ID   PER2_HORVU              Reviewed;         170 AA.
AC   Q01548;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   16-JUN-2009, entry version 61.
DE   RecName: Full=Peroxidase 2;
DE            EC=1.11.1.7;
DE   Flags: Fragment;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Pooideae; Triticeae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Carina; TISSUE=Leaf;
RX   AGRICOLA=IND93004675; DOI=10.1016/0885-5765(92)90031-P;
RA   Thordal-Christensen H., Brandt J., Cho B.H., Rasmussen S.K.,
RA   Gregersen P.L., Smedegaard-Petersen V., Collinge D.B.;
RT   "cDNA cloning and characterization of two barley peroxidase
RT   transcripts induced differentially by the powdery mildew fungus
RT   Erysiphe graminis.";
RL   Physiol. Mol. Plant Pathol. 40:395-409(1992).
CC   -!- FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants,
CC       biosynthesis and degradation of lignin, suberization, auxin
CC       catabolism, response to environmental stresses such as wounding,
CC       pathogen attack and oxidative stress. These functions might be
CC       dependent on each isozyme/isoform in each plant tissue.
CC   -!- FUNCTION: Involved in defense response to powdery meldew fungus.
CC   -!- CATALYTIC ACTIVITY: Donor + H(2)O(2) = oxidized donor + 2 H(2)O.
CC   -!- COFACTOR: Binds 2 calcium ions per subunit.
CC   -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per
CC       subunit.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Classical plant
CC       (class III) peroxidase subfamily.
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DR   EMBL; X62438; CAA44304.1; -; mRNA.
DR   PIR; S18064; S18064.
DR   HSSP; P22195; 1SCH.
DR   Gramene; Q01548; -.
DR   BRENDA; 1.11.1.7; 283.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
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:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
DR   InterPro; IPR000823; Peroxidase_pln.
DR   InterPro; IPR019794; Peroxidases_AS.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00458; PEROXIDASE.
DR   PRINTS; PR00461; PLPEROXIDASE.
DR   PROSITE; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS00436; PEROXIDASE_2; PARTIAL.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron;
KW   Metal-binding; Oxidoreductase; Peroxidase.
FT   CHAIN        <1    170       Peroxidase 2.
FT                                /FTId=PRO_0000055607.
FT   METAL        24     24       Iron (heme axial ligand) (By similarity).
FT   METAL        25     25       Calcium 2 (By similarity).
FT   METAL        73     73       Calcium 2 (By similarity).
FT   METAL        76     76       Calcium 2 (By similarity).
FT   METAL        81     81       Calcium 2 (By similarity).
FT   CARBOHYD      9      9       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     63     63       N-linked (GlcNAc...) (Potential).
FT   DISULFID     31     59       By similarity.
FT   NON_TER       1      1
SQ   SEQUENCE   170 AA;  18882 MW;  E64B2C012157732B CRC64;
     STLISSFANR SLDVADLVSL SGAHTFGVAH CPAFEDRSSR VRHNPAIDGK FATALRNKCS
     GDNPSGTLTQ KLDVRTPDVF DNKYYFDLIA RQGLFKSDQG LIDHPTTKRM ATRFSLNQGA
     FFEQFARSMT KMSNMDILTG TKGEIRNNCA VPNRRVRTSR PPSPARGDRR
//