ID   DADA_DECAR              Reviewed;         418 AA.
AC   Q479B1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=Daro_3842;
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC   Dechloromonas.
OX   NCBI_TaxID=159087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCB;
RX   PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA   Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA   Lapidus A.;
RT   "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT   indications of a surprisingly complex life-style and cryptic anaerobic
RT   pathways for aromatic degradation.";
RL   BMC Genomics 10:351-351(2009).
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; CP000089; AAZ48570.1; -; Genomic_DNA.
DR   RefSeq; WP_011289565.1; NC_007298.1.
DR   AlphaFoldDB; Q479B1; -.
DR   SMR; Q479B1; -.
DR   STRING; 159087.Daro_3842; -.
DR   EnsemblBacteria; AAZ48570; AAZ48570; Daro_3842.
DR   KEGG; dar:Daro_3842; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_9_2_4; -.
DR   OMA; EPWANPS; -.
DR   OrthoDB; 573710at2; -.
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..418
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_1000066089"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ   SEQUENCE   418 AA;  45831 MW;  03A283AF0EA0CD3B CRC64;
     MRVLVLGAGV VGTTSAWYLA RAGHQVTVVD RQPVAGNETS FANGGQISVS HAEPWANPHV
     LPRVLKWLGR EDAPLLWRWR ADPAQLAWGL RFLGECFPGR VRRNIAAIVS MALYSRGRLQ
     ALREELGLQY DHLERGILHI YTDRDEFSAA LDAARVMRQF GLDRDTVDVD KCLEIEPALS
     GARHLLVGGD YTRSDESGDA NKFTCALAEH AKAAGVDFRY GLTVERIATS GSEIVGVLVQ
     HSEGGPERLT ADAYVVALGS YSPLLLRPIG VGLPVYPAKG YSATLTLAEA SLAPTVSLTD
     DERKLVFSRL GNRLRIAGTA EFNGYNLELN PVRCQALIDR TRQLFPRLEI VGEPTLWCGL
     RPATPSNVPY IGQTRYRNLW LNTGHGTLGW TMACGSAASL AEMISGRRPE PEFPFLRC