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cfa cyclopropane fatty acyl phospholipid synthase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 944811, updated on 26-Mar-2025
Official Symbol
cfa
Official Full Name
cyclopropane fatty acyl phospholipid synthase
Primary source
ECOCYC:EG11531
Locus tag
b1661
See related
ASAP:ABE-0005555
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
cdfA; ECK1657
Summary
Cfa binds a bicarbonate ion that is involved in catalysis. [More information is available at EcoGene: EG11531]. Cyclopropane fatty acyl phospholipid synthase (CFA) catalyzes a modification of the acyl chains of phospholipid bilayers through methylenation of unsaturated fatty acyl chains to their cyclopropane derivatives . [More information is available at EcoCyc: EG11531].
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Sequence:
NC_000913.3 (1741413..1742561)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene DNA-binding transcriptional repressor PurR Neighboring gene DNA-binding transcriptional activator PunR Neighboring gene purine nucleoside transporter PunC Neighboring gene riboflavin synthase Neighboring gene multidrug efflux pump MdtK

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Phospholipid modifications in bacteria. Cronan JE Jr. Curr Opin Microbiol, 2002 Apr. PMID 11934618
  2. Cyclopropane fatty acid synthase of Escherichia coli. Stabilization, purification, and interaction with phospholipid vesicles. Taylor FR, et al. Biochemistry, 1979 Jul 24. PMID 380648
  3. Selection and properties of Escherichia coli mutants defective in the synthesis of cyclopropane fatty acids. Taylor F, et al. J Bacteriol, 1976 Feb. PMID 1107324, Free PMC Article
  4. Cyclopropane fatty acid synthase of Escherichia coli: deduced amino acid sequence, purification, and studies of the enzyme active site. Wang AY, et al. Biochemistry, 1992 Nov 17. PMID 1445840
  5. Characterization of Escherichia coli mutants completely defective in synthesis of cyclopropane fatty acids. Grogan DW, et al. J Bacteriol, 1986 Jun. PMID 3519583, Free PMC Article

See all (36) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. both chemical steps of this enzymatic cyclopropanation, the methyl addition onto the double bond and the deprotonation step, are rate determining, a common situation in efficient enzymes.
    Title: Insight into the reaction mechanism of the Escherichia coli cyclopropane fatty acid synthase: isotope exchange and kinetic isotope effects.
  2. N-terminus verified by Edman degradation on mature peptide
    Title: Cyclopropane fatty acid synthase of Escherichia coli: deduced amino acid sequence, purification, and studies of the enzyme active site.
  3. Experiments are described that distinguish between two mechanistic scenarios for the cyclopropanation of unactivated olefins by cyclopropane fatty acid synthase.
    Title: Isotope and elemental effects indicate a rate-limiting methyl transfer as the initial step in the reaction catalyzed by Escherichia coli cyclopropane fatty acid synthase.
  4. report mutagenetic and chemical rescue experiments that confirm an important role for bicarbonate in E. coli CFAS catalysis; propose that residue E239, one of the bicarbonate ligands, could form a catalytic dyad with this ion
    Title: Escherichia coli cyclopropane fatty acid synthase: is a bound bicarbonate ion the active-site base?
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables bicarbonate binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables cyclopropane-fatty-acyl-phospholipid synthase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables cyclopropane-fatty-acyl-phospholipid synthase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables cyclopropane-fatty-acyl-phospholipid synthase activity IEA
Inferred from Electronic Annotation
more info
  
enables methyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein homodimerization activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables transferase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in fatty acid biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in lipid biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in lipid biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in lipid metabolic process IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within lipid modification IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in methylation IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
located_in extrinsic component of cytoplasmic side of plasma membrane IC
Inferred by Curator
more info
 PubMed 
Preferred Names
cyclopropane fatty acyl phospholipid synthase
NP_416178.1

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    1741413..1742561
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_416178.1 cyclopropane fatty acyl phospholipid synthase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_416178.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A376K1H9, A0A3P5DR19, A0AAD2U8S9
    Conserved Domains (1) summary
    PRK11705
    Location:1 → 382
    PRK11705; cyclopropane fatty acyl phospholipid synthase
Nucleotide Protein
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