DADA_BURMA
ID DADA_BURMA Reviewed; 428 AA.
AC Q62M46;
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=BMA0408;
OS Burkholderia mallei (strain ATCC 23344).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=243160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23344;
RX PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT "Structural flexibility in the Burkholderia mallei genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(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; CP000010; AAU48784.1; -; Genomic_DNA.
DR RefSeq; WP_004189387.1; NC_006348.1.
DR RefSeq; YP_102222.1; NC_006348.1.
DR AlphaFoldDB; Q62M46; -.
DR SMR; Q62M46; -.
DR STRING; 243160.BMA0408; -.
DR EnsemblBacteria; AAU48784; AAU48784; BMA0408.
DR GeneID; 56596462; -.
DR KEGG; bma:BMA0408; -.
DR PATRIC; fig|243160.12.peg.414; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_9_2_4; -.
DR OMA; NDLYPRG; -.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000006693; 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.
FT CHAIN 1..428
FT /note="D-amino acid dehydrogenase"
FT /id="PRO_1000066077"
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; 46175 MW; 0AC24145CC22B8EE 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 GGGDTAKATF WTGLRPMTPD
GTPIVGRTPV PNLFLNTGHG TLGWTMSCGS GQLLADLMSG KKPAIRADDL SVHRYLSETD
GEHRPAYA
