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Protein

Thymidylate synthase

Gene

thyA

Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
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 sitei22dUMPUniRule annotation1
Active sitei197NucleophileUniRule annotation1
Binding sitei2205,10-methylenetetrahydrofolateUniRule annotation1
Binding sitei228dUMPUniRule annotation1
Binding sitei3145,10-methylenetetrahydrofolate; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi177 – 178dUMP; shared with dimeric partnerUniRule annotation2
Nucleotide bindingi217 – 220dUMPUniRule annotation4
Nucleotide bindingi258 – 260dUMPUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Enzyme and pathway databases

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:EF_1576
OrganismiEnterococcus faecalis (strain ATCC 700802 / V583)
Taxonomic identifieri226185 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus
Proteomesi
  • UP000001415 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1795144.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001409571 – 315Thymidylate synthaseAdd BLAST315

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi226185.EF1576.

Chemistry databases

BindingDBiQ834R3.

Structurei

Secondary structure

1315
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 15Combined sources14
Beta strandi17 – 20Combined sources4
Beta strandi26 – 38Combined sources13
Helixi39 – 41Combined sources3
Beta strandi47 – 49Combined sources3
Helixi53 – 64Combined sources12
Helixi71 – 75Combined sources5
Helixi83 – 91Combined sources9
Beta strandi92 – 94Combined sources3
Helixi103 – 109Combined sources7
Helixi111 – 115Combined sources5
Helixi120 – 130Combined sources11
Helixi132 – 138Combined sources7
Helixi145 – 150Combined sources6
Helixi162 – 172Combined sources11
Beta strandi180 – 182Combined sources3
Turni186 – 188Combined sources3
Helixi189 – 191Combined sources3
Beta strandi192 – 194Combined sources3
Beta strandi197 – 206Combined sources10
Beta strandi209 – 220Combined sources12
Turni221 – 223Combined sources3
Helixi224 – 242Combined sources19
Beta strandi246 – 260Combined sources15
Helixi261 – 263Combined sources3
Helixi264 – 271Combined sources8
Beta strandi280 – 283Combined sources4
Helixi290 – 292Combined sources3
Helixi295 – 297Combined sources3
Beta strandi298 – 302Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UWLX-ray2.07A/B/C/D1-315[»]
4O7UX-ray2.40A/B/C/D1-315[»]
5J7WX-ray2.50A/B/C/D1-315[»]
ProteinModelPortaliQ834R3.
SMRiQ834R3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

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

Family and domain databases

CDDicd00351. TS_Pyrimidine_HMase. 1 hit.
Gene3Di3.30.572.10. 2 hits.
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. 1 hit.
PROSITEiPS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q834R3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEAYLALGK KILEEGHFKE DRTGTGTYSL FGYQMRFDLA KGFPLLTTKR
60 70 80 90 100
VPFGLIKSEL LWFLKGDTNI RYLLERNNHI WDEWAFERYV KSADYQGPDM
110 120 130 140 150
TDFGHRVLQD PAFAEQYKEE HQKFCDAILN DAEFAEKYGE LGNIYGAQWR
160 170 180 190 200
HWETKDGSFI DQLANVIEMI KTNPDSRRLI VSAWNPEDVP SMALPPCHTM
210 220 230 240 250
FQFYVNEGKL SCQLYQRSAD VFLGVPFNIA SYALLTHLIA HETGLEVGEF
260 270 280 290 300
VHTLGDAHLY QNHVEQMQEQ LSREVRSFPT LVLNPDKASV FDFDMEDIKV
310
EGYDPHPTIK APIAV
Length:315
Mass (Da):36,344
Last modified:June 1, 2003 - v1
Checksum:i0593A11D77D2D0A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016830 Genomic DNA. Translation: AAO81363.1.
RefSeqiNP_815293.1. NC_004668.1.
WP_002357569.1. NZ_KE136528.1.

Genome annotation databases

EnsemblBacteriaiAAO81363; AAO81363; EF_1576.
GeneIDi1200476.
KEGGiefa:EF1576.
PATRICi21853508. VBIEntFae7065_1480.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016830 Genomic DNA. Translation: AAO81363.1.
RefSeqiNP_815293.1. NC_004668.1.
WP_002357569.1. NZ_KE136528.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UWLX-ray2.07A/B/C/D1-315[»]
4O7UX-ray2.40A/B/C/D1-315[»]
5J7WX-ray2.50A/B/C/D1-315[»]
ProteinModelPortaliQ834R3.
SMRiQ834R3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226185.EF1576.

Chemistry databases

BindingDBiQ834R3.
ChEMBLiCHEMBL1795144.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO81363; AAO81363; EF_1576.
GeneIDi1200476.
KEGGiefa:EF1576.
PATRICi21853508. VBIEntFae7065_1480.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00575.

Family and domain databases

CDDicd00351. TS_Pyrimidine_HMase. 1 hit.
Gene3Di3.30.572.10. 2 hits.
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. 1 hit.
PROSITEiPS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTYSY_ENTFA
AccessioniPrimary (citable) accession number: Q834R3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: June 1, 2003
Last modified: November 30, 2016
This is version 93 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, Reference 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.