DADA_PARDP
ID DADA_PARDP Reviewed; 433 AA.
AC A1B072;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Pden_0804;
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=318586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000489; ABL68916.1; -; Genomic_DNA.
DR RefSeq; WP_011747144.1; NC_008686.1.
DR AlphaFoldDB; A1B072; -.
DR SMR; A1B072; -.
DR STRING; 318586.Pden_0804; -.
DR PRIDE; A1B072; -.
DR EnsemblBacteria; ABL68916; ABL68916; Pden_0804.
DR KEGG; pde:Pden_0804; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_9_2_5; -.
DR OMA; FWYKEDG; -.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000000361; Chromosome 1.
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..433
FT /note="D-amino acid dehydrogenase"
FT /id="PRO_1000066103"
FT BINDING 3..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ SEQUENCE 433 AA; 46754 MW; 292430F16B30C451 CRC64;
MKIVVLGAGV LGVTSAWYLA KAGHEVTVID RQEGPALETS FANAGEISPG YSSPWAAPGV
PLKALKWMFQ RHAPLVVQPR LDWQRVSWMA RMLANCTSSA YAVNKSRMVR LAEYSRDCLG
ELRAETGIRY DERTQGTLQV FRKQQQLDAA GKDIEVLRAD GVPFEVLDRD GCVAAEPGLA
GSAERIVGGL RLPGDETGDC FLFTNRLAEM ATEAGVTFRW GVSIEALEAE GGRISAVRTD
KGRLTADRYV LAMGSYSPRM VRHLGLKLPV YPLKGYSLTI DIQDESRAPV STVMDETYKV
AITRLGDRIR VGGLAEIAGY DLSLNPRRKE TLAKSVGELF GGAGDAEQAL FWTGLRPMTP
DGTPIVGATP IPNLYLNTGH GTLGWTMSAG SGRLIADLIS GRKPDIAAED LGYARYMRGA
KAAGRPALQP ARA
