DADA1_PSEAE
ID DADA1_PSEAE Reviewed; 432 AA.
AC Q9HTQ0;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=D-amino acid dehydrogenase 1;
DE EC=1.4.99.- {ECO:0000269|PubMed:21378189};
DE AltName: Full=D-alanine dehydrogenase 1;
GN Name=dadA1; Synonyms=dadA; OrderedLocusNames=PA5304;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS,
RP COFACTOR, DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=21378189; DOI=10.1128/jb.00036-11;
RA He W., Li C., Lu C.D.;
RT "Regulation and characterization of the dadRAX locus for D-amino acid
RT catabolism in Pseudomonas aeruginosa PAO1.";
RL J. Bacteriol. 193:2107-2115(2011).
CC -!- FUNCTION: Catalyzes the oxidative deamination of D-amino acids. Has
CC very broad substrate specificity; all the D-amino acids tested can be
CC used as the substrate except D-Glu and D-Gln. Participates in the
CC utilization of several D-amino acids as the sole source of nitrogen,
CC i.e. D-alanine, D-histidine, D-phenylalanine, D-serine, D-threonine,
CC and D-valine. {ECO:0000269|PubMed:21378189}.
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:21378189};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000305|PubMed:21378189};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.46 mM for D-alanine {ECO:0000269|PubMed:21378189};
CC KM=0.81 mM for D-histidine {ECO:0000269|PubMed:21378189};
CC KM=1.07 mM for D-phenylalanine {ECO:0000269|PubMed:21378189};
CC KM=1.78 mM for D-tyrosine {ECO:0000269|PubMed:21378189};
CC KM=1.82 mM for D-proline {ECO:0000269|PubMed:21378189};
CC KM=1.65 mM for D-serine {ECO:0000269|PubMed:21378189};
CC KM=2.47 mM for D-threonine {ECO:0000269|PubMed:21378189};
CC KM=3.01 mM for D-valine {ECO:0000269|PubMed:21378189};
CC KM=5.37 mM for D-arginine {ECO:0000269|PubMed:21378189};
CC Note=kcat is 0.74 sec(-1) with D-alanine as substrate. kcat is 0.84
CC sec(-1) with D-histidine as substrate. kcat is 1.10 sec(-1) with D-
CC phenylalanine as substrate. kcat is 1.10 sec(-1) with D-tyrosine as
CC substrate. kcat is 0.97 sec(-1) with D-proline as substrate. kcat is
CC 0.80 sec(-1) with D-serine as substrate. kcat is 0.68 sec(-1) with D-
CC threonine as substrate. kcat is 0.78 sec(-1) with D-valine as
CC substrate. kcat is 1.27 sec(-1) with D-arginine as substrate.;
CC -!- PATHWAY: Amino-acid degradation; D-alanine degradation; NH(3) and
CC pyruvate from D-alanine: step 1/1.
CC -!- INDUCTION: Is highly up-regulated by L- and D-alanine. However, it is
CC likely that intracellular L-Ala is the signal for induction of the
CC dadAX genes through DadR binding to several putative operator sites.
CC {ECO:0000269|PubMed:21378189}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene lose the ability to
CC utilize D-alanine, D-histidine, D-phenylalanine, D-serine, D-threonine,
CC and D-valine as the sole source of nitrogen.
CC {ECO:0000269|PubMed:21378189}.
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}.
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DR EMBL; AE004091; AAG08689.1; -; Genomic_DNA.
DR PIR; H82982; H82982.
DR RefSeq; NP_253991.1; NC_002516.2.
DR RefSeq; WP_003098274.1; NZ_QZGE01000020.1.
DR AlphaFoldDB; Q9HTQ0; -.
DR SMR; Q9HTQ0; -.
DR STRING; 287.DR97_2675; -.
DR PaxDb; Q9HTQ0; -.
DR PRIDE; Q9HTQ0; -.
DR DNASU; 878057; -.
DR EnsemblBacteria; AAG08689; AAG08689; PA5304.
DR GeneID; 878057; -.
DR KEGG; pae:PA5304; -.
DR PATRIC; fig|208964.12.peg.5558; -.
DR PseudoCAP; PA5304; -.
DR HOGENOM; CLU_007884_9_2_6; -.
DR InParanoid; Q9HTQ0; -.
DR OMA; NDLYPRG; -.
DR PhylomeDB; Q9HTQ0; -.
DR BioCyc; PAER208964:G1FZ6-5425-MON; -.
DR BRENDA; 1.4.99.6; 5087.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008718; F:D-amino-acid dehydrogenase activity; IDA:PseudoCAP.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0055130; P:D-alanine catabolic process; IBA:GO_Central.
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 FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..432
FT /note="D-amino acid dehydrogenase 1"
FT /id="PRO_0000166138"
FT REGION 410..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 432 AA; 47140 MW; CD15DB2FB5A30215 CRC64;
MRVLVLGSGV IGTASAYYLA RAGFEVVVVD RQDGPALETS FANAGQVSPG YASPWAAPGI
PLKAMKWLLE KHAPLAIKLT SDPSQYAWML QMLRNCTAER YAVNKERMVR LSEYSRDCLD
ELRAETGIAY EGRTLGTTQL FRTQAQLDAA GKDIAVLERS GVPYEVLDRD GIARVEPALA
KVADKLVGAL RLPNDQTGDC QLFTTRLAEM AKGLGVEFRF GQNIERLDFA GDRINGVLVN
GELLTADHYV LALGSYSPQL LKPLGIKAPV YPLKGYSLTV PITNPEMAPT STILDETYKV
AITRFDQRIR VGGMAEIAGF DLSLNPRRRE TLEMITTDLY PEGGDISQAT FWTGLRPATP
DGTPIVGATR YRNLFLNTGH GTLGWTMACG SGRYLADLMA KKRPQISTEG LDISRYSNSP
ENAKNAHPAP AH
