ID A0A086H453_STRSC Unreviewed; 671 AA.
AC A0A086H453;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=2,4-dienoyl-CoA reductase {ECO:0000313|EMBL:KFG02421.1};
DE EC=1.3.1.34 {ECO:0000313|EMBL:KFG02421.1};
GN Name=fadH {ECO:0000313|EMBL:KFG02421.1};
GN ORFNames=IQ62_01925 {ECO:0000313|EMBL:KFG02421.1};
OS Streptomyces scabiei.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1930 {ECO:0000313|EMBL:KFG02421.1, ECO:0000313|Proteomes:UP000028722};
RN [1] {ECO:0000313|EMBL:KFG02421.1, ECO:0000313|Proteomes:UP000028722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 4086 {ECO:0000313|EMBL:KFG02421.1,
RC ECO:0000313|Proteomes:UP000028722};
RA Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT "Genome sequencing of plant-pathogenic Streptomyces species.";
RL Submitted (JUL-2014) 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:KFG02421.1}.
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DR EMBL; JPPX01000036; KFG02421.1; -; Genomic_DNA.
DR RefSeq; WP_037689062.1; NZ_KL997394.1.
DR AlphaFoldDB; A0A086H453; -.
DR OrthoDB; 3169239at2; -.
DR Proteomes; UP000028722; Unassembled WGS sequence.
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; PR00411; PNDRDTASEI.
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:KFG02421.1}.
FT DOMAIN 7..331
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 377..633
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 671 AA; 72330 MW; 1287B74EFE0FA947 CRC64;
MSRYPHLLSP LDLGFTTLPN RVLMGSMHVG LEEAERGFER MAEFYAARAR GGVGLIVTGG
IAPNEAGRPY EGGAKLTTDA EAEKHREITD AVHREGGRIA MQILHFGRYA YHRDLVAPSA
LQAPISPYVP HALTDAEVEQ TIDDYVRAAR LARRAGYDGV EIMGSEGYLI NEFIAAGTNR
RDDRWGGSYE NRTRFPVEIV RRVREAVGED FIVVYRLSML DLVPGGSSFD EVVTLAKAVE
AAGATIINTG IGWHEARIPT IATSVPRGAY SWVTRRLMGA VSVPLVTTNR INTPEVAEEL
LADGHADMVS MARPMLADPD FVNKAREGRS DAINTCIGCN QACLDHTFSG KITSCLVNPR
ACHETELVLS PTRLRKRVAV VGAGPAGLAC AVSAAERGHE VTLFDAASEV GGQLNVARKV
PGKQEFDETL RYFRHQLDAH GVDVRLDTRV EADDLTAYDE VVVATGVTPR IPELPGVDHP
KVLGYLDVLR DGAPVGDRVA VLGAGGIGFD VAEFLTDGGE KTSEDPAAYF RQWGVDMDYR
APGGLAAPER PAPPRSVHLL QRKTSKVGAG LGKTTGWIHR TELKHRGVTM VPGVQYDLID
DAGLHVTVDG VRQVLEVDTV VLCTGQDPRR GLYDELIAAG RSAHLIGGAD VAAELDAKRA
IKQGTELAAA L
//
