|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
|Biological Process:||GO:0071468 - cellular response to acidic pH
GO:0008152 - metabolic process [GOA01]
GO:0033611 - oxalate catabolic process [UniProtGOA12]
|Molecular Function:||GO:0033608 - formyl-CoA transferase activity
[GOA01a, GOA01, Toyota08]
GO:0003824 - catalytic activity [GOA01]
GO:0008410 - CoA-transferase activity [GOA06]
GO:0016740 - transferase activity [UniProtGOA11]
|Cellular Component:||GO:0005829 - cytosol [DiazMejia09]|
|MultiFun Terms:||metabolism → metabolism of other compounds|
Enzymatic reaction of: formyl-CoA transferase
Synonyms: formyl-CoA:oxalate CoA-transferase
EC Number: 126.96.36.199
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, 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||137 -> 140|
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. 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
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