ID   PHKR_MYCBP              Reviewed;         381 AA.
AC   A1KMU5;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Phthiodiolone/phenolphthiodiolone dimycocerosates ketoreductase;
DE            EC=1.2.-.-;
GN   OrderedLocusNames=BCG_2972c;
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: 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; AM408590; CAL72961.1; -; Genomic_DNA.
DR   RefSeq; WP_003414891.1; NC_008769.1.
DR   AlphaFoldDB; A1KMU5; -.
DR   SMR; A1KMU5; -.
DR   KEGG; mbb:BCG_2972c; -.
DR   HOGENOM; CLU_027853_5_3_11; -.
DR   OMA; EPYGVDW; -.
DR   Proteomes; UP000001472; 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.
FT   CHAIN           1..381
FT                   /note="Phthiodiolone/phenolphthiodiolone dimycocerosates
FT                   ketoreductase"
FT                   /id="PRO_0000309348"
SQ   SEQUENCE   381 AA;  41348 MW;  B04C942A84D8528B CRC64;
     MGGLRFGFVD ALVHSRLPPT LPARSSMAAA TVMGADSYWV GDHLNALVPR SIATSEYLGI
     AAKFVPKIDA NYEPWTMLGN LAFGLPSRLR LGVCVTDAGR RNPAVTAQAA ATLHLLTRGR
     AILGIGVGER EGNEPYGVEW TKPVARFEEA LATIRALWNS NGELISRESP YFPLHNALFD
     LPPYRGKWPE IWVAAHGPRM LRATGRYADA WIPIVVVRPS DYSRALEAVR SAASDAGRDP
     MSITPAAVRG IITGRNRDDV EEALESVVVK MTALGVPGEA WARHGVEHPM GADFSGVQDI
     IPQTMDKQTV LSYAAKVPAA LMKEVVFSGT PDEVIDQVAE WRDHGLRYVV LINGSLVNPS
     LRKTVTAVLP HAKVLRGLKK L