ID   TAER_MYCUA              Reviewed;         418 AA.
AC   A0PQ21;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Trans-acting enoyl reductase;
DE            EC=1.3.1.-;
GN   OrderedLocusNames=MUL_2000;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA   Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
CC   -!- FUNCTION: Involved in the reduction of the double bond between C-4 and
CC       C-5 during phthiocerol dimycocerosates (DIM A) and glycosylated
CC       phenolphthiocerol dimycocerosates (PGL) biosynthesis. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the saccharopine dehydrogenase family. Enoyl
CC       reductase subfamily. {ECO:0000305}.
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DR   EMBL; CP000325; ABL04440.1; -; Genomic_DNA.
DR   RefSeq; WP_011740059.1; NC_008611.1.
DR   AlphaFoldDB; A0PQ21; -.
DR   EnsemblBacteria; ABL04440; ABL04440; MUL_2000.
DR   KEGG; mul:MUL_2000; -.
DR   eggNOG; COG3268; Bacteria.
DR   HOGENOM; CLU_031002_0_2_11; -.
DR   OMA; GPYQLYG; -.
DR   Proteomes; UP000000765; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR005097; Sacchrp_dh_NADP.
DR   Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis; Lipid metabolism; Oxidoreductase.
FT   CHAIN           1..418
FT                   /note="Trans-acting enoyl reductase"
FT                   /id="PRO_0000304696"
SQ   SEQUENCE   418 AA;  45062 MW;  7892DE3787EE5DB4 CRC64;
     MSSAQREFEI VLYGATGFSG MLTGQHLAQR DTNARIALAG RSPQRLRAVR DKLGPLASDW
     PLVVADASQP ATLEEMATRA QVILTTVGPY TRYGLPLVAA CAKAGTDYAD LTGELMFCRN
     SIDLYHKQAA DTGARIVLAC GFDSIPSDLN VHHLYRRAAE DGTGELAETN LVLRSFSQRW
     ASGGSVATYS EAMRTASSDP EAYRLVNDPY TLTTDRSAEP DLGPQPDFSM RRGRDLAPEL
     AGFWTGAFVQ GPFNTRIVRR SNALQDWAYG KQFRYSETMS LGRSFAAPIA SAAVTGAIAG
     GIGLGNKYFS RLPQRALERV TPKPGTGPSQ KSRERGHYRC ETYTTTTTGA RYLATFAHNV
     DAYASTAVLL GESGLALALD RDRLSELRGV LTPAAAMGDA LLARLPQTGV VVSATRLH