ID   CFA_CITFR               Reviewed;          89 AA.
AC   P45509;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Cyclopropane-fatty-acyl-phospholipid synthase;
DE            Short=CFA synthase;
DE            Short=Cyclopropane fatty acid synthase;
DE            EC=2.1.1.79;
DE   Flags: Fragment;
GN   Name=cfa;
OS   Citrobacter freundii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX   NCBI_TaxID=546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 6750 / DSM 30040 / NCIB 8173 / M8BK;
RA   Daniel R., Gottschalk G.;
RL   Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transfers a methylene group from S-adenosyl-L-methionine to
CC       the cis double bond of an unsaturated fatty acid chain resulting in the
CC       replacement of the double bond with a methylene bridge. {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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; U09771; AAB48842.1; -; Genomic_DNA.
DR   AlphaFoldDB; P45509; -.
DR   SMR; P45509; -.
DR   STRING; 1333848.CFNIH1_02655; -.
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:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lipid biosynthesis; Lipid metabolism; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           <1..89
FT                   /note="Cyclopropane-fatty-acyl-phospholipid synthase"
FT                   /id="PRO_0000089570"
FT   ACT_SITE        61
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   89 AA;  10609 MW;  7D0DDB9F377F72EA CRC64;
     ISHIAEASES RFVMEDWHNF GSDYDKTLMA WHERFNQAWP ELSSRYSATF RRMFNYYLCA
     CAGAFRARDI ELWQVLFSRG VEGGIRVYR