ID   DADA_VIBCH              Reviewed;         421 AA.
AC   Q9KTV1;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=VC_0786;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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   -!- SIMILARITY: Belongs to the DadA oxidoreductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01202}.
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DR   EMBL; AE003852; AAF93951.1; -; Genomic_DNA.
DR   PIR; F82279; F82279.
DR   RefSeq; NP_230435.1; NC_002505.1.
DR   AlphaFoldDB; Q9KTV1; -.
DR   SMR; Q9KTV1; -.
DR   STRING; 243277.VC_0786; -.
DR   DNASU; 2615329; -.
DR   EnsemblBacteria; AAF93951; AAF93951; VC_0786.
DR   KEGG; vch:VC_0786; -.
DR   PATRIC; fig|243277.26.peg.748; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_9_2_6; -.
DR   OMA; FWYKEDG; -.
DR   BioCyc; VCHO:VC0786-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0008718; F:D-amino-acid dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0055130; P:D-alanine catabolic process; IBA:GO_Central.
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..421
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_0000166152"
FT   BINDING         4..18
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ   SEQUENCE   421 AA;  46267 MW;  C7233E7FC87FBBB4 CRC64;
     MMEVLVLGSG VVGLTSAWYL AQAGHDVTVV DRQPRGAEET SFANAGQISY GYSSPWAAPG
     IPQKALKWML EKHAPLKIQP SLDPALLSWM GKMLLNCQLS RYQVNKSRML AIANYSRECL
     KALNQTYSLD YQGRQRGTLQ VFRDEKQLTA IEKDMQLLAQ SGVRFELLNV AQCLTHEPGL
     APVQEKLVGG LWLPDDETGD CYLFCQQLTE LAKQQGVRFH FDCHIQQLVC EGKKIIGVQT
     DLGLLKADAY VVALGSYSTS LLKPLGIEIP VYPVKGYSLT LPIIDEKFAP QSTVMDETYK
     VALTRFSDRI RVAGTAELAG FDPAIPEARK ATIEMVARDL FPHGGDFAKG QFWTGFRPMT
     PDGTPIIGAT PYTNLYTNTG HGTLGWTMAC GSASILADVL THGESPLSRL GLDLFRYPKA
     S