ID   TAER_MYCBP              Reviewed;         418 AA.
AC   A1KMU7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Trans-acting enoyl reductase;
DE            EC=1.3.1.-;
GN   OrderedLocusNames=BCG_2974;
OS   Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=410289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Pasteur 1173P2;
RX   PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA   Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA   Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA   Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA   Barrell B.G., Parkhill J., Cole S.T.;
RT   "Genome plasticity of BCG and impact on vaccine efficacy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(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; AM408590; CAL72963.1; -; Genomic_DNA.
DR   RefSeq; WP_003414903.1; NC_008769.1.
DR   AlphaFoldDB; A1KMU7; -.
DR   KEGG; mbb:BCG_2974; -.
DR   HOGENOM; CLU_031002_0_2_11; -.
DR   OMA; GPYQLYG; -.
DR   Proteomes; UP000001472; 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_0000304692"
SQ   SEQUENCE   418 AA;  45104 MW;  98FB2577F69F36FF CRC64;
     MSPAEREFDI VLYGATGFSG KLTAEHLAHS GSTARIALAG RSSERLRGVR MMLGPNAADW
     PLILADASQP LTLEAMAARA QVVLTTVGPY TRYGLPLVAA CAKAGTDYAD LTGELMFCRN
     SIDLYHKQAA DTGARIILAC GFDSIPSDLN VYQLYRRSVE DGTGELCDTD LVLRSFSQRW
     VSGGSVATYS EAMRTASSDP EARRLVTDPY TLTTDRGAEP ELGAQPDFLR RPGRDLAPEL
     AGFWTGGFVQ APFNTRIVRR SNALQEWAYG RRFRYSETMS LGKSMAAPIL AAAVTGTVAG
     TIGLGNKYFD RLPRRLVERV TPKPGTGPSR KTQERGHYTF ETYTTTTTGA RYRATFAHNV
     DAYKSTAVLL AQSGLALALD RDRLAELRGV LTPAAAMGDA LLARLPGAGV VMGTTRLS