ID   CMAS1_MYCTA             Reviewed;         287 AA.
AC   A5U866; Q11195;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Cyclopropane mycolic acid synthase 1;
DE            Short=CMAS;
DE            EC=2.1.1.79 {ECO:0000269|PubMed:7604045};
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 {ECO:0000303|PubMed:7604045};
GN   OrderedLocusNames=MRA_3431;
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], FUNCTION AS A CYCLOPROPANE SYNTHASE,
RP   CATALYTIC ACTIVITY, AND NOMENCLATURE.
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=7604045; DOI=10.1073/pnas.92.14.6630;
RA   Yuan Y., Lee R.E., Besra G.S., Belisle J.T., Barry C.E. III;
RT   "Identification of a gene involved in the biosynthesis of cyclopropanated
RT   mycolic acids in Mycobacterium tuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:6630-6634(1995).
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: 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.
CC       {ECO:0000269|PubMed:7604045}.
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         Evidence={ECO:0000269|PubMed:7604045};
CC   -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC       {ECO:0000305|PubMed:7604045}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WPB7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
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DR   EMBL; U27357; AAA75624.1; -; Genomic_DNA.
DR   EMBL; CP000611; ABQ75216.1; -; Genomic_DNA.
DR   RefSeq; WP_003900041.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U866; -.
DR   SMR; A5U866; -.
DR   EnsemblBacteria; ABQ75216; ABQ75216; MRA_3431.
DR   KEGG; mra:MRA_3431; -.
DR   eggNOG; COG2230; Bacteria.
DR   HOGENOM; CLU_026434_3_0_11; -.
DR   OMA; AQHFFTG; -.
DR   OrthoDB; 1518440at2; -.
DR   UniPathway; UPA00915; -.
DR   Proteomes; UP000001988; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008825; F:cyclopropane-fatty-acyl-phospholipid synthase activity; IMP:UniProtKB.
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   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_0000300063"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000250|UniProtKB:P9WPB7"
FT   BINDING         33..34
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPB7"
FT   BINDING         68..76
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPB7"
FT   BINDING         94..99
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPB7"
FT   BINDING         123..124
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPB7"
SQ   SEQUENCE   287 AA;  32461 MW;  7E254C15DF5FFF97 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
     AALQANKGQA IALQSEEVYE RYMKYLTGCA EMFRIGYIDV NQFTCQK