CFA_ECOLI
ID CFA_ECOLI Reviewed; 382 AA.
AC P0A9H7; P30010;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000303|PubMed:1445840};
DE Short=CFA synthase {ECO:0000303|PubMed:1445840};
DE Short=Cyclopropane fatty acid synthase;
DE EC=2.1.1.79 {ECO:0000269|PubMed:1445840, ECO:0000269|PubMed:30057024};
GN Name=cfa; Synonyms=cdfA; OrderedLocusNames=b1661, JW1653;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-9, ACTIVITY
RP REGULATION, CATALYTIC ACTIVITY, AND ACTIVE SITE.
RC STRAIN=K12;
RX PubMed=1445840; DOI=10.1021/bi00160a011;
RA Wang A.-Y., Grogan D.W., Cronan J.E. Jr.;
RT "Cyclopropane fatty acid synthase of Escherichia coli: deduced amino acid
RT sequence, purification, and studies of the enzyme active site.";
RL Biochemistry 31:11020-11028(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / RR28;
RA Eberhardt S.M.R., Richter G., Gimbel W., Werner T., Bacher A.;
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6] {ECO:0007744|PDB:6BQC}
RP X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 2-382, SUBUNIT, DOMAIN,
RP MUTAGENESIS OF GLU-308 AND TYR-317, AND CATALYTIC ACTIVITY.
RX PubMed=30057024; DOI=10.1016/j.str.2018.06.008;
RA Hari S.B., Grant R.A., Sauer R.T.;
RT "Structural and Functional Analysis of E.coli Cyclopropane Fatty Acid
RT Synthase.";
RL Structure 26:1251-1258.e3(2018).
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 Evidence={ECO:0000269|PubMed:1445840, ECO:0000269|PubMed:30057024};
CC -!- ACTIVITY REGULATION: Inhibited by sinefungin, A9145C and S-adenosyl-L-
CC homocysteine. {ECO:0000269|PubMed:1445840}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBUNIT: Homodimer (PubMed:30057024). Homodimerization is required for
CC catalysis (PubMed:30057024). One subunit probably binds to the lipid
CC bilayer and positions the other subunit for catalysis
CC (PubMed:30057024). {ECO:0000269|PubMed:30057024}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: Each of the subunit of the dimer contains a smaller N-domain
CC that associates tightly with a larger catalytic C-domain.
CC {ECO:0000269|PubMed:30057024}.
CC -!- SIMILARITY: Belongs to the CFA/CMAS family. {ECO:0000305}.
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DR EMBL; M98330; AAA23562.1; -; Genomic_DNA.
DR EMBL; X69109; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U00096; AAC74733.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15428.1; -; Genomic_DNA.
DR PIR; A44292; A44292.
DR RefSeq; NP_416178.1; NC_000913.3.
DR RefSeq; WP_000098896.1; NZ_SSZK01000001.1.
DR PDB; 6BQC; X-ray; 2.07 A; A=2-382.
DR PDBsum; 6BQC; -.
DR AlphaFoldDB; P0A9H7; -.
DR SMR; P0A9H7; -.
DR BioGRID; 4263376; 307.
DR DIP; DIP-48026N; -.
DR IntAct; P0A9H7; 4.
DR STRING; 511145.b1661; -.
DR jPOST; P0A9H7; -.
DR PaxDb; P0A9H7; -.
DR PRIDE; P0A9H7; -.
DR EnsemblBacteria; AAC74733; AAC74733; b1661.
DR EnsemblBacteria; BAA15428; BAA15428; BAA15428.
DR GeneID; 944811; -.
DR KEGG; ecj:JW1653; -.
DR KEGG; eco:b1661; -.
DR PATRIC; fig|1411691.4.peg.596; -.
DR EchoBASE; EB1493; -.
DR eggNOG; COG2230; Bacteria.
DR HOGENOM; CLU_026434_6_0_6; -.
DR InParanoid; P0A9H7; -.
DR OMA; LHCITAQ; -.
DR PhylomeDB; P0A9H7; -.
DR BioCyc; EcoCyc:CFA-MON; -.
DR BioCyc; MetaCyc:CFA-MON; -.
DR BRENDA; 2.1.1.79; 2026.
DR SABIO-RK; P0A9H7; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:P0A9H7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0071890; F:bicarbonate binding; IDA:EcoCyc.
DR GO; GO:0008825; F:cyclopropane-fatty-acyl-phospholipid synthase activity; IDA:EcoCyc.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0030258; P:lipid modification; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Lipid biosynthesis;
KW Lipid metabolism; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1445840"
FT CHAIN 2..382
FT /note="Cyclopropane-fatty-acyl-phospholipid synthase"
FT /id="PRO_0000089572"
FT ACT_SITE 354
FT /evidence="ECO:0000305|PubMed:1445840"
FT BINDING 137..138
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 171..179
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:1445840"
FT BINDING 197..202
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MUTAGEN 308
FT /note="E->Q: Loss of dimerization and catalytic activity."
FT /evidence="ECO:0000269|PubMed:30057024"
FT MUTAGEN 317
FT /note="Y->F: Complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:30057024"
FT CONFLICT 2
FT /note="S -> R (in Ref. 2; X69109)"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="E -> G (in Ref. 2; X69109)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="S -> N (in Ref. 2; X69109)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="I -> T (in Ref. 2; X69109)"
FT /evidence="ECO:0000305"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:6BQC"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:6BQC"
FT HELIX 46..63
FT /evidence="ECO:0007829|PDB:6BQC"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:6BQC"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:6BQC"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:6BQC"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:6BQC"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:6BQC"
FT HELIX 148..163
FT /evidence="ECO:0007829|PDB:6BQC"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:6BQC"
FT HELIX 180..188
FT /evidence="ECO:0007829|PDB:6BQC"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:6BQC"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:6BQC"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:6BQC"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:6BQC"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:6BQC"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:6BQC"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:6BQC"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:6BQC"
FT HELIX 246..256
FT /evidence="ECO:0007829|PDB:6BQC"
FT STRAND 257..274
FT /evidence="ECO:0007829|PDB:6BQC"
FT HELIX 279..284
FT /evidence="ECO:0007829|PDB:6BQC"
FT HELIX 294..301
FT /evidence="ECO:0007829|PDB:6BQC"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:6BQC"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:6BQC"
FT HELIX 314..335
FT /evidence="ECO:0007829|PDB:6BQC"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:6BQC"
FT HELIX 341..359
FT /evidence="ECO:0007829|PDB:6BQC"
FT STRAND 362..372
FT /evidence="ECO:0007829|PDB:6BQC"
SQ SEQUENCE 382 AA; 43909 MW; 861FF3314FDAF2C4 CRC64;
MSSSCIEEVS VPDDNWYRIA NELLSRAGIA INGSAPADIR VKNPDFFKRV LQEGSLGLGE
SYMDGWWECD RLDMFFSKVL RAGLENQLPH HFKDTLRIAG ARLFNLQSKK RAWIVGKEHY
DLGNDLFSRM LDPFMQYSCA YWKDADNLES AQQAKLKMIC EKLQLKPGMR VLDIGCGWGG
LAHYMASNYD VSVVGVTISA EQQKMAQERC EGLDVTILLQ DYRDLNDQFD RIVSVGMFEH
VGPKNYDTYF AVVDRNLKPE GIFLLHTIGS KKTDLNVDPW INKYIFPNGC LPSVRQIAQS
SEPHFVMEDW HNFGADYDTT LMAWYERFLA AWPEIADNYS ERFKRMFTYY LNACAGAFRA
RDIQLWQVVF SRGVENGLRV AR
