Reviewed,
UniProtKB/Swiss-Prot A8XJ44 (OXDA2_CAEBR)
Last modified
November 3, 2009.
Version 16.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: D-amino-acid oxidase 2 Short name=DAMOX 2 Short name=DAAO 2 Short name=DAO 2 EC=1.4.3.3 | ||
| Gene names |
| ||
| Organism | Caenorhabditis briggsae [Complete proteome] | ||
| Taxonomic identifier | 6238 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis |
Protein attributes
| Sequence length | 329 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids By similarity. UniProtKB P14920 |
| Catalytic activity | A D-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2. |
| Cofactor | FAD By similarity. UniProtKB P14920 |
| Subunit structure | Homodimer By similarity. UniProtKB P14920 |
| Subcellular location | Peroxisome By similarity. UniProtKB P14920 |
| Sequence similarities | Belongs to the DAMOX/DASOX family. |
| Sequence caution | The sequence CAP32671.2 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Peroxisome |
| Domain | Signal |
| Ligand | FAD Flavoprotein |
| Molecular function | Oxidoreductase |
| PTM | Glycoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | D-amino-acid oxidase activity Inferred from electronic annotation. Source: EC bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | Potential | ||||||
| Chain | 20 – 329 | 310 | D-amino-acid oxidase 2 | PRO_0000317124 | |||||
Regions | |||||||||
| Nucleotide binding | 4 – 18 | 15 | FAD By similarity UniProtKB P14920 | ||||||
| Nucleotide binding | 34 – 35 | 2 | FAD By similarity | ||||||
| Nucleotide binding | 41 – 42 | 2 | FAD By similarity | ||||||
| Nucleotide binding | 46 – 48 | 3 | FAD By similarity | ||||||
| Nucleotide binding | 298 – 302 | 5 | FAD By similarity | ||||||
| Motif | 327 – 329 | 3 | Microbody targeting signal Potential | ||||||
Sites | |||||||||
| Binding site | 162 | 1 | FAD; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Binding site | 182 | 1 | FAD By similarity | ||||||
| Binding site | 220 | 1 | Substrate By similarity | ||||||
| Binding site | 275 | 1 | Substrate By similarity | ||||||
| Binding site | 299 | 1 | Substrate; via carbonyl oxygen By similarity | ||||||
| Binding site | 303 | 1 | FAD By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 39 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 180 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 224 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The genome sequence of Caenorhabditis briggsae: a platform for comparative genomics." Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., Hillier L.W. Waterston R.H.PLoS Biol. 1:166-192(2003) [PubMed: 14624247] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AF16. |
| [2] | The C.briggsae Sequencing Consortium Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. Strain: AF16. |
Cross-references
Sequence databases | |
|---|---|
| CAAC02000520 Genomic DNA. Translation: CAP32671.2. Sequence problems. | |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GenomeReviews | Gene locus CBG13882 in contig CU538967_GR. |
Organism-specific databases | |
| WormBase | WBGene00034568. CBG13882. |
Phylogenomic databases | |
| OMA | RYISTEY. |
Enzyme and pathway databases | |
| BRENDA | 1.4.3.3. 261794. |
Family and domain databases | |
| InterPro | IPR006076. FAD-dep_OxRdtase. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| Pfam | PF01266. DAO. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | OXDA2_CAEBR | ||||||||
| Accession | Primary (citable) accession number: A8XJ44 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Caenorhabditis annotation project | ||||||||

Clusters with


