Methylenetetrahydrofolate reductase 2 (P53128)

Identification
NameMethylenetetrahydrofolate reductase 2
Synonyms
  • YmL45
Gene NameMET13
Enzyme Class
Biological Properties
General FunctionInvolved in methylenetetrahydrofolate reductase (NADPH) activity
Specific Function5-methyltetrahydrofolate + NAD(P)(+) = 5,10- methylenetetrahydrofolate + NAD(P)H
Cellular LocationNot Available
SMPDB PathwaysNot Available
KEGG Pathways
Methane metabolismec00680 Map00680
One carbon pool by folateec00670 Map00670
SMPDB ReactionsNot Available
KEGG Reactions
5,10-Methylene-THF + NADPH + hydron → NADP + 5-Methyltetrahydrofolic acid
Metabolites
YMDB IDNameView
YMDB002385-Methyltetrahydrofolic acidShow
YMDB002605,10-Methylene-THFShow
YMDB00426NADPHShow
YMDB00427NADPShow
YMDB00848(6R)-5,10-methylenetetrahydrofolic acidShow
YMDB00862hydronShow
GO Classification
Component
Not Available
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on the CH-NH group of donors
oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
methylenetetrahydrofolate reductase (NADPH) activity
Process
methionine metabolic process
metabolic process
cellular metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
oxidation reduction
sulfur amino acid metabolic process
Gene Properties
Chromosome Locationchromosome 7
LocusYGL125W
Gene Sequence>YGL125W MET13 SGDID:S000003093, Chr VII from 272520-274322, Verified ORF, "Major isozyme of methylenetetrahydrofolate reductase, catalyzes the reduction of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate in the methionine biosynthesis pathway" ATGAAGATCACAGAAAAATTAGAGCAACATAGACAGACCTCTGGCAAGCCCACTTACTCA TTCGAGTACTTCGTCCCGAAGACTACACAAGGTGTACAGAACCTGTATGACCGGATGGAC CGGATGTACGAGGCTTCTTTGCCCCAATTTATTGACATCACCTGGAATGCAGGCGGTGGA CGGTTGTCACATCTGTCCACGGACTTGGTTGCGACAGCGCAGTCTGTGCTTGGTTTGGAA ACGTGCATGCACCTTACCTGCACCAATATGCCCATTTCGATGATTGACGACGCTTTAGAA AACGCTTATCACTCCGGTTGCCAGAACATCCTAGCGCTGAGAGGAGATCCTCCTAGGGAC GCAGAAAACTGGACTCCCGTTGAAGGTGGCTTCCAGTATGCCAAGGACTTGATTAAGTAT ATCAAGTCCAAGTACGGTGACCATTTCGCTATCGGCGTTGCCGGCTACCCGGAGTGCCAT CCGGAGTTGCCTAACAAAGACGTGAAGCTTGATCTCGAGTATTTGAAGCAGAAGATCGAC GCCGGCGGCGACTTCATCATCACTCAGATGTTTTACGATGTTGATAATTTCATCAACTGG TGTTCCCAAGTTAGAGCTGCGGGCATGGACGTGCCCATTATTCCCGGGATCATGCCGATC ACTACCTACGCGGCCTTCTTGAGAAGGGCCCAATGGGGCCAAATCTCCATCCCTCAACAT TTCTCGTCCCGATTGGATCCTATCAAGGACGATGACGAGTTGGTCCGTGATATCGGAACT AACTTGATCGTGGAAATGTGTCAAAAATTGCTCGACAGTGGTTACGTTTCTCACTTGCAC ATCTACACCATGAACTTGGAAAAAGCGCCTCTCATGATTCTGGAAAGATTGAACATTCTA CCTACGGAATCAGAGTTCAATGCACATCCATTGGCCGTGTTGCCATGGAGAAAATCTTTG AATCCAAAGCGTAAAAACGAGGAAGTCAGACCTATCTTCTGGAAGAGAAGACCTTACTCC TATGTCGCAAGAACCTCTCAATGGGCCGTGGACGAATTCCCCAACGGTAGATTCGGTGAT TCGTCTTCTCCTGCGTTCGGTGACTTGGATCTGTGTGGTTCAGACTTGATCAGGCAATCA GCGAACAAATGTCTCGAATTATGGTCCACCCCTACTTCCATCAACGACGTCGCCTTCTTG GTCATCAACTACTTGAATGGAAACTTGAAGTGTTTACCTTGGAGTGATATCCCCATCAAT GATGAAATAAATCCAATCAAAGCACACTTGATTGAGCTGAACCAGCATTCTATCATCACT ATAAACTCTCAACCTCAAGTCAACGGCATTAGGTCCAATGACAAAATTCATGGTTGGGGA CCCAAGGATGGTTACGTTTACCAGAAGCAATATTTGGAATTTATGTTGCCCAAGACTAAG TTGCCCAAGTTGATTGACACCTTGAAAAACAATGAGTTCTTGACCTACTTCGCCATCGAC TCTCAAGGTGACCTGCTAAGTAATCATCCAGACAACTCCAAGTCCAACGCTGTGACTTGG GGTATTTTCCCCGGCAGAGAAATTCTTCAACCTACCATTGTCGAGAAAATTTCGTTCTTA GCGTGGAAGGAGGAGTTCTATCATATCTTGAATGAATGGAAACTAAACATGAATAAATAC GATAAACCGCATAGTGCCCAATTCATTCAGTCCTTGATTGACGATTACTGCTTGGTCAAT ATTGTTGACAATGACTACATTTCTCCAGATGATCAAATCCATTCCATCCTACTAAGCCTA TAA
Protein Properties
Pfam Domain Function
Protein Residues600
Protein Molecular Weight68559.5
Protein Theoretical pI5.58
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Methylenetetrahydrofolate reductase 2 MKITEKLEQHRQTSGKPTYSFEYFVPKTTQGVQNLYDRMDRMYEASLPQFIDITWNAGGG RLSHLSTDLVATAQSVLGLETCMHLTCTNMPISMIDDALENAYHSGCQNILALRGDPPRD AENWTPVEGGFQYAKDLIKYIKSKYGDHFAIGVAGYPECHPELPNKDVKLDLEYLKQKID AGGDFIITQMFYDVDNFINWCSQVRAAGMDVPIIPGIMPITTYAAFLRRAQWGQISIPQH FSSRLDPIKDDDELVRDIGTNLIVEMCQKLLDSGYVSHLHIYTMNLEKAPLMILERLNIL PTESEFNAHPLAVLPWRKSLNPKRKNEEVRPIFWKRRPYSYVARTSQWAVDEFPNGRFGD SSSPAFGDLDLCGSDLIRQSANKCLELWSTPTSINDVAFLVINYLNGNLKCLPWSDIPIN DEINPIKAHLIELNQHSIITINSQPQVNGIRSNDKIHGWGPKDGYVYQKQYLEFMLPKTK LPKLIDTLKNNEFLTYFAIDSQGDLLSNHPDNSKSNAVTWGIFPGREILQPTIVEKISFL AWKEEFYHILNEWKLNMNKYDKPHSAQFIQSLIDDYCLVNIVDNDYISPDDQIHSILLSL
References
External Links
ResourceLink
Saccharomyces Genome Database MET13
Uniprot IDP53128
Uniprot NameMTHR2_YEAST
General Reference
  • Tizon, B., Rodriguez-Torres, M., Rodriguez-Belmonte, E., Cadahia, J. L., Cerdan, E. (1996). "Identification of a putative methylenetetrahydrofolate reductase by sequence analysis of a 6.8 kb DNA fragment of yeast chromosome VII." Yeast 12:1047-1051.8896269
  • Tettelin, H., Agostoni Carbone, M. L., Albermann, K., Albers, M., Arroyo, J., Backes, U., Barreiros, T., Bertani, I., Bjourson, A. J., Bruckner, M., Bruschi, C. V., Carignani, G., Castagnoli, L., Cerdan, E., Clemente, M. L., Coblenz, A., Coglievina, M., Coissac, E., Defoor, E., Del Bino, S., Delius, H., Delneri, D., de Wergifosse, P., Dujon, B., Kleine, K., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Nature 387:81-84.9169869
  • Kitakawa, M., Graack, H. R., Grohmann, L., Goldschmidt-Reisin, S., Herfurth, E., Wittmann-Liebold, B., Nishimura, T., Isono, K. (1997). "Identification and characterization of the genes for mitochondrial ribosomal proteins of Saccharomyces cerevisiae." Eur J Biochem 245:449-456.9151978
  • Raymond, R. K., Kastanos, E. K., Appling, D. R. (1999). "Saccharomyces cerevisiae expresses two genes encoding isozymes of methylenetetrahydrofolate reductase." Arch Biochem Biophys 372:300-308.10600168
  • Roje, S., Chan, S. Y., Kaplan, F., Raymond, R. K., Horne, D. W., Appling, D. R., Hanson, A. D. (2002). "Metabolic engineering in yeast demonstrates that S-adenosylmethionine controls flux through the methylenetetrahydrofolate reductase reaction in vivo." J Biol Chem 277:4056-4061.11729203
  • 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