P00471 (TYSY_BPT4) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 94.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Thymidylate synthase Short name=TS Short name=TSase EC=2.1.1.45 | ||
| Gene names |
| ||
| Organism | Enterobacteria phage T4 (Bacteriophage T4) [Reference proteome] | ||
| Taxonomic identifier | 10665 [NCBI] | ||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Caudovirales › Myoviridae › Tevenvirinae › T4likevirus › ![]() | ||
| Virus host | Escherichia coli [TaxID: 562] |
Protein attributes
| Sequence length | 286 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP. |
| Pathway | |
| Subunit structure | Homodimer. |
| Miscellaneous | This enzyme is also expressed by the thyA gene of E.coli; the phage and host synthases exhibit striking dissimilarities in both structure and function. |
| Sequence similarities | Belongs to the thymidylate synthase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Nucleotide biosynthesis |
| Molecular function | Methyltransferase Transferase |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | dTMP biosynthetic process Inferred from electronic annotation. Source: InterPro dTTP biosynthetic processInferred from electronic annotation. Source: UniProtKB-UniPathway |
| Molecular_function | thymidylate synthase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 286 | 286 | Thymidylate synthase | PRO_0000141061 | |||||||||||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||||||||||||
| Active site | 156 | 1 | Ref.1 | ||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 3 – 12 | 10 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 26 – 30 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 33 – 37 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 38 – 40 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 53 – 63 | 11 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 69 – 77 | 9 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 80 – 83 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 88 – 91 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 92 – 95 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 96 – 98 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 109 – 114 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 121 – 131 | 11 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 145 – 150 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 156 – 164 | 9 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 166 – 179 | 14 | |||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 180 – 183 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 184 – 202 | 19 | |||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 205 – 221 | 17 | |||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 224 – 226 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 227 – 229 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 247 – 251 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 254 – 262 | 9 | |||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 266 – 268 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Intervening sequence in the thymidylate synthase gene of bacteriophage T4." Chu F.K., Maley G.F., Maley F., Belfort M. Proc. Natl. Acad. Sci. U.S.A. 81:3049-3053(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Bacteriophage T4 genome." Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W. Microbiol. Mol. Biol. Rev. 67:86-156(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [3] | "Nucleotide sequence reveals overlap between T4 phage genes encoding dihydrofolate reductase and thymidylate synthase." Purohit S., Mathews C.K. J. Biol. Chem. 259:6261-6266(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42. |
| [4] | "Characterization of the intron in the phage T4 thymidylate synthase gene and evidence for its self-excision from the primary transcript." Chu F.K., Maley G.F., West D.K., Belfort M., Maley F. Cell 45:157-166(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 179-188. |
| [5] | "Total sequence, flanking regions, and transcripts of bacteriophage T4 nrdA gene, coding for alpha chain of ribonucleoside diphosphate reductase." Tseng M.J., Hilfinger J.M., Walsh A., Greenberg G.R. J. Biol. Chem. 263:16242-16251(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 251-286. |
| [6] | "Crystal structure of thymidylate synthase from T4 phage: component of a deoxynucleoside triphosphate-synthesizing complex." Finer-Moore J.S., Maley G.F., Maley F., Montfort W.R., Stroud R.M. Biochemistry 33:15459-15468(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS). |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | K02035, K01804 Genomic DNA. Translation: AAA32492.1. AF158101 Genomic DNA. Translation: AAD42662.1. M12742 Genomic DNA. Translation: AAC12816.1. J03968 Genomic DNA. Translation: AAA32525.1. | ||||||||||||
| PIR | SYBPT4. A00550. | ||||||||||||
| RefSeq | NP_049848.1. NC_000866.4. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P00471. | ||||||||||||
| SMR | P00471. Positions 1-286. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 1258770. | ||||||||||||
Phylogenomic databases | |||||||||||||
| ProtClustDB | CLSP2343285. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| UniPathway | UPA00575. | ||||||||||||
Family and domain databases | |||||||||||||
| Gene3D | 3.30.572.10. 1 hit. | ||||||||||||
| InterPro | IPR023451. Thymidate_synth/dCMP_Mease. IPR000398. Thymidylate_synthase. IPR020940. Thymidylate_synthase_AS. [Graphical view] | ||||||||||||
| Pfam | PF00303. Thymidylat_synt. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00108. THYMDSNTHASE. | ||||||||||||
| SUPFAM | SSF55831. Thymidylat_synth_C. 1 hit. | ||||||||||||
| TIGRFAMs | TIGR03284. thym_sym. 1 hit. | ||||||||||||
| PROSITE | PS00091. THYMIDYLATE_SYNTHASE. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | P00471. | ||||||||||||
Entry information
| Entry name | TYSY_BPT4 | ||||||||
| Accession | Primary (citable) accession number: P00471 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Viral Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
