DADA_ACIAD
ID DADA_ACIAD Reviewed; 419 AA.
AC Q6FFR5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=ACIAD0115;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG67092.1; -; Genomic_DNA.
DR RefSeq; WP_004930721.1; NC_005966.1.
DR AlphaFoldDB; Q6FFR5; -.
DR SMR; Q6FFR5; -.
DR STRING; 62977.ACIAD0115; -.
DR EnsemblBacteria; CAG67092; CAG67092; ACIAD0115.
DR GeneID; 45232637; -.
DR KEGG; aci:ACIAD0115; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_9_2_6; -.
DR OMA; FWYKEDG; -.
DR OrthoDB; 573710at2; -.
DR BioCyc; ASP62977:ACIAD_RS00535-MON; -.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000000430; 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..419
FT /note="D-amino acid dehydrogenase"
FT /id="PRO_1000066066"
FT BINDING 3..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ SEQUENCE 419 AA; 46299 MW; C8DEA58CDCF9D5D0 CRC64;
MRVIVLGSGV IGVASAYYLA QQGAHVTVLD RQTGPAEETS FGNAGQISPG YSTPWAAPGI
PFKAVKWMFQ HHAPLAINLD GSMWQLQWMA QMLKNCNPQS YSQNKERMMR VAEYSRDCLK
SLRETTGISY ENRAKGTLQV FRKEAQLEAV QRDIEVLQEC GVSYELLYQD DLARVEPALE
HAKDKLVGGL HLPNDETGDC YLFTNALAQK AKELGVNFQF NQNVEGLVVE GDEIKGVRVN
GQVLKADRYV LAFGSYSRDF LKPLALNLPV YPVKGYSLTI PIVQPEFAPQ STVLDETYKI
AITRFDQRIR VGGMAELSGF NLGLNQDRRA TLEMVTQDLF PGGNMAEASF WTGLRPMTPD
STPIIGATRF KNLFLNTGHG TLGWTMACGS GKLISDIVLS HQTEISTEGL SLQRYSTAA
