Transketolase

Details

Name
Transketolase
Kind
protein
Synonyms
  • 2.2.1.1
  • TK
Gene Name
TKT
UniProtKB Entry
P29401Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
Amino acid sequence
>lcl|BSEQ0000078|Transketolase
MESYHKPDQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKS
QDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLAEAELLNLRKISSDLDGHPVPKQAFTDV
ATGSLGQGLGAACGMAYTGKYFDKASYRVYCLLGDGELSEGSVWEAMAFASIYKLDNLVA
ILDINRLGQSDPAPLQHQMDIYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKHQPTAIIA
KTFKGRGITGVEDKESWHGKPLPKNMAEQIIQEIYSQIQSKKKILATPPQEDAPSVDIAN
IRMPSLPSYKVGDKIATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPDRFI
ECYIAEQNMVSIAVGCATRNRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVS
IGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGICFIRTSRPENAII
YNNNEDFQVGQAKVVLKSKDDQVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPL
DRKLILDSARATKGRILTVEDHYYEGGIGEAVSSAVVGEPGITVTHLAVNRVPRSGKPAE
LLKMFGIDRDAIAQAVRGLITKA
Number of residues
623
Molecular Weight
67876.95
Theoretical pI
7.73
GO Classification
Functions
protein homodimerization activity / transketolase activity
Processes
glyceraldehyde-3-phosphate biosynthetic process / pentose-phosphate shunt / pentose-phosphate shunt, non-oxidative branch / regulation of growth
Components
cytosol / extracellular exosome / nucleoplasm / peroxisome / vesicle
General Function
Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate
Specific Function
calcium ion binding
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0010138|Transketolase (TKT)
ATGGAGAGCTACCACAAGCCTGACCAGCAGAAGCTGCAGGCCTTGAAGGACACGGCCAAC
CGCCTACGTATCAGCTCCATCCAGGCCACCACTGCGGCGGGCTCTGGCCACCCCACGTCA
TGCTGCAGCGCCGCAGAGATCATGGCTGTCCTCTTTTTCCACACCATGCGCTACAAGTCC
CAGGACCCCCGGAATCCGCACAATGACCGCTTTGTGCTCTCCAAGGGCCATGCAGCTCCC
ATCCTCTACGCGGTCTGGGCTGAAGCTGGTTTCCTGGCCGAGGCGGAGCTGCTGAACCTG
AGGAAGATCAGCTCCGACTTGGACGGGCACCCGGTCCCGAAACAAGCTTTCACCGACGTG
GCCACTGGCTCCCTGGGCCAGGGCCTCGGGGCCGCTTGTGGGATGGCCTACACCGGCAAA
TACTTCGACAAGGCCAGCTACCGAGTCTATTGCTTGCTGGGAGACGGGGAGCTGTCAGAG
GGCTCTGTATGGGAGGCCATGGCCTTCGCCAGCATCTATAAGCTGGACAACCTTGTGGCC
ATTCTAGACATCAATCGCCTGGGCCAGAGTGACCCGGCCCCACTGCAGCACCAGATGGAC
ATCTACCAGAAGCGGTGCGAGGCCTTCGGTTGGCATGCCATCATCGTGGATGGACACAGC
GTGGAGGAGCTGTGCAAGGCCTTTGGCCAGGCCAAGCACCAGCCAACAGCCATCATTGCC
AAGACCTTCAAGGGCCGAGGGATCACGGGGGTAGAAGATAAGGAGTCTTGGCATGGGAAG
CCCCTCCCCAAAAACATGGCTGAGCAGATCATCCAGGAGATCTACAGCCAGATCCAGAGC
AAAAAGAAGATCCTGGCAACCCCTCCACAGGAGGACGCACCCTCAGTGGACATTGCCAAC
ATCCGCATGCCCAGCCTGCCCAGCTACAAAGTTGGGGACAAGATAGCCACCCGCAAGGCC
TACGGGCAGGCACTGGCCAAGCTGGGCCATGCCAGTGACCGCATCATCGCCCTGGATGGG
GACACCAAAAATTCCACCTTCTCGGAGATCTTCAAAAAGGAGCACCCGGACCGCTTCATC
GAGTGCTACATTGCTGAGCAGAACATGGTGAGCATCGCGGTGGGCTGTGCCACCCGCAAC
AGGACGGTGCCCTTCTGCAGCACTTTTGCAGCCTTCTTCACGCGGGCCTTTGACCAGATT
CGCATGGCCGCCATCTCCGAGAGCAACATCAACCTCTGCGGCTCCCACTGCGGCGTTTCC
ATCGGGGAAGACGGGCCCTCCCAGATGGCCCTAGAAGATCTGGCTATGTTTCGGTCAGTC
CCCACATCAACTGTCTTTTACCCAAGTGATGGCGTTGCTACAGAGAAGGCAGTGGAACTA
GCCGCCAATACAAAGGGTATCTGCTTCATCCGGACCAGCCGCCCAGAAAATGCCATCATC
TATAACAACAATGAGGACTTCCAGGTCGGACAAGCCAAGGTGGTCCTGAAGAGCAAGGAT
GACCAGGTGACCGTTATCGGGGCTGGGGTGACCCTGCACGAGGCCTTGGCCGCTGCCGAA
CTGCTGAAGAAAGAAAAGATCAACATCCGCGTGCTGGACCCCTTCACCATCAAGCCCCTG
GACAGAAAACTCATTCTCGACAGCGCTCGTGCCACCAAGGGCAGGATCCTCACCGTGGAG
GACCATTATTATGAAGGTGGCATTGGTGAGGCTGTGTCCAGTGCAGTAGTGGGCGAGCCT
GGCATCACTGTCACCCACCTGGCAGTTAACCGGGTACCAAGAAGTGGGAAGCCGGCTGAG
CTGCTGAAGATGTTTGGTATCGACAGGGATGCCATTGCACAAGCTGTGAGGGGCCTCATC
ACCAAGGCCTAG
Chromosome Location
3
Locus
3p21.1
External Identifiers
ResourceLink
UniProtKB IDP29401
UniProtKB Entry NameTKT_HUMAN
GenBank Protein ID37267
GenBank Gene IDX67688
GeneCard IDTKT
GenAtlas IDTKT
HGNC IDHGNC:11834
PDB ID(s)3MOS, 3OOY, 4KXU, 4KXV, 4KXW, 4KXX, 4KXY, 6HA3, 6HAD, 6RJB, 8WA8, 8WA9, 8WAA
KEGG IDhsa:7086
NCBI Gene ID7086
General References
  1. McCool BA, Plonk SG, Martin PR, Singleton CK: Cloning of human transketolase cDNAs and comparison of the nucleotide sequence of the coding region in Wernicke-Korsakoff and non-Wernicke-Korsakoff individuals. J Biol Chem. 1993 Jan 15;268(2):1397-404. [Article]
  2. Schenk G, Layfield R, Candy JM, Duggleby RG, Nixon PF: Molecular evolutionary analysis of the thiamine-diphosphate-dependent enzyme, transketolase. J Mol Evol. 1997 May;44(5):552-72. [Article]
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  8. Jung EH, Takeuchi T, Nishino K, Itokawa Y: Studies on the nature of thiamine pyrophosphate binding and dependency on divalent cations of transketolase from human erythrocytes. Int J Biochem. 1988;20(11):1255-9. [Article]
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  18. Mitschke L, Parthier C, Schroder-Tittmann K, Coy J, Ludtke S, Tittmann K: The crystal structure of human transketolase and new insights into its mode of action. J Biol Chem. 2010 Oct 8;285(41):31559-70. doi: 10.1074/jbc.M110.149955. Epub 2010 Jul 28. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
Copperapproved, investigationalunknowntargetDetails