ID   MMAA2_MYCBO             Reviewed;         287 AA.
AC   Q7U1J9; A0A1R3XVZ3; P94923; X2BFN6;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=Cyclopropane mycolic acid synthase MmaA2;
DE            Short=CMAS;
DE            EC=2.1.1.79;
DE   AltName: Full=Cyclopropane-fatty-acyl-phospholipid synthase;
DE            Short=CFA 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=cmaC; Synonyms=mmaA2, mmas-2; OrderedLocusNames=BQ2027_MB0663C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN OXYGEN-CONTAINING MYCOLATES
RP   BIOSYNTHESIS, AND NOMENCLATURE.
RC   STRAIN=BCG / Pasteur;
RX   PubMed=9044265; DOI=10.1046/j.1365-2958.1997.2301589.x;
RA   Dubnau E., Laneelle M.-A., Soares S., Benichou A., Vaz T., Prome D.,
RA   Prome J.-C., Daffe M., Quemard A.;
RT   "Mycobacterium bovis BCG genes involved in the biosynthesis of cyclopropyl
RT   keto- and hydroxy-mycolic acids.";
RL   Mol. Microbiol. 23:313-322(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- FUNCTION: Catalyzes the conversion of a double bond to a cis
CC       cyclopropane ring at the distal position of an alpha mycolic acid via
CC       the transfer of a methylene group from S-adenosyl-L-methionine. MmaA2
CC       also catalyzes the biosynthesis of the cis-cyclopropanated
CC       methoxymycolates. Cyclopropanated mycolic acids are key factors
CC       participating in cell envelope permeability, host immunomodulation and
CC       persistence (By similarity). {ECO:0000250, ECO:0000269|PubMed:9044265}.
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   -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
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DR   EMBL; U77466; AAC44874.1; -; Genomic_DNA.
DR   EMBL; LT708304; SIT99261.1; -; Genomic_DNA.
DR   RefSeq; NP_854321.1; NC_002945.3.
DR   RefSeq; WP_003403304.1; NC_002945.4.
DR   AlphaFoldDB; Q7U1J9; -.
DR   SMR; Q7U1J9; -.
DR   PATRIC; fig|233413.5.peg.723; -.
DR   UniPathway; UPA00915; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0008825; F:cyclopropane-fatty-acyl-phospholipid synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008168; F:methyltransferase activity; IMP:UniProtKB.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0071768; P:mycolic acid biosynthetic process; IMP:UniProtKB.
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   1: Evidence at protein level;
KW   Lipid biosynthesis; Lipid metabolism; Methyltransferase;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..287
FT                   /note="Cyclopropane mycolic acid synthase MmaA2"
FT                   /id="PRO_0000398360"
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         72..74
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"
FT   BINDING         136
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        208
FT                   /note="I -> S (in Ref. 1; AAC44874)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   287 AA;  32681 MW;  4894FF920B090129 CRC64;
     MVNDLTPHFE DVQAHYDLSD DFFRLFLDPT QTYSCAHFER EDMTLEEAQI AKIDLALGKL
     GLQPGMTLLD IGCGWGATMR RAIAQYDVNV VGLTLSKNQA AHVQKSFDEM DTPLDRRVLL
     AGWEQFNEPV DRIVSIGAFE HFGHDRHADF FARAHKILPP DGVLLLHTIT GLTRQQMVDH
     GLPLTLWLAR FLKFIATEIF PGGQPPTIEM VEEQSAKTGF TLTRRQSLQP HYARTLDLWA
     EALQEHKSEA IAIQSEEVYE RYMKYLTGCA KLFRVGYIDV NQFTLAK
//