DADA_SALPA
ID DADA_SALPA Reviewed; 432 AA.
AC Q5PCU1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=SPA1070;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV77041.1; -; Genomic_DNA.
DR RefSeq; WP_001266935.1; NC_006511.1.
DR AlphaFoldDB; Q5PCU1; -.
DR SMR; Q5PCU1; -.
DR EnsemblBacteria; AAV77041; AAV77041; SPA1070.
DR KEGG; spt:SPA1070; -.
DR HOGENOM; CLU_007884_9_2_6; -.
DR OMA; FWYKEDG; -.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000008185; 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_1000066114"
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