D-aspartate oxidase 1 - Caenorhabditis briggsae

Preferred order of sections

Names and origin

Protein names

Recommended name:
D-aspartate oxidase 1
Short name=DASOX 1
Short name=DDO 1
EC=1.4.3.1

Gene names

ORF Names:

CBG04460

Organism

Caenorhabditis briggsae

Taxonomic identifier

6238 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	331 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate By similarity. UniProtKB Q19564
Catalytic activity	D-aspartate + H₂O + O₂ = oxaloacetate + NH₃ + H₂O₂.
Cofactor	FAD By similarity. UniProtKB P14920
Sequence similarities	Belongs to the DAMOX/DASOX family.
Caution	The conserved active site Tyr residue in position 221 is replaced by a Phe.

Ontologies

Keywords
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular function	D-amino-acid oxidase activity Inferred from electronic annotation. Source: InterPro D-aspartate oxidase activity Inferred from sequence or structural similarity. Source: UniProtKB D-glutamate oxidase activity Inferred from sequence or structural similarity. Source: UniProtKB nucleotide 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

Chain

1 – 331

331

D-aspartate oxidase 1

PRO_0000317122

Regions

Nucleotide binding

5 – 19

15

FAD By similarity UniProtKB P14920

Nucleotide binding

35 – 36

2

FAD By similarity

Nucleotide binding

42 – 43

2

FAD By similarity

Nucleotide binding

47 – 49

3

FAD By similarity

Nucleotide binding

307 – 311

5

FAD By similarity

Sites

Binding site

163

1

FAD; via amide nitrogen and carbonyl oxygen By similarity

Binding site

276

1

Substrate By similarity

Binding site

312

1

FAD By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

A8WXM1 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 87BE766D5D2E7FBD
Show »

FASTA

331

37,518

        10         20         30         40         50         60 
MLPKIAVIGE GVIGCTSALQ IAKAIPNSKI TIFHDKPFEN SCSAGPAGLF RIDYEENTEY 

        70         80         90        100        110        120 
GRASFAWFSH LYRTTKGAET GVKLVSGHIQ SDNLESLKQQ QRAYGDIVYN FRFLDDRERL 

       130        140        150        160        170        180 
DIFPSPSKHC IHYTAYASEG NKYVPYLKRL LLEQKVEFQQ KNVENLDTIA DAGYDVIVNC 

       190        200        210        220        230        240 
AGLYGGKLAG DDDQCYPIRG VILEVDAPWH KHFNYRDFTT FTIPKENSVV IGSTKQDNRW 

       250        260        270        280        290        300 
DLEITDEDRN DILSRYIELH PGMREPKILK EWSALRPGRK HVRIESQQRK TTETGKEYTV 

       310        320        330 
VHHYGHGSNG FTLGWGTAIE ATKLVKKALG L

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Caenorhabditis briggsae: a platform for comparative genomics." Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., Hillier L.W. Waterston R.H. PLoS Biol. 1:166-192(2003) [PubMed: 14624247] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AF16.
[2]	The C.briggsae Sequencing Consortium Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. Strain: AF16.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CAAC02000460 Genomic DNA. Translation: CAP25156.1.
RefSeq	XP_002634445.1. XM_002634399.1.
3D structure databases
ProteinModelPortal	A8WXM1.
ModBase	Search...
Protein-protein interaction databases
STRING	A8WXM1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	8576441.
KEGG	cbr:CBG04460.
Organism-specific databases
CTD	8576441.
WormBase	CBG04460; CBP06757; WBGene00027125.
Phylogenomic databases
HOGENOM	HBG735740.
OMA	FSHLYRT.
PhylomeDB	A8WXM1.
Family and domain databases
InterPro	IPR023209. D-aa_oxidase. 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. 3 hits.
KO	K00272.
PANTHER	PTHR11530. PTHR11530. 1 hit.
Pfam	PF01266. DAO. 1 hit. [Graphical view]
PIRSF	PIRSF000189. D-aa_oxidase. 1 hit.
PROSITE	PS00677. DAO. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

OXDD1_CAEBR

Accession

Primary (citable) accession number: A8WXM1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	January 15, 2008
Last modified:	December 14, 2011
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents