DADA_PECCP
ID DADA_PECCP Reviewed; 417 AA.
AC C6DGU9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=PC1_1957;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) 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; CP001657; ACT12998.1; -; Genomic_DNA.
DR RefSeq; WP_015840191.1; NC_012917.1.
DR AlphaFoldDB; C6DGU9; -.
DR SMR; C6DGU9; -.
DR STRING; 561230.PC1_1957; -.
DR EnsemblBacteria; ACT12998; ACT12998; PC1_1957.
DR KEGG; pct:PC1_1957; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_9_2_6; -.
DR OMA; FWYKEDG; -.
DR OrthoDB; 573710at2; -.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000002736; 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_1000213848"
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; 46153 MW; B02F9E8337E43C2F CRC64;
MRVVILGSGV VGVSTAWYLA QEGHDVTVID RQPEPALETS AGNAGQISPG YAAPWAAPGI
PLKAIKWMFQ RHAPLAIRPD FTAAQLCWMW QMLLNCDARH YKTNKARMVR LAEYSRDCLQ
QLRRDTGIQY EGRQGGTLQL FRTEQQYDNA TRDIAVLEEA GVPYQLLTRH ELASVEPALA
NVAEKLTGGL RLPHDETGDC QLFTRQLAAM AADAGVTFKL GRHVRQLRVE GQNVTGVQCD
DEMIVADAYV MACGSYSTGL LRQWFDIPVY PLKGYSLTIP LADDASAPVS TVLDETYKVA
ITRFDRRIRV GGMAEVVGFN TDLNPKRRET LEMVVRDLYP HCGPIEQATF WTGLRPMTPD
GTPLVGRSPL KNLYLNTGHG TLGWTMACGS GKLLADILSD KSPEIEANDL SVERYVR
