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Reviewed, UniProtKB/Swiss-Prot P31228 (OXDD_BOVIN)

Last modified June 16, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

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

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General annotation (Comments)

Catalytic activity

D-aspartate + H2O + O2 = oxaloacetate + NH3 + H2O2.

Cofactor

FAD or 6-hydroxyflavin adenine dinucleotide.

Subunit structure

Monomer.

Subcellular location

Peroxisome.

Sequence similarities

Belongs to the DAMOX/DASOX family.

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Ontologies

Keywords
   Cellular componentPeroxisome
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionD-amino-acid oxidase activity

Inferred from electronic annotation. Source: InterPro

D-aspartate oxidase activity

Inferred from electronic annotation. Source: EC

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 341341D-aspartate oxidase
PRO_0000162769

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

Amino acid modifications

Modified residue11Blocked amino end (Met)

Natural variations

Natural variant2281V → I in some molecules.

Experimental info

Sequence conflict2741K → R AA sequence Ref.2
Sequence conflict2831S → G AA sequence Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P31228-1 [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: 355EF4EE42C53B49

FASTA34137,660
        10         20         30         40         50         60 
MDTVRIAVVG AGVMGLSTAV CISKMVPGCS ITVISDKFTP ETTSDVAAGM LIPPTYPDTP 

        70         80         90        100        110        120 
IQKQKQWFKE TFDHLFAIVN SAEAEDAGVI LVSGWQIFQS IPTEEVPYWA DVVLGFRKMT 

       130        140        150        160        170        180 
KDELKKFPQH VFGHAFTTLK CEGPAYLPWL QKRVKGNGGL ILTRRIEDLW ELHPSFDIVV 

       190        200        210        220        230        240 
NCSGLGSRQL AGDSKIFPVR GQVLKVQAPW VKHFIRDSSG LTYIYPGVSN VTLGGTRQKG 

       250        260        270        280        290        300 
DWNLSPDAEI SKEILSRCCA LEPSLRGAYD LREKVGLRPT RPSVRLEKEL LAQDSRRLPV 

       310        320        330        340 
VHHYGHGSGG IAMHWGTALE ATRLVNECVQ VLRTPAPKSK L

« Hide

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References

[1]"cDNA cloning and expression of the flavoprotein D-aspartate oxidase from bovine kidney cortex."
Simonic T., Duga S., Negri A., Tedeschi G., Malcovati M., Tenchini M.L., Ronchi S.
Biochem. J. 322:729-735(1997) [PubMed: 9148742] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney cortex.
[2]"The primary structure of the flavoprotein D-aspartate oxidase from beef kidney."
Negri A., Ceciliani F., Tedeschi G., Simonic T., Ronchi S.
J. Biol. Chem. 267:11865-11871(1992) [PubMed: 1601857] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-338.
Tissue: Kidney.

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Cross-references

Sequence databases

X95310 mRNA. Translation: CAA64622.1.
IPIIPI00699629.
PIRA44132.
RefSeqNP_776333.1.
UniGeneBt.25930

3D structure databases

HSSPHSSP built from PDB template 1AN9 based on UniProtKB P00371.
ModBaseSearch...

Genome annotation databases

EnsemblENSBTAG00000033367. Bos taurus. [Contig view]
GeneID280763.
KEGGbta:280763.

Phylogenomic databases

HOVERGENP31228.

Enzyme and pathway databases

BRENDA1.4.3.1. 251.

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...

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Entry information

Entry nameOXDD_BOVIN
AccessionPrimary (citable) accession number: P31228
Secondary accession number(s): O02846, Q9TRA3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 15, 1999
Last modified: June 16, 2009
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

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