ID   DADA_SPHWW              Reviewed;         416 AA.
AC   A5V4F9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   16-JUN-2009, entry version 17.
DE   RecName: Full=D-amino acid dehydrogenase small subunit;
DE            EC=1.4.99.1;
GN   Name=dadA; OrderedLocusNames=Swit_0808;
OS   Sphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=392499;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Halden R.U., Miller T.R.,
RA   Salzberg S.L., Eisen J.A., Richardson P.;
RT   "Complete sequence of chromosome of Sphingomonas wittichii RW1.";
RL   Submitted (MAY-2007) 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; CP000699; ABQ67175.1; -; Genomic_DNA.
DR   RefSeq; YP_001261313.1; -.
DR   GeneID; 5197426; -.
DR   GenomeReviews; CP000699_GR; Swit_0808.
DR   KEGG; swi:Swit_0808; -.
DR   NMPDR; fig|392499.4.peg.1129; -.
DR   OMA; A5V4F9; MFQKHAP.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
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   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
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_1000066121.
FT   NP_BIND       3     17       FAD (Potential).
SQ   SEQUENCE   416 AA;  44460 MW;  A19CFEBF99022256 CRC64;
     MKVVILGAGV IGVTSAWYLA RAGHEVVVVD RQDGPALETS FANAGEISPG YASPWAAPGI
     PAKALRWLFM RHAPLIVRPG FDPAMVRWLV AMLGNCTARA YRVNKGRMVR LAEFSRDRLI
     ELRQETGIRY DERSQGTLQL FRREKDLAGV AKDIEVLKAD GVPFELLDAA GCIAAEPGLA
     NSASPIAGGL RLPNDETGDC FKFTNALAEL AKAEGVRFVL GRRIDAIVAS GNRIAHVRTD
     RGDISGDAYL VALGSHSPLL LSPLGIRLPV YPVKGYSITV PIVDPARAPV STLLDESFKV
     AITRLGDRIR VGGMAEISGY SNDLPPARRA TLDHCVGSLF PDAGDLSQAS FWTGLRPMTP
     DGTPVIGATG YRNLFLNTGH GTLGWTMACG SGHVIADIIG GKRPAIETGD LAIDRY
//