ID   PHKR_MYCSJ              Reviewed;         380 AA.
AC   A3Q7Z7;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Phthiodiolone/phenolphthiodiolone dimycocerosates ketoreductase;
DE            EC=1.2.-.-;
GN   OrderedLocusNames=Mjls_5511;
OS   Mycobacterium sp. (strain JLS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=164757;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J.,
RA   Sims R.C., Richardson P.;
RT   "Complete sequence of Mycobacterium sp. JLS.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000580; ABO01275.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3Q7Z7; -.
DR   SMR; A3Q7Z7; -.
DR   STRING; 164757.Mjls_5511; -.
DR   KEGG; mjl:Mjls_5511; -.
DR   HOGENOM; CLU_027853_5_3_11; -.
DR   OMA; EPYGVDW; -.
DR   BioCyc; MSP164757:G1G8C-5573-MON; -.
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..380
FT                   /note="Phthiodiolone/phenolphthiodiolone dimycocerosates
FT                   ketoreductase"
FT                   /id="PRO_0000309351"
SQ   SEQUENCE   380 AA;  41966 MW;  DF9F5750A47132F5 CRC64;
     MTGFRVGVGD GIPAARPAAE TMTRANYLGA VANRVDSFWV PDHLNQLFPR SLWKQKYCGA
     TKLIPRVDAV MEPWTMLGHI AARNRAGRLR LGVAVTDSGR RNPAVTAQAA ATLHLLTRGR
     AILGIGPGER EGNEPYGVDW SKPVARFEEA MATIRALWDS GGELVNRDSP FFPLRKAIFD
     LPPYRGKWPE IWIAAHGPRM LRAAGRYADA YFPSFAHLPT EYAQRLDSVR SAASDVGRDP
     MAILPAVQMF VVTGSTRDDV DEALDSELLR AFGLNASDDV FTRHGGRHPM GAGFSGAQDL
     LPHDMDEQTA LSHVAVIPPG VTREFLLNGT SDEVIQQAAQ WRDCVRYMVL VNVSFLQRNL
     RKGLMSVKPF NKIVRELKKL