ID C1AVU3_RHOOB Unreviewed; 674 AA.
AC C1AVU3;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=2,4-dienoyl-CoA reductase {ECO:0000313|EMBL:BAH49373.1};
DE EC=1.3.1.34 {ECO:0000313|EMBL:BAH49373.1};
GN Name=fadH {ECO:0000313|EMBL:BAH49373.1};
GN OrderedLocusNames=ROP_11260 {ECO:0000313|EMBL:BAH49373.1};
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH49373.1, ECO:0000313|Proteomes:UP000002212};
RN [1] {ECO:0000313|EMBL:BAH49373.1, ECO:0000313|Proteomes:UP000002212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:BAH49373.1,
RC ECO:0000313|Proteomes:UP000002212};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) 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; AP011115; BAH49373.1; -; Genomic_DNA.
DR RefSeq; WP_012688354.1; NC_012522.1.
DR AlphaFoldDB; C1AVU3; -.
DR STRING; 632772.ROP_11260; -.
DR KEGG; rop:ROP_11260; -.
DR PATRIC; fig|632772.20.peg.1195; -.
DR HOGENOM; CLU_012153_1_0_11; -.
DR OrthoDB; 3169239at2; -.
DR Proteomes; UP000002212; Chromosome.
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; PR00469; PNDRDTASEII.
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:BAH49373.1}.
FT DOMAIN 7..332
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 377..647
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 674 AA; 73109 MW; C2C21C6B4A6E23C4 CRC64;
MTQFPQLLAP LDLGFTTLKN RVIMGSIHTG LEDRAKDVPR LAEYFAERAR GGVALIVTGG
YAPNRTGWLL PFGAKLTNRV EARRHRAITK AVHDEGGKIA LQILHAGRYS YQPFSVSASS
IKAPINPFRP RKLTGRGVRW QIRNFVRCAR LAQQANYDGV EIMGGEGYFV NQFLCERTNK
RTDEWGGTPG NRRRMAVEIV RRTRAAVGPD FIIIFRLSMA DLVEGGQTWD EIVALAEEVE
AAGATIINTD IGWHESRVPT IVTSVPRAAF ADITGKLEKH VTIPVAASNR INMPEVAEEI
LTRGDAQLIS MARPMLADPD WVRKAEAGTP DEINTCIACN QACLDHAFVR KHVSCLLNPR
AGRETELTLA PTRTAKRVAV VGAGPAGLSA ALGLAHRGHS VTLFEAHSEI GGQFGIARRI
PGKEEFAETI RYYNRQLPLA GVDLRLDTRV TAAELVGTYD EVIVATGVTP RVPSIPGIDH
PKVLTYPEVV RGGKPVGRSV AVIGAGGIGV DVSEFLTHEH SPTLDLKEWK QEWGVTEPEA
AAGALTTPIP EPSPREVYLL QRKSGRIGAG LAKTTGWVHR AALKSKGVQE LSGVNYERID
DDGLHITFGA KREKPRTLAV DNVVICAGQE SVRDLVDELT VAGVTTHVIG GADVAAELDA
KRAIEQGTRL AARI
//
