5-formyltetrahydrofolate cyclo-ligase (P40099)

Identification
Name5-formyltetrahydrofolate cyclo-ligase
Synonyms
  • 5,10-methenyl-tetrahydrofolate synthetase
  • MTHFS
  • Methenyl-THF synthetase
Gene NameFAU1
Enzyme Class
Biological Properties
General FunctionInvolved in ATP binding
Specific FunctionUtilizes 5-formyltetrahydrofolate (folinic acid) as substrate in an alternative way of folate biosynthesis
Cellular LocationMitochondrion
SMPDB PathwaysNot Available
KEGG Pathways
One carbon pool by folateec00670 Map00670
SMPDB ReactionsNot Available
KEGG Reactions
Adenosine triphosphate + N5-Formyl-THF → (6R)-5,10-Methenyltetrahydrofolic acid + phosphate + ADP
Metabolites
YMDB IDNameView
YMDB00109Adenosine triphosphateShow
YMDB001765,10-Methenyltetrahydrofolic acidShow
YMDB00298N5-Formyl-THFShow
YMDB00515(6R)-5,10-Methenyltetrahydrofolic acidShow
YMDB005165-Formyltetrahydrofolic acidShow
YMDB008795,10-MethenyltetrahydrofolateShow
YMDB00907phosphateShow
YMDB00914ADPShow
GO Classification
Component
Not Available
Function
ligase activity
ligase activity, forming carbon-nitrogen bonds
binding
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
cyclo-ligase activity
catalytic activity
5-formyltetrahydrofolate cyclo-ligase activity
Process
cellular metabolic process
cellular aromatic compound metabolic process
folic acid and derivative metabolic process
folic acid and derivative biosynthetic process
metabolic process
Gene Properties
Chromosome Locationchromosome 5
LocusYER183C
Gene Sequence>636 bp ATGGCCACTAAGCAATTACTGAGACGTCAAATCAAAAGGGTAATAAATGCTCTTGACTAC GATATTATCGCTGCAGAGTCGCATACTATTTCTCAAGCAGTACGCTCATTGATCGCTTCC GCCAATTCTAGGCGTGTAGCGTGTTATATGAGCATGGATAAAGGAGAAGTAACGACTGGA GAAATCATTAAGAATTTATTTCAAGATGGCCAGGAGGTCTTTCTGCCAAGATGTACTCAT ACTTCTGAATCGAAACACTTCAAATTACGGGAAGATCATCATCCACATTTAATATTCCAT CGAATGAGTAGTTTGAAAATGGTTCGTGATTTGAAGCCTCAAGGTCCATATCAACTAAAA GAGCCTGAACCGCATATTGAGGAATCAGATATTCTAGATGTCGTATTGGTGCCTGGAGTG GCGTTTGATATTAAAACTGGTGCAAGGATGGGTCACGGTGCTGGGTATTATGACGATTTT TTCCAACGGTATAAGATACTGCATGAAGGCCAAAAGCCCCTCCTAGTTGGACTATGTCTT ATGGAACAGGTGGCCTCTCCAATTCCTTTAGAAAAACATGATTATTCCATGGATTGTATA GTATGCGGAGATGGATCCATACATTGGTTTCAATAA
Protein Properties
Pfam Domain Function
Protein Residues211
Protein Molecular Weight24058.5
Protein Theoretical pI7.14
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>5-formyltetrahydrofolate cyclo-ligase MATKQLLRRQIKRVINALDYDIIAAESHTISQAVRSLIASANSRRVACYMSMDKGEVTTG EIIKNLFQDGQEVFLPRCTHTSESKHFKLREDHHPHLIFHRMSSLKMVRDLKPQGPYQLK EPEPHIEESDILDVVLVPGVAFDIKTGARMGHGAGYYDDFFQRYKILHEGQKPLLVGLCL MEQVASPIPLEKHDYSMDCIVCGDGSIHWFQ
References
External Links
ResourceLink
Saccharomyces Genome Database FAU1
Uniprot IDP40099
Uniprot NameFTHC_YEAST
GenBank Gene IDU18922
Genebank Protein ID603424
General Reference
  • Dietrich, F. S., Mulligan, J., Hennessy, K., Yelton, M. A., Allen, E., Araujo, R., Aviles, E., Berno, A., Brennan, T., Carpenter, J., Chen, E., Cherry, J. M., Chung, E., Duncan, M., Guzman, E., Hartzell, G., Hunicke-Smith, S., Hyman, R. W., Kayser, A., Komp, C., Lashkari, D., Lew, H., Lin, D., Mosedale, D., Davis, R. W., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Nature 387:78-81.9169868
  • Holmes, W. B., Appling, D. R. (2002). "Cloning and characterization of methenyltetrahydrofolate synthetase from Saccharomyces cerevisiae." J Biol Chem 277:20205-20213.11923304
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Sickmann, A., Reinders, J., Wagner, Y., Joppich, C., Zahedi, R., Meyer, H. E., Schonfisch, B., Perschil, I., Chacinska, A., Guiard, B., Rehling, P., Pfanner, N., Meisinger, C. (2003). "The proteome of Saccharomyces cerevisiae mitochondria." Proc Natl Acad Sci U S A 100:13207-13212.14576278
  • Kung, L. A., Tao, S. C., Qian, J., Smith, M. G., Snyder, M., Zhu, H. (2009). "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes." Mol Syst Biol 5:308.19756047