ID DADA_BRUSU Reviewed; 416 AA. AC Q8FVC0; DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 16-JUN-2009, entry version 40. DE RecName: Full=D-amino acid dehydrogenase small subunit; DE EC=1.4.99.1; GN Name=dadA; OrderedLocusNames=BRA0924; OS Brucella suis. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=29461; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1330 / Biovar 1; RX MEDLINE=22247741; PubMed=12271122; DOI=10.1073/pnas.192319099; RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., RA Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., RA Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., RA Fraser C.M.; RT "The Brucella suis genome reveals fundamental similarities between RT animal and plant pathogens and symbionts."; RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002). 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 -!- 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; AE014292; AAN34096.1; -; Genomic_DNA. DR RefSeq; NP_700091.1; -. DR GeneID; 1165368; -. DR GenomeReviews; AE014292_GR; BRA0924. DR KEGG; bms:BRA0924; -. DR NMPDR; fig|204722.1.peg.3000; -. DR TIGR; BRA0924; -. DR HOGENOM; Q8FVC0; -. DR OMA; Q8FVC0; MFQKHAP. DR BioCyc; BSUI204722:BR_A0924-MON; -. DR BRENDA; 1.4.99.1; 281610. 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 1 416 D-amino acid dehydrogenase small subunit. FT /FTId=PRO_0000166129. FT NP_BIND 3 17 FAD (Potential). SQ SEQUENCE 416 AA; 45094 MW; 25CF556CD82D0CA5 CRC64; MQITILGSGV IGVTTAYYLA KLGHEVTVID REEGPAPETS FANAGQVSPG YASPWAAPGI PLKAAKWLFQ KHAPLILRLT TDPVQYRWLL QMLANCTDSR YKINKTRMVR VAEYSRDCLI ELRKDTGIEY DQRSQGTLQL FREQYQLDGI GKDIEVLRQD GVPFEVLDRD GCVNVEPALA HAKDKFVGGL RLPNDETGDC FKFTNALAKI AEGLGVKFRF GVNIKSLLMS GGKISGVETS EGIVTAERYV VALGSYTPAL IKALGLNAPI YPVKGYSITA PIVDESRAPV STVLDESYKI AITRLGDRIR VGGMAEVSGF TDDLPAARRA TLDLSVTDLF PGGDLKAATF WSGLRPMTPD STPIIGGTRY DNLFINAGHG TLGWTMACGS GRLLADLISG NKADIRADDL GIARYN //