ID F2DTV9_HORVV Unreviewed; 339 AA. AC F2DTV9; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 29-SEP-2021, entry version 44. DE RecName: Full=Peroxidase {ECO:0000256|ARBA:ARBA00012313, ECO:0000256|RuleBase:RU362060}; DE EC=1.11.1.7 {ECO:0000256|ARBA:ARBA00012313, 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|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., Itoh T., RA Sato K.; RT "Comprehensive sequence analysis of 24,783 barley full-length cDNAs derived RT 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 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU362060}. 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 EMBL; AK367327; BAJ98530.1; -; mRNA. DR OMA; NKVLFKS; -. 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|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR600823-3}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, KW ECO:0000256|PIRSR:PIRSR600823-5}; KW Heme {ECO:0000256|ARBA:ARBA00022617, 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|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU362060}; KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU362060}; KW Pyrrolidone carboxylic acid {ECO:0000256|ARBA:ARBA00023283}; KW Secreted {ECO:0000256|RuleBase:RU362060}; KW Signal {ECO:0000256|RuleBase:RU362060}. FT SIGNAL 1..26 FT /evidence="ECO:0000256|RuleBase:RU362060" FT CHAIN 27..339 FT /note="Peroxidase" FT /evidence="ECO:0000256|RuleBase:RU362060" FT /id="PRO_5005129126" FT DOMAIN 30..335 FT /note="PEROXIDASE_4" FT /evidence="ECO:0000259|PROSITE:PS50873" FT ACT_SITE 59 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1" FT METAL 60 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 63 FT /note="Calcium 1; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 65 FT /note="Calcium 1; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 67 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 69 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 82 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 184 FT /note="Iron (heme axial ligand)" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 250 FT /note="Calcium 2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 263 FT /note="Calcium 2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 154 FT /note="Substrate; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-2" FT SITE 55 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-4" FT DISULFID 61..66 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 110..331 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" 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 //