Thymidylate kinase

NameThymidylate kinase
Synonyms
  • 2.7.4.9
  • dTMP kinase
  • Thymidine monophosphate kinase
  • TMPK
Gene Nametmk
OrganismMycobacterium tuberculosis
Amino acid sequence
>lcl|BSEQ0051201|Thymidylate kinase
MLIAIEGVDGAGKRTLVEKLSGAFRAAGRSVATLAFPRYGQSVAADIAAEALHGEHGDLA
SSVYAMATLFALDRAGAVHTIQGLCRGYDVVILDRYVASNAAYSAARLHENAAGKAAAWV
QRIEFARLGLPKPDWQVLLAVSAELAGERSRGRAQRDPGRARDNYERDAELQQRTGAVYA
ELAAQGWGGRWLVVGADVDPGRLAATLAPPDVPS
Number of residuesNone
Molecular Weight22634.285
Theoretical pINone
GO Classification
Functions
  • ATP binding
  • GTP binding
  • thymidylate kinase activity
  • magnesium ion binding
  • protein homodimerization activity
  • uridylate kinase activity
Processes
  • dTTP biosynthetic process
  • dTDP biosynthetic process
  • dUDP biosynthetic process
  • TMP metabolic process
Components
  • cytoplasm
General FunctionCatalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with ITP, GTP, CTP and UTP.
Specific FunctionAtp binding
Transmembrane Regions
GenBank Protein ID
UniProtKB IDP9WKE1
UniProtKB Entry Name
Cellular LocationNone
Gene sequence
>lcl|BSEQ0051202|Thymidylate kinase (tmk)
GTGCTAATCGCGATTGAGGGCGTTGACGGCGCTGGCAAGCGGACGTTGGTGGAAAAGCTG
TCCGGGGCCTTTCGAGCAGCCGGGAGATCGGTGGCCACACTGGCGTTCCCGCGCTACGGA
CAGTCGGTGGCCGCCGACATCGCAGCGGAGGCGCTGCACGGCGAGCACGGTGACCTCGCA
TCGTCGGTGTATGCGATGGCGACGCTGTTCGCGCTCGACCGCGCTGGCGCGGTCCACACG
ATCCAGGGGCTGTGTCGCGGCTACGACGTGGTGATCCTGGATCGCTACGTCGCCTCCAAC
GCGGCCTACAGCGCGGCGCGCCTACATGAAAACGCGGCCGGGAAGGCAGCGGCCTGGGTT
CAGCGGATCGAATTTGCAAGACTCGGGTTGCCCAAGCCCGACTGGCAGGTGCTCCTTGCG
GTCTCTGCCGAGCTCGCCGGGGAACGATCCCGCGGCCGTGCCCAGCGTGACCCCGGTCGG
GCGCGCGACAATTACGAACGCGACGCTGAACTTCAGCAGCGCACCGGTGCGGTCTACGCC
GAGTTGGCGGCCCAAGGGTGGGGCGGCCGGTGGCTGGTTGTCGGCGCCGATGTTGATCCG
GGCCGACTAGCGGCGACTTTGGCGCCTCCAGACGTGCCAAGTTGA
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
References
  1. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [9634230 ]
  2. Munier-Lehmann H, Chaffotte A, Pochet S, Labesse G: Thymidylate kinase of Mycobacterium tuberculosis: a chimera sharing properties common to eukaryotic and bacterial enzymes. Protein Sci. 2001 Jun;10(6):1195-205. [11369858 ]
  3. Li de la Sierra I, Munier-Lehmann H, Gilles AM, Barzu O, Delarue M: Crystallization and preliminary X-ray analysis of the thymidylate kinase from Mycobacterium tuberculosis. Acta Crystallogr D Biol Crystallogr. 2000 Feb;56(Pt 2):226-8. [10666613 ]
  4. Raman K, Yeturu K, Chandra N: targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis. BMC Syst Biol. 2008 Dec 19;2:109. doi: 10.1186/1752-0509-2-109. [19099550 ]
  5. Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3. [21969609 ]
  6. Li de la Sierra I, Munier-Lehmann H, Gilles AM, Barzu O, Delarue M: X-ray structure of TMP kinase from Mycobacterium tuberculosis complexed with TMP at 1.95 A resolution. J Mol Biol. 2001 Aug 3;311(1):87-100. [11469859 ]
  7. Ursby T, Weik M, Fioravanti E, Delarue M, Goeldner M, Bourgeois D: Cryophotolysis of caged compounds: a technique for trapping intermediate states in protein crystals. Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):607-14. Epub 2002 Mar 22. [11914484 ]
  8. Haouz A, Vanheusden V, Munier-Lehmann H, Froeyen M, Herdewijn P, Van Calenbergh S, Delarue M: Enzymatic and structural analysis of inhibitors designed against Mycobacterium tuberculosis thymidylate kinase. New insights into the phosphoryl transfer mechanism. J Biol Chem. 2003 Feb 14;278(7):4963-71. Epub 2002 Nov 25. [12454011 ]
  9. Fioravanti E, Haouz A, Ursby T, Munier-Lehmann H, Delarue M, Bourgeois D: Mycobacterium tuberculosis thymidylate kinase: structural studies of intermediates along the reaction pathway. J Mol Biol. 2003 Apr 11;327(5):1077-92. [12662932 ]
  10. Fioravanti E, Adam V, Munier-Lehmann H, Bourgeois D: The crystal structure of Mycobacterium tuberculosis thymidylate kinase in complex with 3'-azidodeoxythymidine monophosphate suggests a mechanism for competitive inhibition. Biochemistry. 2005 Jan 11;44(1):130-7. [15628853 ]

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