ID A0A8I6WSH2_HORVV Unreviewed; 323 AA. AC A0A8I6WSH2; DT 25-MAY-2022, integrated into UniProtKB/TrEMBL. DT 25-MAY-2022, sequence version 1. DT 24-JUL-2024, entry version 12. 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|Proteomes:UP000011116} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Morex {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. These functions might be dependent on each CC isozyme/isoform in each plant tissue. {ECO:0000256|ARBA:ARBA00002322}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 OMA; GMSHCNS; -. DR Proteomes; UP000011116; Chromosome 2H. 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 Gene3D; 1.10.520.10; -; 1. DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 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:SF41; PEROXIDASE; 1. 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|RuleBase:RU362060}; KW Hydrogen peroxide {ECO:0000256|RuleBase:RU362060}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR600823-3}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR600823-3}; KW Oxidoreductase {ECO:0000256|RuleBase:RU362060}; KW Peroxidase {ECO:0000256|RuleBase:RU362060}; KW Pyrrolidone carboxylic acid {ECO:0000256|ARBA:ARBA00023283}; 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="Plant heme peroxidase family profile" 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 //