ID   PER1_HORVU              Reviewed;         315 AA.
AC   P27337;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-NOV-2008, entry version 65.
DE   RecName: Full=Peroxidase 1;
DE            EC=1.11.1.7;
DE   Flags: Precursor;
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. Pallas / P-01; TISSUE=Seedling 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   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- SIMILARITY: Belongs to the peroxidase family. Classical plant
CC       (class III) peroxidase subfamily.
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DR   EMBL; X58396; CAA41294.1; -; mRNA.
DR   PIR; S14611; S14611.
DR   PIR; T06164; T06164.
DR   UniGene; Hv.23479; -.
DR   HSSP; P22195; 1SCH.
DR   PeroxiBase; 69; HVPEROXI.
DR   Gramene; P27337; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
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   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00458; PEROXIDASE.
DR   PRINTS; PR00461; PLPEROXIDASE.
DR   PROSITE; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW   Oxidoreductase; Peroxidase; Pyrrolidone carboxylic acid; Secreted;
KW   Signal.
FT   SIGNAL        1     21       Potential.
FT   CHAIN        22    315       Peroxidase 1.
FT                                /FTId=PRO_0000023748.
FT   ACT_SITE     63     63       Proton acceptor (By similarity).
FT   METAL        64     64       Calcium 1 (By similarity).
FT   METAL        67     67       Calcium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        69     69       Calcium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        71     71       Calcium 1 (By similarity).
FT   METAL        73     73       Calcium 1 (By similarity).
FT   METAL       186    186       Iron (heme axial ligand) (By similarity).
FT   METAL       187    187       Calcium 2 (By similarity).
FT   METAL       234    234       Calcium 2 (By similarity).
FT   METAL       237    237       Calcium 2 (By similarity).
FT   METAL       242    242       Calcium 2 (By similarity).
FT   BINDING     155    155       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   SITE         59     59       Transition state stabilizer (By
FT                                similarity).
FT   MOD_RES      22     22       Pyrrolidone carboxylic acid (By
FT                                similarity).
FT   CARBOHYD    158    158       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    265    265       N-linked (GlcNAc...) (Potential).
FT   DISULFID     32    107       By similarity.
FT   DISULFID     65     70       By similarity.
FT   DISULFID    113    310       By similarity.
FT   DISULFID    193    219       By similarity.
SQ   SEQUENCE   315 AA;  32976 MW;  4867179BD0296172 CRC64;
     MASSSYTSLL VLVALVTAAS AQLSPTFYDT SCPRALATIK SGVMAAVTSD PRMGASLLRL
     HFHDCFVQGC DASVLLSGME QNAIPNAGSL RGFGVIDSIK TQIEAICKQT VSCADILTVA
     ARDSVVALGG PSWTVPLGRR DSIDANENEA NTDLPGFNSS RAELEAAFLK KGGLNTVDMV
     ALSGAHTIGQ AQCSTFRARI YGGDTNINAA YAASLRANCP QTVGSGDGSL ANLDTTTANT
     FDNAYYTNLM SQKGLLHSDQ VLFNNDTTDN TVRNFASNPA AFSSSFTTAM IKMGNIAPKT
     GTQGQIRLSC SRVNS
//