DADA_YERPS
ID DADA_YERPS Reviewed; 434 AA.
AC Q66AQ6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=D-amino acid dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01202};
DE EC=1.4.99.- {ECO:0000255|HAMAP-Rule:MF_01202};
GN Name=dadA {ECO:0000255|HAMAP-Rule:MF_01202}; OrderedLocusNames=YPTB2074;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
CC -!- FUNCTION: Oxidative deamination of D-amino acids. {ECO:0000255|HAMAP-
CC Rule:MF_01202}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_01202};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01202};
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.
CC {ECO:0000255|HAMAP-Rule:MF_01202}.
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DR EMBL; BX936398; CAH21312.1; -; Genomic_DNA.
DR RefSeq; WP_002211686.1; NZ_CP009712.1.
DR AlphaFoldDB; Q66AQ6; -.
DR SMR; Q66AQ6; -.
DR EnsemblBacteria; CAH21312; CAH21312; YPTB2074.
DR GeneID; 66841493; -.
DR KEGG; ypo:BZ17_390; -.
DR KEGG; yps:YPTB2074; -.
DR PATRIC; fig|273123.14.peg.417; -.
DR OMA; FWYKEDG; -.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000001011; 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.
FT CHAIN 1..434
FT /note="D-amino acid dehydrogenase"
FT /id="PRO_1000066129"
FT BINDING 3..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ SEQUENCE 434 AA; 47204 MW; 75737D0371EC3345 CRC64;
MRVVILGSGV VGVTSAWYLA KEGHDVTVID RQDGPAQETS AGNAGQISPG YAAPWAAPGV
PLKAIKWMFQ RHAPLAIRLD GSSLQLRWMW QMLRNCDTSH YMVNKSRMVR LAEYSRDCLK
DLRAATGIQY EGRQGGTLQL FRTEQQFDNA AKDIAVLDDA GVPYSLLTAE QLATVEPALA
KVAHKLTGGL RLPNDETGDC KLFTERLAKM AEQAGVKFIF NRSVDKLLVE GDQIAGVLCG
DDIIKADAYV VAFGAYSTAL LAGLVSIPVY PLKGYSLTIP ITDPASAPFS TVLDETYKIA
ITRFDDRIRV GGMAEIVGFN TQLAPARRET LEMVVRDLYP HGGDISQAVF WSGLRPMTPD
GTPIVGRTPL KNLYLNTGHG TLGWTMACGS GQLLADIIQG RRPAIVADDL SVARYRAGFQ
PLNIAPLHDI HPIR
