ID A0A1G7B8B2_9BURK Unreviewed; 415 AA.
AC A0A1G7B8B2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN05421548_13813 {ECO:0000313|EMBL:SDE23329.1};
OS Paraburkholderia lycopersici.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=416944 {ECO:0000313|EMBL:SDE23329.1, ECO:0000313|Proteomes:UP000198908};
RN [1] {ECO:0000313|Proteomes:UP000198908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TNe-862 {ECO:0000313|Proteomes:UP000198908};
RA Varghese N., Submissions S.;
RL Submitted (SEP-2016) 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 -!- SIMILARITY: Belongs to the DadA oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00009410, ECO:0000256|HAMAP-Rule:MF_01202}.
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DR EMBL; FMYQ01000038; SDE23329.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7B8B2; -.
DR STRING; 416944.SAMN05421548_13813; -.
DR OrthoDB; 18526at2; -.
DR Proteomes; UP000198908; 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 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}.
FT DOMAIN 2..398
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 415 AA; 44414 MW; D3088F5C6158AE3D CRC64;
MRVCVLGGGV IGVTTAYALA RDGHEVTLVE RHADVAREAS HANGGQLSYS YVAPLADPSV
LPKLPQWLFS RDAALRFVPR LDPHQWHWCL AFLRACTRAR SRATTAELLG LGFLSQRLMH
EVVEREALSF DYVRNGKLVV YRDRESFAGA RSQAAYQAQL GCVQHALDGA ACVALEPALA
HIGGKIVGGI HTPGEEAADC GQFTRGLARA AQRHGVSLQL ATEFAGLRTK GLRVLAAQTS
RGDIEADAFV VCLGFQSQPI LASLGVNVPV YPLKGYSLTL PHADAHGAPR VSVTDAHHKV
VYAPLGERLR VAGMVDLTGM NPHADEARIA LLTRQARDTF PAAGDYGAIQ TWTGMRPATP
DSKPLIGATH FRNLWLNTGH GALGFTLAPG SAQLLADLLA ERELPIDGDA FAPGR
//
