ID D9W443_9ACTN Unreviewed; 440 AA.
AC D9W443;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Crotonyl-CoA reductase {ECO:0000313|EMBL:EFL19671.1};
GN ORFNames=SSNG_06923 {ECO:0000313|EMBL:EFL19671.1};
OS Streptomyces sp. C.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL19671.1, ECO:0000313|Proteomes:UP000005763};
RN [1] {ECO:0000313|EMBL:EFL19671.1, ECO:0000313|Proteomes:UP000005763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C {ECO:0000313|EMBL:EFL19671.1,
RC ECO:0000313|Proteomes:UP000005763};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. strain C.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GG657751; EFL19671.1; -; Genomic_DNA.
DR RefSeq; WP_007268596.1; NZ_GG657751.1.
DR AlphaFoldDB; D9W443; -.
DR SMR; D9W443; -.
DR STRING; 253839.SSNG_06923; -.
DR eggNOG; COG0604; Bacteria.
DR HOGENOM; CLU_026673_5_0_11; -.
DR Proteomes; UP000005763; Unassembled WGS sequence.
DR GO; GO:0043880; F:crotonyl-CoA reductase activity; IEA:InterPro.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 2.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR010085; Crot_CoA_red.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR NCBIfam; TIGR01751; crot-CoA-red; 1.
DR PANTHER; PTHR44154; QUINONE OXIDOREDUCTASE; 1.
DR PANTHER; PTHR44154:SF1; QUINONE OXIDOREDUCTASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
FT DOMAIN 47..410
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 440 AA; 47531 MW; E4A7A29813A342F4 CRC64;
MSTPLADAVI EGRSGEELLS LPLPGRMKAV TVHKDQTGMF DGVADKDVRK SMHVEDVPIP
ELAPDEVLVA VMAGAINFNT VWSATFEPVP TFRFLEQMGR RGGWDARHDL PYHILGSDAS
GVVVRTGSAV RRWNAGDHVV IGTAYVDEQD PATHRDGMLG EDQRAWGFET NFGGLAEYTV
VRASQLLPKP ALLTWEEAAA NPLCAGTAYR MLVSDRGARM KQGDVVLIWG ATGGLGAYAV
QLVRNGGGIP VGVVSSAEKA EVLRKLGCEA VIDRSAIEQG DRTLLQRPEG WKKLGKAIRD
AVGEDPHIVF EHVGKATFGA SVFLARRGGT VVTCGSSTGY DHQYDNRYLW MKLKNIIGSH
GANLNEQWET NRLIEMGRVL PALSATYALD DAGEAARSVQ VNEHLGKVGV LGLAPRAGLG
VTDAQARARV GEERFRLFRS
//
