ID OXDD1_CAEEL Reviewed; 334 AA. AC Q19564; Q08I99; Q8I7K8; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 25-NOV-2008, entry version 53. DE RecName: Full=D-aspartate oxidase 1; DE Short=DASOX 1; DE EC=1.4.3.1; DE AltName: Full=DDO 1; GN ORFNames=F18E3.7; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=Bristol N2; RX PubMed=17140416; DOI=10.1111/j.1742-4658.2006.05571.x; RA Katane M., Seida Y., Sekine M., Furuchi T., Homma H.; RT "Caenorhabditis elegans has two genes encoding functional D-aspartate RT oxidases."; RL FEBS J. 274:137-149(2007). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE RP SPLICING. RC STRAIN=Bristol N2; RX MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). CC -!- FUNCTION: Selectively catalyzes the oxidative deamination of D- CC aspartate and its N-methylated derivative, N-methyl D-aspartate. CC -!- CATALYTIC ACTIVITY: D-aspartate + H(2)O + O(2) = oxaloacetate + CC NH(3) + H(2)O(2). CC -!- COFACTOR: FAD (By similarity). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.38 mM for D-Asp; CC KM=0.25 mM for D-Glu; CC KM=1.84 mM for NMDA; CC Vmax=4.40 umol/min/mg enzyme with D-Asp as substrate; CC Vmax=3.03 umol/min/mg enzyme with D-Glu as substrate; CC Vmax=4.31 umol/min/mg enzyme with NMDA as substrate; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=a; CC IsoId=Q19564-1; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=b; CC IsoId=Q19564-2; Sequence=VSP_014356, VSP_014357, VSP_014358, CC VSP_014359; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family. CC -!- CAUTION: The conserved active site Tyr residue in position 224 is CC replaced by a Phe. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB275892; BAF34315.1; -; mRNA. DR EMBL; U53139; AAK18939.1; -; Genomic_DNA. DR EMBL; U53139; AAN84824.1; -; Genomic_DNA. DR PIR; T29219; T29219. DR RefSeq; NP_504908.1; -. DR UniGene; Cel.4023; -. DR HSSP; P00371; 1AN9. DR Ensembl; F18E3.7; Caenorhabditis elegans. DR GeneID; 179130; -. DR KEGG; cel:F18E3.7; -. DR NMPDR; fig|6239.3.peg.18465; -. DR WormBase; WBGene00017565; F18E3.7. DR WormPep; F18E3.7a; CE07083. DR WormPep; F18E3.7b; CE32864. DR NextBio; 904050; -. DR ArrayExpress; Q19564; -. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0003884; F:D-amino-acid oxidase activity; IEA:InterPro. DR GO; GO:0008445; F:D-aspartate oxidase activity; IEA:EC. DR GO; GO:0009792; P:embryonic development ending in birth or eg...; IMP:WormBase. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR006181; D-amino_acid_oxidase_CS. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR InterPro; IPR016040; NAD(P)-bd. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Pfam; PF01266; DAO; 1. DR PROSITE; PS00677; DAO; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; FAD; Flavoprotein; KW Oxidoreductase. FT CHAIN 1 334 D-aspartate oxidase 1. FT /FTId=PRO_0000162772. FT NP_BIND 8 22 FAD (Potential). FT ACT_SITE 305 305 By similarity. FT VAR_SEQ 1 222 Missing (in isoform b). FT /FTId=VSP_014356. FT VAR_SEQ 223 228 TFTIPK -> MCQIFR (in isoform b). FT /FTId=VSP_014357. FT VAR_SEQ 268 273 EPKIIK -> VRISFF (in isoform b). FT /FTId=VSP_014358. FT VAR_SEQ 274 334 Missing (in isoform b). FT /FTId=VSP_014359. SQ SEQUENCE 334 AA; 37608 MW; 90B1731A702BB6FD CRC64; MANIIPKIAI IGEGVIGCTS ALQISKAIPN AKITVLHDKP FKKSCSAGPA GLFRIDYEEN TEYGRASFAW FSHLYRTTKG SETGVKLVSG HIQSDNLESL KQQQRAYGDI VYNFRFLDDR ERLDIFPEPS KHCIHYTAYA SEGNKYVPYL KNLLLEQKIE FKQQEVTSLD AVADAGYDVI VNCAGLYGGK LAGDDDTCYP IRGVILEVDA PWHKHFNYRD FTTFTIPKEH SVVVGSTKQD NRWDLEITDE DRNDILKRYI ALHPGMREPK IIKEWSALRP GRKHVRIEAQ KRTSVGNSKD YMVVHHYGHG SNGFTLGWGT AIEATKLVKT ALGL //