ID   PHMT_MYCLE              Reviewed;         270 AA.
AC   Q9CD86;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Phthiotriol/phenolphthiotriol dimycocerosates methyltransferase;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=ML0130;
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 methylation of the lipid moiety of the
CC       intermediate compounds phthiotriol and glycosylated phenolphthiotriol
CC       dimycoserosates to form phthiocerol dimycocerosates (DIM A) and
CC       glycosylated phenolphthiocerol dimycocerosates (PGL). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       Phthiotriol/phenolphthiotriol dimycocerosates methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AL583917; CAC29638.1; -; Genomic_DNA.
DR   PIR; B86925; B86925.
DR   RefSeq; NP_301224.1; NC_002677.1.
DR   RefSeq; WP_010907549.1; NC_002677.1.
DR   AlphaFoldDB; Q9CD86; -.
DR   SMR; Q9CD86; -.
DR   STRING; 272631.ML0130; -.
DR   EnsemblBacteria; CAC29638; CAC29638; CAC29638.
DR   KEGG; mle:ML0130; -.
DR   PATRIC; fig|272631.5.peg.198; -.
DR   Leproma; ML0130; -.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_068661_0_0_11; -.
DR   OMA; EWILRAH; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis; Lipid metabolism; Methyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..270
FT                   /note="Phthiotriol/phenolphthiotriol dimycocerosates
FT                   methyltransferase"
FT                   /id="PRO_0000305164"
SQ   SEQUENCE   270 AA;  30641 MW;  ADEB3309002A2924 CRC64;
     MAFTRIHSFL ASAGNTSMYK RVWRFWYPLM THKLGTDEIM FINWAYEEDP PMALPLEASD
     EPNRAHINLY HRTATQVNLS GKRILEVSCG HGGGASYLTR ALHPASYTGL DLNPAGIKLC
     QKRHQLPGLE FVRGDAENLP FDNESFDVVI NIEASHCYPH FPRFLAEVVR VLRPGGHLAY
     ADLRPSNKVG EWEVDFANSR LQQLSQREIN AEVLRGIASN SQKSRDLVDR HLPAFLRFAG
     REFIGVQGTQ LSRYLEGGEL SYRMYSFAKD