ID   DADA_CITK8              Reviewed;         432 AA.
AC   A8AFS0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=CKO_01193;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) 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; CP000822; ABV12333.1; -; Genomic_DNA.
DR   RefSeq; WP_012132085.1; NC_009792.1.
DR   AlphaFoldDB; A8AFS0; -.
DR   SMR; A8AFS0; -.
DR   STRING; 290338.CKO_01193; -.
DR   PRIDE; A8AFS0; -.
DR   EnsemblBacteria; ABV12333; ABV12333; CKO_01193.
DR   GeneID; 45135322; -.
DR   KEGG; cko:CKO_01193; -.
DR   HOGENOM; CLU_007884_9_2_6; -.
DR   OMA; FWYKEDG; -.
DR   OrthoDB; 573710at2; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000008148; 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..432
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_1000066088"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ   SEQUENCE   432 AA;  47691 MW;  08083788AF42A7B1 CRC64;
     MRVVILGSGV VGVTSAWYLC QAGHDVTVID REPGPALETS AANAGQISPG YAAPWAAPGV
     PLKAIKWMFQ RHAPLAVRLD GTQFQLKWMW QMLRNCDTRH YMENKGRMVR LAEYSRDCLK
     ALRASTGIQY EGRQGGTLQL FRTAQQYENA TRDIAVLEDA GVPYQLLESS RLAEVEPALA
     EVAHKLTGGL RLPNDETGDC QLFTQRLAQM AEQAGVTFRF NTPVEKLLYE GEQIYGVKCG
     DDIIKADAYV MAFGSYSTAM LKGIVDIPVY PLKGYSLTIP VAQDDGAPVS TILDETYKIA
     ITRFDKRIRV GGMAEIVGFN TELLQPRRET LEMVVRDLFP RGGHVEQATF WTGLRPMTPD
     GTPVIGRTRF KNLWLNTGHG TLGWTMACGS GQLLSDILSG RTPAIPYDDL SVARYSPGFT
     PSRPRHLHGA HN