ID   CMAS2_MYCTO             Reviewed;         302 AA.
AC   P9WPB4; L0T3U0; P0A5P0; Q11196;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Cyclopropane mycolic acid synthase 2;
DE            Short=CMAS;
DE            EC=2.1.1.79;
DE   AltName: Full=Cyclopropane-fatty-acyl-phospholipid synthase;
DE            Short=CFA synthase;
DE            Short=Cyclopropane fatty acid synthase;
DE   AltName: Full=Mycolic acid methyltransferase;
DE            Short=MA-MT;
DE   AltName: Full=S-adenosylmethionine-dependent methyltransferase;
DE            Short=AdoMet-MT;
DE            Short=SAM-MT;
GN   Name=cmaA2; Synonyms=cma2, CMAS-2; OrderedLocusNames=MT0524;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Catalyzes the formation of trans cyclopropanated ketomycolate
CC       or methoxymycolate through the conversion of a double bond to a
CC       cyclopropane ring at the proximal position of an oxygenated mycolic
CC       acid via the transfer of a methylene group from S-adenosyl-L-
CC       methionine. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-
CC         methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid
CC         + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11988,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:76593, ChEBI:CHEBI:76594; EC=2.1.1.79;
CC   -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK44747.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK44747.1; ALT_INIT; Genomic_DNA.
DR   PIR; B70746; B70746.
DR   RefSeq; WP_003402621.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPB4; -.
DR   SMR; P9WPB4; -.
DR   EnsemblBacteria; AAK44747; AAK44747; MT0524.
DR   KEGG; mtc:MT0524; -.
DR   PATRIC; fig|83331.31.peg.555; -.
DR   HOGENOM; CLU_026434_3_0_11; -.
DR   UniPathway; UPA00915; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008825; F:cyclopropane-fatty-acyl-phospholipid synthase activity; IEA:UniProtKB-EC.
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   Cytoplasm; Lipid biosynthesis; Lipid metabolism; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..302
FT                   /note="Cyclopropane mycolic acid synthase 2"
FT                   /id="PRO_0000426981"
FT   ACT_SITE        284
FT                   /evidence="ECO:0000250"
FT   BINDING         41..42
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         76..84
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         102..107
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         131..132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   302 AA;  34660 MW;  63AAA95627F95755 CRC64;
     MTSQGDTTSG TQLKPPVEAV RSHYDKSNEF FKLWLDPSMT YSCAYFERPD MTLEEAQYAK
     RKLALDKLNL EPGMTLLDIG CGWGSTMRHA VAEYDVNVIG LTLSENQYAH DKAMFDEVDS
     PRRKEVRIQG WEEFDEPVDR IVSLGAFEHF ADGAGDAGFE RYDTFFKKFY NLTPDDGRML
     LHTITIPDKE EAQELGLTSP MSLLRFIKFI LTEIFPGGRL PRISQVDYYS SNAGWKVERY
     HRIGANYVPT LNAWADALQA HKDEAIALKG QETYDIYMHY LRGCSDLFRD KYTDVCQFTL
     VK