ID A0A078I7F1_BRANA Unreviewed; 326 AA. AC A0A078I7F1; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 27-MAR-2024, entry version 43. 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=DARMORV10_A10P03790.1 {ECO:0000313|EMBL:CAF2312558.1}, GN 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). RN [2] {ECO:0000313|EMBL:CDY46845.1} RP NUCLEOTIDE SEQUENCE. RA Genoscope - CEA; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:CAF2312558.1} RP NUCLEOTIDE SEQUENCE. RG Genoscope - CEA; RA William W.; RL Submitted (JAN-2021) 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 catabolism, CC response to environmental stresses such as wounding, pathogen attack CC and oxidative stress. These functions might be dependent on each CC isozyme/isoform in each plant tissue. {ECO:0000256|ARBA:ARBA00002322}. 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 -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|PIRSR:PIRSR600823-3, CC ECO:0000256|RuleBase:RU362060}; CC Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR600823- CC 3, ECO:0000256|RuleBase:RU362060}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000256|PIRSR:PIRSR600823-3, CC ECO:0000256|RuleBase:RU362060}; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. CC {ECO:0000256|PIRSR:PIRSR600823-3, ECO:0000256|RuleBase:RU362060}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU362060}. CC -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase CC subfamily. {ECO:0000256|ARBA:ARBA00006873}. 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; HG994364; CAF2312558.1; -; Genomic_DNA. DR EMBL; LK032687; CDY46845.1; -; Genomic_DNA. DR RefSeq; XP_013666551.1; XM_013811097.1. DR STRING; 3708.A0A078I7F1; -. DR PaxDb; 3708-A0A078I7F1; -. DR EnsemblPlants; CDY46845; CDY46845; GSBRNA2T00086290001. DR GeneID; 106371076; -. DR Gramene; CDY46845; CDY46845; GSBRNA2T00086290001. DR KEGG; bna:106371076; -. DR OMA; RIRNKMA; -. DR OrthoDB; 1010072at2759; -. DR Proteomes; UP000028999; Unassembled WGS sequence. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0009505; C:plant-type cell wall; IBA:GO_Central. DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule. DR GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central. 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 Gene3D; 1.10.520.10; -; 1. DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 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 PANTHER; PTHR31235:SF302; PEROXIDASE; 1. DR PANTHER; PTHR31235; PEROXIDASE 25-RELATED; 1. DR Pfam; PF00141; peroxidase; 1. DR PRINTS; PR00458; PEROXIDASE. DR PRINTS; PR00461; PLPEROXIDASE. DR SUPFAM; SSF48113; Heme-dependent peroxidases; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR600823-3}; 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_5041001383" FT DOMAIN 25..325 FT /note="Plant heme peroxidase family profile" FT /evidence="ECO:0000259|PROSITE:PS50873" FT ACT_SITE 66 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-1" FT BINDING 67 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 70 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 72 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 74 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 76 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 87 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 161 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-2" FT BINDING 191 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 192 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 244 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" FT BINDING 252 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR600823-3" 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 //