ID   A0A1I6ZJT0_9BURK        Unreviewed;       424 AA.
AC   A0A1I6ZJT0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=D-amino-acid dehydrogenase {ECO:0000313|EMBL:SFT62948.1};
GN   ORFNames=SAMN05192563_1002402 {ECO:0000313|EMBL:SFT62948.1};
OS   Paraburkholderia aspalathi.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1324617 {ECO:0000313|EMBL:SFT62948.1, ECO:0000313|Proteomes:UP000198844};
RN   [1] {ECO:0000313|EMBL:SFT62948.1, ECO:0000313|Proteomes:UP000198844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 27731 {ECO:0000313|EMBL:SFT62948.1,
RC   ECO:0000313|Proteomes:UP000198844};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the DadA oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00009410}.
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; FPBH01000002; SFT62948.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6ZJT0; -.
DR   OrthoDB; 18526at2; -.
DR   Proteomes; UP000198844; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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   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;
FT   DOMAIN          13..404
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   424 AA;  46035 MW;  5BF0F1A48C212203 CRC64;
     MTQQVQNSRT TPDVVVIGGG IVGLACAWAA LRDGATVTII DRDFEGDRTS HGNAGGIAVT
     ESTPISVNGL YMKALKWLFD PLGPLALDWK HVPTALPWFM EFQRSGNKDR FREISLALAQ
     LNNRVYDDIV PMFEDIGAMD SFYRRGALTV YETDEAFAAD QHEWEFKRDL GVRWHAMSAD
     EVRDCEPSLA PVFRHGVFLD DWSHIGDPKR LVTQLRERVK QLGATFVVGA VKALDLADAL
     APAAVTETGE RVKGRRLVVA TGAWSAALAG SIGDRVLLDS ERGYNTTLPA HGISLSREVI
     FAERKFVATP LDIGVRIGGA AEFAGLKAPP NYKRSDALLA LGKRFLPGIN DKGAVKWMGH
     RPATPDSLPV IGQSPRAPSV IYAFGHGHLG LTQSATTGAL VADLLANRTP GIGLEPYSIS
     RFRN
//