DADA_PSESM
ID DADA_PSESM Reviewed; 433 AA.
AC Q88BB6;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=PSPTO_0101;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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 -!- SIMILARITY: Belongs to the DadA oxidoreductase family.
CC {ECO:0000255|HAMAP-Rule:MF_01202}.
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DR EMBL; AE016853; AAO53655.1; -; Genomic_DNA.
DR RefSeq; NP_789960.1; NC_004578.1.
DR RefSeq; WP_005769533.1; NC_004578.1.
DR AlphaFoldDB; Q88BB6; -.
DR SMR; Q88BB6; -.
DR STRING; 223283.PSPTO_0101; -.
DR EnsemblBacteria; AAO53655; AAO53655; PSPTO_0101.
DR GeneID; 1181709; -.
DR KEGG; pst:PSPTO_0101; -.
DR PATRIC; fig|223283.9.peg.106; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_9_2_6; -.
DR OMA; FWYKEDG; -.
DR OrthoDB; 573710at2; -.
DR PhylomeDB; Q88BB6; -.
DR Proteomes; UP000002515; Chromosome.
DR GO; GO:0008718; F:D-amino-acid dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProtKB-UniRule.
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..433
FT /note="D-amino acid dehydrogenase"
FT /id="PRO_0000166142"
FT BINDING 3..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ SEQUENCE 433 AA; 46928 MW; 16581168E6DB0D87 CRC64;
MRVLVLGSGV IGTTSAYYLA RAGFQVTVVD RQPAVGMETS FANAGQVSPG YASPWAAPGV
PLKAIKWLLQ RHSPLAIKAT ADIDQYLWMA QMLRNCTANR YAVNKERMVR LSEYSRDCLD
ELRIETGIAY EGRSLGTTQL FRTQAQLDNA AKDIAVLEQS GVPYELLDRA GIARVEPALA
GVTGILSGAL RLPNDQTGDC QLFTTRLAQM AVELGVEFRY GQNIERLEHA GDTVSGVWID
GVLETADRYV LALGSYSPQL LKPLGIKAPV YPLKGYSLTV PISNPAMAPT STILDETYKV
AITRFDNRIR VGGMAEIAGF DLSLNPRRRE TLEMIVGDLY PQGGDLSQAS FWTGLRPTTP
DGTPIVGATP LRNLFLNTGH GTLGWTMACG SGRLLADLIA RKRPQISAAG LDISRYGNPQ
ENAQHVNPAP AHQ