DADA_BRUA4
ID DADA_BRUA4 Reviewed; 416 AA.
AC A6WYV7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Oant_1444;
OS Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=439375;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC 15819 / NCTC 12168 / Alc 37;
RX PubMed=21685287; DOI=10.1128/jb.05335-11;
RA Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA Ugalde R.A., Garcia E., Tolmasky M.E.;
RT "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT pathogen and symbiont of several eukaryotic hosts.";
RL J. Bacteriol. 193:4274-4275(2011).
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; CP000758; ABS14161.1; -; Genomic_DNA.
DR RefSeq; WP_010659513.1; NC_009667.1.
DR AlphaFoldDB; A6WYV7; -.
DR SMR; A6WYV7; -.
DR STRING; 439375.Oant_1444; -.
DR EnsemblBacteria; ABS14161; ABS14161; Oant_1444.
DR GeneID; 61318052; -.
DR KEGG; oan:Oant_1444; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_9_2_5; -.
DR OMA; FWYKEDG; -.
DR OrthoDB; 573710at2; -.
DR PhylomeDB; A6WYV7; -.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000002301; Chromosome 1.
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..416
FT /note="D-amino acid dehydrogenase"
FT /id="PRO_1000066102"
FT BINDING 3..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ SEQUENCE 416 AA; 45136 MW; D535372236B10A2B CRC64;
MQITILGSGV IGVTTAYYLA KLGHEVTVVD REEGPALETS FANAGQVSPG YASPWAAPGI
PFKAAKWLFQ KHAPLVLRPT CDPVQYSWLL QMLANCTDSR YKVNKTRMVR VAEYARDCLV
DLRKETGIEY DQRMQGTLQL FREQYQLDGI GKDIEVLRQD GVPFEVLDRE GCAKVEPALA
RVKDKFVGGL RLPHDETGDC FKFTNALAKI AEGLGVKFRF GVNIKSLLMS GGKVSGVETS
EGVLTADRYV VALGSYTPAL VKSLGLNAPI YPVKGYSITA PIVDEDRAPV STVLDESYKI
AITRLGDRIR VGGMAEVSGF TTDLPAARRA TLDLSVTDLF PGGDLKAATF WSGLRPMTPD
STPIIGATRY DNVFINAGHG TLGWTMSCGS GKLLADLISG NKPDIRADDL GISRYE
