ID   MMAA1_MYCBO             Reviewed;         286 AA.
AC   P0A5Q1; A0A1R3XY38; P72025; P94922; P96934; X2BFH5;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Mycolic acid methyltransferase MmaA1;
DE            EC=2.1.1.-;
DE   AltName: Full=S-adenosylmethionine-dependent methyltransferase;
DE            Short=AdoMet-MT;
DE            Short=SAM-MT;
GN   Name=cmaD; Synonyms=mma1, mmaA1, mmas-1; OrderedLocusNames=BQ2027_MB0664C;
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 [GENOMIC DNA].
RC   STRAIN=BCG / Pasteur;
RX   PubMed=9044265; DOI=10.1046/j.1365-2958.1997.2301589.x;
RA   Dubnau E., Laneelle M.-A., Soares S., Benichou A., Vaz T., Prome D.,
RA   Prome J.-C., Daffe M., Quemard A.;
RT   "Mycobacterium bovis BCG genes involved in the biosynthesis of cyclopropyl
RT   keto- and hydroxy-mycolic acids.";
RL   Mol. Microbiol. 23:313-322(1997).
RN   [2]
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   [3]
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: Involved in the conversion of a cis-olefin into a trans-
CC       olefin with concomitant introduction of an allylic methyl branch at the
CC       proximal position of the precursor to both the methoxy and ketomycolic
CC       acids. It directly affects the cis- to trans ratio and indirectly
CC       affects the keto to methoxy ratio (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC   -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
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DR   EMBL; U77466; AAC44873.1; -; Genomic_DNA.
DR   EMBL; LT708304; SIT99262.1; -; Genomic_DNA.
DR   RefSeq; NP_854322.1; NC_002945.3.
DR   RefSeq; WP_003403310.1; NC_002945.4.
DR   AlphaFoldDB; P0A5Q1; -.
DR   SMR; P0A5Q1; -.
DR   EnsemblBacteria; SIT99262; SIT99262; BQ2027_MB0664C.
DR   GeneID; 45424605; -.
DR   PATRIC; fig|233413.5.peg.724; -.
DR   OMA; AFKKERW; -.
DR   UniPathway; UPA00915; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR003333; Mycolic_cyclopropane_synthase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PIRSF; PIRSF003085; CMAS; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis; Lipid metabolism; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..286
FT                   /note="Mycolic acid methyltransferase MmaA1"
FT                   /id="PRO_0000096503"
FT   ACT_SITE        268
FT                   /evidence="ECO:0000250"
FT   BINDING         32..33
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         71..73
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         93..98
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         122..123
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   286 AA;  33149 MW;  229EB252DCA8C552 CRC64;
     MAKLRPYYEE SQSAYDISDD FFALFLDPTW VYTCAYFERD DMTLEEAQLA KVDLALDKLN
     LEPGMTLLDV GCGWGGALVR AVEKYDVNVI GLTLSRNHYE RSKDRLAAIG TQRRAEARLQ
     GWEEFEENVD RIVSFEAFDA FKKERYLTFF ERSYDILPDD GRMLLHSLFT YDRRWLHEQG
     IALTMSDLRF LKFLRESIFP GGELPSEPDI VDNAQAAGFT IEHVQLLQQH YARTLDAWAA
     NLQAARERAI AVQSEEVYNN FMHYLTGCAE RFRRGLINVA QFTMTK