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Database: UniProt
Entry: A0A0J6WU74_9FIRM
LinkDB: A0A0J6WU74_9FIRM
Original site: A0A0J6WU74_9FIRM 
ID   A0A0J6WU74_9FIRM        Unreviewed;       667 AA.
AC   A0A0J6WU74;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=2,4-dienoyl-CoA reductase {ECO:0000313|EMBL:KMO85733.1};
GN   ORFNames=AB840_11935 {ECO:0000313|EMBL:KMO85733.1};
OS   Megasphaera cerevisiae DSM 20462.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=1122219 {ECO:0000313|EMBL:KMO85733.1, ECO:0000313|Proteomes:UP000036503};
RN   [1] {ECO:0000313|EMBL:KMO85733.1, ECO:0000313|Proteomes:UP000036503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20462 {ECO:0000313|EMBL:KMO85733.1,
RC   ECO:0000313|Proteomes:UP000036503};
RA   Kutumbaka K., Pasmowitz J., Mategko J., Reyes D., Friedrich A., Han S.,
RA   Martens-Habbena W., Neal-McKinney J., Janagama H.K., Nadala C.,
RA   Samadpour M.;
RT   "Draft genome sequence of beer spoilage bacterium Megasphaera cerevisiae
RT   type strain 20462.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KMO85733.1}.
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DR   EMBL; LEKT01000048; KMO85733.1; -; Genomic_DNA.
DR   RefSeq; WP_048515074.1; NZ_LEKT01000048.1.
DR   AlphaFoldDB; A0A0J6WU74; -.
DR   STRING; 39029.BSR42_09490; -.
DR   PATRIC; fig|1122219.3.peg.2361; -.
DR   InParanoid; A0A0J6WU74; -.
DR   OrthoDB; 9772736at2; -.
DR   Proteomes; UP000036503; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd02803; OYE_like_FMN_family; 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; 2.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000036503}.
FT   DOMAIN          8..338
FT                   /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00724"
FT   DOMAIN          382..431
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          472..618
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   667 AA;  73378 MW;  C9E1A7A7B73AF93B CRC64;
     MSRNYPHIFE PLTVKRTTFK NRVIMPPMGS NLATFTGEVS EDMKKYYGLR ARGGTALITV
     ENACIDYPLA TNGTKQLRID KNQFIPGLYE LTERIHAYGA LASIQLNHAG ASAYPERLQG
     LQSVSASSVP SKEGNPAPRP LTKQEILNIV TKYAEAAQRA VQAGFDMVEI HGGHSYLLDQ
     FLSPLYNKRT DEFGGSYENR ARFARLVIEA VRSAVGKWIP ISFRISAAEF IDGGNTLDDT
     LKLLEYIQPE VDIINVSAAV NDSIQYQIDK CDLPDGWRAY LSQAVKDKFG KPVILSGNIR
     NPEIADQLLA DGKTDFLAIG RGLIADPDWA RKAQSGRANY IRKCISCNIG CADHRISKSQ
     PLRCTVNPDL IYGEAYKKNN VTRDLHVVVI GGGTSGLETA CTAAEAGCRV TLIERERELG
     GLARKIARFP EKSRIEDFPA YLEQRASHLP NLTIKCGTTA TKKMLIELKP DILYAATGSK
     PMLPPIEGLR ELTDAEGTQV KSIYGFMDNI PYFEQNAAGK NVAIIGCGAV GLDVMEFFTL
     RKAHVTMIEM MPSFGKDADV VSKSTFKELL ATHPVDMHLG TALQKVCPNK FIASHDGHLA
     EYPFDYGFIC MGLIPDIPAE DPFKTYAEEQ GIPFCNLGNS RKTGQIIHGT EAGRNILHTI
     DMIGGFD
//
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