DADA_SALPB
ID DADA_SALPB Reviewed; 432 AA.
AC A9MVW7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=SPAB_01416;
OS Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1016998;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1250 / SPB7;
RG The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-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; CP000886; ABX66823.1; -; Genomic_DNA.
DR RefSeq; WP_001266937.1; NC_010102.1.
DR AlphaFoldDB; A9MVW7; -.
DR SMR; A9MVW7; -.
DR KEGG; spq:SPAB_01416; -.
DR PATRIC; fig|1016998.12.peg.1335; -.
DR HOGENOM; CLU_007884_9_2_6; -.
DR OMA; FWYKEDG; -.
DR BioCyc; SENT1016998:SPAB_RS05795-MON; -.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000008556; 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_1000085516"
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; 47883 MW; 3C34D2EBBC75F0ED CRC64;
MRVVILGSGV VGVTSAWYLS QAGHDVTVID RESGPAQETS AANAGQISPG YAAPWAAPGV
PLKAIKWMFQ RHAPLAVRLD GTPFQLKWMW QMLRNCDTRH YMENKGRMVR LAEYSRDCLK
TLRAATGIEY EGRQGGTLQL FRTAQQYENA TRDIAVLEDA GVPYQLLESS 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
PTPPQRLHSA HN