ID   MMAA1_MYCTA             Reviewed;         286 AA.
AC   A5U030; P0A5Q0; P72025; P94922; P96934;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=mmaA1; Synonyms=mma1; OrderedLocusNames=MRA_0656;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX   PubMed=8917504; DOI=10.1073/pnas.93.23.12828;
RA   Yuan Y., Barry C.E. III;
RT   "A common mechanism for the biosynthesis of methoxy and cyclopropyl mycolic
RT   acids in Mycobacterium tuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:12828-12833(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
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; U66108; AAC44616.1; -; Genomic_DNA.
DR   EMBL; CP000611; ABQ72380.1; -; Genomic_DNA.
DR   RefSeq; WP_003403310.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U030; -.
DR   SMR; A5U030; -.
DR   STRING; 419947.MRA_0656; -.
DR   EnsemblBacteria; ABQ72380; ABQ72380; MRA_0656.
DR   GeneID; 45424605; -.
DR   KEGG; mra:MRA_0656; -.
DR   eggNOG; COG2230; Bacteria.
DR   HOGENOM; CLU_026434_3_0_11; -.
DR   OMA; AFKKERW; -.
DR   OrthoDB; 1518440at2; -.
DR   UniPathway; UPA00915; -.
DR   Proteomes; UP000001988; 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   1: Evidence at protein level;
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_0000300064"
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"
FT   CONFLICT        187..193
FT                   /note="DLRFLKF -> ELPIPQI (in Ref. 1; AAC44616)"
FT                   /evidence="ECO:0000305"
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