ID   PHKR_MYCTU              Reviewed;         381 AA.
AC   P9WIB7; L0TB46; P95140; Q50465; Q7D6D6;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Phthiodiolone/phenolphthiodiolone dimycocerosates ketoreductase;
DE            EC=1.2.-.-;
GN   OrderedLocusNames=Rv2951c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [3]
RP   FUNCTION AS A KETOREDUCTASE.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=17371506; DOI=10.1111/j.1742-4658.2007.05740.x;
RA   Simeone R., Constant P., Malaga W., Guilhot C., Daffe M., Chalut C.;
RT   "Molecular dissection of the biosynthetic relationship between phthiocerol
RT   and phthiodiolone dimycocerosates and their critical role in the virulence
RT   and permeability of Mycobacterium tuberculosis.";
RL   FEBS J. 274:1957-1969(2007).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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:0000269|PubMed:17371506}.
CC   -!- SIMILARITY: Belongs to the mer family.
CC       Phthiodiolone/phenolphthiodiolone dimycocerosates ketoreductase
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA50933.1; Type=Frameshift; Evidence={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; U00024; AAA50933.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL123456; CCP45755.1; -; Genomic_DNA.
DR   PIR; D70669; D70669.
DR   RefSeq; NP_217467.1; NC_000962.3.
DR   RefSeq; WP_003414891.1; NZ_NVQJ01000015.1.
DR   AlphaFoldDB; P9WIB7; -.
DR   SMR; P9WIB7; -.
DR   STRING; 83332.Rv2951c; -.
DR   PaxDb; P9WIB7; -.
DR   DNASU; 887887; -.
DR   GeneID; 887887; -.
DR   KEGG; mtu:Rv2951c; -.
DR   TubercuList; Rv2951c; -.
DR   eggNOG; COG2141; Bacteria.
DR   OMA; EPYGVDW; -.
DR   PhylomeDB; P9WIB7; -.
DR   BioCyc; MetaCyc:G185E-7205-MON; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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   1: Evidence at protein level;
KW   Lipid biosynthesis; Lipid metabolism; Oxidoreductase; Reference proteome.
FT   CHAIN           1..381
FT                   /note="Phthiodiolone/phenolphthiodiolone dimycocerosates
FT                   ketoreductase"
FT                   /id="PRO_0000309352"
FT   CONFLICT        195..196
FT                   /note="Missing (in Ref. 1; AAA50933)"
FT                   /evidence="ECO:0000305"
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