Transketolase 1
Details
- Name
- Transketolase 1
- Synonyms
- 2.2.1.1
- TK 1
- tkt
- Gene Name
- tktA
- UniProtKB Entry
- P27302Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- 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
- Functionsmanganese ion binding / thiamine pyrophosphate binding / transketolase activityProcessespentose-phosphate shunt, non-oxidative branchComponentscytosol
- 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
- Signal Regions
- Not Available
- 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
Resource Link UniProtKB ID P27302 UniProtKB Entry Name TKT1_ECOLI GenBank Gene ID X68025 PDB ID(s) 1QGD, 2R5N, 2R8O, 2R8P KEGG ID ecj:JW5478 NCBI Gene ID 947420 - General References
- Sprenger GA: Nucleotide sequence of the Escherichia coli K-12 transketolase (tkt) gene. Biochim Biophys Acta. 1993 Nov 16;1216(2):307-10. [Article]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
Associated Data
- Bio-Entities
Bio-Entity Type Transketolase 1 (Escherichia coli (strain K12)) protein primary- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Cocarboxylase approved, experimental unknown target Details