ID A0A0J8CS88_BETVV Unreviewed; 648 AA. AC A0A0J8CS88; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 27-MAR-2024, entry version 35. 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 -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|PIRSR:PIRSR600823-3}; CC Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR600823- CC 3}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000256|PIRSR:PIRSR600823-3}; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. CC {ECO:0000256|PIRSR:PIRSR600823-3}; CC -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase CC subfamily. {ECO:0000256|ARBA:ARBA00006873}. 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 AlphaFoldDB; A0A0J8CS88; -. DR EnsemblPlants; KMT16467; KMT16467; BVRB_3g050870. DR Gramene; KMT16467; KMT16467; BVRB_3g050870. DR eggNOG; ENOG502QPX7; Eukaryota. DR OMA; NEREWQE; -. DR Proteomes; UP000035740; Chromosome 3. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; 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 Gene3D; 1.10.520.10; -; 2. DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 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 PANTHER; PTHR31235:SF399; PEROXIDASE; 1. DR PANTHER; PTHR31235; PEROXIDASE 25-RELATED; 1. DR Pfam; PF00141; peroxidase; 2. DR PRINTS; PR00458; PEROXIDASE. DR PRINTS; PR00461; PLPEROXIDASE. DR SUPFAM; SSF48113; Heme-dependent peroxidases; 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="Plant heme peroxidase family profile" FT /evidence="ECO:0000259|PROSITE:PS50873" FT DOMAIN 335..636 FT /note="Plant heme peroxidase family profile" FT /evidence="ECO:0000259|PROSITE:PS50873" FT ACT_SITE 74 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1" FT BINDING 75 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 78 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 80 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 82 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 84 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 96 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 171 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-2" FT BINDING 201 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 202 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 254 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 262 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" 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 //