ID   DADA_RHIL3              Reviewed;         416 AA.
AC   Q9RAE6; Q1M446;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 123.
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=pRL120417;
OS   Rhizobium leguminosarum bv. viciae (strain 3841).
OG   Plasmid pRL12.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=216596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10792736; DOI=10.1046/j.1365-2958.2000.01884.x;
RA   Allaway D.A., Lodwig E.M., Crompton L.A., Wood M., Parsons R.,
RA   Wheeler T.R., Poole P.S.;
RT   "Identification of alanine dehydrogenase and its role in mixed secretion of
RT   ammonium and alanine by pea bacteroids.";
RL   Mol. Microbiol. 36:508-515(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3841; PLASMID=pRL12;
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA   Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA   East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA   Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT   components.";
RL   Genome Biol. 7:R34.1-R34.20(2006).
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; AJ249196; CAB53548.1; -; Genomic_DNA.
DR   EMBL; AM236086; CAK12126.1; -; Genomic_DNA.
DR   RefSeq; WP_011649182.1; NC_008378.1.
DR   AlphaFoldDB; Q9RAE6; -.
DR   SMR; Q9RAE6; -.
DR   STRING; 216596.pRL120417; -.
DR   EnsemblBacteria; CAK12126; CAK12126; pRL120417.
DR   KEGG; rle:pRL120417; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_9_2_5; -.
DR   OMA; NDLYPRG; -.
DR   OrthoDB; 573710at2; -.
DR   UniPathway; UPA00043; UER00498.
DR   Proteomes; UP000006575; Plasmid pRL12.
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; Plasmid.
FT   CHAIN           1..416
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_0000166148"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ   SEQUENCE   416 AA;  44838 MW;  335AEDA6141AC006 CRC64;
     MKVIVLGAGI VGVTSAYQLA KAGHDVTVVD RQPGPALETS FANAGEVSFG YCSPWAAPGI
     PMKAMKWLFM KHAPLILRPK LDMAMLSWMA RMLSNCTSER YAINKSRMLR LADYSRIALA
     DLRAETGIAY DERMQGTLQL FRTQQQLEAS AKDVKALAAD GIPYEVLDRD GCIRFEPALK
     HVRDKIVGGL LTPKDETGDC FKFTNALAAK AEALGVRFAY GTTIKALDVE AGRVRGVITD
     RERMSAEAVV VALGSYSPLL LKPLGIRLPV YPVKGYSLTI PIADASRAPE STVMDETYKI
     AITRLGDRIR VGGMAEISGY TNDLGLARRS TLEYSVTDLF PGGDISKASF WSGLRPMTPD
     GTPVIGPTKV AGLFLNTGHG TLGWTMSTGS ARLIGDLVGG GQPEIDARDL AITRYG