DADA2_PSEAE
ID DADA2_PSEAE Reviewed; 416 AA.
AC Q9HU99;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=D-amino acid dehydrogenase 2;
DE EC=1.4.99.-;
GN Name=dadA2; OrderedLocusNames=PA5084;
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).
CC -!- FUNCTION: Oxidative deamination of D-amino acids. {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the DadA oxidoreductase family. {ECO:0000305}.
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DR EMBL; AE004091; AAG08469.1; -; Genomic_DNA.
DR PIR; F83010; F83010.
DR RefSeq; NP_253771.1; NC_002516.2.
DR RefSeq; WP_003095928.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; Q9HU99; -.
DR SMR; Q9HU99; -.
DR STRING; 287.DR97_2439; -.
DR PaxDb; Q9HU99; -.
DR EnsemblBacteria; AAG08469; AAG08469; PA5084.
DR GeneID; 880266; -.
DR KEGG; pae:PA5084; -.
DR PATRIC; fig|208964.12.peg.5329; -.
DR PseudoCAP; PA5084; -.
DR HOGENOM; CLU_007884_9_2_6; -.
DR InParanoid; Q9HU99; -.
DR OMA; WAGMRPA; -.
DR PhylomeDB; Q9HU99; -.
DR BioCyc; PAER208964:G1FZ6-5200-MON; -.
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 3: Inferred from homology;
KW FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..416
FT /note="D-amino acid dehydrogenase 2"
FT /id="PRO_0000166139"
FT BINDING 5..19
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 416 AA; 44767 MW; 1EDE536FD784FF6F CRC64;
MAQRVCIIGA GVVGLATAYA LVREGFDVTL VEARERGGLE TSYANGGQLS YRYVAPLADS
GVPAQALGWL LRNDAPLRLR PRLDPAQWRW LLGFLAACRG SLNRRNAAHL LRLALLSQRT
LQDWREEDGL DGFDWRRNGK LVAFRQPASF ARARQGLADP SAQFVLTAAE CLALEPALSA
APFVGGIHTP DEEVADCHAF CVQLAERLQA SGHCRQLHGR RVTKIVEGGA AVRGVEVGGD
LIEADHVVLA AGYRSAELML PGLRLPLYPL KGYSLTLPVG AQHRAPDTSI TDYDRKIVYA
RIGERLRIAA MVDIVGFDPG LEPARLALLR QQARDTFPQG GDFDAAVEWA GMRPATPTGV
PLVGNGGYRN LWLNLGHGAL GFTLACGSGR LLAEQIGRRP PSIDTTGLLP RGALAG
