ID A0A0J8CS88_BETVV Unreviewed; 648 AA. AC A0A0J8CS88; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 29-SEP-2021, entry version 27. DE RecName: Full=Peroxidase {ECO:0000256|ARBA:ARBA00012313}; DE EC=1.11.1.7 {ECO:0000256|ARBA:ARBA00012313}; GN ORFNames=BVRB_3g050870 {ECO:0000313|EMBL:KMT16467.1}; OS Beta vulgaris subsp. vulgaris (Beet). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC Caryophyllales; Chenopodiaceae; Betoideae; 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., Zakrzewski F., RA Tafer H., Rupp O., Sorensen T.R., Stracke R., Reinhardt R., Goesmann A., RA Kraft T., Schulz B., Stadler P.F., Schmidt T., Gabaldon T., Lehrach H., RA 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: 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 -!- 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 STRING; 161934.XP_010671316.1; -. DR EnsemblPlants; KMT16467; KMT16467; BVRB_3g050870. DR Gramene; KMT16467; KMT16467; BVRB_3g050870. DR eggNOG; ENOG502QPX7; Eukaryota. 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:0042744; P:hydrogen peroxide catabolic process; IEA:InterPro. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR CDD; cd00693; secretory_peroxidase; 2. 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; 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 Calcium {ECO:0000256|PIRSR:PIRSR600823-3}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, KW ECO:0000256|PIRSR:PIRSR600823-5}; Heme {ECO:0000256|ARBA:ARBA00022617}; 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 Peroxidase {ECO:0000256|ARBA:ARBA00022559}; KW Reference proteome {ECO:0000313|Proteomes:UP000035740}. FT DOMAIN 33..334 FT /note="PEROXIDASE_4" FT /evidence="ECO:0000259|PROSITE:PS50873" FT DOMAIN 335..636 FT /note="PEROXIDASE_4" FT /evidence="ECO:0000259|PROSITE:PS50873" FT ACT_SITE 74 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1" FT METAL 75 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 78 FT /note="Calcium 1; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 80 FT /note="Calcium 1; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 82 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 84 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 96 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 201 FT /note="Iron (heme axial ligand)" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 202 FT /note="Calcium 2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 254 FT /note="Calcium 2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 262 FT /note="Calcium 2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 171 FT /note="Substrate; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-2" FT SITE 70 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-4" FT DISULFID 43..123 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 76..81 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 129..330 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 208..240 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" 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 //