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P0A884 (TYSY_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thymidylate synthase
Short name=TS
Short name=TSase
EC=2.1.1.45
Gene names
Name:thyA
Ordered Locus Names:b2827, JW2795
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length264 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Provides the sole de novo source of dTMP for DNA biosynthesis. This protein also binds to its mRNA thus repressing its own translation. HAMAP-Rule MF_00008

Catalytic activity

5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP. HAMAP-Rule MF_00008

Pathway

Pyrimidine metabolism; dTTP biosynthesis. HAMAP-Rule MF_00008

Subunit structure

Homodimer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00008.

Post-translational modification

Although not discussed in the published references, Met-1 is represented in the submitted PDB entries as being modified by either a formyl, or a carboxyl group. The N-terminal is probably N-(dihydroxymethyl)methionine, the hydrated form of N-formylmethionine. HAMAP-Rule MF_00008

Sequence similarities

Belongs to the thymidylate synthase family. Bacterial-type ThyA subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 264264Thymidylate synthase HAMAP-Rule MF_00008
PRO_0000140954

Sites

Active site1461

Amino acid modifications

Modified residue11N-formylmethionine Probable

Secondary structure

1 ............................................... 264
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A884 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 0E6D88ED98D24D22

FASTA26430,480
        10         20         30         40         50         60 
MKQYLELMQK VLDEGTQKND RTGTGTLSIF GHQMRFNLQD GFPLVTTKRC HLRSIIHELL 

        70         80         90        100        110        120 
WFLQGDTNIA YLHENNVTIW DEWADENGDL GPVYGKQWRA WPTPDGRHID QITTVLNQLK 

       130        140        150        160        170        180 
NDPDSRRIIV SAWNVGELDK MALAPCHAFF QFYVADGKLS CQLYQRSCDV FLGLPFNIAS 

       190        200        210        220        230        240 
YALLVHMMAQ QCDLEVGDFV WTGGDTHLYS NHMDQTHLQL SREPRPLPKL IIKRKPESIF 

       250        260 
DYRFEDFEIE GYDPHPGIKA PVAI

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of the Escherichia coli thyA gene and its thymidylate synthase product."
Belfort M., Maley G.F., Pedersen-Lane J., Maley F.
Proc. Natl. Acad. Sci. U.S.A. 80:4914-4918(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: K12 / JM103 / ATCC 39403 / DSM 2829 / NCIMB 12044.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Complete nucleotide sequence of the Escherichia coli recC gene and of the thyA-recC intergenic region."
Finch P.W., Wilson R.E., Brown K., Hickson I.D., Tomkinson A.E., Emmerson P.T.
Nucleic Acids Res. 14:4437-4451(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 63-264.
[5]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[6]"Structure, multiple site binding, and segmental accommodation in thymidylate synthase on binding dUMP and an anti-folate."
Montfort W.R., Perry K.M., Fauman E.B., Finer-Moore J.S., Maley G.F., Hardy L., Maley F., Stroud R.M.
Biochemistry 29:6964-6977(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS).
[7]"Characterization of a specific interaction between Escherichia coli thymidylate synthase and Escherichia coli thymidylate synthase mRNA."
Voeller D.M., Changchien L.-M., Maley G.F., Maley F., Takechi T., Turner R.E., Montfort W.R., Allegra C.J., Chu E.
Nucleic Acids Res. 23:869-875(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MECHANISM OF TRANSLATION REGULATION.
[8]"Amino acid substitution analysis of E. coli thymidylate synthase: the study of a highly conserved region at the N-terminus."
Kim C.W., Michaels M.L., Miller J.F.
Proteins 13:352-363(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[9]"Plastic adaptation toward mutations in proteins: structural comparison of thymidylate synthases."
Perry K.M., Fauman E.B., Finer-Moore J.S., Montfort W.R., Maley G.F., Maley F., Stroud R.M.
Proteins 8:315-333(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[10]"Water-mediated substrate/product discrimination: the product complex of thymidylate synthase at 1.83 A."
Fauman E.B., Rutenber E.E., Maley G.F., Maley F., Stroud R.M.
Biochemistry 33:1502-1511(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
[11]"An essential role for water in an enzyme reaction mechanism: the crystal structure of the thymidylate synthase mutant E58Q."
Sage C.R., Rutenber E.E., Stout T.J., Stroud R.M.
Biochemistry 35:16270-16281(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT GLN-58.
[12]"Crystal structures of a marginally active thymidylate synthase mutant, Arg 126-->Glu."
Strop P., Changchien L., Maley F., Montfort W.R.
Protein Sci. 6:2504-2511(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT GLU-126.
[13]"Inactivity of N229A thymidylate synthase due to water-mediated effects: isolating a late stage in methyl transfer."
Reyes C.L., Sage C.R., Rutenber E.E., Nissen R.M., Finer-Moore J.S., Stroud R.M.
J. Mol. Biol. 284:699-712(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT ALA-177.
[14]"Site-directed ligand discovery."
Erlanson D.A., Braisted A.C., Raphael D.R., Randal M., Stroud R.M., Gordon E.M., Wells J.A.
Proc. Natl. Acad. Sci. U.S.A. 97:9367-9372(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J01710 Genomic DNA. Translation: AAA24675.1.
U29581 Genomic DNA. Translation: AAB40474.1.
U00096 Genomic DNA. Translation: AAC75866.1.
AP009048 Genomic DNA. Translation: BAE76896.1.
X03966 Genomic DNA. Translation: CAA27600.1.
PIRSYECT. A00549.
RefSeqNP_417304.1. NC_000913.2.
YP_491032.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AIQX-ray2.20A/B1-264[»]
1AJMX-ray2.40A1-264[»]
1AN5X-ray2.60A/B1-264[»]
1AOBX-ray2.10A1-264[»]
1AXWX-ray1.70A/B1-264[»]
1BDUX-ray2.10A1-264[»]
1BIDX-ray2.20A1-264[»]
1BJGX-ray2.30A2-264[»]
1BQ1X-ray2.50A/B1-264[»]
1BQ2X-ray2.20A1-264[»]
1DDUX-ray2.10A/B1-264[»]
1DNAX-ray2.20A/B2-264[»]
1EV5X-ray1.70A1-264[»]
1EV8X-ray2.60A1-264[»]
1EVFX-ray1.70A1-264[»]
1EVGX-ray2.00A1-264[»]
1F4BX-ray1.75A1-264[»]
1F4CX-ray2.00A/B1-264[»]
1F4DX-ray2.15A/B1-264[»]
1F4EX-ray1.90A1-264[»]
1F4FX-ray2.00A/B1-264[»]
1F4GX-ray1.75A/B1-264[»]
1FFLX-ray2.94A1-264[»]
1FWMX-ray2.20A/B1-264[»]
1JG0X-ray2.00A/B1-264[»]
1JTQX-ray2.50A/B1-264[»]
1JTUX-ray2.20A/B1-264[»]
1JUTX-ray2.70A/B1-264[»]
1KCEX-ray2.00A/B1-264[»]
1KZIX-ray1.75A/B1-264[»]
1KZJX-ray2.60A/B/C/D/E/F1-264[»]
1NCEX-ray2.40A/B1-264[»]
1QQQX-ray1.50A1-264[»]
1SYNX-ray2.00A/B1-264[»]
1TDUX-ray2.10A/B1-264[»]
1TJSX-ray2.20A1-264[»]
1TLCX-ray2.10A/B1-264[»]
1TLSX-ray2.60A/B1-264[»]
1TRGX-ray1.90A1-264[»]
1TSDX-ray1.95A/B1-264[»]
1TSNX-ray2.20A1-264[»]
1TYSX-ray1.80A1-264[»]
1ZPRX-ray2.50A/B1-264[»]
2A9WX-ray1.65A/B/C/D1-264[»]
2BBQX-ray2.30A/B1-264[»]
2FTNX-ray1.60A1-264[»]
2FTOX-ray2.00X1-264[»]
2FTQX-ray1.81A1-264[»]
2G8XX-ray1.83A/B1-264[»]
2KCEX-ray2.20A/B1-264[»]
2TSCX-ray1.97A/B1-264[»]
2VETX-ray2.20A1-264[»]
2VF0X-ray3.00A/B1-264[»]
3B5BX-ray2.70A/B1-264[»]
3B9HX-ray2.49A1-264[»]
3BFIX-ray2.20A1-264[»]
3BGXX-ray1.93A1-264[»]
3BHLX-ray1.40A/B1-264[»]
3BHRX-ray1.90A1-264[»]
3TMSX-ray2.10A1-264[»]
4F2VX-ray2.49A/B1-264[»]
4GEVX-ray1.30A/B1-264[»]
4IW5X-ray1.30A/B1-264[»]
ProteinModelPortalP0A884.
SMRP0A884. Positions 2-264.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-48261N.
IntActP0A884. 5 interactions.
MINTMINT-1265510.
STRING511145.b2827.

Proteomic databases

PaxDbP0A884.
PRIDEP0A884.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75866; AAC75866; b2827.
BAE76896; BAE76896; BAE76896.
GeneID12933064.
949035.
KEGGecj:Y75_p2761.
eco:b2827.
PATRIC32121072. VBIEscCol129921_2925.

Organism-specific databases

EchoBASEEB0995.
EcoGeneEG11002. thyA.

Phylogenomic databases

eggNOGCOG0207.
HOGENOMHOG000257900.
KOK00560.
OMADTNVAYL.
ProtClustDBPRK01827.

Enzyme and pathway databases

BioCycEcoCyc:THYMIDYLATESYN-MONOMER.
ECOL316407:JW2795-MONOMER.
MetaCyc:THYMIDYLATESYN-MONOMER.
SABIO-RKP0A884.
UniPathwayUPA00575.

Gene expression databases

GenevestigatorP0A884.

Family and domain databases

Gene3D3.30.572.10. 1 hit.
HAMAPMF_00008. Thymidy_synth_bact.
InterProIPR023451. Thymidate_synth/dCMP_Mease.
IPR000398. Thymidylate_synthase.
IPR020940. Thymidylate_synthase_AS.
[Graphical view]
PfamPF00303. Thymidylat_synt. 1 hit.
[Graphical view]
PRINTSPR00108. THYMDSNTHASE.
SUPFAMSSF55831. Thymidylat_synth_C. 1 hit.
TIGRFAMsTIGR03284. thym_sym. 2 hits.
PROSITEPS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP0A884.
ChEMBLCHEMBL2555.
EvolutionaryTraceP0A884.

Entry information

Entry nameTYSY_ECOLI
AccessionPrimary (citable) accession number: P0A884
Secondary accession number(s): P00470, Q2MA10
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents