DADA_BRUSU
ID DADA_BRUSU Reviewed; 416 AA.
AC Q8FVC0; G0KDT4;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=BRA0924, BS1330_II0916;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(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 -!- SIMILARITY: Belongs to the DadA oxidoreductase family.
CC {ECO:0000255|HAMAP-Rule:MF_01202}.
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DR EMBL; AE014292; AAN34096.1; -; Genomic_DNA.
DR EMBL; CP002998; AEM20372.1; -; Genomic_DNA.
DR RefSeq; WP_004690359.1; NZ_KN046805.1.
DR AlphaFoldDB; Q8FVC0; -.
DR SMR; Q8FVC0; -.
DR EnsemblBacteria; AEM20372; AEM20372; BS1330_II0916.
DR GeneID; 45053921; -.
DR KEGG; bms:BRA0924; -.
DR KEGG; bsi:BS1330_II0916; -.
DR PATRIC; fig|204722.21.peg.375; -.
DR HOGENOM; CLU_007884_9_2_5; -.
DR OMA; NDLYPRG; -.
DR PhylomeDB; Q8FVC0; -.
DR Proteomes; UP000007104; Chromosome II.
DR GO; GO:0008718; F:D-amino-acid dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProtKB-UniRule.
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.
FT CHAIN 1..416
FT /note="D-amino acid dehydrogenase"
FT /id="PRO_0000166129"
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; 45094 MW; 25CF556CD82D0CA5 CRC64;
MQITILGSGV IGVTTAYYLA KLGHEVTVID REEGPAPETS FANAGQVSPG YASPWAAPGI
PLKAAKWLFQ KHAPLILRLT TDPVQYRWLL QMLANCTDSR YKINKTRMVR VAEYSRDCLI
ELRKDTGIEY DQRSQGTLQL FREQYQLDGI GKDIEVLRQD GVPFEVLDRD GCVNVEPALA
HAKDKFVGGL RLPNDETGDC FKFTNALAKI AEGLGVKFRF GVNIKSLLMS GGKISGVETS
EGIVTAERYV VALGSYTPAL IKALGLNAPI YPVKGYSITA PIVDESRAPV STVLDESYKI
AITRLGDRIR VGGMAEVSGF TDDLPAARRA TLDLSVTDLF PGGDLKAATF WSGLRPMTPD
STPIIGGTRY DNLFINAGHG TLGWTMACGS GRLLADLISG NKADIRADDL GIARYN