DADA_PSEU2
ID DADA_PSEU2 Reviewed; 433 AA.
AC Q4ZZW4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Psyr_0235;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY35308.1; -; Genomic_DNA.
DR RefSeq; WP_003403947.1; NC_007005.1.
DR RefSeq; YP_233346.1; NC_007005.1.
DR AlphaFoldDB; Q4ZZW4; -.
DR SMR; Q4ZZW4; -.
DR STRING; 205918.Psyr_0235; -.
DR EnsemblBacteria; AAY35308; AAY35308; Psyr_0235.
DR KEGG; psb:Psyr_0235; -.
DR PATRIC; fig|205918.7.peg.234; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_9_2_6; -.
DR OMA; FWYKEDG; -.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000000426; 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..433
FT /note="D-amino acid dehydrogenase"
FT /id="PRO_1000066108"
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; 47175 MW; 76C71151B139BB43 CRC64;
MRVLVLGSGV IGTTSAYYLA RAGFQVTVVD RQPAAAMETS FANAGQVSPG YASPWAAPGV
PLKALKWLLQ RHAPLAIKAT ADIDQYLWMA QMLRNCTASR YAINKERMVR LSEYSRDCLD
ELRLETGIAY EGRSLGTTQL FRTQAQLDNA AKDIAVLEQS GVPYELLDRD GIARVEPALA
GVTGILSGAL RLPNDQTGDC QLFTTRLAEM AVALGVEFRY GQNIERLDHA GDRINGVWID
GKLETADRYV LALGSYSPQL LKPLGIKAPV YPLKGYSLTV PITNPDMAPT STILDETYKV
AITRFDNRIR VGGMAEIAGF DLSLNPRRRE TLEMIVGDLY PQGGDLTQAD FWTGLRPTTP
DGTPIVGATP FRNLFLNTGH GTLGWTMACG SGRLLADLIA RKTPRISAEG LDISRYGNTQ
ENAQHVHPAP AHQ
