ID F2LAL8_BURGS Unreviewed; 413 AA.
AC F2LAL8;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=D-amino-acid dehydrogenase {ECO:0000313|EMBL:AEA59405.1};
GN OrderedLocusNames=bgla_1g07130 {ECO:0000313|EMBL:AEA59405.1};
OS Burkholderia gladioli (strain BSR3).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=999541 {ECO:0000313|EMBL:AEA59405.1, ECO:0000313|Proteomes:UP000008316};
RN [1] {ECO:0000313|EMBL:AEA59405.1, ECO:0000313|Proteomes:UP000008316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSR3 {ECO:0000313|EMBL:AEA59405.1,
RC ECO:0000313|Proteomes:UP000008316};
RX PubMed=21478339; DOI=10.1128/JB.00420-11;
RA Seo Y.S., Lim J., Choi B.S., Kim H., Goo E., Lee B., Lim J.S., Choi I.Y.,
RA Moon J.S., Kim J., Hwang I.;
RT "Complete genome sequence of Burkholderia gladioli BSR3.";
RL J. Bacteriol. 193:3149-3149(2011).
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}.
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DR EMBL; CP002599; AEA59405.1; -; Genomic_DNA.
DR RefSeq; WP_013696761.1; NC_015381.1.
DR AlphaFoldDB; F2LAL8; -.
DR STRING; 999541.bgla_1g07130; -.
DR KEGG; bgd:bgla_1g07130; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_9_2_4; -.
DR Proteomes; UP000008316; Chromosome 1.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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 3..398
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 413 AA; 43648 MW; 8280A00A41DDDCB3 CRC64;
MHILIVGAGV IGLSSAYTLS RAGHAVTVVE RGPEVAGQTS AGNGGQLSYS YVAPLADPGV
IGKLPGWLTR RDSPVRFQPS LDPRQWRWCF AFLAACTRSR SALTTRRLLS LSFLSRTLMH
ELIAAEPSLD FDFVPSGKLV LHREPAAMQA AIAQLELQRA LGCEQAALEM DACIALEPSL
TRLRGRFAGG IHTPSEDTAD CQRFCTGLAA LLRERGVSIL TDTAIDALHA GRDGRVTALH
RGEPLAADHL VIAAGAAAPA LLCPLGIQVP IWPLKGYSLT YHLPPGAGVP RASLTDFARK
VVYARLGTRL RAAGIADIDA SPAPDPARLA SLEAEVAALF PEIAACAEPQ RWCGLRPATP
TGTPIIGPTR YRNLWLNLGH GALGFTLATG SAALLADWLA GDSGHALRAS FAH
//
