ID   DADA_XANP2              Reviewed;         421 AA.
AC   A7IHQ4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Xaut_2304;
OS   Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Xanthobacter.
OX   NCBI_TaxID=78245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1158 / Py2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT   "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL   Submitted (JUL-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; CP000781; ABS67547.1; -; Genomic_DNA.
DR   RefSeq; WP_012114324.1; NC_009720.1.
DR   AlphaFoldDB; A7IHQ4; -.
DR   SMR; A7IHQ4; -.
DR   STRING; 78245.Xaut_2304; -.
DR   PRIDE; A7IHQ4; -.
DR   EnsemblBacteria; ABS67547; ABS67547; Xaut_2304.
DR   KEGG; xau:Xaut_2304; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_9_2_5; -.
DR   OMA; NDLYPRG; -.
DR   OrthoDB; 573710at2; -.
DR   PhylomeDB; A7IHQ4; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000002417; 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..421
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_1000138674"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ   SEQUENCE   421 AA;  45349 MW;  105D7AEA43AB3A5D CRC64;
     MRILILGSGV VGTASAYYLA KAGHEVTVLD RQRAAGMETS FANAGQVSPG YSAPWAGPGI
     PVKAIKWLLM HHRPLVVWPS LDPKLYLWLA KMLANCTEEA YRRNKARMVA LAEYSRDALD
     ALRSETGIAY DERMLGTLQL FRTRKQLDHV HSDTEVLDAH NVRYELLDPS GCIRAEPALA
     RVRDKFVGGL RLPGDETGDA HIFTRNLADI CARQGVTFRY GVTVEGLRHE AGRITGVALA
     GGEIATADIY VAAMGSYTPA LLAPLGIRLP VYPVKGYSLT LPITDPDAAP RSTVMDETYK
     VAITRLGERI RVGGTAELAG FDLSLREPRR ATLAHSVGDL FPAGGDISKA TFWTGLRPMT
     PDGTPIIGPT KLDNLFTNTG HGTLGWTMAC GSGRVLADLI GGRAPDIDTA DLSVARYAEA
     A