DADA_NEIG2
ID DADA_NEIG2 Reviewed; 419 AA.
AC B4RR07;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=NGK_2465;
OS Neisseria gonorrhoeae (strain NCCP11945).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=521006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCCP11945;
RX PubMed=18586945; DOI=10.1128/jb.00566-08;
RA Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.;
RT "Complete genome sequence of Neisseria gonorrhoeae NCCP11945.";
RL J. Bacteriol. 190:6035-6036(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001050; ACF31065.1; -; Genomic_DNA.
DR RefSeq; WP_003690316.1; NC_011035.1.
DR AlphaFoldDB; B4RR07; -.
DR SMR; B4RR07; -.
DR EnsemblBacteria; ACF31065; ACF31065; NGK_2465.
DR GeneID; 66754332; -.
DR KEGG; ngk:NGK_2465; -.
DR HOGENOM; CLU_007884_9_2_4; -.
DR OMA; NDLYPRG; -.
DR OrthoDB; 573710at2; -.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000002564; 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..419
FT /note="D-amino acid dehydrogenase"
FT /id="PRO_1000138659"
FT BINDING 3..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ SEQUENCE 419 AA; 46845 MW; F435775806AABDE3 CRC64;
MKVLVLGAGV AGVSSVWYLA EAGHEVTVID RTEGVAMETS FANAGQLSYG YTTPWAAPGI
PTKALKRLFK SHPPLLFRPD GGLYQIEWLW RMLQNCTATR YQINKERMVR ISEYSREMFR
RFEAQTDMNF EGRKKGTLQI FRQTEEVEAA KQDIAVLERY GVPYRRLKPE ECAEFEPALA
RVTAKIVGGL HLPADATGDC RLFTENLYKL CQEKGVRFYF NQTISRIDHN GLRIKAVETE
TGRFETDAVV CALGCFSRTV LAQLDLNLPI YPVKGYSLTL PVTNSDGAPV STVLDESYKV
AITRFDNRIR VGGMAELSGY ETKLPEKRRE TLALVVNDLF PEGGDLSQAL SWSGLRPMTP
DSTPLIGRTR FENLFLNTGH GTLGWTMSPG SAKLTADIVS GKDTEIRSDD LSLSRYQKL