ID   PHMT2_MYCUA             Reviewed;         258 AA.
AC   A0PQ29;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Probable phthiotriol/phenolphthiotriol dimycocerosates methyltransferase 2;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MUL_2009;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA   Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
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; CP000325; ABL04448.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0PQ29; -.
DR   SMR; A0PQ29; -.
DR   STRING; 362242.MUL_2009; -.
DR   EnsemblBacteria; ABL04448; ABL04448; MUL_2009.
DR   KEGG; mul:MUL_2009; -.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_068661_0_0_11; -.
DR   OMA; VVFLNYG; -.
DR   Proteomes; UP000000765; 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; Transferase.
FT   CHAIN           1..258
FT                   /note="Probable phthiotriol/phenolphthiotriol
FT                   dimycocerosates methyltransferase 2"
FT                   /id="PRO_0000305168"
SQ   SEQUENCE   258 AA;  28934 MW;  F6B9393268B47502 CRC64;
     MALSRTHRVV AGVAHTRVYK KIWKYWYPLM TRGLGADELV FINWAYEEDP PMDLPLEATD
     EPDRCHINLY HRTATQADLS GKRVLEVSCG HGGGASYLTR TLGPASYTAL DLNPAGIKFC
     QQRHHLPGLD FVQGDAEDLP FEDESFDVVL NVEASHCYPR FPVFLEEVKR VLRPGGYFAY
     ADIRPCTEIA EWEAALAAAG LQQISHREIN AEVLRGIDIN TPKSRERVKR HLPIFLRAAG
     RNYIGATGTP PIPPDAKR