ID   CMAS1_MYCTO             Reviewed;         287 AA.
AC   P9WPB6; L0TCE3; P0C5C2; Q11195;
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 1;
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=cmaA1; Synonyms=cma1, CMAS-1; OrderedLocusNames=MT3499;
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 conversion of a double bond to a cyclopropane
CC       ring at the distal position of an alpha mycolic acid via the transfer
CC       of a methylene group from S-adenosyl-L-methionine. Cyclopropanated
CC       mycolic acids are key factors participating in cell envelope
CC       permeability, host immunomodulation and persistence (By similarity).
CC       {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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK47836.1; -; Genomic_DNA.
DR   PIR; G70974; G70974.
DR   RefSeq; WP_003917785.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPB6; -.
DR   SMR; P9WPB6; -.
DR   DrugCentral; P9WPB6; -.
DR   EnsemblBacteria; AAK47836; AAK47836; MT3499.
DR   KEGG; mtc:MT3499; -.
DR   PATRIC; fig|83331.31.peg.3756; -.
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..287
FT                   /note="Cyclopropane mycolic acid synthase 1"
FT                   /id="PRO_0000426980"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000250"
FT   BINDING         33..34
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         68..76
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         94..99
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         123..124
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   287 AA;  32505 MW;  3F254C15DF58F8E7 CRC64;
     MPDELKPHFA NVQAHYDLSD DFFRLFLDPT QTYSCAYFER DDMTLQEAQI AKIDLALGKL
     GLQPGMTLLD VGCGWGATMM RAVEKYDVNV VGLTLSKNQA NHVQQLVANS ENLRSKRVLL
     AGWEQFDEPV DRIVSIGAFE HFGHERYDAF FSLAHRLLPA DGVMLLHTIT GLHPKEIHER
     GLPMSFTFAR FLKFIVTEIF PGGRLPSIPM VQECASANGF TVTRVQSLQP HYAKTLDLWS
     AALQANKGQD IALQSEEVYE RYMKYLTGCA EMFRIGYIDV NQFTCQK