PERE5_ARMRU
ID PERE5_ARMRU Reviewed; 306 AA.
AC P59121;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Peroxidase E5;
DE EC=1.11.1.7;
GN Name=HRPE5;
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, PYROGLUTAMATE FORMATION AT GLN-1, AND X-RAY
RP CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RA Morita Y., Mikami B., Yamashita H., Lee J.Y., Aibara S., Sato M.,
RA Katsube Y., Tanaka N.;
RT "Primary and crystal structures of horseradish peroxidase isozyme E5.";
RL (In) Lobarzewski J., Greppin H., Penel C., Gaspar T. (eds.);
RL Biochemical, molecular, and physiological aspects of plant peroxidases,
RL pp.81-88, University of M. Curie-Sklodowska and University of Geneva,
RL Lublin and Geneva (1991).
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; P59121; -.
DR SMR; P59121; -.
DR PeroxiBase; 67; AruPrx05.
DR SABIO-RK; P59121; -.
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..306
FT /note="Peroxidase E5"
FT /id="PRO_0000055603"
FT ACT_SITE 42
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 170
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 225
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 230
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|Ref.1"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 11..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 44..49
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 97..300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 177..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ SEQUENCE 306 AA; 33722 MW; A8A344197078EFE6 CRC64;
QLRPDFYSRT CPSVFNIIKN VIVDELQTDP RIAASILRLH FHDCFVRGCD ASILLDTSKS
FRTEKDAAPN VNSARGFNVI DRMKTALERA CPRTVSCADI LTIASQISVL LSGGPSWAVP
LGRRDSVEAF FDLANTALPS PFFTLAQLKK AFADVGLNRP SDLVALSGGH TFGRARCLFV
TARLYNFNGT NRPDPTLNPS YLADLRRLCP RNGNGTVLVN FDVMTPNTFD NQFYTNLRNG
KGLIQSDQEL FSTPGADTIP LVNLYSSNTL SFFGAFADAM IRMGNLRPLT GTQGEIRQNC
RVVNSR
