CMAS1_MYCTU
ID CMAS1_MYCTU Reviewed; 287 AA.
AC P9WPB7; L0TCE3; P0C5C2; Q11195;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Cyclopropane mycolic acid synthase 1 {ECO:0000303|PubMed:7592990};
DE Short=CMAS-1 {ECO:0000303|PubMed:7592990};
DE EC=2.1.1.79 {ECO:0000269|PubMed:7592990};
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=cmaA1 {ECO:0000303|PubMed:7592990}; Synonyms=cma1, CMAS-1;
GN OrderedLocusNames=Rv3392c; ORFNames=MTV004.50;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION AS A CYCLOPROPANE SYNTHASE, CATALYTIC ACTIVITY, AND NOMENCLATURE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=7592990; DOI=10.1074/jbc.270.45.27292;
RA George K.M., Yuan Y., Sherman D.R., Barry C.E. III;
RT "The biosynthesis of cyclopropanated mycolic acids in Mycobacterium
RT tuberculosis. Identification and functional analysis of CMAS-2.";
RL J. Biol. Chem. 270:27292-27298(1995).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4] {ECO:0007744|PDB:1KP9, ECO:0007744|PDB:1KPG, ECO:0007744|PDB:1KPH}
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 18-287 IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE AND SUBSTRATE ANALOG, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=11756461; DOI=10.1074/jbc.m111698200;
RA Huang C.-C., Smith C.V., Glickman M.S., Jacobs W.R. Jr., Sacchettini J.C.;
RT "Crystal structures of mycolic acid cyclopropane synthases from
RT Mycobacterium tuberculosis.";
RL J. Biol. Chem. 277:11559-11569(2002).
CC -!- FUNCTION: Catalyzes the conversion of a double bond to a cyclopropane
CC ring at the distal position of an alpha mycolic acid via the transfer
CC of a methylene group from S-adenosyl-L-methionine. Cyclopropanated
CC mycolic acids are key factors participating in cell envelope
CC permeability, host immunomodulation and persistence.
CC {ECO:0000269|PubMed:7592990}.
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:7592990};
CC -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC {ECO:0000305|PubMed:7592990}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11756461}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46213.1; -; Genomic_DNA.
DR PIR; G70974; G70974.
DR RefSeq; NP_217909.1; NC_000962.3.
DR RefSeq; WP_003900041.1; NZ_NVQJ01000027.1.
DR PDB; 1KP9; X-ray; 2.21 A; A/B=1-287.
DR PDB; 1KPG; X-ray; 2.00 A; A/B/C/D=2-287.
DR PDB; 1KPH; X-ray; 2.00 A; A/B/C/D=1-287.
DR PDBsum; 1KP9; -.
DR PDBsum; 1KPG; -.
DR PDBsum; 1KPH; -.
DR AlphaFoldDB; P9WPB7; -.
DR SMR; P9WPB7; -.
DR STRING; 83332.Rv3392c; -.
DR DrugBank; DB01718; Cetrimonium.
DR PaxDb; P9WPB7; -.
DR DNASU; 887961; -.
DR GeneID; 887961; -.
DR KEGG; mtu:Rv3392c; -.
DR TubercuList; Rv3392c; -.
DR eggNOG; COG2230; Bacteria.
DR OMA; AQHFFTG; -.
DR PhylomeDB; P9WPB7; -.
DR UniPathway; UPA00915; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0008825; F:cyclopropane-fatty-acyl-phospholipid synthase activity; IDA:MTBBASE.
DR GO; GO:0008610; P:lipid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0071768; P:mycolic acid biosynthetic process; IDA:MTBBASE.
DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IDA:MTBBASE.
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 3D-structure; Cytoplasm; Lipid biosynthesis; Lipid metabolism;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..287
FT /note="Cyclopropane mycolic acid synthase 1"
FT /id="PRO_0000089566"
FT ACT_SITE 269
FT /evidence="ECO:0000305"
FT BINDING 33..34
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:11756461"
FT BINDING 68..76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:11756461"
FT BINDING 94..99
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:11756461"
FT BINDING 123..124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:11756461"
FT HELIX 9..16
FT /evidence="ECO:0007829|PDB:1KPG"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:1KPG"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1KPG"
FT HELIX 45..57
FT /evidence="ECO:0007829|PDB:1KPG"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:1KPG"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:1KPG"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:1KPG"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:1KPG"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:1KPG"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1KP9"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:1KPG"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:1KPG"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:1KPG"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:1KPG"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:1KPG"
FT HELIX 147..157
FT /evidence="ECO:0007829|PDB:1KPG"
FT STRAND 163..171
FT /evidence="ECO:0007829|PDB:1KPG"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:1KPG"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:1KPG"
FT HELIX 185..198
FT /evidence="ECO:0007829|PDB:1KPG"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:1KPG"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:1KPG"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:1KPG"
FT HELIX 229..245
FT /evidence="ECO:0007829|PDB:1KPG"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:1KPG"
FT HELIX 256..274
FT /evidence="ECO:0007829|PDB:1KPG"
FT STRAND 277..286
FT /evidence="ECO:0007829|PDB:1KPG"
SQ SEQUENCE 287 AA; 32461 MW; 7E254C15DF5FFF97 CRC64;
MPDELKPHFA NVQAHYDLSD DFFRLFLDPT QTYSCAYFER DDMTLQEAQI AKIDLALGKL
GLQPGMTLLD VGCGWGATMM RAVEKYDVNV VGLTLSKNQA NHVQQLVANS ENLRSKRVLL
AGWEQFDEPV DRIVSIGAFE HFGHERYDAF FSLAHRLLPA DGVMLLHTIT GLHPKEIHER
GLPMSFTFAR FLKFIVTEIF PGGRLPSIPM VQECASANGF TVTRVQSLQP HYAKTLDLWS
AALQANKGQA IALQSEEVYE RYMKYLTGCA EMFRIGYIDV NQFTCQK
