PHMT_MYCBO
ID PHMT_MYCBO Reviewed; 270 AA.
AC Q7TXK3; A0A1R3Y329; X2BMB7;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Phthiotriol/phenolphthiotriol dimycocerosates methyltransferase;
DE EC=2.1.1.-;
GN OrderedLocusNames=BQ2027_MB2976;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIU01598.1; -; Genomic_DNA.
DR RefSeq; NP_856621.1; NC_002945.3.
DR RefSeq; WP_003414900.1; NC_002945.4.
DR AlphaFoldDB; Q7TXK3; -.
DR SMR; Q7TXK3; -.
DR EnsemblBacteria; SIU01598; SIU01598; BQ2027_MB2976.
DR PATRIC; fig|233413.5.peg.3270; -.
DR OMA; EWILRAH; -.
DR BioCyc; MetaCyc:MON-19635; -.
DR Proteomes; UP000001419; 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..270
FT /note="Phthiotriol/phenolphthiotriol dimycocerosates
FT methyltransferase"
FT /id="PRO_0000305162"
SQ SEQUENCE 270 AA; 30652 MW; 92116ADD4261EDE7 CRC64;
MAFSRTHSLL ARAGSTSTYK RVWRYWYPLM TRGLGNDEIV FINWAYEEDP PMDLPLEASD
EPNRAHINLY HRTATQVDLG GKQVLEVSCG HGGGASYLTR TLHPASYTGL DLNQAGIKLC
KKRHRLPGLD FVRGDAENLP FDDESFDVVL NVEASHCYPH FRRFLAEVVR VLRPGGYFPY
ADLRPNNEIA AWEADLAATP LRQLSQRQIN AEVLRGIGNN SQKSRDLVDR HLPAFLRFAG
REFIGVQGTQ LSRYLEGGEL SYRMYCFTKD