Reviewed,
UniProtKB/Swiss-Prot Q99489 (OXDD_HUMAN)
Last modified
June 16, 2009.
Version 82.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
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Names and origin
| Protein names | Recommended name: D-aspartate oxidase Short name=DASOX EC=1.4.3.1 Alternative name(s): DDO | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 341 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate. |
| Catalytic activity | D-aspartate + H2O + O2 = oxaloacetate + NH3 + H2O2. |
| Cofactor | FAD or 6-hydroxyflavin adenine dinucleotide. |
| Subcellular location | |
| Sequence similarities | Belongs to the DAMOX/DASOX family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Peroxisome |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Ligand | FAD Flavoprotein |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | aspartate catabolic process Ref.1 Traceable author statement. Source: UniProtKB oxidation reduction Ref.1Traceable author statement. Source: UniProtKB |
| Cellular component | peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | D-amino-acid oxidase activity Inferred from electronic annotation. Source: InterPro D-aspartate oxidase activity Ref.1Traceable author statement. Source: UniProtKB bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform DDO-1 (identifier: Q99489-1) Also known as: A; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform DDO-2 (identifier: Q99489-2) The sequence of this isoform differs from the canonical sequence as follows: 95-153: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 341 | 341 | D-aspartate oxidase | PRO_0000162770 | |||||
Regions | |||||||||
| Nucleotide binding | 6 – 20 | 15 | FAD By similarity | ||||||
| Nucleotide binding | 36 – 37 | 2 | FAD By similarity | ||||||
| Nucleotide binding | 43 – 44 | 2 | FAD By similarity | ||||||
| Nucleotide binding | 48 – 50 | 3 | FAD By similarity | ||||||
| Nucleotide binding | 307 – 311 | 5 | FAD By similarity | ||||||
| Motif | 339 – 341 | 3 | Microbody targeting signal Potential | ||||||
Sites | |||||||||
| Binding site | 166 | 1 | FAD; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Binding site | 183 | 1 | FAD By similarity | ||||||
| Binding site | 223 | 1 | Substrate By similarity | ||||||
| Binding site | 278 | 1 | Substrate By similarity | ||||||
| Binding site | 312 | 1 | FAD By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 95 – 153 | 59 | Missing in isoform DDO-2. | VSP_001269 | |||||
| Natural variant | 136 | 1 | F → L in a breast cancer sample; somatic mutation. Ref.4 | VAR_036244 | |||||
| Natural variant | 189 | 1 | Q → E: dbSNP rs17622. | VAR_014939 | |||||
| Natural variant | 230 | 1 | H → Y: dbSNP rs17621. | VAR_014940 | |||||
| Natural variant | 255 | 1 | L → R: dbSNP rs17623. | VAR_014941 | |||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Structural and functional characterization of the human brain D-aspartate oxidase." Setoyama C., Miura R. J. Biochem. 121:798-803(1997) [PubMed: 9163533] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS DDO-1 AND DDO-2). Tissue: Brain. |
| [2] | "The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. Beck S.Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [3] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DDO-1). Tissue: Brain. |
| [4] | "The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. Velculescu V.E.Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-136. |
Cross-references
Sequence databases | |
|---|---|
| D89858 mRNA. Translation: BAA14031.1. AL050350 Genomic DNA. Translation: CAI42511.1. BC032786 mRNA. Translation: AAH32786.3. Different initiation. | |
| IPI | IPI00015389. IPI00215860. |
| PIR | JC5438. JC5439. |
| RefSeq | NP_003640.2. NP_004023.2. |
| UniGene | Hs.591348 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1AN9 based on UniProtKB P00371. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | Q99489. |
Genome annotation databases | |
| Ensembl | ENSG00000203797. Homo sapiens. [Contig view] |
| GeneID | 8528. |
| KEGG | hsa:8528. |
Organism-specific databases | |
| GeneCards | GC06M110758. |
| H-InvDB | HIX0022729. |
| HGNC | HGNC:2727. DDO. |
| MIM | 124450. gene. |
| PharmGKB | PA27194. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOVERGEN | Q99489. |
Enzyme and pathway databases | |
| BRENDA | 1.4.3.1. 247. |
Gene expression databases | |
| ArrayExpress | Q99489. |
| Bgee | Q99489. |
| CleanEx | HS_DDO. |
| GermOnline | ENSG00000203797. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR006181. D-amino_acid_oxidase_CS. 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] |
| PROSITE | PS00677. DAO. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 31934. |
| SOURCE | Search... |
Entry information
| Entry name | OXDD_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q99489 Secondary accession number(s): Q5JXM4, Q8N552 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 6 Human chromosome 6: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


