ID   DADA1_PSEPK             Reviewed;         432 AA.
AC   Q88EM0;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   04-NOV-2008, entry version 35.
DE   RecName: Full=D-amino acid dehydrogenase 1 small subunit;
DE            EC=1.4.99.1;
GN   Name=dadA1; Synonyms=dadA-1; OrderedLocusNames=PP_4434;
OS   Pseudomonas putida (strain KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22423060; PubMed=12534463;
RX   DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M.,
RA   Hance I., Chris Lee P., Holtzapple E.K., Scanlan D., Tran K.,
RA   Moazzez A., Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D.,
RA   Wedler H., Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S.,
RA   Kiewitz C., Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B.,
RA   Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the
RT   metabolically versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(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.
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DR   EMBL; AE015451; AAN70011.1; -; Genomic_DNA.
DR   RefSeq; NP_746547.1; -.
DR   GeneID; 1041878; -.
DR   GenomeReviews; AE015451_GR; PP_4434.
DR   KEGG; ppu:PP_4434; -.
DR   NMPDR; fig|160488.1.peg.4377; -.
DR   TIGR; PP_4434; -.
DR   HOGENOM; Q88EM0; -.
DR   BioCyc; PPUT160488:PP_4434-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   InterPro; IPR003042; Rng_hydrolase.
DR   Pfam; PF01266; DAO; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
PE   3: Inferred from homology;
KW   Complete proteome; FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN         1    432       D-amino acid dehydrogenase 1 small
FT                                subunit.
FT                                /FTId=PRO_0000166140.
FT   NP_BIND       3     17       FAD (Potential).
SQ   SEQUENCE   432 AA;  47155 MW;  4D1B8B220915C751 CRC64;
     MRVLILGSGV VGTVSAYYLA REGFEVVVVD RQDGPAMETS FANAGQVSPG YASPWSAPGV
     PLKAIRWMLQ QHAPLAIKPT SSLDQYRWMI QMLRNCNPAS YAVNKERMVR ISEYSRDCLD
     ELRAETGISY EARQLGTTQL FRTQAQVDNA AKDIAILKQS GVPFELLDRD GIAKAEPALA
     SVRDKLAGAL RLPNDQTGDC QMFTRKLAKM AEELGVEFRF GCNIDRLECS GDTISGVWID
     GKLEVADQYV LALGSYSPHM LKPLGIQAPI YPLKGYSLTI PITDASMAPS STILDETYKV
     AITRFDDRIR VGGMAEIAGF DLSLNARRRD TLELVVGDLY PKGGDLTKAT FWTGLRPATP
     DGTPIVGKTK YRNLFLNTGH GTLGWTMSCG SGRLLADLMA GKKPKISAKG LDISRYSNQK
     EAHNHGNPAT AL
//