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Trans-aconitate 3-methyltransferase (P32643)

Identification
NameTrans-aconitate 3-methyltransferase
SynonymsNot Available
Gene NameTMT1
Enzyme Class
Biological Properties
General FunctionInvolved in methyltransferase activity
Specific FunctionCatalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate and 3-isopropylmalate at high affinity and of other molecules like cis-aconitate, isocitrate, and citrate at lower velocities and affinities. The function of trans-aconitate methylation appears to be in reducing the toxicity of this spontaneous breakdown product of cis-aconitate. The role of 3-isopropylmalate methylation is unclear but may represent a metabolic branch at 3-isopropylmalate, where some of the material is taken in the pathway leading to leucine and some is taken in a pathway to the 3-isopropylmalate methyl ester, a molecule that provides a signal to switch from vegetative to invasive growth in response to amino acid starvation
Cellular LocationCytoplasm
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG Reactions
3-Isopropylmalate + S-Adenosylmethionine → S-Adenosylhomocysteine + 3-hydroxy-2-isopropyl-4-methoxy-4-oxobutanoate
trans-Aconitic acid + S-Adenosylmethionine → S-Adenosylhomocysteine + (2E)-3-(methoxycarbonyl)pent-2-enedioic acid
Metabolites
YMDB IDNameView
YMDB00122(2E)-2-(methoxycarbonylmethyl)but-2-enedioic acidShow
YMDB00198S-AdenosylhomocysteineShow
YMDB00297S-AdenosylmethionineShow
YMDB00340trans-Aconitic acidShow
YMDB003683-IsopropylmalateShow
YMDB00438S-Adenosyl-L-methionineShow
YMDB004813-hydroxy-2-isopropyl-4-methoxy-4-oxobutanoateShow
YMDB00776(2E)-3-(methoxycarbonyl)pent-2-enedioic acidShow
GO Classification
Component
Not Available
Function
transferase activity
transferase activity, transferring one-carbon groups
methyltransferase activity
catalytic activity
Process
metabolic process
Gene Properties
Chromosome Locationchromosome 5
LocusYER175C
Gene Sequence>900 bp ATGTCTACCTTTTCTGCTTCTGATTTCAACTCAGAAAGATATTCATCTTCAAGACCTTCT TATCCCTCCGATTTTTACAAGATGATTGATGAATACCACGACGGAGAAAGGAAATTACTC GTAGATGTTGGCTGTGGACCAGGTACTGCCACTTTACAAATGGCTCAGGAGTTAAAACCA TTCGAACAAATTATCGGAAGCGATCTCTCCGCTACCATGATTAAGACTGCAGAAGTAATA AAGGAAGGAAGTCCTGATACATACAAAAACGTTTCATTTAAGATTTCTTCAAGTGATGAT TTTAAATTCCTAGGCGCGGATTCAGTAGACAAACAGAAAATTGATATGATTACCGCAGTA GAATGTGCTCATTGGTTCGATTTCGAAAAATTTCAGCGATCTGCTTATGCCAATTTGAGA AAAGATGGTACTATCGCTATTTGGGGTTATGCGGACCCAATTTTCCCGGACTACCCTGAA TTTGATGATCTGATGATTGAAGTTCCTTACGGGAAGCAAGGACTGGGACCCTATTGGGAA CAACCGGGGAGATCTCGCCTTCGTAATATGCTGAAAGACTCTCACTTAGACCCAGAACTT TTCCATGATATACAAGTTTCATATTTTTGTGCAGAAGATGTGAGAGACAAAGTAAAACTC CACCAGCATACAAAGAAGCCATTGCTAATCAGAAAGCAGGTCACCCTAGTGGAGTTTGCA GATTATGTCAGAACCTGGAGCGCTTACCATCAGTGGAAGCAGGATCCAAAGAACAAAGAT AAAGAAGATGTAGCAGATTGGTTTATTAAAGAGTCACTAAGGAGGAGGCCGGAACTTTCC ACCAACACCAAAATTGAAGTTGTTTGGAATACTTTTTACAAACTTGGCAAAAGGGTCTGA
Protein Properties
Pfam Domain Function
Protein Residues299
Protein Molecular Weight34768.0
Protein Theoretical pI6.18
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Trans-aconitate 3-methyltransferase MSTFSASDFNSERYSSSRPSYPSDFYKMIDEYHDGERKLLVDVGCGPGTATLQMAQELKP FEQIIGSDLSATMIKTAEVIKEGSPDTYKNVSFKISSSDDFKFLGADSVDKQKIDMITAV ECAHWFDFEKFQRSAYANLRKDGTIAIWGYADPIFPDYPEFDDLMIEVPYGKQGLGPYWE QPGRSRLRNMLKDSHLDPELFHDIQVSYFCAEDVRDKVKLHQHTKKPLLIRKQVTLVEFA DYVRTWSAYHQWKQDPKNKDKEDVADWFIKESLRRRPELSTNTKIEVVWNTFYKLGKRV
References
External Links
ResourceLink
Saccharomyces Genome Database TMT1
Uniprot IDP32643
Uniprot NameTMT1_YEAST
GenBank Gene IDU18922
Genebank Protein ID603416
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
  • Cai, H., Dumlao, D., Katz, J. E., Clarke, S. (2001). "Identification of the gene and characterization of the activity of the trans-aconitate methyltransferase from Saccharomyces cerevisiae." Biochemistry 40:13699-13709.11695919
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • 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
  • Katz, J. E., Dumlao, D. S., Wasserman, J. I., Lansdown, M. G., Jung, M. E., Faull, K. F., Clarke, S. (2004). "3-Isopropylmalate is the major endogenous substrate of the Saccharomyces cerevisiae trans-aconitate methyltransferase." Biochemistry 43:5976-5986.15147181
  • Dumlao, D. S., Hertz, N., Clarke, S. (2008). "Secreted 3-isopropylmalate methyl ester signals invasive growth during amino acid starvation in Saccharomyces cerevisiae." Biochemistry 47:698-709.18092814
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956