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DADA_BRADU
ID   DADA_BRADU              Reviewed;         421 AA.
AC   Q89T28;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=blr2222;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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   -!- SIMILARITY: Belongs to the DadA oxidoreductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01202}.
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DR   EMBL; BA000040; BAC47487.1; -; Genomic_DNA.
DR   RefSeq; NP_768862.1; NC_004463.1.
DR   RefSeq; WP_011085010.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89T28; -.
DR   SMR; Q89T28; -.
DR   STRING; 224911.27350477; -.
DR   EnsemblBacteria; BAC47487; BAC47487; BAC47487.
DR   GeneID; 64021969; -.
DR   KEGG; bja:blr2222; -.
DR   PATRIC; fig|224911.44.peg.1754; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_9_2_5; -.
DR   InParanoid; Q89T28; -.
DR   OMA; FWYKEDG; -.
DR   PhylomeDB; Q89T28; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0008718; F:D-amino-acid dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0015079; F:potassium ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0055130; P:D-alanine catabolic process; IBA:GO_Central.
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   InterPro; IPR006036; K_uptake_TrkA.
DR   Pfam; PF01266; DAO; 1.
DR   PRINTS; PR00335; KUPTAKETRKA.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..421
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_0000166127"
FT   BINDING         3..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ   SEQUENCE   421 AA;  45326 MW;  4859B8F71BFCB76C CRC64;
     MKVLILGSGV IGVTSAYYLA GAGHDVTVVD RQPEPALETS FANAGEVSPG YSSPWAGPGV
     PVKAVKWLLM KHGPLVIRPK LDPVMWVWLL KMLRNCTSAR YAVNKSRMIP IAEYSRDCLR
     DLRRDIGIQY DERSQGTLQL FRHQAQLDGT GEDIAVLKQY GVPFEVLGRE GCIAVEPALA
     GVKEKFAGGL RLPQDETGDC HMFTQALAKH AQALGVRFMF NTGIDRIVTD GARVSGVVTS
     AGVLQADAYV LALGSWSSRL VAPLGISLPV YPVKGYSITV PIKDASGAPE STVMDESYKV
     AITRLGNRIR VGGTAEISGF SSKLYDARRA TLDHSLTDLF PRGGDLSKAT FWSGLRPMTP
     DGPPVIGPTQ YANLHLNTGH GTLGWTMSCG SGRVLADMLS GKKPEVDVSA LTVDRYAHRF
     G
 
 
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