ID   DADA_ACIB5              Reviewed;         421 AA.
AC   B7I1Q9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 72.
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};
GN   OrderedLocusNames=AB57_0138;
OS   Acinetobacter baumannii (strain AB0057).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=480119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB0057;
RX   PubMed=18931120; DOI=10.1128/jb.00834-08;
RA   Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA   MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA   Bonomo R.A., Gill S.R.;
RT   "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT   baumannii.";
RL   J. Bacteriol. 190:8053-8064(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; Evidence={ECO:0000255|HAMAP-
CC         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; CP001182; ACJ39569.1; -; Genomic_DNA.
DR   RefSeq; WP_001263980.1; NC_011586.2.
DR   AlphaFoldDB; B7I1Q9; -.
DR   SMR; B7I1Q9; -.
DR   GeneID; 60877609; -.
DR   KEGG; abn:AB57_0138; -.
DR   HOGENOM; CLU_007884_9_2_6; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000007094; 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; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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   PANTHER; PTHR13847:SF280; D-AMINO ACID DEHYDROGENASE; 1.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..421
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_1000138635"
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;  46426 MW;  D0449A9235CA9AA5 CRC64;
     MRVIVLGSGV IGVASAYYLA RQGAEVTVLD RQSGPAEETS FGNAGQISPG YSTPWAAPGI
     PFKAVKWMFQ HHAPLAINLD GSMWQLQWMA QMLKNCNPQS YAVNKERMMR VAEYSRDCLR
     ELRKDTGIHY ENRAKGTLQL FRKEAQMEAV QRDISVLEEC GVSYELLNGN ELGRVEPALA
     NAQDKLVGGL HLPNDETGDC YLFTNALAQI AKELGVNFQF NQNVEKLIVE GDQIKGVQVN
     GKVLTADRYV LAFGSYSRDF LKPLDLQLPV YPVKGYSLTI PIVDPAFAPQ STVLDETYKI
     AITRFDQRIR VGGMAELSGF NLGLNEDRRA TLQMVTQDLF PGGDMAQASF WTGLRPMTPD
     STPIIGATRF KNLFLNTGHG TLGWTMACGS GKLISDIVLN HKTDISTDGL SIQRYSHAHA
     A
//