CMAS2_MYCLE
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 03-AUG-2022, entry version 117.
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; Actinobacteria; Corynebacteriales; 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.ML2426; -.
DR EnsemblBacteria; CAC31942; CAC31942; CAC31942.
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 OMA; ERHHFIG; -.
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 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 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