ID   DADA_PROMH              Reviewed;         434 AA.
AC   B4EXU2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=PMI1509;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(2008).
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; AM942759; CAR43171.1; -; Genomic_DNA.
DR   RefSeq; WP_004243273.1; NC_010554.1.
DR   AlphaFoldDB; B4EXU2; -.
DR   SMR; B4EXU2; -.
DR   STRING; 529507.PMI1509; -.
DR   PRIDE; B4EXU2; -.
DR   EnsemblBacteria; CAR43171; CAR43171; PMI1509.
DR   GeneID; 6801033; -.
DR   KEGG; pmr:PMI1509; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_9_2_6; -.
DR   OMA; FWYKEDG; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000008319; 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"
FT                   /id="PRO_1000138661"
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;  47717 MW;  E371796447B1BBE6 CRC64;
     MKVIILGGGV IGVTSAWYLV QQGHEVIVVD RQSSAAEETS AGNAGQISPG YATPWGAPGI
     PLKAVKWMFQ KHAPLAIRPD GSLFQLRWMW QMLRNCDASH YAMNKSRMVR IAEYSRDCIR
     QLRQDTGIEY EGRQGGTLQL FRDQKQFDNA ANDIAVLKQE GVAYELLTAE QLKSAEPALE
     HVSHKLTGGL RLPNDETGDC QIFTKKLAKM AEEAGVTFLF NKEIKHLLFD GDKVTGVQCH
     DGLLTADHYV VAMGSYSTEF LKNKITIPVY PLKGYSLTMP IIDASRAPTS TILDETYKIA
     VTRFDNRIRV GGMAEVVGFN LNILKSRCET LKMVVQDLYE GGGDISKATF WTGLRPMTPD
     GTPIVGPTAY RNLSLNTGHG TLGWTMACGS GQLLADLISG NKTAIAADDL SVFRYIDGFN
     TKLLRPGQKL DAVY