ID C5WNL8_SORBI Unreviewed; 250 AA. AC C5WNL8; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 22-FEB-2023, entry version 63. DE RecName: Full=L-ascorbate peroxidase {ECO:0000256|ARBA:ARBA00012940}; DE EC=1.11.1.11 {ECO:0000256|ARBA:ARBA00012940}; GN ORFNames=SORBI_3001G410200 {ECO:0000313|EMBL:EER95051.1}; OS Sorghum bicolor (Sorghum) (Sorghum vulgare). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum. OX NCBI_TaxID=4558 {ECO:0000313|EMBL:EER95051.1, ECO:0000313|Proteomes:UP000000768}; RN [1] {ECO:0000313|EMBL:EER95051.1, ECO:0000313|Proteomes:UP000000768} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768}; RX PubMed=19189423; DOI=10.1038/nature07723; RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J., RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J., RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J., RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M., RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L., RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P., RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman, RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.; RT "The Sorghum bicolor genome and the diversification of grasses."; RL Nature 457:551-556(2009). RN [2] {ECO:0000313|Proteomes:UP000000768} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768}; RX PubMed=29161754; DOI=10.1111/tpj.13781; RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D., RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A., RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.; RT "The Sorghum bicolor reference genome: improved assembly, gene annotations, RT a transcriptome atlas, and signatures of genome organization."; RL Plant J. 93:338-354(2018). CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O2 + L-ascorbate = 2 H2O + L-dehydroascorbate; CC Xref=Rhea:RHEA:22996, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:38290, ChEBI:CHEBI:58539; EC=1.11.1.11; CC Evidence={ECO:0000256|ARBA:ARBA00000939}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000256|ARBA:ARBA00001970}; 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; CM000760; EER95051.1; -; Genomic_DNA. DR RefSeq; XP_002468053.1; XM_002468008.1. DR AlphaFoldDB; C5WNL8; -. DR STRING; 4558.Sb01g038760.1; -. DR EnsemblPlants; EER95051; EER95051; SORBI_3001G410200. DR GeneID; 8081447; -. DR Gramene; EER95051; EER95051; SORBI_3001G410200. DR KEGG; sbi:8081447; -. DR eggNOG; ENOG502QR1E; Eukaryota. DR HOGENOM; CLU_036959_3_0_1; -. DR InParanoid; C5WNL8; -. DR OMA; MAKNYPV; -. DR OrthoDB; 168803at2759; -. DR Proteomes; UP000000768; Chromosome 1. DR GO; GO:0009507; C:chloroplast; IBA:GO_Central. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0016688; F:L-ascorbate peroxidase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central. DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central. DR GO; GO:0000302; P:response to reactive oxygen species; IBA:GO_Central. DR CDD; cd00691; ascorbate_peroxidase; 1. DR Gene3D; 1.10.520.10; -; 1. DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 1. DR InterPro; IPR044831; Ccp1-like. DR InterPro; IPR002016; Haem_peroxidase. DR InterPro; IPR010255; Haem_peroxidase_sf. DR InterPro; IPR002207; Peroxidase_I. DR InterPro; IPR019794; Peroxidases_AS. DR InterPro; IPR019793; Peroxidases_heam-ligand_BS. DR PANTHER; PTHR31356:SF57; L-ASCORBATE PEROXIDASE 1, CYTOSOLIC; 1. DR PANTHER; PTHR31356; THYLAKOID LUMENAL 29 KDA PROTEIN, CHLOROPLASTIC-RELATED; 1. DR Pfam; PF00141; peroxidase; 1. DR PRINTS; PR00459; ASPEROXIDASE. DR PRINTS; PR00458; PEROXIDASE. 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|ARBA:ARBA00022837}; KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Peroxidase {ECO:0000256|ARBA:ARBA00022559}; KW Potassium {ECO:0000256|ARBA:ARBA00022958}; KW Reference proteome {ECO:0000313|Proteomes:UP000000768}. FT DOMAIN 74..250 FT /note="Plant heme peroxidase family profile" FT /evidence="ECO:0000259|PROSITE:PS50873" FT REGION 113..137 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 121..137 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 250 AA; 27217 MW; 0C6676CD995F761C CRC64; MAKSYPTVSA EYSEAVEKAR QKLRALIAEK SCAPLMLRLA WHSAGTFDVS SRTGGPFGTM KNPAELAHGA NAGLDIAVRL LEPIKEEFPI LSYADFYQLA GVVAVEVTGG PQIPFHPGRE DKPQPPPEGR LPDATKGSDH LRQVFGKQMG LSDQDIVALS GGHTLGRCHK ERSGFEGAWT SNPLVFDNSY FKELLSGDKE GLLQLPSDKA LLSDPAFRPL VDKYAADEKA FFEDYKEAHL KLSELGFADA //