Reviewed, UniProtKB/Swiss-Prot Q95XG9 (OXDA2_CAEEL)

Names and origin

Protein names

Recommended name:
    D-amino-acid oxidase 2
      Short name=DAMOX 2
      Short name=DAAO 2
      Short name=DAO 2
    EC=1.4.3.3

Gene names

ORF Names:

Y69A2AR.5

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	322 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Could act as a detoxifying agent which removes D-amino acids accumulated during aging By similarity. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids. Ref.1 UniProtKB P14920
Catalytic activity	A D-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.
Cofactor	FAD By similarity. UniProtKB P14920
Subunit structure	Homodimer By similarity. UniProtKB P14920
Subcellular location	Peroxisome Probable. Ref.1
Sequence similarities	Belongs to the DAMOX/DASOX family.
Biophysicochemical properties	Kinetic parameters: KM=1.72 mM for D-Ala Ref.1 KM=0.11 mM for D-Arg Ref.1 KM=1.22 mM for D-Met Ref.1 Vmax=5.41 µmol/min/mg enzyme with D-Ala as substrate Ref.1 Vmax=2.52 µmol/min/mg enzyme with D-Arg as substrate Ref.1 Vmax=7.43 µmol/min/mg enzyme with D-Met as substrate Ref.1

Ontologies

Keywords
Cellular component	Peroxisome
Domain	Signal
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	D-amino-acid oxidase activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Potential
	Chain	18 – 322	305	D-amino-acid oxidase 2		PRO_0000317125
Regions
	Nucleotide binding	4 – 18	15	FAD By similarity UniProtKB P14920
	Nucleotide binding	34 – 35	2	FAD By similarity
	Nucleotide binding	41 – 42	2	FAD By similarity
	Nucleotide binding	46 – 48	3	FAD By similarity
	Nucleotide binding	293 – 297	5	FAD By similarity
	Motif	320 – 322	3	Microbody targeting signal Potential
Sites
	Binding site	160	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	177	1	FAD By similarity
	Binding site	215	1	Substrate By similarity
	Binding site	270	1	Substrate By similarity
	Binding site	294	1	Substrate; via carbonyl oxygen By similarity
	Binding site	298	1	FAD By similarity
Amino acid modifications
	Glycosylation	39	1	N-linked (GlcNAc...) Potential
	Glycosylation	63	1	N-linked (GlcNAc...) Potential
	Glycosylation	175	1	N-linked (GlcNAc...) Potential
	Glycosylation	219	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q95XG9-1 [UniParc]. Last modified July 5, 2004. Version 2. Checksum: 862044F6523AD76E	FASTA	322	36,117
	10 20 30 40 50 60 MPKIAVLGAG INGIASALAI QERLPNCEVT IIAEKFSPNT TSDVAAGLIE PFLCDDDVDR 70 80 90 100 110 120 IINWTSATIS RIHEYQADGN PGAEEQSGYW LQSVKSEPKW LKLMKNVHIL TDAEMKQVAR 130 140 150 160 170 180 RPEHKFGIFY TTWYLEPTPY IKWCTDKFLK NGGKFKKQKI ENIDDVARSY DVTVNCTGLG 190 200 210 220 230 240 SRALIGDKEV YPTRGQILKV SCPRVKHFFI DDKYYALLND STITLGGTFE AHQWDLTINS 250 260 270 280 290 300 ELSQKILKEN IHNIPSLRTA QILSSHVDMR PSRGTVRLQA ELGRSLVHNY GHGGSGITLH 310 320 WGCALECAEI VENVLKMKKS KL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Caenorhabditis elegans has two genes encoding functional D-aspartate oxidases." Katane M., Seida Y., Sekine M., Furuchi T., Homma H. FEBS J. 274:137-149(2007) [PubMed: 17140416] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: Bristol N2.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB275890 mRNA. Translation: BAF34313.1. AC084158 Genomic DNA. Translation: AAL27265.2.
RefSeq	NP_500234.3.
UniGene	Cel.20197
3D structure databases
HSSP	HSSP built from PDB template 1VE9 based on UniProtKB P00371.
ModBase	Search...
Genome annotation databases
Ensembl	Y69A2AR.5. Caenorhabditis elegans. [Contig view]
GeneID	3565775.
KEGG	cel:Y69A2AR.5.
NMPDR	fig|6239.3.peg.12687.
Organism-specific databases
WormBase	WBGene00022076. Y69A2AR.5.
WormPep	Y69A2AR.5. CE36371. [WorfDB]
Phylogenomic databases
OMA	Q95XG9. RYISTEY.
Enzyme and pathway databases
BRENDA	1.4.3.3. 672.
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	957813.

Entry information

Entry name

OXDA2_CAEEL

Accession

Primary (citable) accession number: Q95XG9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	July 5, 2004
Last modified:	June 16, 2009
This is version 44 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project