ID OXDD_BOVIN Reviewed; 341 AA. AC P31228; O02846; Q9TRA3; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 2. DT 25-NOV-2008, entry version 57. DE RecName: Full=D-aspartate oxidase; DE Short=DASOX; DE EC=1.4.3.1; DE AltName: Full=DDO; GN Name=DDO; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Kidney cortex; RX MEDLINE=97220379; PubMed=9148742; RA Simonic T., Duga S., Negri A., Tedeschi G., Malcovati M., RA Tenchini M.L., Ronchi S.; RT "cDNA cloning and expression of the flavoprotein D-aspartate oxidase RT from bovine kidney cortex."; RL Biochem. J. 322:729-735(1997). RN [2] RP PROTEIN SEQUENCE OF 1-338. RC TISSUE=Kidney; RX MEDLINE=92291057; PubMed=1601857; RA Negri A., Ceciliani F., Tedeschi G., Simonic T., Ronchi S.; RT "The primary structure of the flavoprotein D-aspartate oxidase from RT beef kidney."; RL J. Biol. Chem. 267:11865-11871(1992). CC -!- CATALYTIC ACTIVITY: D-aspartate + H(2)O + O(2) = oxaloacetate + CC NH(3) + H(2)O(2). CC -!- COFACTOR: FAD or 6-hydroxyflavin adenine dinucleotide. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Peroxisome. CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family. 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; X95310; CAA64622.1; -; mRNA. DR PIR; A44132; A44132. DR RefSeq; NP_776333.1; -. DR UniGene; Bt.25930; -. DR HSSP; P00371; 1AN9. DR Ensembl; ENSBTAG00000033367; Bos taurus. DR GeneID; 280763; -. DR KEGG; bta:280763; -. DR HOVERGEN; P31228; -. DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW. 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: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 Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase; KW Peroxisome. FT CHAIN 1 341 D-aspartate oxidase. FT /FTId=PRO_0000162769. FT NP_BIND 6 20 FAD (Potential). FT MOTIF 339 341 Microbody targeting signal (Potential). FT ACT_SITE 223 223 By similarity. FT ACT_SITE 302 302 By similarity. FT MOD_RES 1 1 Blocked amino end (Met). FT VARIANT 228 228 V -> I (in some molecules). FT CONFLICT 274 274 K -> R (in Ref. 2; AA sequence). FT CONFLICT 283 283 S -> G (in Ref. 2; AA sequence). SQ SEQUENCE 341 AA; 37660 MW; 355EF4EE42C53B49 CRC64; MDTVRIAVVG AGVMGLSTAV CISKMVPGCS ITVISDKFTP ETTSDVAAGM LIPPTYPDTP IQKQKQWFKE TFDHLFAIVN SAEAEDAGVI LVSGWQIFQS IPTEEVPYWA DVVLGFRKMT KDELKKFPQH VFGHAFTTLK CEGPAYLPWL QKRVKGNGGL ILTRRIEDLW ELHPSFDIVV NCSGLGSRQL AGDSKIFPVR GQVLKVQAPW VKHFIRDSSG LTYIYPGVSN VTLGGTRQKG DWNLSPDAEI SKEILSRCCA LEPSLRGAYD LREKVGLRPT RPSVRLEKEL LAQDSRRLPV VHHYGHGSGG IAMHWGTALE ATRLVNECVQ VLRTPAPKSK L //