ID A0A078I7F1_BRANA Unreviewed; 326 AA. AC A0A078I7F1; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 22-JUL-2015, entry version 7. DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS00064294}; DE EC=1.11.1.7 {ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS00064294}; 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae; OC Brassica. OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY46845.1}; RN [1] {ECO:0000313|EMBL:CDY46845.1} RP NUCLEOTIDE SEQUENCE. 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). RN [2] {ECO:0000313|EMBL:CDY46845.1} RP NUCLEOTIDE SEQUENCE. RA Genoscope - CEA; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. 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: 2 phenolic donor + H(2)O(2) = 2 phenoxyl CC radical of the donor + 2 H(2)O. {ECO:0000256|RuleBase:RU362060, CC ECO:0000256|SAAS:SAAS00064309}. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|RuleBase:RU362060}; CC Note=Binds 2 calcium ions per subunit. CC {ECO:0000256|RuleBase:RU362060}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000256|RuleBase:RU362060}; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per CC subunit. {ECO:0000256|RuleBase:RU362060}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU362060, CC ECO:0000256|SAAS:SAAS00218951}. CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant CC (class 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 GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. 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; 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|RuleBase:RU362060}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00064273}; KW Heme {ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS00129880}; KW Hydrogen peroxide {ECO:0000256|RuleBase:RU362060}; KW Iron {ECO:0000256|RuleBase:RU362060, ECO:0000256|SAAS:SAAS00129897}; KW Metal-binding {ECO:0000256|RuleBase:RU362060, KW ECO:0000256|SAAS:SAAS00129877}; KW Oxidoreductase {ECO:0000256|RuleBase:RU362060, KW ECO:0000256|SAAS:SAAS00129893}; KW Peroxidase {ECO:0000256|RuleBase:RU362060, KW ECO:0000256|SAAS:SAAS00129885}; 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_5001414014. 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 //