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

Comments

CATALYTIC ACTIVITY: D-aspartate + H₂O + O₂ = oxaloacetate + NH₃ + H₂O₂.
COFACTOR: FAD or 6-hydroxyflavin adenine dinucleotide.
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Peroxisome.
SIMILARITY: Belongs to the DAMOX/DASOX family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X95310; CAA64622.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A44132; A44132.

NP_776333.1; -.

3D structure databases

HSSP

P00371; 1AN9. [HSSP ENTRY / PDB]

ModBase

P31228.

Family and domain databases

InterPro

IPR006181; D-amino_acid_oxidase_CS.
IPR006076; FAD-dep_OxRdtase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF01266; DAO; 1.
Pfam graphical view of domain structure.

PROSITE

PS00677; DAO; 1.

BLOCKS

P31228.

Genome annotation databases

Ensembl

ENSBTAG00000033367; Bos taurus. [Contig view]

GeneID

280763; -.

KEGG

bta:280763; -.

Phylogenomic databases

HOVERGEN

P31228; -.

Other

ProtoNet

P31228.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase; Peroxisome.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 341`	`341`	`D-aspartate oxidase.`	`PRO_0000162769`
`NP_BIND`	`6 20`	`15`	`FAD (Potential).`
`MOTIF`	`339 341`	`3`	`Microbody targeting signal (Potential).`
`ACT_SITE`	`223 223`		`By similarity.`
`ACT_SITE`	`302 302`		`By similarity.`
`MOD_RES`	`1 1`		`Blocked amino end (Met).`
`VARIANT`	`228 228`	`1`	`V -> I (in some molecules).`
`CONFLICT`	`274 274`		`K -> R (in Ref. 2; AA sequence).`
`CONFLICT`	`283 283`		`S -> G (in Ref. 2; AA sequence).`

Sequence information

Length: 341 AA [This is the length of the unprocessed precursor]

Molecular weight: 37660 Da [This is the MW of the unprocessed precursor]

CRC64: 355EF4EE42C53B49 [This is a checksum on the sequence]

        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

P31228 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools