ID DADA_BURXL Reviewed; 429 AA. AC Q13VE3; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 16-JUN-2009, entry version 21. DE RecName: Full=D-amino acid dehydrogenase small subunit; DE EC=1.4.99.1; GN Name=dadA; OrderedLocusNames=Bxeno_A3408; ORFNames=Bxe_A1001; OS Burkholderia xenovorans (strain LB400). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=266265; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17030797; DOI=10.1073/pnas.0606924103; RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L., RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., RA Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., RA Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M., RA Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., RA Tiedje J.M.; RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp RT genome shaped for versatility."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006). CC -!- FUNCTION: Oxidative deamination of D-amino acids (By similarity). CC -!- CATALYTIC ACTIVITY: A D-amino acid + H(2)O + acceptor = a 2-oxo CC acid + NH(3) + reduced acceptor. CC -!- COFACTOR: FAD (By similarity). CC -!- PATHWAY: Amino-acid degradation; D-alanine degradation; NH(3) and CC pyruvate from D-alanine: step 1/1. CC -!- SUBUNIT: Heterodimer of a small and a large subunit (By CC similarity). CC -!- SIMILARITY: Belongs to the dadA oxidoreductase 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; CP000270; ABE31946.1; -; Genomic_DNA. DR RefSeq; YP_559998.1; -. DR GeneID; 4003991; -. DR GenomeReviews; CP000270_GR; Bxeno_A3408. DR KEGG; bxe:Bxe_A1001; -. DR HOGENOM; Q13VE3; -. DR OMA; Q13VE3; MFQKHAP. DR GO; GO:0008718; F:D-amino-acid dehydrogenase activity; IEA:HAMAP. DR GO; GO:0006524; P:alanine catabolic process; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_01202; -; 1. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR Pfam; PF01266; DAO; 1. PE 3: Inferred from homology; KW Complete proteome; FAD; Flavoprotein; Oxidoreductase. FT CHAIN 1 429 D-amino acid dehydrogenase small subunit. FT /FTId=PRO_1000066086. FT NP_BIND 3 17 FAD (Potential). SQ SEQUENCE 429 AA; 46194 MW; CDB9833D372207EB CRC64; MRVVVLGSGV VGVTSAYYLA RAGHEVTVID REAGPALETS FANAGQISPG YASPWAAPGV PLKAVKWMFQ KHAPLAIRLD GTQFQLQWMW QMLQNCTSSR YAVNKGRMVR LAEYSRDCLQ ALRAETGIQY EGRTGGTLQV FRTQQQFEGA AKDIAVLREA SVPYELLSPA ELAQAEPALA AVSHKLTGGL RLPGDETGDC QMFTTRLAAL AEQLGVKFRY NTPIDALAMA GDRIAGVKCG EELVRADSFV VALGSYSTQF LSGLVKIPVY PLKGYSITAP IVNEASAPVS TVLDETYKIA ITRFDDRIRV GGMAEIVGFD KSLREARRET LELCVNDLFP GGGDTSKATF WSGLRPMTPD GTPIVGRTPV ANLFLNTGHG TLGWTMSCGS GQLLADVMSG KQPAIKADDL SVHRYLGETR GAHRPAYAA //