DADA_SALPK
ID DADA_SALPK Reviewed; 432 AA.
AC B5BI50;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=SSPA0999;
OS Salmonella paratyphi A (strain AKU_12601).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=554290;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AKU_12601;
RX PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA Mungall K., Dougan G., Parkhill J.;
RT "Pseudogene accumulation in the evolutionary histories of Salmonella
RT enterica serovars Paratyphi A and Typhi.";
RL BMC Genomics 10:36-36(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; FM200053; CAR59150.1; -; Genomic_DNA.
DR RefSeq; WP_001266935.1; NC_011147.1.
DR AlphaFoldDB; B5BI50; -.
DR SMR; B5BI50; -.
DR KEGG; sek:SSPA0999; -.
DR HOGENOM; CLU_007884_9_2_6; -.
DR OMA; FWYKEDG; -.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000001869; 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_1000138668"
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; 47926 MW; 670458E36795F0EB CRC64;
MRVVILGSGV VGVTSAWYLS QAGHDVTVID RESGPAQETS AANAGQISPG YAAPWAAPGV
PLKAIKWMFQ RHAPLAVRLD GTPFQLKWMW QMLRNCDTRH YMENKGRMVR LAEYSRDCLK
TLRAATGIEY EGRQGGTLQL FRTAQQYENA TRDIAVLEDA GVPYQLLEAS RLAEVEPALA
EVAHKLTGGL RLPNDETGDC QLFTQRLARM AEQAGVTFRF NTPVEKLLYE NDQIYGVKCA
DEIIKADAYV MAFGSYSTAM LKGIVDIPVY PLKGYSLTIP IVEPDGAPVS TILDETYKIA
ITRFDKRIRV GGMAEIVGFN TDLLQPRRET LEMVVRDLFP RGGHIEQATF WTGLRPMTPD
GTPVVGRTRY KNLWLNTGHG TLGWTMACGS GQLLSDILSG RTPAIPYDDL SVARYRSDFT
PTRPQRLHSA HN