|Gene:||frc||Accession Numbers: G7237 (MetaCyc), b2374, ECK2370|
Species: Escherichia coli K-12 substr. MG1655
Subunit composition of
formyl-CoA transferase = [Frc]2
formyl-CoA transferase monomer = Frc
YfdW (Frc) is a formyl-CoA transferase with sequence and structural similarity to Frc from Oxalobacter formigenes, a strictly anaerobic bacterium found in the mammalian gut [Gruez03, Toyota08]. Unlike the O. formigenes enzyme, the E. coli enzyme shows high substrate specificity [Toyota08].
Crystal structures of apo-YfdW and YfdW with CoA, acetyl-CoA, or both acetyl-CoA and oxalate have been solved. YfdW is a homodimer; the ring-shaped monomers are concatenated like links of a chain [Gruez03, Gogos04].
The enzymatic reaction mechanism is predicted by structural similarity to related enzymes; residue D169 is predicted to catalyze the reaction [Gruez03]. Biochemical data indicates that the kinetic mechanism is ordered bi-bi sequential [Toyota08].
Frc is required during the adaption phase of an oxalate-induced acid tolerance response [Fontenot13]. Expression of frc is increased when the EvgAS two-component regulatory system is overexpressed [Masuda02].
|Map Position: [2,490,026 <- 2,491,276]|
Molecular Weight of Polypeptide: 45.828 kD (from nucleotide sequence)
Unification Links: ASAP:ABE-0007828, EchoBASE:EB3897, EcoGene:EG14145, EcoliWiki:b2374, ModBase:P69902, OU-Microarray:b2374, PortEco:frc, PR:PRO_000022685, Pride:P69902, Protein Model Portal:P69902, RefSeq:NP_416875, RegulonDB:G7237, SMR:P69902, String:511145.b2374, UniProt:P69902
Relationship Links: InterPro:IN-FAMILY:IPR003673, InterPro:IN-FAMILY:IPR017659, InterPro:IN-FAMILY:IPR023606, Panther:IN-FAMILY:PTHR11837, PDB:Structure:1PQY, PDB:Structure:1PT5, PDB:Structure:1PT7, PDB:Structure:1PT8, PDB:Structure:1Q6Y, PDB:Structure:1Q7E, Pfam:IN-FAMILY:PF02515
|MultiFun Terms:||metabolism → metabolism of other compounds|
Enzymatic reaction of: formyl-CoA transferase
Synonyms: formyl-CoA:oxalate CoA-transferase
EC Number: 188.8.131.52formyl-CoA + oxalate ⇄ formate + oxalyl-CoA
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.
The reaction is favored in the direction shown.
Oxalate at concentrations above 2.5 mM inhibit the activity [Toyota08].
|Protein-Segment||17 -> 18|
|Protein-Segment||72 -> 75|
|Protein-Segment||96 -> 98|
|Protein-Segment||137 -> 140|
|Protein-Segment||248 -> 250|
|Protein-Segment||273 -> 275|
Peter D. Karp on Thu Jan 16, 2003:
Predicted gene function revised as a result of E. coli genome reannotation by Serres et al. [Serres01].
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
Fontenot13: Fontenot EM, Ezelle KE, Gabreski LN, Giglio ER, McAfee JM, Mills AC, Qureshi MN, Salmon KM, Toyota CG (2013). "YfdW and YfdU are required for oxalate-induced acid tolerance in Escherichia coli K-12." J Bacteriol 195(7);1446-55. PMID: 23335415
Gruez03: Gruez A, Roig-Zamboni V, Valencia C, Campanacci V, Cambillau C (2003). "The crystal structure of the E. coli yfdW gene product reveals a new fold of two interlaced rings identifying a wide family of CoA transferases." J Biol Chem 278(36);34582-6. PMID: 12844490
Toyota08: Toyota CG, Berthold CL, Gruez A, Jonsson S, Lindqvist Y, Cambillau C, Richards NG (2008). "Differential substrate specificity and kinetic behavior of Escherichia coli YfdW and Oxalobacter formigenes formyl coenzyme A transferase." J Bacteriol 190(7):2556-64. PMID: 18245280
©2016 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493