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DADA2_PSEPK
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   03-AUG-2022, entry version 104.
DE   RecName: Full=D-amino acid dehydrogenase 2;
DE            EC=1.4.99.-;
GN   Name=dadA2; Synonyms=dadA-2; OrderedLocusNames=PP_5270;
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   -!- PATHWAY: Amino-acid degradation; D-alanine degradation; NH(3) and
CC       pyruvate from D-alanine: step 1/1.
CC   -!- SIMILARITY: Belongs to the DadA oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AE015451; AAN70835.1; -; Genomic_DNA.
DR   RefSeq; NP_747371.1; NC_002947.4.
DR   RefSeq; WP_010955780.1; NC_002947.4.
DR   AlphaFoldDB; Q88CB1; -.
DR   SMR; Q88CB1; -.
DR   STRING; 160488.PP_5270; -.
DR   EnsemblBacteria; AAN70835; AAN70835; PP_5270.
DR   KEGG; ppu:PP_5270; -.
DR   PATRIC; fig|160488.4.peg.5623; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_9_2_6; -.
DR   OMA; NDLYPRG; -.
DR   PhylomeDB; Q88CB1; -.
DR   BioCyc; PPUT160488:G1G01-5628-MON; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000000556; Chromosome.
DR   GO; GO:0008718; F:D-amino-acid dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0055130; P:D-alanine catabolic process; IEA:UniProtKB-UniPathway.
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..434
FT                   /note="D-amino acid dehydrogenase 2"
FT                   /id="PRO_0000166141"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
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
 
 
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