| IED ID | IndEnz0018000999 |
| Enzyme Type ID | peroxidase000999 |
| Protein Name |
L-ascorbate oxidase AAO AO ASO Ascorbase EC 1.10.3.3 |
| Gene Name | AAO AO At5g21100 T10F18.130 |
| Organism | Arabidopsis thaliana (Mouse-ear cress) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
| Enzyme Sequence | MAVIVWWLLTVVVVAFHSASAAVVESTWEVEYKYWWPDCKEGIVMAINGQFPGPTIDAVAGDTVIIHVVNKLSTEGVVIHWHGIRQKGTPWADGAAGVTQCPINPGETFTYKFIVDKAGTHFYHGHYGMQRSSGLYGMLIVRSPKERLIYDGEFNLLLSDWWHQSIHAQELALSSRPMRWIGEPQSLLINGRGQFNCSQAAYFNKGGEKDVCTFKENDQCAPQTLRVEPNRVYRLRIASTTALASLNLAVQGHQLVVVEADGNYVAPFTVNDIDVYSGETYSVLLKTNALPSKKYWISVGVRGREPKTPQALTVINYVDATESRPSHPPPVTPIWNDTDRSKSFSKKIFAAKGYPKPPEKSHDQLILLNTQNLYEDYTKWSINNVSLSVPVTPYLGSIRYGLKSAYDLKSPAKKLIMDNYDIMKPPPNPNTTKGSGIYNFAFGIVVDVILQNANVLKGVISEIHPWHIHGHDFWVLGYGEGKFKPGIDEKTFNLKNPPLRNTVVLYPFGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGVVFVEGVDRIGKMEIPDEALGCGLTRKWLMNRGRP |
| Enzyme Length | 573 |
| Uniprot Accession Number | Q8LPL3 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=4 L-ascorbate + O2 = 2 H2O + 4 monodehydro-L-ascorbate radical; Xref=Rhea:RHEA:30243, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:38290, ChEBI:CHEBI:59513; EC=1.10.3.3; Evidence={ECO:0000269|PubMed:15883131}; |
| DNA Binding | |
| EC Number | 1.10.3.3 |
| Enzyme Function | FUNCTION: Ascorbate oxidase involved in a redox system involving ascorbic acid (AsA) (PubMed:15883131, PubMed:27255930). The oxidation of AsA represses responses to high salinity and oxidative stress conditions such as vegetative growth and seed production reductions (PubMed:15883131). Negative regulator of defense responses toward incompatible Turnip mosaic virus (TuMV strain UK1) by preventing jasmonic acid (JA)- dependent accumulation of ascorbic acid (AsA, AS) and dehydroascobic acid (DHA) (PubMed:27255930). {ECO:0000269|PubMed:15883131, ECO:0000269|PubMed:27255930}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Cofactor degradation; L-ascorbate degradation. {ECO:0000269|PubMed:15883131}. |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (3); Domain (3); Glycosylation (4); Metal binding (12); Signal peptide (1) |
| Keywords | Copper;Disulfide bond;Glycoprotein;Metal-binding;Oxidoreductase;Plant defense;Reference proteome;Repeat;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Repressed progressively during incompatible Turnip mosaic virus (TuMV) infection (strain UK1) (PubMed:27255930). When the plant is infected by a compatible TuMV strain (UK1 m2), the down-regulation is transient and last two days (PubMed:27255930). {ECO:0000269|PubMed:27255930}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P37064}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15634197; 16927206; 17526915; 18650403; 18753283; 20736450; 8624413; |
| Motif | |
| Gene Encoded By | |
| Mass | 64,266 |
| Kinetics | |
| Metal Binding | METAL 80; /note=Copper 1; type 2; /evidence=ECO:0000250|UniProtKB:P37064; METAL 82; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:P37064; METAL 124; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:P37064; METAL 126; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:P37064; METAL 464; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:P37064; METAL 467; /note=Copper 1; type 2; /evidence=ECO:0000250|UniProtKB:P37064; METAL 469; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:P37064; METAL 526; /note=Copper 3; type 3; /evidence=ECO:0000250|UniProtKB:P37064; METAL 527; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:P37064; METAL 528; /note=Copper 2; type 3; /evidence=ECO:0000250|UniProtKB:P37064; METAL 532; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:P37064; METAL 537; /note=Copper 4; type 1; /evidence=ECO:0000250|UniProtKB:P37064 |
| Rhea ID | RHEA:30243 |
| Cross Reference Brenda |