MMAA2_MYCTA
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 03-AUG-2022, entry version 71.
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; Actinobacteria; Corynebacteriales; 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 STRING; 419947.MRA_0655; -.
DR EnsemblBacteria; ABQ72379; ABQ72379; MRA_0655.
DR GeneID; 45424604; -.
DR KEGG; mra:MRA_0655; -.
DR eggNOG; COG2230; Bacteria.
DR HOGENOM; CLU_026434_3_0_11; -.
DR OMA; LHCITAQ; -.
DR OrthoDB; 1518440at2; -.
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 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 Lipid biosynthesis; Lipid metabolism; Methyltransferase;
KW 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
