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   03-AUG-2022, entry version 100.
DE   RecName: Full=D-amino acid dehydrogenase 1;
DE            EC=1.4.99.-;
GN   Name=dadA1; Synonyms=dadA-1; OrderedLocusNames=PP_4434;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; 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., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
CC   -!- FUNCTION: Oxidative deamination of D-amino acids. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + a D-alpha-amino acid + H2O = a 2-oxocarboxylate + AH2 +
CC         NH4(+); Xref=Rhea:RHEA:18125, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC         ChEBI:CHEBI:59871;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the DadA oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AE015451; AAN70011.1; -; Genomic_DNA.
DR   RefSeq; NP_746547.1; NC_002947.4.
DR   RefSeq; WP_010955142.1; NC_002947.4.
DR   AlphaFoldDB; Q88EM0; -.
DR   SMR; Q88EM0; -.
DR   STRING; 160488.PP_4434; -.
DR   EnsemblBacteria; AAN70011; AAN70011; PP_4434.
DR   KEGG; ppu:PP_4434; -.
DR   PATRIC; fig|160488.4.peg.4715; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_9_2_6; -.
DR   OMA; FWYKEDG; -.
DR   PhylomeDB; Q88EM0; -.
DR   BioCyc; PPUT160488:G1G01-4715-MON; -.
DR   Proteomes; UP000000556; Chromosome.
DR   GO; GO:0008718; F:D-amino-acid dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; -; 2.
DR   HAMAP; MF_01202; DadA; 1.
DR   InterPro; IPR023080; DadA.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..432
FT                   /note="D-amino acid dehydrogenase 1"
FT                   /id="PRO_0000166140"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
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