Reviewed,
UniProtKB/Swiss-Prot A8WXM1 (OXDD1_CAEBR)
Last modified
November 25, 2008.
Version 9.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: D-aspartate oxidase 1 Short name=DASOX 1 EC=1.4.3.1 Alternative name(s): DDO 1 | ||
| Gene names |
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| Organism | Caenorhabditis briggsae [Complete proteome] | ||
| Taxonomic identifier | 6238 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis |
Protein attributes
| Sequence length | 331 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate By similarity. |
| Catalytic activity | D-aspartate + H(2)O + O(2) = oxaloacetate + NH(3) + H(2)O(2). |
| Cofactor | FAD By similarity. |
| Sequence similarities | Belongs to the DAMOX/DASOX family. |
| Caution | The conserved active site Tyr residue in position 221 is replaced by a Phe. |
Ontologies
Keywords | |
|---|---|
| Ligand | FAD Flavoprotein |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | D-amino-acid oxidase activity Inferred from electronic annotation. Source: InterPro D-aspartate oxidase activityInferred from electronic annotation. Source: EC bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
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 | |
|---|---|
| CAAC02000460 Genomic DNA. Translation: CAP25156.1. | |
3D structure databases | |
| ModBase | Search... |
Organism-specific databases | |
| WormBase | WBGene00027125. CBG04460. |
Family and domain databases | |
| InterPro | IPR006181. D-amino_acid_oxidase_CS. IPR006076. FAD-dep_OxRdtase. IPR016040. NAD(P)-bd. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| Pfam | PF01266. DAO. 1 hit. [Graphical view] |
| PROSITE | PS00677. DAO. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | OXDD1_CAEBR | ||||||||
| Accession | Primary (citable) accession number: A8WXM1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Caenorhabditis annotation project | ||||||||

Clusters with


