DADA_CROS8
ID DADA_CROS8 Reviewed; 432 AA.
AC A7MKD3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=ESA_01469;
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894;
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU76727.1; -; Genomic_DNA.
DR RefSeq; WP_012124512.1; NC_009778.1.
DR AlphaFoldDB; A7MKD3; -.
DR SMR; A7MKD3; -.
DR PRIDE; A7MKD3; -.
DR EnsemblBacteria; ABU76727; ABU76727; ESA_01469.
DR KEGG; esa:ESA_01469; -.
DR PATRIC; fig|290339.8.peg.1302; -.
DR HOGENOM; CLU_007884_9_2_6; -.
DR OMA; FWYKEDG; -.
DR OrthoDB; 573710at2; -.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000000260; Chromosome.
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..432
FT /note="D-amino acid dehydrogenase"
FT /id="PRO_1000066094"
FT BINDING 3..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ SEQUENCE 432 AA; 47402 MW; 196877CD56892737 CRC64;
MHVVVLGSGV VGVASAWYLR QAGHEVTVID REPGPALETS AANAGQISPG YAAPWAAPGV
PLKAIKWMFQ RHAPLAISLD GTHFQLKWMW QMLRNCDTRH YMQNKGRMVR LAEYSRDCLK
ALRESTGIQY EGRQGGTLQL FRTEQQYENA SRDIAVLESE GVPFRLLKAA ELAQVEPALA
DVAHKLTGGL QLPNDETGDC QLFTTRLAQM AEAAGVVFRY NTPVDRLLSE GQRIYGVKCG
DEVIKADGYV MAFGSYSTAM LKGIVDIPVY PLKGYSLTIP IADESGAPVS TVLDETYKIA
ITRFDNRIRV GGMAEIVGFN TELLKPRQET LEMVVRDLYP RGGHIEQAKF WTGLRPMTPD
GTPVVGRTEF KNLWLNTGHG TLGWTMACGS GQLLSDIISG RTPAIPFEDL SVARYAPGFT
PSSSHRLHGA HP
