ID B4E657_BURCJ Unreviewed; 667 AA.
AC B4E657;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=2,4-dienoyl-CoA reductase {ECO:0000313|EMBL:CAR51634.1};
DE EC=1.3.1.34 {ECO:0000313|EMBL:CAR51634.1};
GN Name=fadH {ECO:0000313|EMBL:CAR51634.1};
GN ORFNames=BCAL1336 {ECO:0000313|EMBL:CAR51634.1};
OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=216591 {ECO:0000313|EMBL:CAR51634.1, ECO:0000313|Proteomes:UP000001035};
RN [1] {ECO:0000313|EMBL:CAR51634.1, ECO:0000313|Proteomes:UP000001035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 /
RC CF5610 {ECO:0000313|Proteomes:UP000001035};
RX PubMed=18931103; DOI=10.1128/JB.01230-08;
RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT cystic fibrosis patients.";
RL J. Bacteriol. 191:261-277(2009).
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR EMBL; AM747720; CAR51634.1; -; Genomic_DNA.
DR AlphaFoldDB; B4E657; -.
DR KEGG; bcj:BCAL1336; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG1902; Bacteria.
DR HOGENOM; CLU_012153_1_0_4; -.
DR Proteomes; UP000001035; Chromosome 1.
DR GO; GO:0008670; F:2,4-dienoyl-CoA reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0010181; F:FMN binding; 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;
KW Oxidoreductase {ECO:0000313|EMBL:CAR51634.1}.
FT DOMAIN 3..326
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 371..635
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 667 AA; 71866 MW; 77DD2570B14D7FFC CRC64;
MTTPLELGFT SLRNRVLMGS MHVGLEEAPN GFERMAAFYA ERARGEAGLI VTGGFAPNER
GRPAPGGAML TTEADAERHR VVTRAVQAEG GRIALQILHF GRYAYHPALA APSALKAPIN
PFTPHALTSD EVDETIADFV RCAALAQHAG YDGVEIMGSE GYLINEFIAA RTNHRDDAWG
GAYDNRIRFA VEIVRRVRER VGANFIVIYR LSMLDLVEGG STLDEVIRLA RAIEAAGATI
LNTGIGWHEA RIPTIATKVP RAAYAWVTRQ LMGKVGIPLV ATNRINTPEV AEQLLADGYC
DMVSMARPFL ADAEFVRKAR EGRADEINTC IGCNQACLDH TFSGRITSCL VNPRACHETE
LVIAPAPRRK RIAVVGAGPA GLGFAVTAAE RGHAVTLYEA GAEIGGQFNL ARKVPGKEEF
NETLRYFRRQ IELRGIALHV DTRATAEMLL QGEFDEVVIA TGIVPRTPPI DGVGHPKALG
YLDVLRDDKA VGNSVAIVGA GGIGFDVAEY LVHRDRGEHG DADRFFSEWG VDRSYANAGG
LGAARPEPAA REVHLLQRKA SKVGDGLGKT TGWIHRTALK ARGVGMSSSV TYRRIDDDGF
HVTIDGVERT LPVDNVVICA GQEPSRELAE QLQAAGCRVH LIGGAYEAAE LDAKRAIHQG
TTLAATL
//
