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Database: UniProt
Entry: F2LFA4_BURGS
LinkDB: F2LFA4_BURGS
Original site: F2LFA4_BURGS 
ID   F2LFA4_BURGS            Unreviewed;       673 AA.
AC   F2LFA4;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   SubName: Full=NADH:flavin oxidoreductase/NADH oxidase {ECO:0000313|EMBL:AEA60691.1};
GN   OrderedLocusNames=bgla_1g20530 {ECO:0000313|EMBL:AEA60691.1};
OS   Burkholderia gladioli (strain BSR3).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=999541 {ECO:0000313|EMBL:AEA60691.1, ECO:0000313|Proteomes:UP000008316};
RN   [1] {ECO:0000313|EMBL:AEA60691.1, ECO:0000313|Proteomes:UP000008316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSR3 {ECO:0000313|EMBL:AEA60691.1,
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=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR   EMBL; CP002599; AEA60691.1; -; Genomic_DNA.
DR   RefSeq; WP_013698023.1; NC_015381.1.
DR   AlphaFoldDB; F2LFA4; -.
DR   STRING; 999541.bgla_1g20530; -.
DR   KEGG; bgd:bgla_1g20530; -.
DR   eggNOG; COG0446; Bacteria.
DR   eggNOG; COG1902; Bacteria.
DR   HOGENOM; CLU_012153_1_1_4; -.
DR   OMA; QFLAAHT; -.
DR   Proteomes; UP000008316; Chromosome 1.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd02930; DCR_FMN; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR001155; OxRdtase_FMN_N.
DR   PANTHER; PTHR42917; 2,4-DIENOYL-COA REDUCTASE; 1.
DR   PANTHER; PTHR42917:SF2; 2,4-DIENOYL-COA REDUCTASE [(2E)-ENOYL-COA-PRODUCING]; 1.
DR   Pfam; PF00724; Oxidored_FMN; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE   4: Predicted;
FT   DOMAIN          7..331
FT                   /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00724"
FT   DOMAIN          377..645
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   673 AA;  72946 MW;  7BBD6E8A3BA64A8B CRC64;
     MIPYPNLLRP LDLGFTTLRN RVLMGSMHIG LEEAPNGFER MAAFYAERAR GEVGLIVTGG
     IAPNERGRPI RGGAMLSNEA EAEPHRRVTD AVHAEGGKIA MQILHFGRYA YQPNLVAPSA
     IQAPINPFVP HELGDEEVEQ TIDDFVRCAA LAQHAGYDGV EIMGSEGYLI NEFIAARTNH
     RKDRWGGDYT QRIRFPVEIV RRVRERVGPR FILIYRLSML DLVEGGSTLD EVIQLARAIE
     QAGATIINTG IGWHEARVPT IATKVPRAAY AWVTQALMGQ VSVPLVATNR INTPETAESL
     LADGACDMVS MARPFLADAD FVRKAREGRG DEINTCIGCN QACLDHTFAG KVTSCLVNPR
     ACHETEIVIA PAGQRKRIAV VGAGPAGLAC AVTAAERGHE VTLIEAAAEI GGQFNLAKKV
     PGKEEFHETL RYFRRRIEST GVTLRLGERA SGEALLREQF DEVVVATGIV PRRPPIEGLD
     HPKALAYLDV LRDDKPVGRK VAIVGAGGIG FDVAEYLVHE GESASLDAAK FFAEWGVDTA
     YAERGGLRLP QPARAARQVY LLQRKASKVG DGLGKTTGWI HRAALKARGV KMVPAVEYRR
     IDDEGLHLSI DGEPQVLPVD NVVICAGQEP LRELADQLEA AGVRVHVIGG AAEAGELDAK
     RAIHQGTTLA ARL
//
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