ID   PHKR_MYCKA              Reviewed;         367 AA.
AC   Q4VHK1;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Phthiodiolone/phenolphthiodiolone dimycocerosates ketoreductase;
DE            EC=1.2.-.-;
DE   Flags: Fragment;
OS   Mycobacterium kansasii.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1768;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 12478 / DSM 44162 / CIP 104589 / JCM 6379 / NCTC 13024 / TMC
RC   1204 / P-16;
RX   PubMed=15995190; DOI=10.1128/jb.187.14.4760-4766.2005;
RA   Onwueme K.C., Vos C.J., Zurita J., Soll C.E., Quadri L.E.N.;
RT   "Identification of phthiodiolone ketoreductase, an enzyme required for
RT   production of mycobacterial diacyl phthiocerol virulence factors.";
RL   J. Bacteriol. 187:4760-4766(2005).
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}.
CC   -!- CAUTION: According to PubMed:15995190, this enzyme is not functional in
CC       M.kansasii, due to mutations outside this fragment, possibly in the
CC       ribosome-binding site or promoter/regulatory regions. {ECO:0000305}.
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DR   EMBL; AY906857; AAX98285.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4VHK1; -.
DR   SMR; Q4VHK1; -.
DR   STRING; 1768.B1T50_23930; -.
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..367
FT                   /note="Phthiodiolone/phenolphthiodiolone dimycocerosates
FT                   ketoreductase"
FT                   /id="PRO_0000309349"
FT   NON_TER         1
SQ   SEQUENCE   367 AA;  39761 MW;  E5B72275FFB68BAA CRC64;
     SRFRPGWLAR SSMVAATLTG ADSYWVGDHL NGLVPRSIAT PEYLGIAAKL VPSVDANYEP
     WTMLGNLAYG RPKRLRLGIC VTDAGRRNPA VTAQAAATLQ LLTRGNAILG IGVGEREGNE
     PYGVEWTRPV ARFEEALATI RALWNSNGEL VSRESAYFPL QNAAFELPPY RGKWPEIWVA
     AHGPRMLRAT GRYADAWVPI VLVRPGDYST ALEAVRTAAS DAGRDPMSII PSAVRGVITG
     RDRDDVEEAL DSVVVKMTAL GVPGTAWARH GVEHPMGADF AGVQDVIPQT MDEQTVLSYT
     AKVPPALMKE VVFSGTPEEV VDQVAQWRDH GLEYLLVING SLVNPSLRKA VAASLPHAKV
     LRGLKKL