Q0J0J1 · Q0J0J1_ORYSJ
- ProteinL-ascorbate oxidase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids574 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score2/5
Function
Catalytic activity
- 4 L-ascorbate + O2 = 2 H2O + 4 monodehydro-L-ascorbate radical
Cofactor
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | copper ion binding | |
Molecular Function | L-ascorbate oxidase activity | |
Molecular Function | oxidoreductase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameL-ascorbate oxidase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionQ0J0J1
- Secondary accessions
Proteomes
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MRTWRLAVLACLCAAAAAAPAEA | ||||||
Chain | PRO_5013530511 | 24-574 | L-ascorbate oxidase | |||
Sequence: KTHHHTWNITYQYKSPDCFRKLAVTINGESPGPTIRAAQGDTLVVTVHNMLDTENTAIHWHGIRQIGSPWADGTAGVTQCPILPGETFTYRFVVDRPGTYMYHAHYGMQRVAGLDGMLVVSVPDGVAEPFAYDGEHTVLLMDWWHQSVYEQAVGLASVPMVFVGEPQSLLINGRGVFNCSPPAASNGGGAACNAFGGECGWPTLFTASPGKTYRLRIGSLTSLASLSFEIEGHTMTVVEADGYYVTPVVVKNLFIYSGETYSVLVTADQDPSRSYWAASHVVSRDPTKTAPGRAVVRYASAAVDHPRTPPPTGPRWNDTASRVAQSRSFAALPGHVEPPPARPDRVLLLLNTQSKIDNHTKWAINGVSLSFPATPYLVAMKHGLRGEFDQRPPPDSYDHGSLNLSSPPASLAVRHAAYRLALGSVVDVVLQNTAIPPPNGRSETHPWHLHGHDFWVLGYGEGKFVPEVDGPGLNAASARGGAVMKNTVALHPMGWTAVRFRASNPGVWLFHCHLEAHVYMGMGVVFEEGVDVLPRLPASIMGCGRTKGHHY |
Proteomic databases
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 32-145 | Plastocyanin-like | ||||
Sequence: ITYQYKSPDCFRKLAVTINGESPGPTIRAAQGDTLVVTVHNMLDTENTAIHWHGIRQIGSPWADGTAGVTQCPILPGETFTYRFVVDRPGTYMYHAHYGMQRVAGLDGMLVVSV | ||||||
Domain | 158-323 | Plastocyanin-like | ||||
Sequence: EHTVLLMDWWHQSVYEQAVGLASVPMVFVGEPQSLLINGRGVFNCSPPAASNGGGAACNAFGGECGWPTLFTASPGKTYRLRIGSLTSLASLSFEIEGHTMTVVEADGYYVTPVVVKNLFIYSGETYSVLVTADQDPSRSYWAASHVVSRDPTKTAPGRAVVRYAS | ||||||
Domain | 438-552 | Plastocyanin-like | ||||
Sequence: HAAYRLALGSVVDVVLQNTAIPPPNGRSETHPWHLHGHDFWVLGYGEGKFVPEVDGPGLNAASARGGAVMKNTVALHPMGWTAVRFRASNPGVWLFHCHLEAHVYMGMGVVFEEG |
Sequence similarities
Belongs to the multicopper oxidase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length574
- Mass (Da)62,053
- Last updated2006-10-03 v1
- ChecksumC5529DC361D35A02
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK110881 EMBL· GenBank· DDBJ | BAG99069.1 EMBL· GenBank· DDBJ | mRNA | ||
AP014965 EMBL· GenBank· DDBJ | BAT08873.1 EMBL· GenBank· DDBJ | Genomic DNA |