DADA_YERPY
ID DADA_YERPY Reviewed; 434 AA.
AC B1JLH4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=YPK_2107;
OS Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YPIII;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000950; ACA68393.1; -; Genomic_DNA.
DR RefSeq; WP_012304098.1; NZ_CP009792.1.
DR AlphaFoldDB; B1JLH4; -.
DR SMR; B1JLH4; -.
DR EnsemblBacteria; ACA68393; ACA68393; YPK_2107.
DR KEGG; ypy:YPK_2107; -.
DR PATRIC; fig|502800.11.peg.2782; -.
DR OMA; FWYKEDG; -.
DR UniPathway; UPA00043; UER00498.
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_1000138679"
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; 47234 MW; 75687CB371EC3345 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 SVARYRTGFQ
PLNIAPLHDI HPIR