ID   MMAA2_MYCTA             Reviewed;         287 AA.
AC   A5U029; P72026;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Cyclopropane mycolic acid synthase MmaA2;
DE            Short=CMAS;
DE            EC=2.1.1.79 {ECO:0000269|PubMed:8917504};
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=mmaA2; Synonyms=mma2; OrderedLocusNames=MRA_0655;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN OXYGEN-CONTAINING MYCOLATES
RP   BIOSYNTHESIS, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=8917504; DOI=10.1073/pnas.93.23.12828;
RA   Yuan Y., Barry C.E. III;
RT   "A common mechanism for the biosynthesis of methoxy and cyclopropyl mycolic
RT   acids in Mycobacterium tuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:12828-12833(1996).
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 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. {ECO:0000269|PubMed:8917504}.
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:8917504};
CC   -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC       {ECO:0000305|PubMed:8917504}.
CC   -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC44617.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U66108; AAC44617.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP000611; ABQ72379.1; -; Genomic_DNA.
DR   PIR; A70614; A70614.
DR   RefSeq; WP_003900985.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U029; -.
DR   SMR; A5U029; -.
DR   GeneID; 45424604; -.
DR   KEGG; mra:MRA_0655; -.
DR   eggNOG; COG2230; Bacteria.
DR   HOGENOM; CLU_026434_3_0_11; -.
DR   UniPathway; UPA00915; -.
DR   Proteomes; UP000001988; Chromosome.
DR   GO; GO:0008825; F:cyclopropane-fatty-acyl-phospholipid synthase activity; IMP:UniProtKB.
DR   GO; GO:0008168; F:methyltransferase activity; IMP:UniProtKB.
DR   GO; GO:0008610; P:lipid biosynthetic process; IMP:UniProtKB.
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   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_0000398361"
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|UniProtKB:Q79FX6"
FT   BINDING         72..74
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q79FX6"
FT   BINDING         94..99
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q79FX6"
FT   BINDING         123..124
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q79FX6"
FT   BINDING         136
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q79FX6"
SQ   SEQUENCE   287 AA;  32724 MW;  669C3224C6B178C0 CRC64;
     MVNDLTPHFE DVQAHYDLSD DFFRLFLDPT QTYSCAHFER EDMTLEEAQI AKIDLALGKL
     GLQPGMTLLD IGCGWGATMR RAIAQYDVNV VGLTLSKNQA AHVQKSFDEM DTPRDRRVLL
     AGWEQFNEPV DRIVSIGAFE HFGHDRHADF FARAHKILPP DGVLLLHTIT GLTRQQMVDH
     GLPLTLWLAR FLKFIATEIF PGGQPPTIEM VEEQSAKTGF TLTRRQSLQP HYARTLDLWA
     EALQEHKSEA IAIQSEEVYE RYMKYLTGCA KLFRVGYIDV NQFTLAK
//