(data stored in ACNUC7421 zone)

SWISSPROT: DADA_STRM5

ID   DADA_STRM5              Reviewed;         434 AA.
AC   B4SIE4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 61.
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=Smal_0444;
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001111; ACF50149.1; -; Genomic_DNA.
DR   RefSeq; WP_004140565.1; NC_011071.1.
DR   SMR; B4SIE4; -.
DR   STRING; 391008.Smal_0444; -.
DR   EnsemblBacteria; ACF50149; ACF50149; Smal_0444.
DR   KEGG; smt:Smal_0444; -.
DR   eggNOG; ENOG4105MWK; Bacteria.
DR   eggNOG; COG0665; LUCA.
DR   HOGENOM; HOG000217450; -.
DR   KO; K00285; -.
DR   OMA; FWYKEDG; -.
DR   OrthoDB; 573710at2; -.
DR   BioCyc; SMAL391008:SMAL_RS02285-MONOMER; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000001867; 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; B4SIE4.
DR   SWISS-2DPAGE; B4SIE4.
KW   Complete proteome; FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN         1    434       D-amino acid dehydrogenase.
FT                                /FTId=PRO_1000138671.
FT   NP_BIND       3     17       FAD. {ECO:0000255|HAMAP-Rule:MF_01202}.
SQ   SEQUENCE   434 AA;  47804 MW;  37AFAA8F32D0A202 CRC64;
     MRVLVLGSGV IGTTSAWYLR QAGFEVTVID RQPGPALETS FANAGQLSFG YTSPWAAPGV
     PKKAIGWLFE KHAPLAIKPG MDLAQYRWLW QMLRNCTHER YAINKARMVR MSEYSRDCLN
     ELRAQIGIEF EGRDLGTTQL FRTQQQLDAS AQDIEILAQY GVPYEVLDRA GIIQAEPALA
     HVDGLVGALR LPRDQTGDCQ LFTRRLAQMC VDAGVEFRFD QDITGLVSDG ERITGVHVNG
     TLETADRFVV ALGSYSPALV APLGMRLPVY PLKGYSLTLP ITDPAMAPTS TILDESYKVA
     VTRFDDRIRV GGMAEVAGFD LSLSQRRRET LELVVSDLYP KGGDLSRAQF WTGLRPATPD
     GTPVIGATPF RNLYLNTGHG TLGWTMACGS GRYLADLMSA RQPQISTEGL DVFRYGQYGH
     APQHENRTCV LPAR
//

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