DADA_ECOLI
ID DADA_ECOLI Reviewed; 432 AA.
AC P0A6J5; P29011;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=D-amino acid dehydrogenase;
DE EC=1.4.99.- {ECO:0000269|PubMed:13292, ECO:0000269|PubMed:15358424};
DE AltName: Full=D-alanine dehydrogenase;
GN Name=dadA; Synonyms=dadR; OrderedLocusNames=b1189, JW1178;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=7906689; DOI=10.1128/jb.176.5.1500-1510.1994;
RA Lobocka M., Hennig J., Wild J., Klopotowski T.;
RT "Organization and expression of the Escherichia coli K-12 dad operon
RT encoding the smaller subunit of D-amino acid dehydrogenase and the
RT catabolic alanine racemase.";
RL J. Bacteriol. 176:1500-1510(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=13292; DOI=10.1007/bf00332894;
RA Franklin F.C., Venables W.A.;
RT "Biochemical, genetic, and regulatory studies of alanine catabolism in
RT Escherichia coli K12.";
RL Mol. Gen. Genet. 149:229-237(1976).
RN [6]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / EC989;
RX PubMed=10383414; DOI=10.1074/jbc.274.27.19109;
RA Soutourina J., Plateau P., Delort F., Peirotes A., Blanquet S.;
RT "Functional characterization of the D-Tyr-tRNATyr deacylase from
RT Escherichia coli.";
RL J. Biol. Chem. 274:19109-19114(1999).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=15358424; DOI=10.1111/j.1574-6968.2004.tb09780.x;
RA Deutch C.E.;
RT "Oxidation of 3,4-dehydro-D-proline and other D-amino acid analogues by D-
RT alanine dehydrogenase from Escherichia coli.";
RL FEMS Microbiol. Lett. 238:383-389(2004).
RN [8]
RP ACTIVITY REGULATION.
RX PubMed=21754980; DOI=10.1371/journal.pone.0020897;
RA Bardaweel S., Ghosh B., Chou T.F., Sadowsky M.J., Wagner C.R.;
RT "E. coli histidine triad nucleotide binding protein 1 (ecHinT) is a
RT catalytic regulator of D-alanine dehydrogenase (DadA) activity in vivo.";
RL PLoS ONE 6:E20897-E20897(2011).
CC -!- FUNCTION: Catalyzes the oxidative deamination of D-amino acids. Has
CC broad substrate specificity; is mostly active on D-alanine, and to a
CC lesser extent, on several other D-amino acids such as D-methionine, D-
CC serine and D-proline, but not on L-alanine. Participates in the
CC utilization of L-alanine and D-alanine as the sole source of carbon,
CC nitrogen and energy for growth. Is also able to oxidize D-amino acid
CC analogs such as 3,4-dehydro-D-proline, D-2-aminobutyrate, D-norvaline,
CC D-norleucine, cis-4-hydroxy-D-proline, and DL-ethionine.
CC {ECO:0000269|PubMed:13292, ECO:0000269|PubMed:15358424}.
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:0000269|PubMed:13292,
CC ECO:0000269|PubMed:15358424};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Is activated by the HinT protein. Is inhibited by
CC D-cycloserine. {ECO:0000269|PubMed:15358424,
CC ECO:0000269|PubMed:21754980}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30 mM for D-alanine {ECO:0000269|PubMed:13292,
CC ECO:0000269|PubMed:15358424};
CC KM=6.4 mM for 3,4-dehydro-D-proline {ECO:0000269|PubMed:13292,
CC ECO:0000269|PubMed:15358424};
CC pH dependence:
CC Optimum pH is about 8.9 with D-alanine as substrate and about 9 with
CC 3,4-dehydro-D-proline as substrate. {ECO:0000269|PubMed:13292,
CC ECO:0000269|PubMed:15358424};
CC -!- PATHWAY: Amino-acid degradation; D-alanine degradation; NH(3) and
CC pyruvate from D-alanine: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:13292,
CC ECO:0000269|PubMed:15358424}; Peripheral membrane protein
CC {ECO:0000269|PubMed:13292, ECO:0000269|PubMed:15358424}.
CC -!- INDUCTION: By D-alanine. Is regulated by catabolite repression.
CC {ECO:0000269|PubMed:13292}.
CC -!- DISRUPTION PHENOTYPE: Loss of the ability to utilize both D- and L-
CC stereoisomers of alanine as sole sources of carbon, nitrogen and energy
CC for growth (PubMed:13292). A double dtd-dadA deletion mutant has a
CC pronounced growth defect in the presence of D-tyrosine
CC (PubMed:10383414). {ECO:0000269|PubMed:10383414,
CC ECO:0000269|PubMed:13292}.
CC -!- SIMILARITY: Belongs to the DadA oxidoreductase family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a heterodimer based on the
CC purification of the enzyme first reported from E.coli B, but results of
CC enzyme assays in PubMed:21378189 have indicated that DadA is solely
CC responsible for the observed dehydrogenase activity. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L02948; AAC36880.1; -; Unassigned_DNA.
DR EMBL; U00096; AAC74273.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36044.1; -; Genomic_DNA.
DR PIR; B53383; B53383.
DR RefSeq; NP_415707.1; NC_000913.3.
DR RefSeq; WP_001266908.1; NZ_STEB01000023.1.
DR AlphaFoldDB; P0A6J5; -.
DR SMR; P0A6J5; -.
DR BioGRID; 4260104; 29.
DR DIP; DIP-6852N; -.
DR IntAct; P0A6J5; 21.
DR STRING; 511145.b1189; -.
DR jPOST; P0A6J5; -.
DR PaxDb; P0A6J5; -.
DR PRIDE; P0A6J5; -.
DR EnsemblBacteria; AAC74273; AAC74273; b1189.
DR EnsemblBacteria; BAA36044; BAA36044; BAA36044.
DR GeneID; 66674991; -.
DR GeneID; 945752; -.
DR KEGG; ecj:JW1178; -.
DR KEGG; eco:b1189; -.
DR PATRIC; fig|1411691.4.peg.1098; -.
DR EchoBASE; EB1379; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_9_2_6; -.
DR InParanoid; P0A6J5; -.
DR OMA; FWYKEDG; -.
DR PhylomeDB; P0A6J5; -.
DR BioCyc; EcoCyc:DALADEHYDROGA-MON; -.
DR BioCyc; MetaCyc:DALADEHYDROGA-MON; -.
DR SABIO-RK; P0A6J5; -.
DR UniPathway; UPA00043; UER00498.
DR PRO; PR:P0A6J5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0008718; F:D-amino-acid dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0055130; P:D-alanine catabolic process; IMP:EcoCyc.
DR GO; GO:0019480; P:L-alanine oxidation to pyruvate via D-alanine; IMP:EcoCyc.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; FAD; Flavoprotein; Membrane;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..432
FT /note="D-amino acid dehydrogenase"
FT /id="PRO_0000166131"
FT BINDING 3..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 432 AA; 47607 MW; EE747358845B6280 CRC64;
MRVVILGSGV VGVASAWYLN QAGHEVTVID REPGAALETS AANAGQISPG YAAPWAAPGV
PLKAIKWMFQ RHAPLAVRLD GTQFQLKWMW QMLRNCDTSH YMENKGRMVR LAEYSRDCLK
ALRAETNIQY EGRQGGTLQL FRTEQQYENA TRDIAVLEDA GVPYQLLESS RLAEVEPALA
EVAHKLTGGL QLPNDETGDC QLFTQNLARM AEQAGVKFRF NTPVDQLLCD GEQIYGVKCG
DEVIKADAYV MAFGSYSTAM LKGIVDIPVY PLKGYSLTIP IAQEDGAPVS TILDETYKIA
ITRFDNRIRV GGMAEIVGFN TELLQPRRET LEMVVRDLYP RGGHVEQATF WTGLRPMTPD
GTPVVGRTRF KNLWLNTGHG TLGWTMACGS GQLLSDLLSG RTPAIPYEDL SVARYSRGFT
PSRPGHLHGA HS
