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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

Provides the sole de novo source of dTMP for DNA biosynthesis.UniRule annotation

Catalytic activityi

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

Pathway: 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei197 – 1971UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Enzyme and pathway databases

BioCyciEFAE226185:GHI1-1562-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:EF_1576
OrganismiEnterococcus faecalis (strain ATCC 700802 / V583)
Taxonomic identifieri226185 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus
ProteomesiUP000001415 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 315315Thymidylate synthasePRO_0000140957Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi226185.EF1576.

Structurei

Secondary structure

1
315
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1514Combined sources
Beta strandi17 – 204Combined sources
Beta strandi26 – 3813Combined sources
Helixi39 – 413Combined sources
Beta strandi47 – 493Combined sources
Helixi53 – 6412Combined sources
Helixi71 – 755Combined sources
Helixi83 – 919Combined sources
Beta strandi92 – 943Combined sources
Helixi103 – 1097Combined sources
Helixi111 – 1155Combined sources
Helixi120 – 13011Combined sources
Helixi132 – 1387Combined sources
Helixi145 – 1506Combined sources
Helixi162 – 17211Combined sources
Beta strandi180 – 1823Combined sources
Turni186 – 1883Combined sources
Helixi189 – 1913Combined sources
Beta strandi192 – 1943Combined sources
Beta strandi197 – 20610Combined sources
Beta strandi209 – 22012Combined sources
Turni221 – 2233Combined sources
Helixi224 – 24219Combined sources
Beta strandi246 – 26015Combined sources
Helixi261 – 2633Combined sources
Helixi264 – 2718Combined sources
Beta strandi280 – 2834Combined sources
Helixi290 – 2923Combined sources
Helixi295 – 2973Combined sources
Beta strandi298 – 3025Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UWLX-ray2.07A/B/C/D1-315[»]
4O7UX-ray2.40A/B/C/D1-315[»]
ProteinModelPortaliQ834R3.
SMRiQ834R3. Positions 1-315.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0207.
KOiK00560.
OMAiNEWADEN.
OrthoDBiEOG6K6V53.

Family and domain databases

Gene3Di3.30.572.10. 2 hits.
HAMAPiMF_00008. Thymidy_synth_bact.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
3UWLX-ray2.07A/B/C/D1-315[»]
4O7UX-ray2.40A/B/C/D1-315[»]
ProteinModelPortaliQ834R3.
SMRiQ834R3. Positions 1-315.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226185.EF1576.

Chemistry

BindingDBiQ834R3.
ChEMBLiCHEMBL1795144.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG0207.
KOiK00560.
OMAiNEWADEN.
OrthoDBiEOG6K6V53.

Enzyme and pathway databases

UniPathwayiUPA00575.
BioCyciEFAE226185:GHI1-1562-MONOMER.

Miscellaneous databases

PROiQ834R3.

Family and domain databases

Gene3Di3.30.572.10. 2 hits.
HAMAPiMF_00008. Thymidy_synth_bact.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700802 / V583.

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: June 24, 2015
This is version 85 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

External Data

Dasty 3

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 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.