Detail Information for IndEnz0018000999
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