DADA_VIBC3
ID DADA_VIBC3 Reviewed; 421 AA.
AC A5F3D0; C3LYF4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, 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=VC0395_A0313, VC395_0803;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
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; CP000627; ABQ20510.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP08820.1; -; Genomic_DNA.
DR AlphaFoldDB; A5F3D0; -.
DR SMR; A5F3D0; -.
DR STRING; 345073.VC395_0803; -.
DR EnsemblBacteria; ABQ20510; ABQ20510; VC0395_A0313.
DR KEGG; vco:VC0395_A0313; -.
DR KEGG; vcr:VC395_0803; -.
DR PATRIC; fig|345073.21.peg.775; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_9_2_6; -.
DR OMA; FWYKEDG; -.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000000249; Chromosome 2.
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..421
FT /note="D-amino acid dehydrogenase"
FT /id="PRO_1000073102"
FT BINDING 4..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ SEQUENCE 421 AA; 46327 MW; AA75EB12983104E4 CRC64;
MMEVLVLGSG VVGLTSAWYL AQAGHDVTVV DRQPRGAEET SFANAGQISY GYSSPWAAPG
IPQKALKWML EKHAPLKIQP SLDPALLSWM GKMLLNCQLS RYQVNKSRML AIANYSRECL
KALNQTYSLD YQGRQRGTLQ VFRDEKQLTA IEKDMQLLAQ SGVRFELLNV AQCLTHEPGL
APVQEKLVGG LWLPDDETGD YYLFCQQLTE LAKQQGVRFH FDCHIQQLVC EGKKIIGVQT
DLGLLKADAY VVALGSYSTS LLKPLGIEIP VYPVKGYSLT LPIIDEKFAP QSTVMDETYK
VALTRFSDRI RVAGTAELAG FDPAIPEARK ATIEMVARDL FPHGGDFAKG QFWTGFRPMT
PDGTPIIGAT PYTNLYTNTG HGTLGWTMAC GSASILADVL THGESPLSRL GLDLFRYPKA
S
