(data stored in ACNUC7421 zone)

SWISSPROT: 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   08-MAY-2019, entry version 80.
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};
GN   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
RT   pv. 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.
CC       {ECO:0000255|HAMAP-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,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:35179, ChEBI:CHEBI:59871;
CC         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}.
DR   EMBL; CP000075; AAY35308.1; -; Genomic_DNA.
DR   RefSeq; WP_003403947.1; NC_007005.1.
DR   RefSeq; YP_233346.1; NC_007005.1.
DR   STRING; 205918.Psyr_0235; -.
DR   PRIDE; Q4ZZW4; -.
DR   EnsemblBacteria; AAY35308; AAY35308; Psyr_0235.
DR   GeneID; 3365711; -.
DR   KEGG; psb:Psyr_0235; -.
DR   PATRIC; fig|205918.7.peg.234; -.
DR   eggNOG; ENOG4105MWK; Bacteria.
DR   eggNOG; COG0665; LUCA.
DR   HOGENOM; HOG000217450; -.
DR   KO; K00285; -.
DR   OMA; FWYKEDG; -.
DR   BioCyc; PSYR205918:G1G4J-236-MONOMER; -.
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;
DR   PRODOM; Q4ZZW4.
DR   SWISS-2DPAGE; Q4ZZW4.
KW   Complete proteome; FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN         1    433       D-amino acid dehydrogenase.
FT                                /FTId=PRO_1000066108.
FT   NP_BIND       3     17       FAD. {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
//

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