DADA_BURPS
ID DADA_BURPS Reviewed; 428 AA.
AC Q63S25;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=BPSL2497;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(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; BX571965; CAH36503.1; -; Genomic_DNA.
DR RefSeq; WP_004544221.1; NZ_CP009538.1.
DR RefSeq; YP_109092.1; NC_006350.1.
DR AlphaFoldDB; Q63S25; -.
DR SMR; Q63S25; -.
DR STRING; 272560.BPSL2497; -.
DR EnsemblBacteria; CAH36503; CAH36503; BPSL2497.
DR KEGG; bps:BPSL2497; -.
DR PATRIC; fig|272560.51.peg.2885; -.
DR eggNOG; COG0665; Bacteria.
DR OMA; NDLYPRG; -.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000000605; 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..428
FT /note="D-amino acid dehydrogenase"
FT /id="PRO_1000066082"
FT BINDING 3..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ SEQUENCE 428 AA; 46233 MW; BEC2462F61E5D243 CRC64;
MRVVILGSGV VGVASAYYLA RAGHEVTVID REAGPALDTS FANAGQISPG YAAPWAAPGV
PLKAVKWMFE KHAPLAIRLD GTRFQLQWMW QMLRNCTTER YALNKGRMVR LAEYSRDCLQ
ALRAETAIQY EGRTGGTLQV FRTQQQLDGA AKDIAVLREA NVPFELLSSD ELKKAEPALA
AVSHKLTGGL RLPGDETGDC QLFTTRLAAL AEQLGVKFRF NTRIDALAVA GGKIAGVQCG
GEMVRADAYV VALGSYSTNL VASLVKIPVY PLKGYSITAP IVDAAKAPVS TVLDETYKIA
ITRFDDRIRV GGMAEIVGFD KRLRDARRGT LEMCVNDLFP GGGDTEKATF WTGLRPMTPD
GTPIVGRTPV PNLFLNTGHG TLGWTMSCGS GQLLADLMSG KKPAIRADDL SVHRYLSETD
GEHRPAYA