PER15_IPOBA
ID PER15_IPOBA Reviewed; 327 AA.
AC Q9LEH3;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Peroxidase 15 {ECO:0000303|PubMed:17936696};
DE Short=Prx15 {ECO:0000303|PubMed:17936696};
DE EC=1.11.1.7;
DE AltName: Full=Anionic peroxidase {ECO:0000303|PubMed:17936696};
DE Flags: Precursor;
GN Name=pod {ECO:0000312|EMBL:CAB94692.1};
OS Ipomoea batatas (Sweet potato) (Convolvulus batatas).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX NCBI_TaxID=4120;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAB94692.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 89-98; 131-163 AND 303-327,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND MASS
RP SPECTROMETRY.
RC TISSUE=Tuber {ECO:0000269|PubMed:17936696};
RX PubMed=17936696; DOI=10.1016/j.bbapap.2007.08.013;
RA Rompel A., Albers M., Naseri J.I., Gerdemann C.,
RA Bueldt-Karentzopoulos K.B., Jasper B., Krebs B.;
RT "Purification, cloning and characterization of a novel peroxidase isozyme
RT from sweetpotatoes (Ipomoea batatas).";
RL Biochim. Biophys. Acta 1774:1422-1430(2007).
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. {ECO:0000305}.
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 Evidence={ECO:0000269|PubMed:17936696};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q42578,
CC ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:Q42578,
CC ECO:0000255|PROSITE-ProRule:PRU00297};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:Q42578,
CC ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:17936696};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297,
CC ECO:0000269|PubMed:17936696};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=408 nm {ECO:0000269|PubMed:17936696};
CC Note=Exhibits smaller absorbance peaks at 497 and 635 nm. After
CC treatment with stoichiometric amounts of hydrogen peroxide the
CC absorption maximum is shifed to 400 nm.
CC {ECO:0000269|PubMed:17936696};
CC pH dependence:
CC Optimum pH is 5.5. Retains more than 50% of activity between pH 4 and
CC 7. {ECO:0000269|PubMed:17936696};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q42578,
CC ECO:0000255|PROSITE-ProRule:PRU00297}.
CC -!- MASS SPECTROMETRY: Mass=42029; Method=MALDI; Note=The measured mass is
CC that of the phosphorylated and glycosylated protein.;
CC Evidence={ECO:0000269|PubMed:17936696};
CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class
CC III) peroxidase subfamily. {ECO:0000255|PROSITE-ProRule:PRU00297}.
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DR EMBL; AJ242742; CAB94692.1; -; mRNA.
DR AlphaFoldDB; Q9LEH3; -.
DR SMR; Q9LEH3; -.
DR PeroxiBase; 296; IbPrx15.
DR PRIDE; Q9LEH3; -.
DR BRENDA; 1.11.1.7; 2773.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IDA:UniProtKB.
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; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..327
FT /note="Peroxidase 15"
FT /id="PRO_5000065280"
FT ACT_SITE 65
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q42578,
FT ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000255|PROSITE-
FT ProRule:PRU10012"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q42578,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q42578,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q42578,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q42578,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q42578,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q42578,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 193
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:0000250|UniProtKB:P00433,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q42578,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q42578,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q42578,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q42578,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT SITE 61
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q42578,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT MOD_RES 24
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:Q42578,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..115
FT /evidence="ECO:0000250|UniProtKB:P00433,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 67..72
FT /evidence="ECO:0000250|UniProtKB:P00433,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 121..323
FT /evidence="ECO:0000250|UniProtKB:P00433,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 200..232
FT /evidence="ECO:0000250|UniProtKB:P00433,
FT ECO:0000255|PROSITE-ProRule:PRU00297"
SQ SEQUENCE 327 AA; 34956 MW; EF7F54274B5505CA CRC64;
MASFSPLLAM ALAIFIFSSH SNAQLSSTFY STTCPNVSAI VRTVVQQALQ NDARIGGSLI
RLHFHDCFVD GCDGSLLLDN NGTTIVSEKD ALPNTNSTRG FDVVDNIKTA VENACPGVVS
CVDILALASE SSVSLAGGPS WNVLLGRRDR RTANQGGANT SLPSPFENLT NLTQKFTNVG
LNVNDLVALS GAHTFGRAQC RTFSPRLFNF SNTGNPDPTL NTTYLATLQQ ICPQGGSGFT
VTNLDPTTPD TFDNNYFSNL QTNRGLLQSD QELFSTSGAP TIAIVNNFSA NQTAFFESFV
QSMINMGNIS PLTGSNGEIR SNCRRPN
