ID   CMAS3_MYCTO             Reviewed;         287 AA.
AC   P9WPB2; L0T6K4; Q6MX38; Q7D9R5;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Cyclopropane mycolic acid synthase 3;
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=pcaA; Synonyms=cma3, cmaA3, CMAS-3; OrderedLocusNames=MT0486;
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: Involved in the phagosome maturation block (PMB). Catalyzes
CC       the conversion of a double bond to a cyclopropane ring at the proximal
CC       position of an alpha mycolic acid via the transfer of a methylene group
CC       from S-adenosyl-L-methionine. It can use cis, cis 11,14-eicosadienoic
CC       acid and linoelaidic acid as substrate. Cyclopropanated mycolic acids
CC       are key factors participating in cell envelope permeability, host
CC       immunomodulation and persistence (By similarity). {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}.
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DR   EMBL; AE000516; AAK44709.1; -; Genomic_DNA.
DR   PIR; B70829; B70829.
DR   RefSeq; WP_003402323.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPB2; -.
DR   SMR; P9WPB2; -.
DR   EnsemblBacteria; AAK44709; AAK44709; MT0486.
DR   GeneID; 45424432; -.
DR   KEGG; mtc:MT0486; -.
DR   PATRIC; fig|83331.31.peg.516; -.
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 3"
FT                   /id="PRO_0000426982"
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;  33028 MW;  B8D2999A4CD81112 CRC64;
     MSVQLTPHFG NVQAHYDLSD DFFRLFLDPT QTYSCAYFER DDMTLQEAQI AKIDLALGKL
     NLEPGMTLLD IGCGWGATMR RAIEKYDVNV VGLTLSENQA GHVQKMFDQM DTPRSRRVLL
     EGWEKFDEPV DRIVSIGAFE HFGHQRYHHF FEVTHRTLPA DGKMLLHTIV RPTFKEGREK
     GLTLTHELVH FTKFILAEIF PGGWLPSIPT VHEYAEKVGF RVTAVQSLQL HYARTLDMWA
     TALEANKDQA IAIQSQTVYD RYMKYLTGCA KLFRQGYTDV DQFTLEK