci M., Gajhede M.,
RA Smulevich G., Welinder K.G.;
RT "Differential activity and structure of highly similar peroxidases.
RT Spectroscopic, crystallographic, and enzymatic analyses of lignifying
RT Arabidopsis thaliana peroxidase A2 and horseradish peroxidase A2.";
RL Biochemistry 40:11013-11021(2001).
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 -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class
CC III) peroxidase subfamily. {ECO:0000255|PROSITE-ProRule:PRU00297}.
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DR AlphaFoldDB; P80679; -.
DR SMR; P80679; -.
DR PeroxiBase; 298; AruPrx53-2.
DR PRIDE; P80679; -.
DR BRENDA; 1.11.1.7; 429.
DR SABIO-RK; P80679; -.
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 Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein; Heme;
KW Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Pyrrolidone carboxylic acid.
FT CHAIN 1..305
FT /note="Peroxidase A2"
FT /id="PRO_0000055604"
FT ACT_SITE 42
FT /note="Proton acceptor"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 46
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 139
FT /ligand="substrate"
FT BINDING 169
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 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT SITE 38
FT /note="Transition state stabilizer"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:Q42578"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 11..91
FT DISULFID 44..49
FT DISULFID 97..299
FT DISULFID 176..208
SQ SEQUENCE 305 AA; 31899 MW; 6A700392151C1737 CRC64;
QLNATFYSGT CPNASAIVRS TIQQAFQSDT RIGASLIRLH FHDCFVDGCD ASILLDDSGS
IQSEKNAGPN ANSARGFNVV DNIKTALENT CPGVVSCSDI LALASEASVS LTGGPSWTVL
LGRRDSLTAN LAGANSAIPS PFEGLSNITS KFSAVGLNTN DLVALSGAHT FGRARCGVFN
NRLFNFSGTN GPDPTLNSTL LSSLQQLCPQ NGSASTITNL DLSTPDAFDN NYFANLQSNN
GLLQSDQELF STLGSATIAV VTSFASNQTL FFQAFAQSMI NMGNISPLTG SNGEIRLDCK
KVDGS
