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Protein

Thymidylate synthase

Gene

thyA

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.UniRule annotation

Catalytic activityi

5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.UniRule annotation

Pathwayi: dTTP biosynthesis

This protein is involved in the pathway dTTP biosynthesis, which is part of Pyrimidine metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway dTTP biosynthesis and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei21dUMPUniRule annotation1
Binding sitei515,10-methylenetetrahydrofolateUniRule annotation1
Active sitei146NucleophileUniRule annotation1
Binding sitei1695,10-methylenetetrahydrofolateUniRule annotation1
Binding sitei177dUMPUniRule annotation1
Binding sitei2635,10-methylenetetrahydrofolate; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi126 – 127dUMP; shared with dimeric partnerUniRule annotation2
Nucleotide bindingi166 – 169dUMPUniRule annotation4
Nucleotide bindingi207 – 209dUMPUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Enzyme and pathway databases

BioCyciECOO157:THYA-MONOMER.
UniPathwayiUPA00575.

Names & Taxonomyi

Protein namesi
Recommended name:
Thymidylate synthaseUniRule annotation (EC:2.1.1.45UniRule annotation)
Short name:
TSUniRule annotation
Short name:
TSaseUniRule annotation
Gene namesi
Name:thyAUniRule annotation
Ordered Locus Names:Z4144, ECs3684
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001409551 – 264Thymidylate synthaseAdd BLAST264

Post-translational modificationi

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

Keywords - PTMi

Formylation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi155864.Z4144.

Structurei

Secondary structure

1264
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 14Combined sources13
Beta strandi16 – 19Combined sources4
Beta strandi25 – 37Combined sources13
Helixi38 – 40Combined sources3
Beta strandi46 – 48Combined sources3
Helixi53 – 64Combined sources12
Helixi70 – 74Combined sources5
Turni79 – 83Combined sources5
Helixi94 – 100Combined sources7
Helixi111 – 121Combined sources11
Beta strandi129 – 131Combined sources3
Helixi135 – 140Combined sources6
Beta strandi141 – 143Combined sources3
Beta strandi146 – 155Combined sources10
Beta strandi158 – 169Combined sources12
Turni170 – 173Combined sources4
Helixi174 – 191Combined sources18
Beta strandi195 – 209Combined sources15
Helixi210 – 212Combined sources3
Helixi213 – 220Combined sources8
Beta strandi229 – 232Combined sources4
Helixi244 – 246Combined sources3
Beta strandi247 – 251Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4LRRX-ray2.41A1-264[»]
ProteinModelPortaliP0A886.
SMRiP0A886.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C0V. Bacteria.
COG0207. LUCA.
HOGENOMiHOG000257900.
KOiK00560.
OMAiIVYELLW.

Family and domain databases

CDDicd00351. TS_Pyrimidine_HMase. 1 hit.
Gene3Di3.30.572.10. 1 hit.
HAMAPiMF_00008. Thymidy_synth_bact. 1 hit.
InterProiIPR023451. Thymidate_synth/dCMP_Mease.
IPR000398. Thymidylate_synthase.
IPR020940. Thymidylate_synthase_AS.
[Graphical view]
PfamiPF00303. Thymidylat_synt. 1 hit.
[Graphical view]
PRINTSiPR00108. THYMDSNTHASE.
SUPFAMiSSF55831. SSF55831. 1 hit.
TIGRFAMsiTIGR03284. thym_sym. 2 hits.
PROSITEiPS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A886-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQYLELMQK VLDEGTQKND RTGTGTLSIF GHQMRFNLQD GFPLVTTKRC
60 70 80 90 100
HLRSIIHELL WFLQGDTNIA YLHENNVTIW DEWADENGDL GPVYGKQWRA
110 120 130 140 150
WPTPDGRHID QITTVLNQLK NDPDSRRIIV SAWNVGELDK MALAPCHAFF
160 170 180 190 200
QFYVADGKLS CQLYQRSCDV FLGLPFNIAS YALLVHMMAQ QCDLEVGDFV
210 220 230 240 250
WTGGDTHLYS NHMDQTHLQL SREPRPLPKL IIKRKPESIF DYRFEDFEIE
260
GYDPHPGIKA PVAI
Length:264
Mass (Da):30,480
Last modified:July 21, 1986 - v1
Checksum:i0E6D88ED98D24D22
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG57938.1.
BA000007 Genomic DNA. Translation: BAB37107.1.
PIRiD91089.
F85934.
RefSeqiNP_311711.1. NC_002695.1.
WP_000816232.1. NZ_LPWC02000002.1.

Genome annotation databases

EnsemblBacteriaiAAG57938; AAG57938; Z4144.
BAB37107; BAB37107; BAB37107.
GeneIDi916501.
KEGGiece:Z4144.
ecs:ECs3684.
PATRICi18356857. VBIEscCol44059_3608.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG57938.1.
BA000007 Genomic DNA. Translation: BAB37107.1.
PIRiD91089.
F85934.
RefSeqiNP_311711.1. NC_002695.1.
WP_000816232.1. NZ_LPWC02000002.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4LRRX-ray2.41A1-264[»]
ProteinModelPortaliP0A886.
SMRiP0A886.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi155864.Z4144.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG57938; AAG57938; Z4144.
BAB37107; BAB37107; BAB37107.
GeneIDi916501.
KEGGiece:Z4144.
ecs:ECs3684.
PATRICi18356857. VBIEscCol44059_3608.

Phylogenomic databases

eggNOGiENOG4105C0V. Bacteria.
COG0207. LUCA.
HOGENOMiHOG000257900.
KOiK00560.
OMAiIVYELLW.

Enzyme and pathway databases

UniPathwayiUPA00575.
BioCyciECOO157:THYA-MONOMER.

Family and domain databases

CDDicd00351. TS_Pyrimidine_HMase. 1 hit.
Gene3Di3.30.572.10. 1 hit.
HAMAPiMF_00008. Thymidy_synth_bact. 1 hit.
InterProiIPR023451. Thymidate_synth/dCMP_Mease.
IPR000398. Thymidylate_synthase.
IPR020940. Thymidylate_synthase_AS.
[Graphical view]
PfamiPF00303. Thymidylat_synt. 1 hit.
[Graphical view]
PRINTSiPR00108. THYMDSNTHASE.
SUPFAMiSSF55831. SSF55831. 1 hit.
TIGRFAMsiTIGR03284. thym_sym. 2 hits.
PROSITEiPS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTYSY_ECO57
AccessioniPrimary (citable) accession number: P0A886
Secondary accession number(s): P00470
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 30, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.