ID Q0S3N5_RHOJR Unreviewed; 654 AA.
AC Q0S3N5;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=2,4-dienoyl-CoA reductase {ECO:0000313|EMBL:ABG97851.1};
DE EC=1.3.1.34 {ECO:0000313|EMBL:ABG97851.1};
GN OrderedLocusNames=RHA1_ro06074 {ECO:0000313|EMBL:ABG97851.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG97851.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR EMBL; CP000431; ABG97851.1; -; Genomic_DNA.
DR RefSeq; WP_011598111.1; NC_008268.1.
DR AlphaFoldDB; Q0S3N5; -.
DR KEGG; rha:RHA1_ro06074; -.
DR PATRIC; fig|101510.16.peg.6125; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG1902; Bacteria.
DR HOGENOM; CLU_012153_1_2_11; -.
DR OrthoDB; 3169239at2; -.
DR Proteomes; UP000008710; 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 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; IPR023967; CHP03996_oxidoreductase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR NCBIfam; TIGR03996; mycofact_OYE_1; 1.
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; PR00419; ADXRDTASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:ABG97851.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT DOMAIN 7..328
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 378..589
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 654 AA; 68755 MW; D293B5990B07AD0B CRC64;
MSAQLTDPIT LAGRHAPARV LLGPHPTNLG AGRALSPRHV AYYERRARGG AGIVVTEVAS
VHASDWPYER APLASDCVGG WRDVVAACRP HGTLVLAGLG HTGLQGSSAY SQAVLWGPSG
IADVISREMP MQMERAEIDG LVEGFRAAAA AAVSADVDGV ELDAGPRGIL RQFHSNLTNV
RDDAYGADPL RLTREVLAAV RDELGPGRVL SLRLSCDEAT SWAGITPSIA AGHARELAED
LDLLVVVRGG PMTPNAYRPD FHRPPSFNTE LCRDIRAAVA GVVPVVLQGS VVDPADARQA
LDEGVADVVE MTRAQIADPD LVVKIRRGAA PRPCVLCNQT CQVLDPRNPV VTCVGNPTAG
HETVDPVEDT AEVATGAVLV VGGGPAGLEA ARVLALRGHR VTVADASARL GGMVRAAVGA
PHLGALTDWL ENECRSLGVE FRLGTAVSDA DIDAAEREGA TVILATGSRP RPLPFPAKGN
VRCVGAADLL DGGPPTKGPH VVFDPVGGPV GVAVAEWLAA QGRDVSIVTQ DSVAGSRLGM
TGDLADANTR MQRAGVTRHL DSRIVSIGDD GMRIRNRYTA EESVVPCTVL IDCSHRLSED
TLGSSRPDAV RIGDCVAPRT LLEAVREGRA EALTWTAHRQ NEFDHHPFTL VNER
//
