ID   DADA2_PSEPK             Reviewed;         434 AA.
AC   Q88CB1;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   16-JUN-2009, entry version 42.
DE   RecName: Full=D-amino acid dehydrogenase 2 small subunit;
DE            EC=1.4.99.1;
GN   Name=dadA2; Synonyms=dadA-2; OrderedLocusNames=PP_5270;
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   -!- 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.
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DR   EMBL; AE015451; AAN70835.1; -; Genomic_DNA.
DR   RefSeq; NP_747371.1; -.
DR   GeneID; 1042325; -.
DR   GenomeReviews; AE015451_GR; PP_5270.
DR   KEGG; ppu:PP_5270; -.
DR   NMPDR; fig|160488.1.peg.5201; -.
DR   TIGR; PP_5270; -.
DR   HOGENOM; Q88CB1; -.
DR   OMA; Q88CB1; MFQKHAP.
DR   BioCyc; PPUT160488:PP_5270-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   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    434       D-amino acid dehydrogenase 2 small
FT                                subunit.
FT                                /FTId=PRO_0000166141.
FT   NP_BIND       3     17       FAD (Potential).
SQ   SEQUENCE   434 AA;  47399 MW;  1A05E3D265711D44 CRC64;
     MRVLVLGSGV IGTASAYYLA RQGFEVTVVD RQPAVAMETS FANAGQISPG YASPWAAPGV
     PLKAIKWLLE RHAPLAIKLT GDVDQYLWMA QMLRNCTASR YAVNKERMVR LSEYSRDCLD
     ELRAETGINY ENRSLGTTQL FRTQAQVDAA AKDIAVLEQS GVPYELLDRD GIARVEPALA
     GVKDILAGAL RLPNDQTGDC QLFTTKLADM ALKLGVEFRF GQDIQRLDFA GDRINGVWID
     GKLETADRYV LALGSYSPQM LKPLGIKAPV YPLKGYSLTV PITNSDMAPT STILDETYKV
     AITRFDNRIR VGGMAEIAGF DLSLNPRRRE TLEMIVNDLY PRGGDLSQAS FWTGLRPATP
     DGTPIVGATA FRNLFLNTGH GTLGWTMACG SGRLLADLIA RKKPQISAEG LDISRYGNSR
     EVAKHGQSAP AHQQ
//