ID   DADA_MAGSA              Reviewed;         422 AA.
AC   Q2W3H2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=amb2799;
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=342108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(2005).
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; AP007255; BAE51603.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2W3H2; -.
DR   SMR; Q2W3H2; -.
DR   STRING; 342108.amb2799; -.
DR   PRIDE; Q2W3H2; -.
DR   EnsemblBacteria; BAE51603; BAE51603; amb2799.
DR   KEGG; mag:amb2799; -.
DR   HOGENOM; CLU_007884_9_2_5; -.
DR   OMA; EPWANPS; -.
DR   OrthoDB; 573710at2; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000007058; 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..422
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_1000066098"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ   SEQUENCE   422 AA;  45716 MW;  839D83EBBDCC218F CRC64;
     MKVVVIGAGV VGTASAWYLA KAGHEVTVVD RREGAGLETS FANGGQISPC HAEPWANPSV
     LPKVLKWLGR EDAPLLFRWN RWDPALWAWG LRFLANCSRS RAEINTERTL RVALYSRACL
     GELRAETGIA YDQQVRGILH VYRDGAEFEH ACRAAEVMIR HGLRRLPRTP AECTAIEPAL
     GAVQGELAGG IYTPDDESGD AHKFTRELAA LAAAKGVEFR WNVPIQSLLA DGDRVAGLAT
     SDGTIRAESY VLAAGCDSPL LARPLGLRLP IIPAKGYSVT VPVDNHAGAP LVSITDDEHK
     MVYSRLGDRL RAAGTAEMAG YDRMPNPVRN RLILDNARRL FPDGGDFDRA EPWAGLRPVT
     PDSVPLLGAT PLRNLWLNTG HGTLGWTMSC GSGRIVADLV SGRPSAISMD GLGIDRFTSY
     LW