ID A0A2G5CL64_AQUCA Unreviewed; 246 AA. AC A0A2G5CL64; DT 31-JAN-2018, integrated into UniProtKB/TrEMBL. DT 31-JAN-2018, sequence version 1. DT 12-AUG-2020, entry version 12. DE RecName: Full=L-ascorbate peroxidase {ECO:0000256|ARBA:ARBA00012940}; DE EC=1.11.1.11 {ECO:0000256|ARBA:ARBA00012940}; GN ORFNames=AQUCO_04600020v1 {ECO:0000313|EMBL:PIA32062.1}; OS Aquilegia coerulea (Rocky mountain columbine). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae; OC Aquilegia. OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA32062.1, ECO:0000313|Proteomes:UP000230069}; RN [1] {ECO:0000313|EMBL:PIA32062.1, ECO:0000313|Proteomes:UP000230069} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069}; RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N., RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.; RT "WGS assembly of Aquilegia coerulea Goldsmith."; RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases. 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. CC {ECO:0000256|RuleBase:RU004241}. 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; KZ305063; PIA32062.1; -; Genomic_DNA. DR Proteomes; UP000230069; Unassembled WGS sequence. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0004601; F:peroxidase activity; IEA:InterPro. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. 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 Pfam; PF00141; peroxidase; 1. DR PRINTS; PR00459; ASPEROXIDASE. DR PRINTS; PR00458; PEROXIDASE. 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 Coiled coil {ECO:0000256|SAM:Coils}; Heme {ECO:0000256|ARBA:ARBA00022617}; KW 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 Reference proteome {ECO:0000313|Proteomes:UP000230069}. FT DOMAIN 74..246 FT /note="PEROXIDASE_4" FT /evidence="ECO:0000259|PROSITE:PS50873" FT REGION 113..137 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 9..29 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 117..137 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 246 AA; 27054 MW; 8D606D2DFF9DA408 CRC64; MGKCYPAVSE EYKKAVDKAK KKLRGFIAEK NCAPLMLRLA WHSAGTYDVK TKTGGPFGTM KHVAELDHGA NNGLDIAVRL LEPIKEQFPI LSYADFYQLA GVVAVEVTGG PEVPFHPGRQ DKPEPPPEGR LPDATKGSDH LRDVFVKQMG LSDKDIVALS GAHTLGRCHK ERSGFEGPWT ANPLIFDNSY FKELLSGEKE GLLQLPSDKA LLADPSFRPL VEKYAADEDA FFEDYAEAHL KLSELG //