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