MMAA2_MYCBO
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 03-AUG-2022, entry version 98.
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; Actinobacteria; Corynebacteriales; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 EnsemblBacteria; SIT99261; SIT99261; BQ2027_MB0663C.
DR PATRIC; fig|233413.5.peg.723; -.
DR OMA; LHCITAQ; -.
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 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_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
