P0A9H7 · CFA_ECOLI
- ProteinCyclopropane-fatty-acyl-phospholipid synthase
- Genecfa
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids382 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Transfers a methylene group from S-adenosyl-L-methionine to the cis double bond of an unsaturated fatty acid chain resulting in the replacement of the double bond with a methylene bridge.
Catalytic activity
- 1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H+ + S-adenosyl-L-homocysteine
Activity regulation
Inhibited by sinefungin, A9145C and S-adenosyl-L-homocysteine.
Pathway
Lipid metabolism; fatty acid biosynthesis.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | extrinsic component of cytoplasmic side of plasma membrane | |
Molecular Function | bicarbonate binding | |
Molecular Function | cyclopropane-fatty-acyl-phospholipid synthase activity | |
Molecular Function | protein homodimerization activity | |
Biological Process | fatty acid biosynthetic process | |
Biological Process | lipid modification | |
Biological Process | methylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCyclopropane-fatty-acyl-phospholipid synthase
- EC number
- Short namesCFA synthase ; Cyclopropane fatty acid synthase
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP0A9H7
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 308 | Loss of dimerization and catalytic activity. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 317 | Complete loss of catalytic activity. | ||||
Sequence: Y → F |
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000089572 | 2-382 | Cyclopropane-fatty-acyl-phospholipid synthase | |||
Sequence: SSSCIEEVSVPDDNWYRIANELLSRAGIAINGSAPADIRVKNPDFFKRVLQEGSLGLGESYMDGWWECDRLDMFFSKVLRAGLENQLPHHFKDTLRIAGARLFNLQSKKRAWIVGKEHYDLGNDLFSRMLDPFMQYSCAYWKDADNLESAQQAKLKMICEKLQLKPGMRVLDIGCGWGGLAHYMASNYDVSVVGVTISAEQQKMAQERCEGLDVTILLQDYRDLNDQFDRIVSVGMFEHVGPKNYDTYFAVVDRNLKPEGIFLLHTIGSKKTDLNVDPWINKYIFPNGCLPSVRQIAQSSEPHFVMEDWHNFGADYDTTLMAWYERFLAAWPEIADNYSERFKRMFTYYLNACAGAFRARDIQLWQVVFSRGVENGLRVAR |
Proteomic databases
Structure
Family & Domains
Domain
Each of the subunit of the dimer contains a smaller N-domain that associates tightly with a larger catalytic C-domain.
Sequence similarities
Belongs to the CFA/CMAS family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length382
- Mass (Da)43,909
- Last updated2007-01-23 v2
- Checksum861FF3314FDAF2C4
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 2 | in Ref. 2; X69109 | ||||
Sequence: S → R | ||||||
Sequence conflict | 8 | in Ref. 2; X69109 | ||||
Sequence: E → G | ||||||
Sequence conflict | 25 | in Ref. 2; X69109 | ||||
Sequence: S → N | ||||||
Sequence conflict | 39 | in Ref. 2; X69109 | ||||
Sequence: I → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M98330 EMBL· GenBank· DDBJ | AAA23562.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X69109 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
U00096 EMBL· GenBank· DDBJ | AAC74733.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAA15428.1 EMBL· GenBank· DDBJ | Genomic DNA |