DADA_BURCJ
ID DADA_BURCJ Reviewed; 428 AA.
AC B4EAP1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=BceJ2315_28690; ORFNames=BCAL2933;
OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=216591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610;
RX PubMed=18931103; DOI=10.1128/jb.01230-08;
RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT cystic fibrosis patients.";
RL J. Bacteriol. 191:261-277(2009).
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; AM747720; CAR53233.1; -; Genomic_DNA.
DR RefSeq; WP_006486941.1; NC_011000.1.
DR AlphaFoldDB; B4EAP1; -.
DR SMR; B4EAP1; -.
DR STRING; 216591.BCAL2933; -.
DR EnsemblBacteria; CAR53233; CAR53233; BCAL2933.
DR KEGG; bcj:BCAL2933; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_9_2_4; -.
DR OMA; NDLYPRG; -.
DR OrthoDB; 573710at2; -.
DR BioCyc; BCEN216591:G1G1V-3242-MON; -.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000001035; 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_1000138643"
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; 46004 MW; 397D79089B0DECD0 CRC64;
MRVVILGSGV VGVASAYYLA RAGHEVTVID REAGPALETS FANAGQISPG YAAPWAAPGV
PLKAVKWMFE KHAPLAIRLD GTRFQLQWMY QMLRNCTAER YAVNKGRMVR LAEYSRDCLQ
ALRADTGIQY EGRTGGTLQL FRTQQQLDGA AKDIAVLQEA NVPFELLSPA ELKKAEPALA
AVSHKLTGGL RLPGDETGDC QLFTTRLAAL AESLGVKFRY NTPIDALAIA GGKIAGVQCG
SETVRADAYV VALGSYSTSF ISNLMKVPVY PLKGYSITAP IVNEAAAPVS TVLDETYKIA
ITRFDQRIRV GGMAEIVGFD KKLRAARRET LEMCVNDLFP GGGDTSKATF WTGLRPMTPD
GTPIVGRTPV SNLFLNTGHG TLGWTMSCGS GQLLADLISG KMPAIQADDL SVHRYLKDVP
GQTRPAYA