ID A0A0J8CS88_BETVU Unreviewed; 648 AA. AC A0A0J8CS88; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 20-JAN-2016, entry version 4. DE RecName: Full=Peroxidase {ECO:0000256|SAAS:SAAS00371569}; DE EC=1.11.1.7 {ECO:0000256|SAAS:SAAS00371569}; GN ORFNames=BVRB_3g050870 {ECO:0000313|EMBL:KMT16467.1}; OS Beta vulgaris subsp. vulgaris. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; Caryophyllales; Amaranthaceae; Beta. OX NCBI_TaxID=3555 {ECO:0000313|EMBL:KMT16467.1, ECO:0000313|Proteomes:UP000035740}; RN [1] {ECO:0000313|EMBL:KMT16467.1, ECO:0000313|Proteomes:UP000035740} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Taproot {ECO:0000313|EMBL:KMT16467.1}; RX PubMed=24352233; DOI=10.1038/nature12817; RA Dohm J.C., Minoche A.E., Holtgrawe D., Capella-Gutierrez S., RA Zakrzewski F., Tafer H., Rupp O., Sorensen T.R., Stracke R., RA Reinhardt R., Goesmann A., Kraft T., Schulz B., Stadler P.F., RA Schmidt T., Gabaldon T., Lehrach H., Weisshaar B., Himmelbauer H.; RT "The genome of the recently domesticated crop plant sugar beet (Beta RT vulgaris)."; RL Nature 505:546-549(2014). CC -!- CATALYTIC ACTIVITY: 2 phenolic donor + H(2)O(2) = 2 phenoxyl CC radical of the donor + 2 H(2)O. {ECO:0000256|SAAS:SAAS00371875}. 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; KQ090056; KMT16467.1; -; Genomic_DNA. DR Proteomes; UP000035740; Chromosome 3. 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; 2. DR PRINTS; PR00458; PEROXIDASE. DR PRINTS; PR00461; PLPEROXIDASE. DR SUPFAM; SSF48113; SSF48113; 2. DR PROSITE; PS00435; PEROXIDASE_1; 2. DR PROSITE; PS00436; PEROXIDASE_2; 2. DR PROSITE; PS50873; PEROXIDASE_4; 2. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035740}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00064273}; 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}; KW Reference proteome {ECO:0000313|Proteomes:UP000035740}. FT DOMAIN 33 334 PEROXIDASE_4. {ECO:0000259|PROSITE: FT PS50873}. FT DOMAIN 335 636 PEROXIDASE_4. {ECO:0000259|PROSITE: FT PS50873}. SQ SEQUENCE 648 AA; 70093 MW; 919CE8A35B4DEDC2 CRC64; MSPIISKCHQ ISTTTIAFLS LILLSLSGFL KADLQPGFYM QSCPMAEFIV KDEVRQAFFS DRGYAAGLVR LHFHDCFVRG CDASVLLDST PGNAAEKDAE ANNPSLRGFD VIDNAKARLE NLCPGTVSCA DILAYAARDS VEMTGGFGYD VPGGRRDGRV SSSSEATRNL PPPFADVDLL TKIFGSKGLT QEEMVILSGA HTIGRSHCTS FSKRLYSFST TAAQDPSINS AYAAQLQRQC PAGNAGANIV VPMDPISPTI SDTAYYRNIL NNRGLFTSDQ ALLSDSTTAS LVTLYARNPG LWGRKFATAM GSMGQIGVLT GDEGEIRSNC RLEAQLRVGF YCNSCPLAER IVREEVMKGF MNDKGIAPGL VRMHFHDCFV RGCDGSVLID STSSNTAEKD SPANSPSLRG FEVIDNAKTR LESQCKGVVS CADILAFAAR DSVAITRGQS YNVPSGRRDG RVSSESEVLQ NLPGFSFNVD QLTQNFANKN LTQEEMVTLS GAHTLGRSHC TSVGSRLYNF NGTNGPDSTL ESKYAGQLQQ QCPEGSTDSS LVVSMDPQTP FVTDVNYYQD LLANRGLFTS DQTLLSNSNT ANEVNQNARN QFLWMRKFAA AMVKMGQIEV LTGNAGEIRA NFLTQNQLLL QANSHGNV //