ID   DADA_PHEZH              Reviewed;         426 AA.
AC   B4RBL4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=PHZ_c0060;
OS   Phenylobacterium zucineum (strain HLK1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Phenylobacterium.
OX   NCBI_TaxID=450851;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLK1;
RX   PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA   Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT   "Complete genome of Phenylobacterium zucineum - a novel facultative
RT   intracellular bacterium isolated from human erythroleukemia cell line
RT   K562.";
RL   BMC Genomics 9:386-386(2008).
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; CP000747; ACG76474.1; -; Genomic_DNA.
DR   RefSeq; WP_012520622.1; NC_011144.1.
DR   AlphaFoldDB; B4RBL4; -.
DR   SMR; B4RBL4; -.
DR   STRING; 450851.PHZ_c0060; -.
DR   PRIDE; B4RBL4; -.
DR   EnsemblBacteria; ACG76474; ACG76474; PHZ_c0060.
DR   KEGG; pzu:PHZ_c0060; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_9_2_5; -.
DR   OMA; FWYKEDG; -.
DR   OrthoDB; 573710at2; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000001868; 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..426
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_1000138660"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ   SEQUENCE   426 AA;  45586 MW;  603C64F9A0669FFD CRC64;
     MKVVVLGAGV IGVTTAWYLA KAGHEVVVLE RQDGAALETS FANAGEISPG YASPWASPGV
     PRKAPKWLLA RHAPLIVRPS LDPALLSWLL AMLRNCTTER YLANKARMVR LAEHSRDCLI
     ALRRETGIQY DQRSRGTLQV FRTQAQMDEA GKDMEVLRDL GVPYELLDRL GCIAREPGLG
     HARDTIVGGL RLPNDETGDC FKFTTALADL CRGQGVDFRF GTTIQGLETA GGEVGGVRTP
     GGTVTGDAYV VCLGSYSEPF LRPHGIRTGV YPVKGYSLTA TITDEAKAPV STLLDETYKV
     AITRLGDRVR IGGLAELAGY DLSLRPSRRA TLEHSAGSLF GGSCDLPSAT FWCGLRPMTP
     TSTPRIGEAP LRRLFLNTGH GTLGWTMACG SAQVLADAVG RQAPALDLTD YAVPGSPAAE
     PLRRAA