ID   DADA_ECOL6              Reviewed;         432 AA.
AC   P0A6J6; P29011;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   16-JUN-2009, entry version 32.
DE   RecName: Full=D-amino acid dehydrogenase small subunit;
DE            EC=1.4.99.1;
GN   Name=dadA; Synonyms=dadR; OrderedLocusNames=c1638;
OS   Escherichia coli O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
RX   MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(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   -!- 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   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane
CC       protein (By similarity).
CC   -!- INDUCTION: By alanine.
CC   -!- SIMILARITY: Belongs to the dadA oxidoreductase family.
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DR   EMBL; AE014075; AAN80103.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_753543.2; -.
DR   GeneID; 1035409; -.
DR   GenomeReviews; AE014075_GR; c1638.
DR   KEGG; ecc:c1638; -.
DR   HOGENOM; P0A6J6; -.
DR   OMA; P0A6J6; MFQKHAP.
DR   BRENDA; 1.4.99.1; 292881.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Cell inner membrane; Cell membrane; Complete proteome; FAD;
KW   Flavoprotein; Membrane; Oxidoreductase.
FT   CHAIN         1    432       D-amino acid dehydrogenase small subunit.
FT                                /FTId=PRO_0000166132.
FT   NP_BIND       3     17       FAD (Potential).
SQ   SEQUENCE   432 AA;  47607 MW;  EE747358845B6280 CRC64;
     MRVVILGSGV VGVASAWYLN QAGHEVTVID REPGAALETS AANAGQISPG YAAPWAAPGV
     PLKAIKWMFQ RHAPLAVRLD GTQFQLKWMW QMLRNCDTSH YMENKGRMVR LAEYSRDCLK
     ALRAETNIQY EGRQGGTLQL FRTEQQYENA TRDIAVLEDA GVPYQLLESS RLAEVEPALA
     EVAHKLTGGL QLPNDETGDC QLFTQNLARM AEQAGVKFRF NTPVDQLLCD GEQIYGVKCG
     DEVIKADAYV MAFGSYSTAM LKGIVDIPVY PLKGYSLTIP IAQEDGAPVS TILDETYKIA
     ITRFDNRIRV GGMAEIVGFN TELLQPRRET LEMVVRDLYP RGGHVEQATF WTGLRPMTPD
     GTPVVGRTRF KNLWLNTGHG TLGWTMACGS GQLLSDLLSG RTPAIPYEDL SVARYSRGFT
     PSRPGHLHGA HS
//