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Reviewed, UniProtKB/Swiss-Prot P0A884 (TYSY_ECOLI)

Last modified June 15, 2010. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
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Names and originHide

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) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia
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Protein attributesHide

Sequence length264 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.
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General annotation (Comments)Hide

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 MF_00008

Catalytic activity

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

Pathway

Pyrimidine metabolism; dTTP biosynthesis. HAMAP MF_00008

Subunit structure

Homodimer. HAMAP MF_00008

Subcellular location

Cytoplasm HAMAP 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 MF_00008

Sequence similarities

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

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OntologiesHide

Keywords
   Biological processNucleotide biosynthesis
Translation regulation
   Cellular componentCytoplasm
   LigandRNA-binding
   Molecular functionMethyltransferase
Repressor
Transferase
   PTMFormylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processdTMP biosynthetic process

Inferred from electronic annotation. Source: HAMAP

regulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

thymidylate synthase activity

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...
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Sequence annotation (Features)Hide

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 264264Thymidylate synthase HAMAP MF_00008
PRO_0000140954

Sites

Active site1461 HAMAP MF_00008

Amino acid modifications

Modified residue11N-formylmethionine Probable

Secondary structure

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

Details...

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SequencesHide

Sequence LengthMass (Da)Tools
P0A884-1 [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

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ReferencesHide

« 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: 6308660] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: K12 / JM103 / ATCC 39403 / DSM 2829 / NCIB 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: 9278503] [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: 16738553] [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: 3520484] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 63-264.
[5]"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: 2223754] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS).
[6]"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: 7708505] [Abstract]
Cited for: MECHANISM OF TRANSLATION REGULATION.
[7]"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: 1518803] [Abstract]
Cited for: MUTAGENESIS.
[8]"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: 2128651] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[9]"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: 8312270] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
[10]"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: 8973201] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT GLN-58.
[11]"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: 9416600] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT GLU-126.
[12]"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: 9826509] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT ALA-177.
[13]"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: 10944209] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
+Additional computationally mapped references.
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Cross-referencesHide

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.
RefSeqAP_003390.1.
NP_417304.1.

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/B3-264[»]
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[»]
2G8MX-ray1.30A/B1-264[»]
2G8OX-ray1.30A/B1-264[»]
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[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-48261N.
MINTMINT-1265510.
STRINGP0A884.

2-D gel databases

ECO2DBASEG029.3. 6TH EDITION.

Genome annotation databases

EnsemblBacteriaEBESCT00000001730; EBESCP00000001730; EBESCG00000001424.
EBESCT00000017304; EBESCP00000016595; EBESCG00000016361.
GeneID949035.
GenomeReviewsGene locus JW2795 in contig AP009048_GR.
Gene locus b2827 in contig U00096_GR.
KEGGecj:JW2795.
eco:b2827.

Organism-specific databases

EchoBASEEB0995.
EcoGeneEG11002. thyA.
CMRSearch...

Phylogenomic databases

eggNOGCOG0207.
HOGENOMHBG588098.
OMAADIPRMK.
ProtClustDBPRK01827.

Enzyme and pathway databases

BioCycEcoCyc:THYMIDYLATESYN-MONOMER.
ECOL168927:B2827-MONOMER.
MetaCyc:THYMIDYLATESYN-MONOMER.

Gene expression databases

GenevestigatorP0A884.

Family and domain databases

HAMAPMF_00008. Thymidy_synth_bact.
[Tree]
InterProIPR000398. Thymidylate_synthase.
IPR020940. Thymidylate_synthase_AS.
[Graphical view]
Gene3DG3DSA:3.30.572.10. Thymidylat_synth_C. 1 hit.
PANTHERPTHR11549:SF2. Thymidylat_synth_C. 1 hit.
PfamPF00303. Thymidylat_synt. 1 hit.
[Graphical view]
PRINTSPR00108. THYMDSNTHASE.
SUPFAMSSF55831. Thymidylat_synth_C. 1 hit.
TIGRFAMsTIGR03284. thym_sym. 1 hit.
PROSITEPS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

BindingDBP0A884.
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Entry informationHide

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: June 15, 2010
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)
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Relevant documentsHide

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents