ID   DADA_NEIMB              Reviewed;         418 AA.
AC   Q9K1H5;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   16-JUN-2009, entry version 51.
DE   RecName: Full=D-amino acid dehydrogenase small subunit;
DE            EC=1.4.99.1;
GN   Name=dadA; OrderedLocusNames=NMB0176;
OS   Neisseria meningitidis serogroup B.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58 / Serogroup B;
RX   MEDLINE=20175755; PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C.,
RA   Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F.,
RA   Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D.,
RA   Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D.,
RA   Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E.,
RA   Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M.,
RA   Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M.,
RA   Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R.,
RA   Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
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; AE002098; AAF40633.1; -; Genomic_DNA.
DR   PIR; A81228; A81228.
DR   RefSeq; NP_273234.1; -.
DR   GeneID; 902283; -.
DR   GenomeReviews; AE002098_GR; NMB0176.
DR   KEGG; nme:NMB0176; -.
DR   NMPDR; fig|122586.1.peg.168; -.
DR   TIGR; NMB0176; -.
DR   HOGENOM; Q9K1H5; -.
DR   OMA; Q9K1H5; MFQKHAP.
DR   BioCyc; NMEN122586:NMB_0176-MON; -.
DR   BRENDA; 1.4.99.1; 293828.
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    418       D-amino acid dehydrogenase small subunit.
FT                                /FTId=PRO_0000166136.
FT   NP_BIND       3     17       FAD (Potential).
SQ   SEQUENCE   418 AA;  46535 MW;  E50C13F9DFBC214D CRC64;
     MKVLVLGAGV AGVSSAWYLA EAGHEVTVID RAEGVAMETS FANAGQLSYG YTTPWAAPGI
     PTKALKWLFK SHPPLLFRPD GSLYQIEWLW QMLQNCTAAH YQTNKERMVR ISEYSREMFR
     RFEAQTGMNF EGRKKGTLQI FRQTKEVEAA KQDIAVLERY GVPYRRLKPE ECAEFEPALA
     RVTAKIAGGL HLPADATGDC RLFTENLYKL CQEKGVRFHF NQNISRIDHN GLRIKTVETE
     TGRFEADAVV CALGCFSRTV LAQLDLNLPI YPVKGYSLTL PVTNSDGAPV STVLDESYKV
     AITRFDNRIR VGGMAELSGY EIKLPEKRRE TLALVVNDLF PEGGDLSQAS FWSGLRPMTP
     DSTPLIGRTR FDNLFLNTGH GTLGWTMSLG SAKLTADIVS GKDTEIRSDD LSLSRYQA
//