ID F2DTV9_HORVD Unreviewed; 339 AA. AC F2DTV9; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 04-FEB-2015, entry version 15. DE RecName: Full=Peroxidase {ECO:0000256|SAAS:SAAS00129889}; DE EC=1.11.1.7 {ECO:0000256|SAAS:SAAS00129889}; OS Hordeum vulgare var. distichum (Domesticated barley). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Pooideae; Triticeae; Hordeum. OX NCBI_TaxID=112509 {ECO:0000313|EMBL:BAJ98530.1}; RN [1] {ECO:0000313|EMBL:BAJ98530.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Shoot and root {ECO:0000313|EMBL:BAJ98530.1}; RX PubMed=21415278; DOI=10.1104/pp.110.171579; RA Matsumoto T., Tanaka T., Sakai H., Amano N., Kanamori H., Kurita K., RA Kikuta A., Kamiya K., Yamamoto M., Ikawa H., Fujii N., Hori K., RA Itoh T., Sato K.; RT "Comprehensive sequence analysis of 24,783 barley full-length cDNAs RT derived from 12 clone libraries."; RL Plant Physiol. 156:20-28(2011). CC -!- CATALYTIC ACTIVITY: 2 phenolic donor + H(2)O(2) = 2 phenoxyl CC radical of the donor + 2 H(2)O. {ECO:0000256|SAAS:SAAS00129878}. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|SAAS:SAAS00177460}; CC Note=Binds 2 calcium ions per subunit. CC {ECO:0000256|SAAS:SAAS00177460}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000256|SAAS:SAAS00177461}; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per CC subunit. {ECO:0000256|SAAS:SAAS00177461}; CC -!- SIMILARITY: Belongs to the peroxidase family. CC {ECO:0000256|RuleBase:RU004241}. 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 EMBL; AK367327; BAJ98530.1; -; mRNA. DR ExpressionAtlas; F2DTV9; baseline. 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; IEA:UniProtKB-KW. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR InterPro; IPR010255; Haem_peroxidase. 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 SUPFAM; SSF48113; SSF48113; 1. 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 Disulfide bond {ECO:0000256|SAAS:SAAS00129890}; KW Heme {ECO:0000256|SAAS:SAAS00129880}; KW Iron {ECO:0000256|SAAS:SAAS00129897}; KW Metal-binding {ECO:0000256|SAAS:SAAS00129877}; KW Oxidoreductase {ECO:0000256|SAAS:SAAS00129893}; KW Peroxidase {ECO:0000256|SAAS:SAAS00129885}. SQ SEQUENCE 339 AA; 36681 MW; E85AA852F55F1762 CRC64; MAKVDAGAAL LCLCLLLACS AGATRAAYVD VEGTVRTEVE KAIKSNPGIG AALVRLVFHD CWVNGCDGSV LLDKTPSGTN TEKKAINNIG LDGFSLIDTI KYKLGDSVSC ADIVVFAARD AARYLSGGKI AYSVPSGRKD GIVSSAVAAD AILPQSTFEF QQLKDNFANK GFTQEELVIL SGAHSIGVSH LSSFQDRLND TTATPIDDNY KQALIHDVEA LKKSQNTSDP IEKNNIRDMS SSFQTTAGYD PTGVNTAAKG ALDNSYYHAN LQNRVLFKSD WVMRTDSDAA DDLTKYMDNA TKWNNDFAAA MIKLSKLPAE GSTRYEIRKN CRVINNKYY //