ID   A0A1H7G2X2_9RHOB        Unreviewed;       659 AA.
AC   A0A1H7G2X2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=2,4-dienoyl-CoA reductase {ECO:0000313|EMBL:SEK30800.1};
GN   ORFNames=SAMN05443999_101181 {ECO:0000313|EMBL:SEK30800.1};
OS   Roseovarius azorensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1287727 {ECO:0000313|EMBL:SEK30800.1, ECO:0000313|Proteomes:UP000199582};
RN   [1] {ECO:0000313|EMBL:SEK30800.1, ECO:0000313|Proteomes:UP000199582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100674 {ECO:0000313|EMBL:SEK30800.1,
RC   ECO:0000313|Proteomes:UP000199582};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR   EMBL; FOAG01000001; SEK30800.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7G2X2; -.
DR   STRING; 1287727.SAMN05443999_101181; -.
DR   OrthoDB; 9784632at2; -.
DR   Proteomes; UP000199582; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd04734; OYE_like_3_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; IPR018247; EF_Hand_1_Ca_BS.
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   PROSITE; PS00018; EF_HAND_1; 1.
PE   4: Predicted;
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199582}.
FT   DOMAIN          7..338
FT                   /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00724"
FT   DOMAIN          387..623
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   659 AA;  71406 MW;  A59D7B1814FC0EE6 CRC64;
     MTDFPHIFRP ATLAGHTLRN RIVFGAHTTN MAEDGLPGAR HIAYYTERAM GGAAMIVVEP
     MPVHPSAVLT RGNFRHSSDD VIPHFARLTK AVKSHGAVVL QQLYHVGAHG DQDNSWHAAW
     SPSGGPSWHD SDGSHEMTLA EIEEIIDSFV AAAIRCQKAG FHGVEVWAAY HGLLDQFWTP
     LSNTRNDDWG GSLENRTRLS REILRRIRAA CGPDFIIGLA VSDGSGVEAA LSLDELQEIV
     ALHDTERLMD YVTCGSGSYF DFHPLMPTFL YPEKLGVDLA QRLKSVVSHA LVTAESHIRT
     PENANAVLGA QQADMVSIVR GQIADPHLVA KAGAGRAEDV RGCISCNQQC WGRRSRDYWI
     SCLINPSVGW EHQWGGDRFT PADRPQNILV IGAGPAGLES ARAAAERGHR VTLHEAAPRI
     GGQLRLAGLQ PRRAQILDLL TWYERQLAHL GVTLHCNSYL DAPDIAAIAA DHVILATGSL
     PTGTGFQKAL PHLPELPGLD GNVWQVEDVM GRAARLGQRV IVLDEGGNWR GGGTAWHLAE
     TGHAVTIVTP HAMIGRELER SAADLPLRRR LAALGTRFVI ESAVASWQNG GAEVVNLLTG
     ETSHIAADSL VLATTNRADM TLFHDLARHG IAAHLIGDAH APRLAAQAFH DGRNLALRL
//