DADA_BURL3
ID DADA_BURL3 Reviewed; 428 AA.
AC Q39IE1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=Bcep18194_A4178;
OS Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS R18194 / 383).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=482957;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia sp. 383.";
RL Submitted (OCT-2005) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000151; ABB07775.1; -; Genomic_DNA.
DR RefSeq; WP_011351352.1; NZ_CABVQI010000023.1.
DR AlphaFoldDB; Q39IE1; -.
DR SMR; Q39IE1; -.
DR EnsemblBacteria; ABB07775; ABB07775; Bcep18194_A4178.
DR GeneID; 45094077; -.
DR KEGG; bur:Bcep18194_A4178; -.
DR PATRIC; fig|482957.22.peg.1065; -.
DR HOGENOM; CLU_007884_9_2_4; -.
DR OMA; NDLYPRG; -.
DR OrthoDB; 573710at2; -.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000002705; 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_1000066083"
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; 45978 MW; D4C011F2203689C3 CRC64;
MRVVILGSGV VGVASAYYLA RAGHEVTVID REAGPALETS FANAGQISPG YAAPWAAPGV
PLKAVKWMFE KHAPLAIRLD GTRFQLQWMY QMLRNCTAER YAVNKGRMVR LAEYSRDCLQ
ALRADTGIQY EGRTGGTLQL FRTQQQLDGA AKDIAVLQEA NVPFELLSPA DLKKAEPALA
AVSHKLTGGL RLPGDETGDC QLFTTRLAAL AESLGVKFRY NTPIDALAIA GGKIAGVQCG
SETVRADAYV VALGSYSTSF ISNLMKIPVY PLKGYSITAP IVNEAAAPVS TVLDETYKIA
ITRFDQRIRV GGMAEIVGFD KKLRAARRET LEMCVNDLFP GGGDTSKATF WTGLRPMTPD
GTPIVGRTPV SNLFLNTGHG TLGWTMSCGS GQLLADLISG KMPAIQADDL SVHRYLKDVA
GQTRPAYA