ID   DADA_SINMW              Reviewed;         416 AA.
AC   A6UB96;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-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=Smed_2093;
OS   Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=366394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM419;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA   Richardson P.;
RT   "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL   Submitted (JUN-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; CP000738; ABR60926.1; -; Genomic_DNA.
DR   RefSeq; WP_011976223.1; NC_009636.1.
DR   RefSeq; YP_001327761.1; NC_009636.1.
DR   AlphaFoldDB; A6UB96; -.
DR   SMR; A6UB96; -.
DR   STRING; 366394.Smed_2093; -.
DR   EnsemblBacteria; ABR60926; ABR60926; Smed_2093.
DR   GeneID; 61613003; -.
DR   KEGG; smd:Smed_2093; -.
DR   PATRIC; fig|366394.8.peg.5251; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_9_2_5; -.
DR   OMA; NDLYPRG; -.
DR   OrthoDB; 573710at2; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000001108; 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.
FT   CHAIN           1..416
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_1000066120"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ   SEQUENCE   416 AA;  44828 MW;  77DDA7D0EB49BFD5 CRC64;
     MKVIVLGAGI IGVTSAYQLS RAGHEVTVID RQPGPALETS FANAGEVSFG YCSPWAAPGI
     PMKALKWLFM QHAPLILRPR IDAAMLSWMA KMLSNCTSRR YAVNKSRMLR LADYSRTSLA
     ALREETAITY DERMQGTLQL FRTEAQLDAS AKDISALAAD GIPYEVLDRD GCIRAEPALG
     RVRDKIVGGL LTPQDETGDC FKFANALAGR AEKLGVCFDY GTEIRALEVD GGRVHGVVTS
     KGRRAADAVV VALGSYSPLL VRRFGIRLPV YPVKGYSLTI PIADASRAPV STVMDETYKI
     AITRLGDRIR VGGMAEISGY TNDLGIARRR TLEHSVMDLF PGGDAAKGSF WSGLRPMTPD
     GTPVIGPTRI AGLFLNTGHG TLGWTMSSGS ARVIADLVSD RKLEIDATDL AIARYG