Transketolase 1

Details

Name
Transketolase 1
Synonyms
  • 2.2.1.1
  • TK 1
  • tkt
Gene Name
tktA
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0012285|Transketolase 1
MSSRKELANAIRALSMDAVQKAKSGHPGAPMGMADIAEVLWRDFLKHNPQNPSWADRDRF
VLSNGHGSMLIYSLLHLTGYDLPMEELKNFRQLHSKTPGHPEVGYTAGVETTTGPLGQGI
ANAVGMAIAEKTLAAQFNRPGHDIVDHYTYAFMGDGCMMEGISHEVCSLAGTLKLGKLIA
FYDDNGISIDGHVEGWFTDDTAMRFEAYGWHVIRDIDGHDAASIKRAVEEARAVTDKPSL
LMCKTIIGFGSPNKAGTHDSHGAPLGDAEIALTREQLGWKYAPFEIPSEIYAQWDAKEAG
QAKESAWNEKFAAYAKAYPQEAAEFTRRMKGEMPSDFDAKAKEFIAKLQANPAKIASRKA
SQNAIEAFGPLLPEFLGGSADLAPSNLTLWSGSKAINEDAAGNYIHYGVREFGMTAIANG
ISLHGGFLPYTSTFLMFVEYARNAVRMAALMKQRQVMVYTHDSIGLGEDGPTHQPVEQVA
SLRVTPNMSTWRPCDQVESAVAWKYGVERQDGPTALILSRQNLAQQERTEEQLANIARGG
YVLKDCAGQPELIFIATGSEVELAVAAYEKLTAEGVKARVVSMPSTDAFDKQDAAYRESV
LPKAVTARVAVEAGIADYWYKYVGLNGAIVGMTTFGESAPAELLFEEFGFTVDNVVAKAK
ELL
Number of residues
663
Molecular Weight
72211.14
Theoretical pI
5.41
GO Classification
Functions
manganese ion binding / thiamine pyrophosphate binding / transketolase activity
Processes
pentose-phosphate shunt, non-oxidative branch
Components
cytosol
General Function
Transketolase activity
Specific Function
Catalyzes the reversible transfer of a two-carbon ketol group from sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate, producing xylulose-5-phosphate and ribose-5-phosphate. 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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0012286|Transketolase 1 (tktA)
ATGTCCTCACGTAAAGAGCTTGCCAATGCTATTCGTGCGCTGAGCATGGACGCAGTACAG
AAAGCCAAATCCGGTCACCCGGGTGCCCCTATGGGTATGGCTGACATTGCCGAAGTCCTG
TGGCGTGATTTCCTGAAACACAACCCGCAGAATCCGTCCTGGGCTGACCGTGACCGCTTC
GTGCTGTCCAACGGCCACGGCTCCATGCTGATCTACAGCCTGCTGCACCTCACCGGTTAC
GATCTGCCGATGGAAGAACTGAAAAACTTCCGTCAGCTGCACTCTAAAACTCCGGGTCAC
CCGGAAGTGGGTTACACCGCTGGTGTGGAAACCACCACCGGTCCGCTGGGTCAGGGTATT
GCCAACGCAGTCGGTATGGCGATTGCAGAAAAAACGCTGGCGGCGCAGTTTAACCGTCCG
GGCCACGACATTGTCGACCACTACACCTACGCCTTCATGGGCGACGGCTGCATGATGGAA
GGCATCTCCCACGAAGTTTGCTCTCTGGCGGGTACGCTGAAGCTGGGTAAACTGATTGCA
TTCTACGATGACAACGGTATTTCTATCGATGGTCACGTTGAAGGCTGGTTCACCGACGAC
ACCGCAATGCGTTTCGAAGCTTACGGCTGGCACGTTATTCGCGACATCGACGGTCATGAC
GCGGCATCTATCAAACGCGCAGTAGAAGAAGCGCGCGCAGTGACTGACAAACCTTCCCTG
CTGATGTGCAAAACCATCATCGGTTTCGGTTCCCCGAACAAAGCCGGTACCCACGACTCC
CACGGTGCGCCGCTGGGCGACGCTGAAATTGCCCTGACCCGCGAACAACTGGGCTGGAAA
TATGCGCCGTTCGAAATCCCGTCTGAAATCTATGCTCAGTGGGATGCGAAAGAAGCAGGC
CAGGCGAAAGAATCCGCATGGAACGAGAAATTCGCTGCTTACGCGAAAGCTTATCCGCAG
GAAGCCGCTGAATTTACCCGCCGTATGAAAGGCGAAATGCCGTCTGACTTCGACGCTAAA
GCGAAAGAGTTCATCGCTAAACTGCAGGCTAATCCGGCGAAAATCGCCAGCCGTAAAGCG
TCTCAGAATGCTATCGAAGCGTTCGGTCCGCTGTTGCCGGAATTCCTCGGCGGTTCTGCT
GACCTGGCGCCGTCTAACCTGACCCTGTGGTCTGGTTCTAAAGCAATCAACGAAGATGCT
GCGGGTAACTACATCCACTACGGTGTTCGCGAGTTCGGTATGACCGCGATTGCTAACGGT
ATCTCCCTGCACGGTGGCTTCCTGCCGTACACCTCCACCTTCCTGATGTTCGTGGAATAC
GCACGTAACGCCGTACGTATGGCTGCGCTGATGAAACAGCGTCAGGTGATGGTTTACACC
CACGACTCCATCGGTCTGGGCGAAGACGGCCCGACTCACCAGCCGGTTGAGCAGGTCGCT
TCTCTGCGCGTAACCCCGAACATGTCTACATGGCGTCCGTGTGACCAGGTTGAATCCGCG
GTCGCGTGGAAATACGGTGTTGAGCGTCAGGACGGCCCGACCGCACTGATCCTCTCCCGT
CAGAACCTGGCGCAGCAGGAACGAACTGAAGAGCAACTGGCAAACATCGCGCGCGGTGGT
TATGTGCTGAAAGACTGCGCCGGTCAGCCGGAACTGATTTTCATCGCTACCGGTTCAGAA
GTTGAACTGGCTGTTGCTGCCTACGAAAAACTGACTGCCGAAGGCGTGAAAGCGCGCGTG
GTGTCCATGCCGTCTACCGACGCATTTGACAAGCAGGATGCTGCTTACCGTGAATCCGTA
CTGCCGAAAGCGGTTACTGCACGCGTTGCTGTAGAAGCGGGTATTGCTGACTACTGGTAC
AAGTATGTTGGCCTGAACGGTGCTATCGTCGGTATGACCACCTTCGGTGAATCTGCTCCG
GCAGAGCTGCTGTTTGAAGAGTTCGGCTTCACTGTTGATAACGTTGTTGCGAAAGCAAAA
GAACTGCTGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP27302
UniProtKB Entry NameTKT1_ECOLI
GenBank Gene IDX68025
General References
  1. Sprenger GA: Nucleotide sequence of the Escherichia coli K-12 transketolase (tkt) gene. Biochim Biophys Acta. 1993 Nov 16;1216(2):307-10. [Article]
  2. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  3. Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G 3rd, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL: Escherichia coli K-12: a cooperatively developed annotation snapshot--2005. Nucleic Acids Res. 2006 Jan 5;34(1):1-9. Print 2006. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Szumanski MB, Boyle SM: Analysis and sequence of the speB gene encoding agmatine ureohydrolase, a putrescine biosynthetic enzyme in Escherichia coli. J Bacteriol. 1990 Feb;172(2):538-47. [Article]
  6. Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y: Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Mol Cell Proteomics. 2009 Feb;8(2):215-25. doi: 10.1074/mcp.M800187-MCP200. Epub 2008 Aug 23. [Article]
  7. Sprenger GA, Schorken U, Sprenger G, Sahm H: Transketolase A of Escherichia coli K12. Purification and properties of the enzyme from recombinant strains. Eur J Biochem. 1995 Jun 1;230(2):525-32. [Article]
  8. Asztalos P, Parthier C, Golbik R, Kleinschmidt M, Hubner G, Weiss MS, Friedemann R, Wille G, Tittmann K: Strain and near attack conformers in enzymic thiamin catalysis: X-ray crystallographic snapshots of bacterial transketolase in covalent complex with donor ketoses xylulose 5-phosphate and fructose 6-phosphate, and in noncovalent complex with acceptor aldose ribose 5-phosphate. Biochemistry. 2007 Oct 30;46(43):12037-52. Epub 2007 Oct 3. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01987Cocarboxylaseapproved, experimentalunknownDetails