DADA_SERP5
ID DADA_SERP5 Reviewed; 434 AA.
AC A8GFF7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=Spro_2746;
OS Serratia proteamaculans (strain 568).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=399741;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=568;
RG US DOE Joint Genome Institute;
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., Taghavi S., Newman L.,
RA Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL Submitted (SEP-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; CP000826; ABV41847.1; -; Genomic_DNA.
DR RefSeq; WP_012145470.1; NC_009832.1.
DR AlphaFoldDB; A8GFF7; -.
DR SMR; A8GFF7; -.
DR STRING; 399741.Spro_2746; -.
DR EnsemblBacteria; ABV41847; ABV41847; Spro_2746.
DR KEGG; spe:Spro_2746; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_9_2_6; -.
DR OMA; FWYKEDG; -.
DR OrthoDB; 573710at2; -.
DR UniPathway; UPA00043; UER00498.
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..434
FT /note="D-amino acid dehydrogenase"
FT /id="PRO_1000066115"
FT BINDING 3..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ SEQUENCE 434 AA; 47212 MW; 82BAA8C3E8298712 CRC64;
MRVVILGSGV VGVASAWYLA KAGHEVTVID RQPGPAMETS AANAGQISPG YAAPWAAPGV
PLKAVKWMFQ RHAPLAVRLD GSSFQLSWMW QMLKNCNTEH YMTNKGRMVR LAEYSRDCIK
ALRQETGIQY EGRQGGTLQL FRTQQQFESA AKDIAVLEDA GVPYKLLEAS QLASVEPALA
QVAHKLTGGL QLPNDETGDC QLFTQQLAKL AQQAGVTFLY NRSVDRLLVE GDKISGVQCG
GEIFKADSYV VAFGSYSTAL LRDLVSIPVY PLKGYSLTIP ITDESAAPFS TVLDETYKIA
ITRFDQRIRV GGMAEIVGFN TQLEQKRRET LEMVVRDLYP NGGRVEDATF WTGLRPMTPD
GTPIVGKTSL KNLFLNTGHG TLGWTMACGS GQLLSDLISG ITPAIPSDDL GVARYSAGFR
SLYTGPLNDV HPAR