DADA_BURM1
ID DADA_BURM1 Reviewed; 428 AA.
AC A9ADT7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Bmul_2240, BMULJ_00999;
OS Burkholderia multivorans (strain ATCC 17616 / 249).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=395019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC
RT 17616.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA Hattori M., Tsuda M.;
RT "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000868; ABX15925.1; -; Genomic_DNA.
DR EMBL; AP009385; BAG42945.1; -; Genomic_DNA.
DR RefSeq; WP_012213831.1; NC_010804.1.
DR AlphaFoldDB; A9ADT7; -.
DR SMR; A9ADT7; -.
DR STRING; 395019.Bmul_2240; -.
DR EnsemblBacteria; BAG42945; BAG42945; BMULJ_00999.
DR KEGG; bmj:BMULJ_00999; -.
DR KEGG; bmu:Bmul_2240; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_9_2_4; -.
DR OMA; NDLYPRG; -.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000008815; 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_1000138644"
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; 46053 MW; 5D7B7757D363FE5B CRC64;
MRVVILGSGV VGVASAYYLA RAGHEVTVID REAGPALETS FANAGQISPG YAAPWAAPGV
PLKAVKWMFE KHAPLAIRLD GTRFQLQWMW QMLRNCTPER YAVNKSRMVR LAEYSRDCLQ
ALRADTGIQY EGRTGGTLQL FRTQQQLDGA AKDIAVLREA NVPFELLSPA ELKNAEPALA
AVSHKLTGGL RLPGDETGDC QLFTTRLAAL AESLGVKFRY NTPIDGLAIA GGKIAGVQCG
SETVRADAYV VALGSYSTNF VANLMKIPVY PLKGYSITAP IVDEAAAPVS TVLDETYKIA
ITRFDQRIRV GGMAEIVGFD KTLRAARRET LEMCVNDLFP GGGDTSKATF WTGLRPMTPD
GTPIVGRTPV SNLFLNTGHG TLGWTMSCGS GQLLADLISG KKPAIQADDL SVHRYLKEVA
GQTRPAYA