ID   CMAS2_MYCLE             Reviewed;         308 AA.
AC   Q49807;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 124.
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; OrderedLocusNames=ML2426; ORFNames=B2168_F3_130;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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. In the absence of MmaA2, CmaA2 has a non-specific cis-
CC       cyclopropanating activity and is able to catalyze the conversion of a
CC       double bond to a cis cyclopropane ring at the distal position of an
CC       alpha mycolic acid. Cyclopropanated mycolic acids are key factors
CC       participating in cell envelope permeability, host immunomodulation and
CC       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; U00018; AAA17222.1; -; Genomic_DNA.
DR   EMBL; AL583925; CAC31942.1; -; Genomic_DNA.
DR   PIR; S72886; S72886.
DR   RefSeq; NP_302570.1; NC_002677.1.
DR   RefSeq; WP_010908890.1; NC_002677.1.
DR   AlphaFoldDB; Q49807; -.
DR   SMR; Q49807; -.
DR   STRING; 272631.gene:17576288; -.
DR   KEGG; mle:ML2426; -.
DR   PATRIC; fig|272631.5.peg.4664; -.
DR   Leproma; ML2426; -.
DR   eggNOG; COG2230; Bacteria.
DR   HOGENOM; CLU_026434_3_0_11; -.
DR   OrthoDB; 9782855at2; -.
DR   UniPathway; UPA00915; -.
DR   Proteomes; UP000000806; 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   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003333; CMAS.
DR   InterPro; IPR047672; CMAS_actinobact.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; NF040660; mycolic_MTase; 1.
DR   PANTHER; PTHR43667; CYCLOPROPANE-FATTY-ACYL-PHOSPHOLIPID SYNTHASE; 1.
DR   PANTHER; PTHR43667:SF1; CYCLOPROPANE-FATTY-ACYL-PHOSPHOLIPID SYNTHASE; 1.
DR   Pfam; PF02353; CMAS; 1.
DR   PIRSF; PIRSF003085; CMAS; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lipid biosynthesis; Lipid metabolism; Methyltransferase;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..308
FT                   /note="Cyclopropane mycolic acid synthase 2"
FT                   /id="PRO_0000089568"
FT   ACT_SITE        290
FT                   /evidence="ECO:0000250"
FT   BINDING         44..45
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         79..87
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         105..110
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         137..138
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   308 AA;  35132 MW;  9068380ED6D324AA CRC64;
     MVPSQSHPAK TPRKQLKPPI EAVQSHYDRS NEFFKLWLDP SMTYSCAYFE RPDLTLEEAQ
     RAKRDLALSK LGLEPGMTLL DIGCGWGSTM LHAIEKYDVN VIGLTLSANQ LAHNKLKFAE
     IDHTRTDRTK DVRLQGWEQF DEPVDRIISL GAFEHFADGA GDAGFERYDS FFKMCYDVLP
     DDGRMLLHTI IVPDAKETKE LGLTTPMSLL RFIKFILTEI FPGGRLPKIS QVDHYSSNAG
     FTVERYHRIG SHYVPTLNAW AAALEAHKDE AIALQGRQIY DTYMHYLTGC SDLFRDRYTD
     VCQFTLVK
//