Reviewed, UniProtKB/Swiss-Prot Q99489 (OXDD_HUMAN)

Names and origin

Protein names

Recommended name:
    D-aspartate oxidase
      Short name=DASOX
    EC=1.4.3.1
Alternative name(s):
    DDO

Gene names

Name:

DDO

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	Peroxisome.
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.1 Traceable 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.1 Traceable author statement. Source: UniProtKB binding Inferred 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

	Sequence		Length	Mass (Da)
	Isoform DDO-1 (A) [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 8CAE7501FB7F215C	FASTA	341	37,535
	10 20 30 40 50 60 MDTARIAVVG AGVVGLSTAV CISKLVPRCS VTIISDKFTP DTTSDVAAGM LIPHTYPDTP 70 80 90 100 110 120 IHTQKQWFRE TFNHLFAIAN SAEAGDAGVH LVSGWQIFQS TPTEEVPFWA DVVLGFRKMT 130 140 150 160 170 180 EAELKKFPQY VFGQAFTTLK CECPAYLPWL EKRIKGSGGW TLTRRIEDLW ELHPSFDIVV 190 200 210 220 230 240 NCSGLGSRQL AGDSKIFPVR GQVLQVQAPW VEHFIRDGSG LTYIYPGTSH VTLGGTRQKG 250 260 270 280 290 300 DWNLSPDAEN SREILSRCCA LEPSLHGACN IREKVGLRPY RPGVRLQTEL LARDGQRLPV 310 320 330 340 VHHYGHGSGG ISVHWGTALE AARLVSECVH ALRTPIPKSN L
	Isoform DDO-2. Checksum: DBD01D57E5B72F7A	FASTA	282	30,522
	10 20 30 40 50 60 MDTARIAVVG AGVVGLSTAV CISKLVPRCS VTIISDKFTP DTTSDVAAGM LIPHTYPDTP 70 80 90 100 110 120 IHTQKQWFRE TFNHLFAIAN SAEAGDAGVH LVSGIKGSGG WTLTRRIEDL WELHPSFDIV 130 140 150 160 170 180 VNCSGLGSRQ LAGDSKIFPV RGQVLQVQAP WVEHFIRDGS GLTYIYPGTS HVTLGGTRQK 190 200 210 220 230 240 GDWNLSPDAE NSREILSRCC ALEPSLHGAC NIREKVGLRP YRPGVRLQTE LLARDGQRLP 250 260 270 280 VVHHYGHGSG GISVHWGTAL EAARLVSECV HALRTPIPKS NL

References

	« Hide 'large scale' referencesShow '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. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., 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. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-136.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 1, 1997
Last modified:	June 16, 2009
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)