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P0A886 (TYSY_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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:Z4144, ECs3684
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length264 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. 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 By similarity.

Subcellular location

Cytoplasm By similarity.

Post-translational modification

The N-terminal is probably N-(dihydroxymethyl)-methionine, the hydrated form of N-formylmethionine By similarity. HAMAP-Rule MF_00008

Sequence similarities

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

Ontologies

Keywords
   Biological processNucleotide biosynthesis
Translation regulation
   Cellular componentCytoplasm
   LigandRNA-binding
   Molecular functionMethyltransferase
Repressor
Transferase
   PTMFormylation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processdTMP biosynthetic process

Inferred from electronic annotation. Source: HAMAP

dTTP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

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 electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 264264Thymidylate synthase HAMAP-Rule MF_00008
PRO_0000140955

Sites

Active site1461 By similarity

Amino acid modifications

Modified residue11N-formylmethionine By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A886 [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

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG57938.1.
BA000007 Genomic DNA. Translation: BAB37107.1.
PIRD91089.
F85934.
RefSeqNP_289379.1. NC_002655.2.
NP_311711.1. NC_002695.1.

3D structure databases

ProteinModelPortalP0A886.
SMRP0A886. Positions 2-264.
ModBaseSearch...

Protein-protein interaction databases

STRING155864.Z4144.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG57938; AAG57938; Z4144.
BAB37107; BAB37107; BAB37107.
GeneID916501.
959426.
KEGGece:Z4144.
ecs:ECs3684.
PATRIC18356857. VBIEscCol44059_3608.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0207.
HOGENOMHOG000257900.
KOK00560.
OMADTNVAYL.
ProtClustDBPRK01827.

Enzyme and pathway databases

BioCycECOL386585:GJFA-3652-MONOMER.
UniPathwayUPA00575.

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

BindingDBP0A886.

Entry information

Entry nameTYSY_ECO57
AccessionPrimary (citable) accession number: P0A886
Secondary accession number(s): P00470
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families