ID   PHKR_MYCLE              Reviewed;         382 AA.
AC   Q9CD85;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Phthiodiolone/phenolphthiodiolone dimycocerosates ketoreductase;
DE            EC=1.2.-.-;
GN   OrderedLocusNames=ML0131;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Catalyzes the reduction of the keto moiety of phthiodiolone
CC       dimycocerosates (DIM B) and glycosylated phenolphthiodiolone
CC       dimycocerosates to form the intermediate compounds phthiotriol and
CC       glycosylated phenolphthiotriol dimycocerosates during phthiocerol
CC       dimycocerosates (DIM A) and glycosylated phenolphthiocerol
CC       dimycocerosates (PGL) biosynthesis. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the mer family.
CC       Phthiodiolone/phenolphthiodiolone dimycocerosates ketoreductase
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AL583917; CAC29639.1; -; Genomic_DNA.
DR   PIR; C86925; C86925.
DR   RefSeq; NP_301225.1; NC_002677.1.
DR   RefSeq; WP_010907550.1; NC_002677.1.
DR   AlphaFoldDB; Q9CD85; -.
DR   SMR; Q9CD85; -.
DR   STRING; 272631.ML0131; -.
DR   EnsemblBacteria; CAC29639; CAC29639; CAC29639.
DR   KEGG; mle:ML0131; -.
DR   PATRIC; fig|272631.5.peg.199; -.
DR   Leproma; ML0131; -.
DR   eggNOG; COG2141; Bacteria.
DR   HOGENOM; CLU_027853_5_3_11; -.
DR   OMA; EPYGVDW; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.30; -; 1.
DR   InterPro; IPR011251; Luciferase-like_dom.
DR   InterPro; IPR036661; Luciferase-like_sf.
DR   Pfam; PF00296; Bac_luciferase; 1.
DR   SUPFAM; SSF51679; SSF51679; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis; Lipid metabolism; Oxidoreductase; Reference proteome.
FT   CHAIN           1..382
FT                   /note="Phthiodiolone/phenolphthiodiolone dimycocerosates
FT                   ketoreductase"
FT                   /id="PRO_0000309350"
SQ   SEQUENCE   382 AA;  41258 MW;  29618F4527314A5F CRC64;
     MAGFRFGFVD ALVHTLFPPS LPARASIVSG AVLGADSYWV GDHLNALVPR SVATPKYLGV
     AAKVVPKIDA NYEPWTMLGN LAAGNRLNGL RLGVCVTDAG RRNPAVTAQA AATLHLLTRG
     KAMLGIGVGE REGNEPYGVE WTKPVARFQE ALATIRALWD SNGELVSRES QFFPLHNALF
     DLPPYRGKWP EIWVAAHGPR MLQATGRYAD AWIPIVLVRP TDYSCALEVV RTAASDAGRD
     PMSITPAAVR GIITGRTRDD VDEALDSVLV RMIALGVPGE AWARHGVEHP MGADFAGVQD
     IIPQTIDEET VVSYAAKVPA ALMKEVLFSG TPEEVIDQVA EWRDHGLKYL VVINGSLVNS
     SLRKTVSALL PHARVLRGLK KL