ID A0A103DYX4_9BURK Unreviewed; 433 AA.
AC A0A103DYX4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=D-amino acid dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01202};
DE EC=1.4.99.- {ECO:0000256|HAMAP-Rule:MF_01202};
GN Name=dadA {ECO:0000256|HAMAP-Rule:MF_01202};
GN ORFNames=BSIN_1116 {ECO:0000313|EMBL:SMG03024.1}, WS67_18560
GN {ECO:0000313|EMBL:KVE25275.1};
OS Burkholderia singularis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=1503053 {ECO:0000313|EMBL:KVE25275.1, ECO:0000313|Proteomes:UP000062788};
RN [1] {ECO:0000313|EMBL:KVE25275.1, ECO:0000313|Proteomes:UP000062788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSV85 {ECO:0000313|EMBL:KVE25275.1,
RC ECO:0000313|Proteomes:UP000062788};
RA Sahl J., Keim P., Wagner D.;
RT "Expanding the genomic diversity of Burkholderia species for the
RT development of highly accurate diagnostics.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SMG03024.1, ECO:0000313|Proteomes:UP000198460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 28154 {ECO:0000313|EMBL:SMG03024.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Oxidative deamination of D-amino acids. {ECO:0000256|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:0000256|ARBA:ARBA00000728,
CC ECO:0000256|HAMAP-Rule:MF_01202};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|HAMAP-Rule:MF_01202};
CC -!- PATHWAY: Amino-acid degradation; D-alanine degradation; NH(3) and
CC pyruvate from D-alanine: step 1/1. {ECO:0000256|ARBA:ARBA00004960}.
CC -!- SIMILARITY: Belongs to the DadA oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00009410, ECO:0000256|HAMAP-Rule:MF_01202}.
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DR EMBL; LOWA01000042; KVE25275.1; -; Genomic_DNA.
DR EMBL; FXAN01000126; SMG03024.1; -; Genomic_DNA.
DR RefSeq; WP_059519089.1; NZ_LOWA01000042.1.
DR AlphaFoldDB; A0A103DYX4; -.
DR OrthoDB; 18526at2; -.
DR Proteomes; UP000062788; Unassembled WGS sequence.
DR Proteomes; UP000198460; Unassembled WGS sequence.
DR GO; GO:0008718; F:D-amino-acid dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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 PANTHER; PTHR13847:SF280; D-AMINO ACID DEHYDROGENASE; 1.
DR PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF01266; DAO; 1.
DR PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|HAMAP-Rule:MF_01202};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01202};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01202,
KW ECO:0000313|EMBL:SMG03024.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000062788}.
FT DOMAIN 2..402
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT BINDING 3..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01202"
SQ SEQUENCE 433 AA; 46702 MW; 44F6BF71F1E830C5 CRC64;
MRVVILGSGV VGVASAYYLA RAGHEVTVID REAGPALETS FANAGQISPG YAAPWAAPGV
PLKALKWMFE KHAPLAIRLD GTRFQLQWMW QMLRNCSAER YTLNKGRMVR LAEYSRDCLQ
ALRADTGIQY EGRTGGTLQV FRTQQQLDGA AKDIAVLRDA NVPFELLSAS ELQKAEPALA
AVSHKLTGGL RLPGDETGDC QLFTTRLAAL AEQLGVTFRF NTRIDALAIA GGKIAGVQCG
SEHSGTEIVR ADAYVVALGA YSTNFVANLV KIPVYPLKGY SITAPIVDAA KAPVSTVLDE
TYKIAITRFD ERIRVGGMAE IVGFDKGLRE ARRETLEMCV NDLFPGGGDT SNATFWTGLR
PMTPDGTPIV GRTPVSNLFL NTGHGTLGWT MSCGSGQLLA DLISGKQPAI RADDLSVHRY
LRETDGEHRP AYA
//
