ID F2DTV9_HORVV Unreviewed; 339 AA. AC F2DTV9; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 13-NOV-2019, entry version 38. DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS01215714}; DE EC=1.11.1.7 {ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS01215714}; 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|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 -!- 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. CC {ECO:0000256|RuleBase:RU362060}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + CC 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; CC EC=1.11.1.7; Evidence={ECO:0000256|RuleBase:RU362060, CC ECO:0000256|SAAS:SAAS01215718}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU362060}. CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant CC (class III) peroxidase subfamily. {ECO:0000256|RuleBase:RU362060, CC ECO:0000256|SAAS:SAAS01215721}. 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 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; IPR019794; Peroxidases_AS. DR InterPro; IPR019793; Peroxidases_heam-ligand_BS. DR InterPro; IPR033905; Secretory_peroxidase. 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 Calcium {ECO:0000256|PIRSR:PIRSR600823-3, KW ECO:0000256|RuleBase:RU362060}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00449210}; KW Heme {ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS01215736}; KW Hydrogen peroxide {ECO:0000256|RuleBase:RU362060}; KW Iron {ECO:0000256|PIRSR:PIRSR600823-3, ECO:0000256|RuleBase:RU362060, KW ECO:0000256|SAAS:SAAS01215715}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR600823-3, KW ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS01215733}; KW Oxidoreductase {ECO:0000256|RuleBase:RU362060, KW ECO:0000256|SAAS:SAAS01215720}; KW Peroxidase {ECO:0000256|RuleBase:RU362060, KW ECO:0000256|SAAS:SAAS01215725}; KW Secreted {ECO:0000256|RuleBase:RU362060}; KW Signal {ECO:0000256|RuleBase:RU362060}. FT SIGNAL 1 26 {ECO:0000256|RuleBase:RU362060}. FT CHAIN 27 339 Peroxidase. {ECO:0000256|RuleBase: FT RU362060}. FT /FTId=PRO_5005129126. FT DOMAIN 30 335 PEROXIDASE_4. {ECO:0000259|PROSITE: FT PS50873}. FT ACT_SITE 59 59 Proton acceptor. {ECO:0000256|PIRSR: FT PIRSR600823-1}. FT METAL 60 60 Calcium 1. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT METAL 63 63 Calcium 1; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR600823-3}. FT METAL 65 65 Calcium 1; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR600823-3}. FT METAL 67 67 Calcium 1. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT METAL 69 69 Calcium 1. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT METAL 82 82 Calcium 1. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT METAL 184 184 Iron (heme axial ligand). FT {ECO:0000256|PIRSR:PIRSR600823-3}. FT METAL 250 250 Calcium 2. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT METAL 263 263 Calcium 2. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT BINDING 154 154 Substrate; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR600823-2}. FT SITE 55 55 Transition state stabilizer. FT {ECO:0000256|PIRSR:PIRSR600823-4}. 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 //