ID F4CVH4_PSEUX Unreviewed; 675 AA.
AC F4CVH4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=2,4-dienoyl-CoA reductase (NADPH) {ECO:0000313|EMBL:AEA23794.1};
DE EC=1.3.1.34 {ECO:0000313|EMBL:AEA23794.1};
GN OrderedLocusNames=Psed_1556 {ECO:0000313|EMBL:AEA23794.1};
OS Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 /
OS CB1190).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=675635 {ECO:0000313|EMBL:AEA23794.1, ECO:0000313|Proteomes:UP000007809};
RN [1] {ECO:0000313|EMBL:AEA23794.1, ECO:0000313|Proteomes:UP000007809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190
RC {ECO:0000313|Proteomes:UP000007809};
RX PubMed=21725009; DOI=10.1128/JB.00415-11;
RA Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T.,
RA Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A.,
RA Alvarez-Cohen L.;
RT "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans
RT strain CB1190.";
RL J. Bacteriol. 193:4549-4550(2011).
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR EMBL; CP002593; AEA23794.1; -; Genomic_DNA.
DR RefSeq; WP_013673727.1; NC_015312.1.
DR AlphaFoldDB; F4CVH4; -.
DR STRING; 675635.Psed_1556; -.
DR KEGG; pdx:Psed_1556; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG1902; Bacteria.
DR HOGENOM; CLU_012153_1_0_11; -.
DR Proteomes; UP000007809; 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:AEA23794.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007809}.
FT DOMAIN 10..334
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 380..655
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 675 AA; 71977 MW; AB600A9832386047 CRC64;
MPDDEAYPHL FTPLDLGFTT LPNRVVMGSM HTGLEDDPAA APRLAAYFAE RARAGVALMV
TGGYAPHANG VLTEGGSLLD DASQLPAHRI VTDAVHEAGG RIALQVLHAG RYSKQPDLVA
PSAIRARINR FVPRPLDEEG IRELIDSYAR CAALAREGGY DGIEIMGSEG YLINTFLAPA
TNTRSDDWGG SPENRRRFAL EVMRASRAAV GDDFVIIFRL SMADLVPDGQ TWDEIVTLAR
GIEDAGATLL NTGIGWHEAQ IPTIATSVPR AAFTNVTASL RPHVGIPVIT SNRISMPDVA
ERVLAAGHAD LVSMARPFLA DPEWIRKARA GTPDDINTCI GCNQACLDHI FADKPMSCLV
NPRAGHETEL VVLPAPTAKR VAVVGAGPAG LSAAVTAAER GHHVELFESA DAIGGQFAIA
SRIPGKEEFS ETIRYYRRRL AQLGVTVHLG TRADVRRIVR GGFHEVVLAT GVEPRTPDIP
GIDHPMVVSY AEAVLGSPVG KRVAVIGAGG IGVDVSEFLT HVGSPSLDVE TWRREWGVAE
PGEVRGSLRP PAPEPSPRRV YLLQRSPGRI GTRLGLTTGW VHRAALAAKG VEQLSGVTYR
RIDDDGVHIT DADGAERVLE VDSVVVCAGQ EPVRELLDQL RDTGLAVHVI GGADVAAELD
AKRAIDQGTR LAAAL
//
