ID S5ULM7_STRC3 Unreviewed; 671 AA.
AC S5ULM7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=2,4-dienoyl-CoA reductase {ECO:0000313|EMBL:AGS67818.1};
GN ORFNames=B446_04950 {ECO:0000313|EMBL:AGS67818.1};
OS Streptomyces collinus (strain DSM 40733 / Tue 365).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1214242 {ECO:0000313|EMBL:AGS67818.1, ECO:0000313|Proteomes:UP000015423};
RN [1] {ECO:0000313|Proteomes:UP000015423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RA Ruckert C., Szczepanowski R., Goesmann A., Pross E.K., Musiol E.M.,
RA Blin K., Wohlleben W., Puhler A., Weber T., Kalinowski J.;
RT "The complete genome sequence of Streptomyces collinus Tu 365.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGS67818.1, ECO:0000313|Proteomes:UP000015423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RX PubMed=24140291; DOI=10.1016/j.jbiotec.2013.10.004;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Iftime D.,
RA Musiol E.M., Blin K., Wohlleben W., Puhler A., Kalinowski J., Weber T.;
RT "Complete genome sequence of the kirromycin producer Streptomyces collinus
RT Tu 365 consisting of a linear chromosome and two linear plasmids.";
RL J. Biotechnol. 168:739-740(2013).
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR EMBL; CP006259; AGS67818.1; -; Genomic_DNA.
DR RefSeq; WP_020938302.1; NC_021985.1.
DR AlphaFoldDB; S5ULM7; -.
DR STRING; 1214242.B446_04950; -.
DR KEGG; sci:B446_04950; -.
DR PATRIC; fig|1214242.5.peg.1028; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG1902; Bacteria.
DR HOGENOM; CLU_012153_1_1_11; -.
DR Proteomes; UP000015423; Chromosome.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; 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 Reference proteome {ECO:0000313|Proteomes:UP000015423}.
FT DOMAIN 7..331
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 377..635
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 671 AA; 72328 MW; A1FFC5D30AB3C1B5 CRC64;
MSRYPHLMSP LDLGFTTLPN RVLMGSMHVG LEEAERGFER MAAFYAARAR GGVGLIVTGG
IAPNDEGRPY EGGAKLTTEA EAERHRAVTD AVHREGGRIA MQILHFGRYA YHRDLVAPSA
LQAPISPFVP RELTDAEVER TIDDYARAAR LARRAGYDGV EIMGSEGYLI NEFIAAQTNR
REDRWGGSYE NRMRFPVEIV RRVREAVGED FIIVYRLSML DLVPGGSSLE EVVTLAKAVE
AAGATIINTG IGWHEARIPT IATSVPRGAY TWVTRKLMGA VDVPLVTTNR INTPELAEQL
LADGHADMVS MARPMLADPD FVNKAAAGRP EAINTCIGCN QACLDHTFSG QITSCLVNPR
ACHETELVLS PTRLRKRVAV VGAGPAGLAC AVSAAERGHD VTLFDAASEI GGQLNVARKV
PGKQEFDETL RYFRHQLDAH GVDVRLDSRV GAADLDGYDE VVVATGVTPR TPDIPGADHP
RVLGYLDVLR DGAPVGDRVA VLGAGGIGFD VAEYLTDGGD KAHEDPATYF RNWGVDMDYT
APGGLAAPER PAPPRTVHLL QRKTTKVGAG LGKTTGWIHR TELKHRGVTM VPGVRYDRID
DAGLHITVGD ESTVLEVDTV VLCTGQEPRR DLYEELVAAG RSAHLIGGAD VAAELDAKRA
IKQGTELAAA L
//
