ID   CFA2_MYCLE              Reviewed;         308 AA.
AC   Q49807;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 56.
DE   RecName: Full=Cyclopropane-fatty-acyl-phospholipid synthase;
DE            Short=Cyclopropane fatty acid synthase;
DE            Short=CFA synthase;
DE            EC=2.1.1.79;
DE   AltName: Full=Cyclopropane mycolic acid synthase;
GN   Name=cmaA2; OrderedLocusNames=ML2426; ORFNames=B2168_F3_130;
OS   Mycobacterium leprae.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=1769;
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   MEDLINE=21128732; 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: Transfers a methylene group from S-adenosyl-L-methionine
CC       to the cis double bond of an unsaturated fatty acid chain
CC       resulting in the replacement of the double bond with a methylene
CC       bridge. Mycolic acids, which represent the major constituent of
CC       mycobacterial cell wall complex, act as substrates (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + phospholipid
CC       olefinic fatty acid = S-adenosyl-L-homocysteine + phospholipid
CC       cyclopropane fatty acid.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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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; -.
DR   HSSP; Q11196; 1KPI.
DR   SMR; Q49807; 15-308.
DR   GeneID; 908573; -.
DR   GenomeReviews; AL450380_GR; ML2426.
DR   KEGG; mle:ML2426; -.
DR   NMPDR; fig|272631.1.peg.1442; -.
DR   Leproma; ML2426; -.
DR   HOGENOM; Q49807; -.
DR   OMA; Q49807; RYHRIGS.
DR   BioCyc; MLEP272631:ML2426-MON; -.
DR   BRENDA; 2.1.1.79; 808.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008825; F:cyclopropane-fatty-acyl-phospholipid syntha...; IEA:EC.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR003333; CMAS.
DR   Pfam; PF02353; CMAS; 1.
DR   PIRSF; PIRSF003085; CMAS; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Lipid synthesis; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    308       Cyclopropane-fatty-acyl-phospholipid
FT                                synthase.
FT                                /FTId=PRO_0000089568.
FT   REGION       44     45       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   REGION       79     87       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   REGION      105    110       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   SITE        290    290       Essential for catalysis (Probable).
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
//