Transketolase 1 (P23254)

Identification
NameTransketolase 1
Synonyms
  • TK 1
Gene NameTKL1
Enzyme Class
Biological Properties
General FunctionInvolved in catalytic activity
Specific FunctionSedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate
Cellular LocationNot Available
SMPDB Pathways
RiboneogenesisPW002511 ThumbThumb?image type=greyscaleThumb?image type=simple
xylitol degradationPW002433 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Pentose phosphate pathwayec00030 Map00030
SMPDB Reactions
Xylulose 5-phosphate + D-Ribose 5-phosphate → L-Glyceraldehyde 3-phosphate + D-Sedoheptulose 7-phosphate
Xylulose 5-phosphate + D-Ribose 5-phosphate → D-Glyceraldehyde 3-phosphate + D-Sedoheptulose 7-phosphate
D-Erythrose 4-phosphate + Xylulose 5-phosphate → β-D-fructofuranose 6-phosphate + D-Glyceraldehyde 3-phosphate
Beta-D-Fructose 6-phosphate + D-Glyceraldehyde 3-phosphate ↔ Xylulose 5-phosphate + D-Erythrose 4-phosphate
D-Sedoheptulose 7-phosphate + D-Glyceraldehyde 3-phosphate ↔ Xylulose 5-phosphate + D-Ribose 5-phosphate
KEGG Reactions
alpha-D-ribose 5-phosphate + Xylulose 5-phosphate ↔ D-Glyceraldehyde 3-phosphate + D-Sedoheptulose 7-phosphate
D-Erythrose 4-phosphate + Xylulose 5-phosphate ↔ D-Glyceraldehyde 3-phosphate + Fructose 6-phosphate
Metabolites
YMDB IDNameView
YMDB00078Fructose 6-phosphateShow
YMDB00115D-Glyceraldehyde 3-phosphateShow
YMDB00119D-Ribose 5-phosphateShow
YMDB00196D-Sedoheptulose 7-phosphateShow
YMDB00223D-Erythrose 4-phosphateShow
YMDB00362Xylulose 5-phosphateShow
YMDB00650alpha-D-ribose 5-phosphateShow
YMDB00752Sedoheptulose 7-phosphateShow
YMDB16176Beta-D-Fructose 6-phosphateShow
YMDB16262β-D-fructofuranose 6-phosphateShow
GO Classification
Component
Not Available
Function
transferase activity
transferase activity, transferring aldehyde or ketonic groups
transketolase activity
catalytic activity
Process
metabolic process
Gene Properties
Chromosome Locationchromosome 16
LocusYPR074C
Gene Sequence>2043 bp ATGACTCAATTCACTGACATTGATAAGCTAGCCGTCTCCACCATAAGAATTTTGGCTGTG GACACCGTATCCAAGGCCAACTCAGGTCACCCAGGTGCTCCATTGGGTATGGCACCAGCT GCACACGTTCTATGGAGTCAAATGCGCATGAACCCAACCAACCCAGACTGGATCAACAGA GATAGATTTGTCTTGTCTAACGGTCACGCGGTCGCTTTGTTGTATTCTATGCTACATTTG ACTGGTTACGATCTGTCTATTGAAGACTTGAAACAGTTCAGACAGTTGGGTTCCAGAACA CCAGGTCATCCTGAATTTGAGTTGCCAGGTGTTGAAGTTACTACCGGTCCATTAGGTCAA GGTATCTCCAACGCTGTTGGTATGGCCATGGCTCAAGCTAACCTGGCTGCCACTTACAAC AAGCCGGGCTTTACCTTGTCTGACAACTACACCTATGTTTTCTTGGGTGACGGTTGTTTG CAAGAAGGTATTTCTTCAGAAGCTTCCTCCTTGGCTGGTCATTTGAAATTGGGTAACTTG ATTGCCATCTACGATGACAACAAGATCACTATCGATGGTGCTACCAGTATCTCATTCGAT GAAGATGTTGCTAAGAGATACGAAGCCTACGGTTGGGAAGTTTTGTACGTAGAAAATGGT AACGAAGATCTAGCCGGTATTGCCAAGGCTATTGCTCAAGCTAAGTTATCCAAGGACAAA CCAACTTTGATCAAAATGACCACAACCATTGGTTACGGTTCCTTGCATGCCGGCTCTCAC TCTGTGCACGGTGCCCCATTGAAAGCAGATGATGTTAAACAACTAAAGAGCAAATTCGGT TTCAACCCAGACAAGTCCTTTGTTGTTCCACAAGAAGTTTACGACCACTACCAAAAGACA ATTTTAAAGCCAGGTGTCGAAGCCAACAACAAGTGGAACAAGTTGTTCAGCGAATACCAA AAGAAATTCCCAGAATTAGGTGCTGAATTGGCTAGAAGATTGAGCGGCCAACTACCCGCA AATTGGGAATCTAAGTTGCCAACTTACACCGCCAAGGACTCTGCCGTGGCCACTAGAAAA TTATCAGAAACTGTTCTTGAGGATGTTTACAATCAATTGCCAGAGTTGATTGGTGGTTCT GCCGATTTAACACCTTCTAACTTGACCAGATGGAAGGAAGCCCTTGACTTCCAACCTCCT TCTTCCGGTTCAGGTAACTACTCTGGTAGATACATTAGGTACGGTATTAGAGAACACGCT ATGGGTGCCATAATGAACGGTATTTCAGCTTTCGGTGCCAACTACAAACCATACGGTGGT ACTTTCTTGAACTTCGTTTCTTATGCTGCTGGTGCCGTTAGATTGTCCGCTTTGTCTGGC CACCCAGTTATTTGGGTTGCTACACATGACTCTATCGGTGTCGGTGAAGATGGTCCAACA CATCAACCTATTGAAACTTTAGCACACTTCAGATCCCTACCAAACATTCAAGTTTGGAGA CCAGCTGATGGTAACGAAGTTTCTGCCGCCTACAAGAACTCTTTAGAATCCAAGCATACT CCAAGTATCATTGCTTTGTCCAGACAAAACTTGCCACAATTGGAAGGTAGCTCTATTGAA AGCGCTTCTAAGGGTGGTTACGTACTACAAGATGTTGCTAACCCAGATATTATTTTAGTG GCTACTGGTTCCGAAGTGTCTTTGAGTGTTGAAGCTGCTAAGACTTTGGCCGCAAAGAAC ATCAAGGCTCGTGTTGTTTCTCTACCAGATTTCTTCACTTTTGACAAACAACCCCTAGAA TACAGACTATCAGTCTTACCAGACAACGTTCCAATCATGTCTGTTGAAGTTTTGGCTACC ACATGTTGGGGCAAATACGCTCATCAATCCTTCGGTATTGACAGATTTGGTGCCTCCGGT AAGGCACCAGAAGTCTTCAAGTTCTTCGGTTTCACCCCAGAAGGTGTTGCTGAAAGAGCT CAAAAGACCATTGCATTCTATAAGGGTGACAAGCTAATTTCTCCTTTGAAAAAAGCTTTC TAA
Protein Properties
Pfam Domain Function
Protein Residues680
Protein Molecular Weight73805.0
Protein Theoretical pI7.01
PDB Fileshow
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Transketolase 1 MTQFTDIDKLAVSTIRILAVDTVSKANSGHPGAPLGMAPAAHVLWSQMRMNPTNPDWINR DRFVLSNGHAVALLYSMLHLTGYDLSIEDLKQFRQLGSRTPGHPEFELPGVEVTTGPLGQ GISNAVGMAMAQANLAATYNKPGFTLSDNYTYVFLGDGCLQEGISSEASSLAGHLKLGNL IAIYDDNKITIDGATSISFDEDVAKRYEAYGWEVLYVENGNEDLAGIAKAIAQAKLSKDK PTLIKMTTTIGYGSLHAGSHSVHGAPLKADDVKQLKSKFGFNPDKSFVVPQEVYDHYQKT ILKPGVEANNKWNKLFSEYQKKFPELGAELARRLSGQLPANWESKLPTYTAKDSAVATRK LSETVLEDVYNQLPELIGGSADLTPSNLTRWKEALDFQPPSSGSGNYSGRYIRYGIREHA MGAIMNGISAFGANYKPYGGTFLNFVSYAAGAVRLSALSGHPVIWVATHDSIGVGEDGPT HQPIETLAHFRSLPNIQVWRPADGNEVSAAYKNSLESKHTPSIIALSRQNLPQLEGSSIE SASKGGYVLQDVANPDIILVATGSEVSLSVEAAKTLAAKNIKARVVSLPDFFTFDKQPLE YRLSVLPDNVPIMSVEVLATTCWGKYAHQSFGIDRFGASGKAPEVFKFFGFTPEGVAERA QKTIAFYKGDKLISPLKKAF
References
External Links
ResourceLink
Saccharomyces Genome Database TKL1
Uniprot IDP23254
Uniprot NameTKT1_YEAST
GenBank Gene IDU51033
Genebank Protein ID1230682
PDB ID
1GPU
General Reference
  • Fletcher, T. S., Kwee, I. L., Nakada, T., Largman, C., Martin, B. M. (1992). "DNA sequence of the yeast transketolase gene." Biochemistry 31:1892-1896.1737042
  • Sundstrom, M., Lindqvist, Y., Schneider, G., Hellman, U., Ronne, H. (1993). "Yeast TKL1 gene encodes a transketolase that is required for efficient glycolysis and biosynthesis of aromatic amino acids." J Biol Chem 268:24346-24352.8226984
  • Bussey, H., Storms, R. K., Ahmed, A., Albermann, K., Allen, E., Ansorge, W., Araujo, R., Aparicio, A., Barrell, B., Badcock, K., Benes, V., Botstein, D., Bowman, S., Bruckner, M., Carpenter, J., Cherry, J. M., Chung, E., Churcher, C., Coster, F., Davis, K., Davis, R. W., Dietrich, F. S., Delius, H., DiPaolo, T., Hani, J., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Nature 387:103-105.9169875
  • Nixon, P. F., Duggleby, R. G. (1991). "The N-terminal amino acid sequence of yeast transketolase." Protein Seq Data Anal 4:325-326.1812485
  • Meshalkina, L., Nilsson, U., Wikner, C., Kostikowa, T., Schneider, G. (1997). "Examination of the thiamin diphosphate binding site in yeast transketolase by site-directed mutagenesis." Eur J Biochem 244:646-652.9119035
  • 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
  • Gruhler, A., Olsen, J. V., Mohammed, S., Mortensen, P., Faergeman, N. J., Mann, M., Jensen, O. N. (2005). "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Mol Cell Proteomics 4:310-327.15665377
  • Li, X., Gerber, S. A., Rudner, A. D., Beausoleil, S. A., Haas, W., Villen, J., Elias, J. E., Gygi, S. P. (2007). "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." J Proteome Res 6:1190-1197.17330950
  • Chi, A., Huttenhower, C., Geer, L. Y., Coon, J. J., Syka, J. E., Bai, D. L., Shabanowitz, J., Burke, D. J., Troyanskaya, O. G., Hunt, D. F. (2007). "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Proc Natl Acad Sci U S A 104:2193-2198.17287358
  • 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
  • Lindqvist, Y., Schneider, G., Ermler, U., Sundstrom, M. (1992). "Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution." EMBO J 11:2373-2379.1628611
  • Nikkola, M., Lindqvist, Y., Schneider, G. (1994). "Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 A resolution." J Mol Biol 238:387-404.8176731
  • Wikner, C., Nilsson, U., Meshalkina, L., Udekwu, C., Lindqvist, Y., Schneider, G. (1997). "Identification of catalytically important residues in yeast transketolase." Biochemistry 36:15643-15649.9398292
  • Wikner, C., Meshalkina, L., Nilsson, U., Backstrom, S., Lindqvist, Y., Schneider, G. (1995). "His103 in yeast transketolase is required for substrate recognition and catalysis." Eur J Biochem 233:750-755.8521838