DADA_AZOVD
ID DADA_AZOVD Reviewed; 432 AA.
AC C1DJZ7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=Avin_47980;
OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=322710;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ / ATCC BAA-1303;
RX PubMed=19429624; DOI=10.1128/jb.00504-09;
RA Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G.,
RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA Dean D.R., Dixon R., Wood D.;
RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT to support diverse anaerobic metabolic processes.";
RL J. Bacteriol. 191:4534-4545(2009).
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; CP001157; ACO80902.1; -; Genomic_DNA.
DR RefSeq; WP_012703264.1; NC_012560.1.
DR AlphaFoldDB; C1DJZ7; -.
DR SMR; C1DJZ7; -.
DR STRING; 322710.Avin_47980; -.
DR PRIDE; C1DJZ7; -.
DR EnsemblBacteria; ACO80902; ACO80902; Avin_47980.
DR KEGG; avn:Avin_47980; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_9_2_6; -.
DR OMA; NDLYPRG; -.
DR OrthoDB; 573710at2; -.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000002424; 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..432
FT /note="D-amino acid dehydrogenase"
FT /id="PRO_1000213845"
FT BINDING 3..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ SEQUENCE 432 AA; 47125 MW; D505A546B014F351 CRC64;
MRVLVLGSGV IGTTTAYYLA RAGFEVVVVD RAEAPAMETS FANAGQVSPG YASPWAAPGV
PLKALKWLFE RHAPLAIRPT ADWRQYLWLA QMLRNCTAGR YALNKERMVR LSEYSRDCLD
ELRAETGIDY EGRQLGTTQL FRTQRQLDAA GKDIAVLARS GVPYELLDRA GIARVEPALA
GVADRLAGAL RLPNDQTGDC HLFTTRLAEL AAGLGVEFRF GQSVERLERD GERIVGVRID
GRLESADLYV LALGSYSPRL LAPLGIRAPI YPLKGYSLTI PIVDPAMAPT STILDETYKV
AITRFETRIR VGGMAELAGF DLSLNPRRRE TLELVVGDLY PRGGDLARAE FWTGLRPATP
DGTPIVGATR YRNLFLNTGH GTLGWTMACG SGRLLADLMA RTRPQISAAG LDISRYGNSQ
ENSTHVHPAP AN