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Reviewed, UniProtKB/Swiss-Prot Q922Z0 (OXDD_MOUSE)

Last modified November 3, 2009. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    D-aspartate oxidase
      Short name=DASOX
    EC=1.4.3.1
Alternative name(s):
    DDO
Gene names
Name: Ddo
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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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 + H2O + O2 = oxaloacetate + NH3 + H2O2.

Cofactor

FAD or 6-hydroxyflavin adenine dinucleotide By similarity.

Subcellular location

Peroxisome By similarity.

Sequence similarities

Belongs to the DAMOX/DASOX family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 341341D-aspartate oxidase
PRO_0000162771

Regions

Nucleotide binding6 – 2015FAD By similarity
Nucleotide binding36 – 372FAD By similarity
Nucleotide binding43 – 442FAD By similarity
Nucleotide binding48 – 503FAD By similarity
Nucleotide binding307 – 3115FAD By similarity
Motif339 – 3413Microbody targeting signal Potential

Sites

Binding site1661FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site1831FAD By similarity
Binding site2231Substrate By similarity
Binding site2781Substrate By similarity
Binding site3121FAD By similarity

Experimental info

Sequence conflict561C → Y in AAH27312. Ref.2
Sequence conflict671W → C in AAH27312. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q922Z0-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: A80BC74CC44A601D

FASTA34137,546
        10         20         30         40         50         60 
MDTVCIAVVG AGVIGLSTAA CISQLVPGCT VTVISDRFTP DTTSNVAAGM LIPHTCADTP 

        70         80         90        100        110        120 
VPTQKRWFRE TFEHLSEIAK SAEAADAGVH LVSGWQIFRS VPAEEVPFWA DVVLGFRKMT 

       130        140        150        160        170        180 
EAELKRFPQY VFGQAFTTLK CETSAYLPWL ERRIKGSGGL LLTRRIEDLW ELQPSFDIVV 

       190        200        210        220        230        240 
NCSGLGSRRL VGDPMISPVR GQVLQARAPW VKHFIRDGGG LTYVYPGMSY VTLGGTRQKG 

       250        260        270        280        290        300 
DWNRSPDAEL SREIFSRCCT LEPSLHRAYD IKEKVGLRPS RPGVRLQKEI LVRGQQTLPV 

       310        320        330        340 
VHNYGHGSGG ISVHWGSALE ATRLVMECIH TLRTPASLSK L

« Hide

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References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Heart, Lung and Pituitary.
[2]"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].
Strain: Czech II and FVB/N.
Tissue: Mammary tumor.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AK033375 mRNA. Translation: BAC28253.1.
AK085947 mRNA. Translation: BAC39577.1.
AK161548 mRNA. Translation: BAE36456.1.
BC006690 mRNA. Translation: AAH06690.1.
BC027312 mRNA. Translation: AAH27312.1.
IPIIPI00454080.
RefSeqNP_081718.2.
UniGeneMm.252862

3D structure databases

HSSPHSSP built from PDB template 1VE9 based on UniProtKB P00371.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ922Z0.

Proteomic databases

PRIDEQ922Z0.

Genome annotation databases

EnsemblENSMUST00000019977; ENSMUSP00000019977; ENSMUSG00000063428; Mus musculus. [Genome view]
GeneID70503.
KEGGmmu:70503.
UCSCuc007exa.1. mouse.

Organism-specific databases

CTD70503.
MGIMGI:1925528. Ddo.

Phylogenomic databases

HOGENOMQ922Z0.
HOVERGENQ922Z0.
OMASTAVCIS.

Enzyme and pathway databases

BRENDA1.4.3.1. 244.

Gene expression databases

ArrayExpressQ922Z0.
BgeeQ922Z0.
CleanExMM_DDO.
GenevestigatorQ922Z0.
GermOnlineENSMUSG00000063428. Mus musculus.

Family and domain databases

InterProIPR006181. D-amino_acid_oxidase_CS.
IPR006076. FAD-dep_OxRdtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF01266. DAO. 1 hit.
[Graphical view]
PROSITEPS00677. DAO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio331757.
SOURCESearch...

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Entry information

Entry nameOXDD_MOUSE
AccessionPrimary (citable) accession number: Q922Z0
Secondary accession number(s): Q3TT69, Q8R2R2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: December 1, 2001
Last modified: November 3, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents