ID A4JSR4_BURVG Unreviewed; 420 AA.
AC A4JSR4;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=D-amino-acid dehydrogenase {ECO:0000313|EMBL:ABO59317.1};
DE EC=1.4.99.1 {ECO:0000313|EMBL:ABO59317.1};
GN OrderedLocusNames=Bcep1808_6420 {ECO:0000313|EMBL:ABO59317.1};
OS Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS (strain R1808)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=269482 {ECO:0000313|EMBL:ABO59317.1, ECO:0000313|Proteomes:UP000002287};
RN [1] {ECO:0000313|Proteomes:UP000002287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G4 / LMG 22486 {ECO:0000313|Proteomes:UP000002287};
RG US DOE Joint Genome Institute;
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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 3 of Burkholderia vietnamiensis G4.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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}.
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; CP000616; ABO59317.1; -; Genomic_DNA.
DR AlphaFoldDB; A4JSR4; -.
DR KEGG; bvi:Bcep1808_6420; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_9_0_4; -.
DR Proteomes; UP000002287; Chromosome 3.
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;
KW Oxidoreductase {ECO:0000313|EMBL:ABO59317.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002287}.
FT DOMAIN 3..391
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 420 AA; 45481 MW; 69CFD53648ED1582 CRC64;
MSDIAILGAG FIGLASAASL IRDGHRVTLF DASGVGQGAS FGNAGTFAHY ACIPVNNPSV
FRDLPRFLLS HDSPFRLRWG YLPQLAPWLV RFMISSLPRR YEGSAGALAA LLGRAQDGYA
PLLEDAELAR FVQARECLYL YSNSESFDAA RPALDLRRKL GVAFDVLSGN DIRALEPSLA
PIFERGVLFS DSWHFSDPQG FLQTLYERLA AQGLTLERST VTAVQPSDDG VTVTLDGVAR
RFGHVVIATG ARSAKFAKQC GDSVPLDTER GYHVRYPGAQ QMISRPVGWA ERGFYMTPMS
DGIRVAGTVE LGGFNEARNR SLLDLLTFSS KRALPALDTP DSTWLGFRPT LPDGVPVLGR
SSASERVIYA FGHQHLGLTL AGISGRIVAD LIAGRTPSLD LTPYAATRFQ IAAGTVQHRH
//
