ID A0A078I7F1_BRANA Unreviewed; 326 AA. AC A0A078I7F1; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 13-NOV-2019, entry version 26. DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS01215714}; DE EC=1.11.1.7 {ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS01215714}; 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; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae; OC 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., RA Chiquet J., Belcram H., Tong C., Samans B., Correa M., Da Silva C., RA Just J., Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., RA Noel B., Labadie K., Alberti A., Charles M., Arnaud D., Guo H., RA Daviaud C., Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., RA Tack D., Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., RA Renault V., Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., RA Chalabi S., Hu Q., Fan C., Tollenaere R., Lu Y., Battail C., Shen J., RA Sidebottom C.H., Wang X., Canaguier A., Chauveau A., Berard A., RA Deniot G., Guan M., Liu Z., Sun F., Lim Y.P., Lyons E., Town C.D., RA Bancroft I., Wang X., Meng J., Ma J., Pires J.C., King G.J., RA Brunel D., Delourme R., Renard M., Aury J.M., Adams K.L., Batley J., RA Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W., Sharpe A.G., RA 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 CC catabolism, response to environmental stresses such as wounding, CC pathogen attack and oxidative stress. CC {ECO:0000256|RuleBase:RU362060}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + CC 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; CC EC=1.11.1.7; Evidence={ECO:0000256|RuleBase:RU362060, CC ECO:0000256|SAAS:SAAS01215718}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU362060}. CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant CC (class III) peroxidase subfamily. {ECO:0000256|RuleBase:RU362060, CC ECO:0000256|SAAS:SAAS01215721}. 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, KW ECO:0000256|RuleBase:RU362060}; KW Complete proteome {ECO:0000313|Proteomes:UP000028999}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00449210}; KW Heme {ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS01215736}; KW Hydrogen peroxide {ECO:0000256|RuleBase:RU362060}; KW Iron {ECO:0000256|PIRSR:PIRSR600823-3, ECO:0000256|RuleBase:RU362060, KW ECO:0000256|SAAS:SAAS01215715}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR600823-3, KW ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS01215733}; KW Oxidoreductase {ECO:0000256|RuleBase:RU362060, KW ECO:0000256|SAAS:SAAS01215720}; KW Peroxidase {ECO:0000256|RuleBase:RU362060, KW ECO:0000256|SAAS:SAAS01215725}; KW Reference proteome {ECO:0000313|Proteomes:UP000028999}; KW Secreted {ECO:0000256|RuleBase:RU362060}; KW Signal {ECO:0000256|RuleBase:RU362060}. FT SIGNAL 1 24 {ECO:0000256|RuleBase:RU362060}. FT CHAIN 25 326 Peroxidase. {ECO:0000256|RuleBase: FT RU362060}. FT /FTId=PRO_5005105599. FT DOMAIN 25 325 PEROXIDASE_4. {ECO:0000259|PROSITE: FT PS50873}. FT ACT_SITE 66 66 Proton acceptor. {ECO:0000256|PIRSR: FT PIRSR600823-1}. FT METAL 67 67 Calcium 1. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT METAL 70 70 Calcium 1; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR600823-3}. FT METAL 72 72 Calcium 1; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR600823-3}. FT METAL 74 74 Calcium 1. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT METAL 76 76 Calcium 1. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT METAL 87 87 Calcium 1. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT METAL 191 191 Iron (heme axial ligand). FT {ECO:0000256|PIRSR:PIRSR600823-3}. FT METAL 192 192 Calcium 2. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT METAL 244 244 Calcium 2. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT METAL 252 252 Calcium 2. {ECO:0000256|PIRSR: FT PIRSR600823-3}. FT BINDING 161 161 Substrate; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR600823-2}. FT SITE 62 62 Transition state stabilizer. FT {ECO:0000256|PIRSR:PIRSR600823-4}. 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 //