DADA_AERS4
ID DADA_AERS4 Reviewed; 417 AA.
AC A4SNB0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=ASA_2333;
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449;
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(2008).
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; CP000644; ABO90382.1; -; Genomic_DNA.
DR RefSeq; WP_005310937.1; NC_009348.1.
DR AlphaFoldDB; A4SNB0; -.
DR SMR; A4SNB0; -.
DR STRING; 382245.ASA_2333; -.
DR EnsemblBacteria; ABO90382; ABO90382; ASA_2333.
DR KEGG; asa:ASA_2333; -.
DR PATRIC; fig|382245.13.peg.2287; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_9_2_6; -.
DR OMA; FWYKEDG; -.
DR OrthoDB; 573710at2; -.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000000225; 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..417
FT /note="D-amino acid dehydrogenase"
FT /id="PRO_1000066068"
FT BINDING 3..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ SEQUENCE 417 AA; 44847 MW; EA3E4B79746C655A CRC64;
MDIVVLGGGV VGVTSAWYLA KAGHKVTLLE RRDGVALETS HANAGQISPG YAAPWAAPGI
PLKAAKWLLQ KHAPFTVRPT SDPFQLRWML KMFANCTPAA YATNKGRMVR LAEYSRDCMK
TLRDELALDY EGRQLGTLQL FRSQAQLDAS KRDIEVLEEY GVPYQSLDAS GCEGVEPALA
RVRGKIVGGL RLPGDETGDC FRFTKALAAE AQKLGVEFVF NCAIDEIELS LGRAVAVRAG
EQRFKADAIV CALGSYATGF LRPLGIDLPV YPVKGYSLTL PMTDADAVPR STVLDETYKV
AITRFNERIR VGGMAELSGF NLALNPKRYD TLAMVVGDLF PEGGDISRAE FWTGLRPMTP
DGTPLVGPSP VPGLWLNTGH GTLGWTMAAG SGQLLSDLIS GSSTAISDEG LTLARYG
