PER1_MAIZE
ID PER1_MAIZE Reviewed; 367 AA.
AC A5H8G4; Q9FEQ9;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Peroxidase 1;
DE EC=1.11.1.7;
DE AltName: Full=Plasma membrane-bound peroxidase 1;
DE Short=pmPOX1;
DE Flags: Precursor;
GN Name=PER1; Synonyms=POX1, PRX1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Wisconsin 64A;
RX PubMed=12727355; DOI=10.1016/s0378-1119(03)00462-1;
RA de Obeso M., Caparros-Ruiz D., Vignols F., Puigdomenech P., Rigau J.;
RT "Characterisation of maize peroxidases having differential patterns of mRNA
RT accumulation in relation to lignifying tissues.";
RL Gene 309:23-33(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Wisconsin 22;
RX PubMed=18603027; DOI=10.1016/j.jprot.2008.06.006;
RA Mika A., Buck F., Luethje S.;
RT "Membrane-bound class III peroxidases: identification, biochemical
RT properties and sequence analysis of isoenzymes purified from maize (Zea
RT mays L.) roots.";
RL J. Proteomics 71:412-424(2008).
RN [3]
RP FUNCTION.
RX PubMed=12857829; DOI=10.1104/pp.103.020396;
RA Mika A., Luethje S.;
RT "Properties of guaiacol peroxidase activities isolated from corn root
RT plasma membranes.";
RL Plant Physiol. 132:1489-1498(2003).
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:0000255|PROSITE-
CC ProRule:PRU00297, ECO:0000269|PubMed:12857829}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=61.9 umol/min/mg enzyme with guaiacol as substrate
CC {ECO:0000269|PubMed:18603027};
CC Note=In the presence of H(2)O(2).;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Vacuole {ECO:0000305}.
CC Note=Carboxy-terminal extension appears to target the protein to
CC vacuoles.
CC -!- TISSUE SPECIFICITY: Expressed in the root tip meristems.
CC {ECO:0000269|PubMed:12727355}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class
CC III) peroxidase subfamily. {ECO:0000255|PROSITE-ProRule:PRU00297}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC21391.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ401274; CAC21391.1; ALT_FRAME; mRNA.
DR EMBL; EF178277; ABN48856.1; -; mRNA.
DR RefSeq; NP_001105144.1; NM_001111674.1.
DR AlphaFoldDB; A5H8G4; -.
DR SMR; A5H8G4; -.
DR STRING; 4577.GRMZM2G104394_P01; -.
DR PeroxiBase; 17; ZmPrx01_W64A.
DR PeroxiBase; 739; ZmPrx01_lineC.
DR PaxDb; A5H8G4; -.
DR PRIDE; A5H8G4; -.
DR GeneID; 542029; -.
DR KEGG; zma:542029; -.
DR eggNOG; ENOG502QPX7; Eukaryota.
DR OrthoDB; 902776at2759; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; A5H8G4; baseline and differential.
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: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; 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; IPR019794; Peroxidases_AS.
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; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal; Vacuole.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..367
FT /note="Peroxidase 1"
FT /id="PRO_0000359402"
FT ACT_SITE 75
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
FT BINDING 76
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 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 202
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 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT SITE 71
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT MOD_RES 34
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 77..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 131..335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT DISULFID 209..244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT CONFLICT 274..278
FT /note="LPRGM -> PASRH (in Ref. 1; CAC21391)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="Q -> P (in Ref. 1; CAC21391)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="L -> S (in Ref. 1; CAC21391)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 38355 MW; DAAD080D7B959A63 CRC64;
MAKESKLTAG VAAALTVVAA CALCLLLPAT ARAQLRVGFY DTSCPNAEAL VRQAVAAAFA
KDAGIAAGLI RLHFHDCFVR GCDGSVLLTV NPGGGQTERD ALPNNPSLRG FDVIDAAKTA
VEQSCPRTVS CADIVAFAAR DSISLTGSVS YQVPAGRRDG RVSNATETVD LPPPTSTAQS
LTDLFKAKEL SVEDMVVLSG AHTVGRSFCA SFFKRVWNTS TNPATAIVDA GLSPSYAQLL
RALCPSNTTQ TTPITTAMDP GTPNVLDNNY YKLLPRGMGL FFSDNQLRVN PQMAALVSSF
ASNETLWKEK FAAAMVKMGR IQVQTGTCGE VRLNCGVVNP SLYSSSSAVE LGSSAPAAVG
EEGYAAS
