ID A0A078I7F1_BRANA Unreviewed; 326 AA. AC A0A078I7F1; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 12-AUG-2020, entry version 29. 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}; GN Name=BnaA10g03290D {ECO:0000313|EMBL:CDY46845.1}; GN ORFNames=GSBRNA2T00086290001 {ECO:0000313|EMBL:CDY46845.1}; OS Brassica napus (Rape). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica. OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY46845.1, ECO:0000313|Proteomes:UP000028999}; RN [1] {ECO:0000313|EMBL:CDY46845.1, ECO:0000313|Proteomes:UP000028999} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999}; RX PubMed=25146293; DOI=10.1126/science.1253435; RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J., RA Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J., RA Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B., RA Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C., RA Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D., RA Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V., RA Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q., RA Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H., RA Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z., RA Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J., RA Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M., RA Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W., RA Sharpe A.G., Paterson A.H., Guan C., Wincker P.; RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic RT Brassica napus oilseed genome."; RL Science 345:950-953(2014). 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; LK032687; CDY46845.1; -; Genomic_DNA. DR EnsemblPlants; CDY46845; CDY46845; GSBRNA2T00086290001. DR Gramene; CDY46845; CDY46845; GSBRNA2T00086290001. DR OMA; EFANSME; -. DR Proteomes; UP000028999; Unassembled WGS sequence. 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 3: Inferred from homology; KW Calcium {ECO:0000256|PIRSR:PIRSR600823-3, ECO:0000256|RuleBase:RU362060}; 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 ECO:0000256|RuleBase:RU362060}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR600823-3, ECO:0000256|RuleBase:RU362060}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU362060}; KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU362060}; KW Reference proteome {ECO:0000313|Proteomes:UP000028999}; KW Secreted {ECO:0000256|RuleBase:RU362060}; KW Signal {ECO:0000256|RuleBase:RU362060}. FT SIGNAL 1..24 FT /evidence="ECO:0000256|RuleBase:RU362060" FT CHAIN 25..326 FT /note="Peroxidase" FT /evidence="ECO:0000256|RuleBase:RU362060" FT /id="PRO_5005105599" FT DOMAIN 25..325 FT /note="PEROXIDASE_4" FT /evidence="ECO:0000259|PROSITE:PS50873" FT ACT_SITE 66 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1" FT METAL 67 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 70 FT /note="Calcium 1; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 72 FT /note="Calcium 1; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 74 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 76 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 87 FT /note="Calcium 1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 191 FT /note="Iron (heme axial ligand)" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 192 FT /note="Calcium 2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 244 FT /note="Calcium 2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT METAL 252 FT /note="Calcium 2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 161 FT /note="Substrate; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-2" FT SITE 62 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-4" FT DISULFID 35..113 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 68..73 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 119..321 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" FT DISULFID 198..231 FT /evidence="ECO:0000256|PIRSR:PIRSR600823-5" SQ SEQUENCE 326 AA; 35052 MW; AB2C3426E2B27733 CRC64; MRCLTTVALS LSLFLVGLVG PIQAQLQMNF YANTCPNAEK IVQDFVSNHI SNAPSLAAAL LRMHFHDCFV RGCDGSVLIN STSGNAEKDA APNLTVRGFG FIEAIKAVLE AQCPGIVSCA DIIALASRDA IVFTGGPNWS VPTGRRDGRI SNASEALANI PPPTSNFTNL QTLFANQGLD LKDLVLLSGA HTIGVSHCSS FTNRLYNFTG RGDQDPALDS EYAANLKSRK CPSLKDNTTI VEMDPGSRKT FDLSYYQLLL KRRGLFQSDS ALTTNPTTLS NINQILKGSV EGFFSEFAKS MEKMGRINVK TGSSGVVRKQ CSVANS //