ID DADA_CHRSD Reviewed; 419 AA. AC Q1QXY5; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 05-MAY-2009, entry version 23. DE RecName: Full=D-amino acid dehydrogenase small subunit; DE EC=1.4.99.1; GN Name=dadA; OrderedLocusNames=Csal_1318; OS Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB OS 13768). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Chromohalobacter. OX NCBI_TaxID=290398; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., RA Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N., RA O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R., RA Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D., RA Canovas D., Richardson P.; RT "Complete sequence of Chromohalobacter salexigens DSM 3043."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000285; ABE58673.1; -; Genomic_DNA. DR RefSeq; YP_573372.1; -. DR GeneID; 4027772; -. DR GenomeReviews; CP000285_GR; Csal_1318. DR KEGG; csa:Csal_1318; -. DR NMPDR; fig|290398.4.peg.1308; -. DR HOGENOM; Q1QXY5; -. DR OMA; Q1QXY5; LEHAGGQ. DR BioCyc; CSAL290398:CSAL_1318-MON; -. 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. DR ProDom; PD000139; FAD_pyr_redox; 1. PE 3: Inferred from homology; KW Complete proteome; FAD; Flavoprotein; Oxidoreductase. FT CHAIN 1 419 D-amino acid dehydrogenase small subunit. FT /FTId=PRO_1000066087. FT NP_BIND 3 17 FAD (Potential). SQ SEQUENCE 419 AA; 46286 MW; 462BEA94DCFF7B00 CRC64; MQVLILGSGV VGVTSAYYLA TQGHEVTVVD RREAPAMETS YGNAGQVSFG FSSPWAAPGI PRKALKWMFQ EHAPLKIQPK RDPAMARFMM AMFNNCTPER YAVNKERMVR VAEYSRQCID ALRRDTGIRY EDRQRGLLQL FRHESQVEAA GKDMRVLSEC GVRHRLLGAE ELVTAEPALA RVPGKFVGGL HLPDDQTGDC HLFTQRLAEH CREHLGVTFR FGVDVQRIER QAGRVERVVT SAGSLRADAY VVCLGSFSPL LVKDLDIRLP IYPVKGYSLT LPVTDDGGAP QSTVMDETFK VAISRFDDRI RVGGTAELAS YDLSLLEKRR ATISMVVRDV FPEGGDAAKA EFWTGLRPMT PDSTPIIGAT RYDNLWLNTG HGTLGWTMSC GSAHLLADLM AGRRPAIDPI GLDVSRYAA //