ID C5WNL8_SORBI Unreviewed; 250 AA. AC C5WNL8; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAR-2024, entry version 68. 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). RN [3] {ECO:0007829|PDB:8DJR, ECO:0007829|PDB:8DJS} RP X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) IN COMPLEX WITH L-ASCORBATE AND HEME RP B. RX PubMed=36575825; DOI=10.1093/plphys/kiac604; RA Zhang B., Lewis J.A., Vermerris W., Sattler S.E., Kang C.; RT "A sorghum ascorbate peroxidase with four binding sites has activity RT against ascorbate and phenylpropanoids."; RL Plant Physiol. 192:102-118(2023). 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 PDB; 8DJR; X-ray; 1.46 A; A=1-250. DR PDB; 8DJS; X-ray; 1.19 A; A=1-250. DR PDB; 8DJT; X-ray; 1.16 A; A=1-250. DR PDB; 8DJU; X-ray; 1.50 A; A=1-250. DR PDB; 8DJW; X-ray; 1.80 A; A=1-250. DR PDB; 8DJX; X-ray; 1.34 A; A=1-250. DR AlphaFoldDB; C5WNL8; -. DR SMR; C5WNL8; -. DR STRING; 4558.C5WNL8; -. 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 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:8DJR, ECO:0007829|PDB:8DJS}; KW Calcium {ECO:0000256|ARBA:ARBA00022837}; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0007829|PDB:8DJR}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0007829|PDB:8DJR}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0007829|PDB:8DJR}; 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" FT BINDING 35 FT /ligand="L-ascorbate" FT /ligand_id="ChEBI:CHEBI:38290" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:8DJS" FT BINDING 35 FT /ligand="L-ascorbate" FT /ligand_id="ChEBI:CHEBI:38290" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:8DJT" FT BINDING 41 FT /ligand="L-ascorbate" FT /ligand_id="ChEBI:CHEBI:38290" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:8DJT" FT BINDING 42 FT /ligand="L-ascorbate" FT /ligand_id="ChEBI:CHEBI:38290" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:8DJT" FT BINDING 75 FT /ligand="L-ascorbate" FT /ligand_id="ChEBI:CHEBI:38290" FT /ligand_label="4" FT /evidence="ECO:0007829|PDB:8DJT" FT BINDING 79 FT /ligand="L-ascorbate" FT /ligand_id="ChEBI:CHEBI:38290" FT /ligand_label="4" FT /evidence="ECO:0007829|PDB:8DJT" FT BINDING 132 FT /ligand="L-ascorbate" FT /ligand_id="ChEBI:CHEBI:38290" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:8DJT" FT BINDING 163 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /ligand_part_note="axial binding residue" FT /evidence="ECO:0007829|PDB:8DJR, ECO:0007829|PDB:8DJS" FT BINDING 167 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /evidence="ECO:0007829|PDB:8DJR, ECO:0007829|PDB:8DJS" FT BINDING 169 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /evidence="ECO:0007829|PDB:8DJR, ECO:0007829|PDB:8DJS" FT BINDING 172 FT /ligand="L-ascorbate" FT /ligand_id="ChEBI:CHEBI:38290" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:8DJS" FT BINDING 172 FT /ligand="L-ascorbate" FT /ligand_id="ChEBI:CHEBI:38290" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:8DJT" FT BINDING 173 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /evidence="ECO:0007829|PDB:8DJR, ECO:0007829|PDB:8DJS" 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 //