PER18_ARATH
ID PER18_ARATH Reviewed; 329 AA.
AC Q9SK52;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Peroxidase 18;
DE Short=Atperox P18;
DE EC=1.11.1.7;
DE Flags: Precursor;
GN Name=PER18; Synonyms=P18; OrderedLocusNames=At2g24800; ORFNames=F27C12.28;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=12034502; DOI=10.1016/s0378-1119(02)00465-1;
RA Tognolli M., Penel C., Greppin H., Simon P.;
RT "Analysis and expression of the class III peroxidase large gene family in
RT Arabidopsis thaliana.";
RL Gene 288:129-138(2002).
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=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00297};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00297};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
CC -!- MISCELLANEOUS: There are 73 peroxidase genes in A.thaliana.
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; AC006585; AAD23032.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07630.1; -; Genomic_DNA.
DR PIR; F84640; F84640.
DR RefSeq; NP_180053.1; NM_128039.2.
DR AlphaFoldDB; Q9SK52; -.
DR SMR; Q9SK52; -.
DR BioGRID; 2369; 1.
DR STRING; 3702.AT2G24800.1; -.
DR PeroxiBase; 99; AtPrx18.
DR PaxDb; Q9SK52; -.
DR PRIDE; Q9SK52; -.
DR EnsemblPlants; AT2G24800.1; AT2G24800.1; AT2G24800.
DR GeneID; 817017; -.
DR Gramene; AT2G24800.1; AT2G24800.1; AT2G24800.
DR KEGG; ath:AT2G24800; -.
DR Araport; AT2G24800; -.
DR TAIR; locus:2047380; AT2G24800.
DR eggNOG; ENOG502QT3T; Eukaryota.
DR HOGENOM; CLU_010543_0_3_1; -.
DR InParanoid; Q9SK52; -.
DR OMA; SAHCGAF; -.
DR OrthoDB; 902776at2759; -.
DR PhylomeDB; Q9SK52; -.
DR BioCyc; ARA:AT2G24800-MON; -.
DR PRO; PR:Q9SK52; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SK52; baseline and differential.
DR Genevisible; Q9SK52; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; IBA:GO_Central.
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; IBA:GO_Central.
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; IPR019793; Peroxidases_heam-ligand_BS.
DR InterPro; IPR033905; Secretory_peroxidase.
DR PANTHER; PTHR31235; PTHR31235; 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; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Calcium; Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..329
FT /note="Peroxidase 18"
FT /id="PRO_0000023684"
FT ACT_SITE 71
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="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:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 194
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 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT SITE 67
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 73..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 122..325
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 201..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ SEQUENCE 329 AA; 35641 MW; DF56B4DCCBD82885 CRC64;
MALQFFSCKP KYTFLSSLLL LLLLSSSVAE LSFNFYAGSC PGAELIVRNT VRSASSSDPS
VLGKLLRLIF HDCFVQGCDG SVLIRGNGTE RSDPGNASLG GFAVIESVKN ILEIFCPGTV
SCADILVLAA RDAVEALGGP VVPIPTGRRD GRVSMAANVR PNIIDTDFTV DKMINIFSSK
GLSVHDLVVL SGAHTIGAAH CNTFNSRFKL DPKGNLELID ASLDNSYAQT LVNKCSSSLD
PTTTVVDNDP ETSSTFDNQY YKNLLAHKGL FQTDSALMED DRTRKIVEIL ANDQESFFDR
WTESFLKMSL MGVRVGEEGE IRRSCSAVN
