ID   A0A8I6WSH2_HORVV        Unreviewed;       323 AA.
AC   A0A8I6WSH2;
DT   25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 1.
DT   14-DEC-2022, entry version 4.
DE   RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU362060};
DE            EC=1.11.1.7 {ECO:0000256|RuleBase:RU362060};
OS   Hordeum vulgare subsp. vulgare (Domesticated barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=112509 {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.2HG0157410.1, ECO:0000313|Proteomes:UP000011116};
RN   [1] {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.2HG0157410.1, ECO:0000313|Proteomes:UP000011116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Morex
RC   {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.2HG0157410.1,
RC   ECO:0000313|Proteomes:UP000011116};
RX   PubMed=23075845; DOI=10.1038/nature11543;
RG   The International Barley Genome Sequencing Consortium;
RA   Mayer K.F., Waugh R., Brown J.W., Schulman A., Langridge P., Platzer M.,
RA   Fincher G.B., Muehlbauer G.J., Sato K., Close T.J., Wise R.P., Stein N.;
RT   "A physical, genetic and functional sequence assembly of the barley
RT   genome.";
RL   Nature 491:711-716(2012).
RN   [2] {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.2HG0157410.1}
RP   IDENTIFICATION.
RC   STRAIN=subsp. vulgare
RC   {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.2HG0157410.1};
RG   EnsemblPlants;
RL   Submitted (JAN-2022) to UniProtKB.
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. {ECO:0000256|RuleBase:RU362060}.
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:0000256|ARBA:ARBA00000189,
CC         ECO:0000256|RuleBase:RU362060};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR600823-3,
CC         ECO:0000256|RuleBase:RU362060};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR600823-
CC       3, ECO:0000256|RuleBase:RU362060};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|PIRSR:PIRSR600823-3,
CC         ECO:0000256|RuleBase:RU362060};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC       {ECO:0000256|PIRSR:PIRSR600823-3, ECO:0000256|RuleBase:RU362060};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU362060}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase
CC       subfamily. {ECO:0000256|ARBA:ARBA00006873}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class
CC       III) peroxidase subfamily. {ECO:0000256|RuleBase:RU362060}.
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DR   EnsemblPlants; HORVU.MOREX.r3.2HG0157410.1; HORVU.MOREX.r3.2HG0157410.1; HORVU.MOREX.r3.2HG0157410.
DR   Gramene; HORVU.MOREX.r3.2HG0157410.1; HORVU.MOREX.r3.2HG0157410.1; HORVU.MOREX.r3.2HG0157410.
DR   Proteomes; UP000011116; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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:0006979; P:response to oxidative stress; IEA:UniProtKB-UniRule.
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; PEROXIDASE 25-RELATED; 1.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00458; PEROXIDASE.
DR   PRINTS; PR00461; PLPEROXIDASE.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR600823-3};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR600823-5};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU362060};
KW   Hydrogen peroxide {ECO:0000256|RuleBase:RU362060};
KW   Iron {ECO:0000256|PIRSR:PIRSR600823-3, ECO:0000256|RuleBase:RU362060};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR600823-3,
KW   ECO:0000256|RuleBase:RU362060};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362060};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU362060};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011116};
KW   Secreted {ECO:0000256|RuleBase:RU362060};
KW   Signal {ECO:0000256|RuleBase:RU362060}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|RuleBase:RU362060"
FT   CHAIN           23..323
FT                   /note="Peroxidase"
FT                   /evidence="ECO:0000256|RuleBase:RU362060"
FT                   /id="PRO_5035340568"
FT   DOMAIN          23..322
FT                   /note="PEROXIDASE_4"
FT                   /evidence="ECO:0000259|PROSITE:PS50873"
FT   ACT_SITE        64
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-1"
FT   BINDING         65
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         68
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         70
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         72
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         74
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         85
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-2"
FT   BINDING         189
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:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         190
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         240
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         243
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   BINDING         248
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-3"
FT   SITE            60
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-4"
FT   DISULFID        33..111
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT   DISULFID        66..71
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT   DISULFID        117..318
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
FT   DISULFID        196..228
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600823-5"
SQ   SEQUENCE   323 AA;  34870 MW;  1DD7B7709B76412F CRC64;
     MATASFLILV AAASLLASFA QADLQYGYYN TTCPGVEELV RTELEAIFAD DSTLRAGLLR
     LHFHDCFVLG CDASLMLNSH NGTAEKHADP NLTVRGYEAI EAIKKVVEKA CPLVVSCADI
     MAMAARDAVN LSAGPYYEVE TGRRDGNISK LVEALTNLPP ADGNVTVLTQ YFAVKNLTMK
     DMVVLSAAHT IGVTHCSSFS KRLYNFTGAG DQDPSLDPAY GKTLRTKCPT DKMASVVPMD
     DVTVDKFDQG YYESVYNHRA VLRSDAALLD DSLTGAYVAL MNNASSFDIF FADFAVAMIN
     MGRVGVLTGT QGEIRETCGV YVD
//