Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Thymidylate synthase

Gene

thyA

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
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 sitei26dUMPUniRule annotation1
Active sitei201NucleophileUniRule annotation1
Binding sitei2245,10-methylenetetrahydrofolateUniRule annotation1
Binding sitei232dUMPUniRule annotation1
Binding sitei3175,10-methylenetetrahydrofolate; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi181 – 182dUMP; shared with dimeric partnerUniRule annotation2
Nucleotide bindingi221 – 224dUMPUniRule annotation4
Nucleotide bindingi262 – 264dUMPUniRule 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:SAV1427
OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
Taxonomic identifieri158878 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000002481 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_00001410181 – 318Thymidylate synthaseAdd BLAST318

Proteomic databases

PaxDbiP67046.
PRIDEiP67046.

2D gel databases

World-2DPAGE0002:P67046.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi158878.SAV1427.

Structurei

Secondary structure

1318
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 19Combined sources16
Beta strandi21 – 23Combined sources3
Beta strandi31 – 42Combined sources12
Helixi43 – 45Combined sources3
Beta strandi51 – 53Combined sources3
Helixi57 – 69Combined sources13
Helixi74 – 78Combined sources5
Turni79 – 81Combined sources3
Helixi86 – 93Combined sources8
Helixi109 – 113Combined sources5
Helixi117 – 134Combined sources18
Helixi136 – 142Combined sources7
Helixi149 – 154Combined sources6
Helixi166 – 176Combined sources11
Beta strandi184 – 186Combined sources3
Helixi190 – 192Combined sources3
Turni193 – 195Combined sources3
Beta strandi196 – 198Combined sources3
Beta strandi201 – 210Combined sources10
Beta strandi213 – 224Combined sources12
Turni225 – 227Combined sources3
Helixi228 – 246Combined sources19
Beta strandi250 – 264Combined sources15
Helixi268 – 276Combined sources9
Beta strandi284 – 287Combined sources4
Helixi293 – 295Combined sources3
Helixi298 – 300Combined sources3
Beta strandi301 – 305Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DQ1X-ray2.71A/B1-318[»]
ProteinModelPortaliP67046.
SMRiP67046.
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.
PhylomeDBiP67046.

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.

P67046-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLNSFDAAYH SLCEEVLEIG NTRNDRTNTG TISKFGHQLR FDLSKGFPLL
60 70 80 90 100
TTKKVSFKLV ATELLWFIKG DTNIQYLLKY NNNIWNEWAF ENYIKSDEYN
110 120 130 140 150
GPDMTDFGHR ALSDPEFNEQ YKEQMKQFKQ RILEDDTFAK QFGDLGNVYG
160 170 180 190 200
KQWRDWVDKD GNHFDQLKTV IEQIKHNPDS RRHIVSAWNP TEIDTMALPP
210 220 230 240 250
CHTMFQFYVQ DGKLSCQLYQ RSADIFLGVP FNIASYALLT HLIAKECGLE
260 270 280 290 300
VGEFVHTFGD AHIYSNHIDA IQTQLARESF NPPTLKINSD KSIFDINYED
310
LEIVDYESHP AIKAPIAV
Length:318
Mass (Da):36,825
Last modified:October 11, 2004 - v1
Checksum:iE7F41BA915C25D37
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB57589.1.
RefSeqiWP_000934894.1. NC_002758.2.

Genome annotation databases

EnsemblBacteriaiBAB57589; BAB57589; SAV1427.
KEGGisav:SAV1427.
PATRICi19563578. VBIStaAur52173_1466.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB57589.1.
RefSeqiWP_000934894.1. NC_002758.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DQ1X-ray2.71A/B1-318[»]
ProteinModelPortaliP67046.
SMRiP67046.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi158878.SAV1427.

2D gel databases

World-2DPAGE0002:P67046.

Proteomic databases

PaxDbiP67046.
PRIDEiP67046.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB57589; BAB57589; SAV1427.
KEGGisav:SAV1427.
PATRICi19563578. VBIStaAur52173_1466.

Phylogenomic databases

eggNOGiENOG4105C0V. Bacteria.
COG0207. LUCA.
KOiK00560.
OMAiIVYELLW.
PhylomeDBiP67046.

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_STAAM
AccessioniPrimary (citable) accession number: P67046
Secondary accession number(s): Q99U61
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: November 30, 2016
This is version 80 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.