Thymidylate synthase
Details
- Name
- Thymidylate synthase
- Synonyms
- 2.1.1.45
- TS
- Gene Name
- thyA
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0011008|Thymidylate synthase MKQYLELMQKVLDEGTQKNDRTGTGTLSIFGHQMRFNLQDGFPLVTTKRCHLRSIIHELL WFLQGDTNIAYLHENNVTIWDEWADENGDLGPVYGKQWRAWPTPDGRHIDQITTVLNQLK NDPDSRRIIVSAWNVGELDKMALAPCHAFFQFYVADGKLSCQLYQRSCDVFLGLPFNIAS YALLVHMMAQQCDLEVGDFVWTGGDTHLYSNHMDQTHLQLSREPRPLPKLIIKRKPESIF DYRFEDFEIEGYDPHPGIKAPVAI
- Number of residues
- 264
- Molecular Weight
- 30479.475
- Theoretical pI
- 5.94
- GO Classification
- FunctionsRNA binding / thymidylate synthase activityProcessesdTMP biosynthetic process / dTTP biosynthetic process / regulation of translationComponentscytosol
- General Function
- Thymidylate synthase activity
- Specific Function
- Provides the sole de novo source of dTMP for DNA biosynthesis. This protein also binds to its mRNA thus repressing its own translation.
- Pfam Domain Function
- Thymidylat_synt (PF00303)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0011009|Thymidylate synthase (thyA) ATGAAACAGTATTTAGAACTGATGCAAAAAGTGCTCGACGAAGGCACACAGAAAAACGAC CGTACCGGAACCGGAACGCTTTCCATTTTTGGTCATCAGATGCGTTTTAACCTGCAAGAT GGATTCCCGCTGGTGACAACTAAACGTTGCCACCTGCGTTCCATCATCCATGAACTGCTG TGGTTTCTGCAGGGCGACACTAACATTGCTTATCTACACGAAAACAATGTCACCATCTGG GACGAATGGGCCGATGAAAACGGCGACCTCGGGCCAGTGTATGGTAAACAGTGGCGCGCC TGGCCAACGCCAGATGGTCGTCATATTGACCAGATCACTACGGTACTGAACCAGCTGAAA AACGACCCGGATTCGCGCCGCATTATTGTTTCAGCGTGGAACGTAGGCGAACTGGATAAA ATGGCGCTGGCACCGTGCCATGCATTCTTCCAGTTCTATGTGGCAGACGGCAAACTCTCT TGCCAGCTTTATCAGCGCTCCTGTGACGTCTTCCTCGGCCTGCCGTTCAACATTGCCAGC TACGCGTTATTGGTGCATATGATGGCGCAGCAGTGCGATCTGGAAGTGGGTGATTTTGTC TGGACCGGTGGCGACACGCATCTGTACAGCAACCATATGGATCAAACTCATCTGCAATTA AGCCGCGAACCGCGTCCGCTGCCGAAGTTGATTATCAAACGTAAACCCGAATCCATCTTC GACTACCGTTTCGAAGACTTTGAGATTGAAGGCTACGATCCGCATCCGGGCATTAAAGCG CCGGTGGCTATCTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0A884 UniProtKB Entry Name TYSY_ECOLI GenBank Protein ID 147987 GenBank Gene ID J01710 - General References
- Belfort M, Maley G, Pedersen-Lane J, Maley F: Primary structure of the Escherichia coli thyA gene and its thymidylate synthase product. Proc Natl Acad Sci U S A. 1983 Aug;80(16):4914-8. [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]
- 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]
- Finch PW, Wilson RE, Brown K, Hickson ID, Tomkinson AE, Emmerson PT: Complete nucleotide sequence of the Escherichia coli recC gene and of the thyA-recC intergenic region. Nucleic Acids Res. 1986 Jun 11;14(11):4437-51. [Article]
- VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
- Montfort WR, Perry KM, Fauman EB, Finer-Moore JS, Maley GF, Hardy L, Maley F, Stroud RM: Structure, multiple site binding, and segmental accommodation in thymidylate synthase on binding dUMP and an anti-folate. Biochemistry. 1990 Jul 31;29(30):6964-77. [Article]
- Voeller DM, Changchien LM, Maley GF, Maley F, Takechi T, Turner RE, Montfort WR, Allegra CJ, Chu E: Characterization of a specific interaction between Escherichia coli thymidylate synthase and Escherichia coli thymidylate synthase mRNA. Nucleic Acids Res. 1995 Mar 11;23(5):869-75. [Article]
- Kim CW, Michaels ML, Miller JH: Amino acid substitution analysis of E. coli thymidylate synthase: the study of a highly conserved region at the N-terminus. Proteins. 1992 Aug;13(4):352-63. [Article]
- Perry KM, Fauman EB, Finer-Moore JS, Montfort WR, Maley GF, Maley F, Stroud RM: Plastic adaptation toward mutations in proteins: structural comparison of thymidylate synthases. Proteins. 1990;8(4):315-33. [Article]
- Fauman EB, Rutenber EE, Maley GF, Maley F, Stroud RM: Water-mediated substrate/product discrimination: the product complex of thymidylate synthase at 1.83 A. Biochemistry. 1994 Feb 15;33(6):1502-11. [Article]
- Sage CR, Rutenber EE, Stout TJ, Stroud RM: An essential role for water in an enzyme reaction mechanism: the crystal structure of the thymidylate synthase mutant E58Q. Biochemistry. 1996 Dec 17;35(50):16270-81. [Article]
- Strop P, Changchien L, Maley F, Montfort WR: Crystal structures of a marginally active thymidylate synthase mutant, Arg 126-->Glu. Protein Sci. 1997 Dec;6(12):2504-11. [Article]
- Reyes CL, Sage CR, Rutenber EE, Nissen RM, Finer-Moore JS, Stroud RM: Inactivity of N229A thymidylate synthase due to water-mediated effects: isolating a late stage in methyl transfer. J Mol Biol. 1998 Dec 4;284(3):699-712. [Article]
- Erlanson DA, Braisted AC, Raphael DR, Randal M, Stroud RM, Gordon EM, Wells JA: Site-directed ligand discovery. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9367-72. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB02031 (6S)-5,6,7,8-tetrahydrofolic acid experimental unknown Details DB02223 LY231514 tetra glu experimental unknown Details DB02256 2'-Deoxyuridine experimental unknown Details DB02301 5,10-Methylene-6-Hydrofolic Acid experimental unknown Details DB02467 L-methionine (S)-S-oxide experimental unknown Details DB02752 Tosyl-D-Proline experimental unknown Details DB02899 N-Carboxymethionine experimental unknown Details DB03038 LY341770 experimental unknown Details DB03157 N,O-didansyl-L-tyrosine experimental unknown Details DB03274 2',5'-Dideoxyuridine experimental unknown Details DB03541 10-Propargyl-5,8-Dideazafolic Acid experimental unknown Details DB03558 SP-876 experimental unknown Details DB03761 5-fluoro-2'-deoxyuridine-5'-monophosphate experimental unknown Details DB03800 Deoxyuridine monophosphate experimental unknown Details DB03818 N-[Tosyl-D-Prolinyl]Amino-Ethanethiol experimental unknown Details DB04447 1,4-Dithiothreitol experimental unknown Details DB04457 2'-Deoxyguanosine-5'-Monophosphate experimental unknown Details DB04503 Sp-722 experimental unknown Details DB04530 S,S-(2-Hydroxyethyl)Thiocysteine experimental unknown Details DB04586 o-Bromophenol experimental unknown Details DB04696 4-CHLORO-3',3''-DIBROMOPHENOL-1,8-NAPHTHALEIN experimental unknown Details DB08131 2-{4-[2-(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDIN-5-YL)-ETHYL]-BENZOYLAMINO}-3-METHYL-BUTYRIC ACID experimental unknown Details