DADA_BORPD
ID DADA_BORPD Reviewed; 434 AA.
AC A9IP97;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=Bpet2578;
OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=340100;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448;
RX PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H.,
RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T.,
RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA Martinez-Arias R.;
RT "The missing link: Bordetella petrii is endowed with both the metabolic
RT versatility of environmental bacteria and virulence traits of pathogenic
RT Bordetellae.";
RL BMC Genomics 9:449-449(2008).
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; AM902716; CAP42920.1; -; Genomic_DNA.
DR AlphaFoldDB; A9IP97; -.
DR SMR; A9IP97; -.
DR STRING; 94624.Bpet2578; -.
DR EnsemblBacteria; CAP42920; CAP42920; Bpet2578.
DR KEGG; bpt:Bpet2578; -.
DR eggNOG; COG0665; Bacteria.
DR OMA; NDLYPRG; -.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000001225; 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; Reference proteome.
FT CHAIN 1..434
FT /note="D-amino acid dehydrogenase"
FT /id="PRO_1000138639"
FT BINDING 3..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ SEQUENCE 434 AA; 46814 MW; 2FFD8FF3F281B5DB CRC64;
MHVIVLGSGV IGTTTAYYLA RQGAKVTVLD RQPEAACETS YANAGQVSPG YSTPWAAPGI
PFKALKWLFQ KDAPLAIRPD GTLYQWRWMA AMLANCTAGR YTVNKERMLR LAEYSRDCLR
ELRADTGIQY EARTLGTLQL FRSASQYQAA QRDIQVLDAC GVPYELLDSA RLQTVEPALA
RTAHKLAGGL RLPNDETGDC RLFTRRLAQL AAGLGVEFRY GQDVEALVAG GAEIRGVRVG
GETLAADRYV AAFGSYTRGF LAPLGLELPV YPVKGYSLTI PLASAEAAPV STVLDETYKV
AITRFDNRIR VGGMAELAGF DLGLNPAHRR TLEHVVTDLY PGCGEVAQAE FWTGLRPMTP
DSTPIVGATR YANLFLNTGH GTLGWTMACG SGKVVADLVT GQRPAIRADD LALARYQAAQ
TRHAGPALGE RSAA
