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Protein

Flavin-dependent thymidylate synthase

Gene

thyX

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 NADPH and FADH2 as the reductant.UniRule annotation

Catalytic activityi

5,10-methylenetetrahydrofolate + dUMP + NADPH = dTMP + tetrahydrofolate + NADP+.UniRule annotation

Cofactori

FADUniRule annotationNote: Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers.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 sitei59FAD; shared with neighboring subunitsUniRule annotation1
Binding sitei90FAD; shared with neighboring subunitsUniRule annotation1
Binding sitei157dUMPUniRule annotation1
Binding sitei179FADUniRule annotation1
Active sitei184Involved in ionization of N3 of dUMP, leading to its activationUniRule annotation1
Binding sitei184dUMP; shared with dimeric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi79 – 82dUMP; shared with dimeric partnerUniRule annotation4
Nucleotide bindingi82 – 84FADUniRule annotation3
Nucleotide bindingi90 – 94dUMPUniRule annotation5
Nucleotide bindingi173 – 175FAD; shared with neighboring subunitsUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

UniPathwayiUPA00575.

Names & Taxonomyi

Protein namesi
Recommended name:
Flavin-dependent thymidylate synthaseUniRule annotation (EC:2.1.1.148UniRule annotation)
Short name:
FDTSUniRule annotation
Alternative name(s):
FAD-dependent thymidylate synthaseUniRule annotation
Thymidylate synthase ThyXUniRule annotation
Short name:
TSUniRule annotation
Short name:
TSaseUniRule annotation
Gene namesi
Name:thyXUniRule annotation
Ordered Locus Names:TTHA1096
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001755811 – 270Flavin-dependent thymidylate synthaseAdd BLAST270

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi300852.TTHA1096.

Structurei

3D structure databases

ProteinModelPortaliQ5SJB8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini13 – 218ThyXUniRule annotationAdd BLAST206

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi82 – 92ThyX motifUniRule annotationAdd BLAST11

Sequence similaritiesi

Belongs to the thymidylate synthase ThyX family.UniRule annotation
Contains 1 thyX (flavin-dependent thymidylate synthase) domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107R2U. Bacteria.
COG1351. LUCA.
HOGENOMiHOG000021807.
KOiK03465.
OMAiGMTKREW.
PhylomeDBiQ5SJB8.

Family and domain databases

HAMAPiMF_01408. ThyX. 1 hit.
InterProiIPR003669. Thymidylate_synthase_ThyX.
[Graphical view]
PfamiPF02511. Thy1. 1 hit.
[Graphical view]
SUPFAMiSSF69796. SSF69796. 1 hit.
TIGRFAMsiTIGR02170. thyX. 1 hit.
PROSITEiPS51331. THYX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5SJB8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGPLTIPVL DKGFVRLVDQ MGDDRAIVQA ARVSYGEGTK TVREDAALID
60 70 80 90 100
YLMRHRHTSP FEMVVFKFHV KAPIFVARQW FRHRTASVNE ISGRYSILKE
110 120 130 140 150
EFYEPEAFRK QAKRNKQASE GALLDEEALA LLRKVQQEAY GAYRALLEKG
160 170 180 190 200
VAREMARMVL PLNLYTEFYW KQDLHNLFHF LKLRLAPEAQ WEIRQYARAI
210 220 230 240 250
AEIVKERVPL AWAAFEEHLL EGAFLSRTEL RALRGLLTPE VYEKALSSLG
260 270
LGGSRLKEAL EKVFGPGEAL
Length:270
Mass (Da):31,006
Last modified:December 21, 2004 - v1
Checksum:i5FED30A827E39907
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70919.1.
RefSeqiWP_011228435.1. NC_006461.1.
YP_144362.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70919; BAD70919; BAD70919.
GeneIDi3168967.
KEGGittj:TTHA1096.
PATRICi23957152. VBITheThe93045_1076.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70919.1.
RefSeqiWP_011228435.1. NC_006461.1.
YP_144362.1. NC_006461.1.

3D structure databases

ProteinModelPortaliQ5SJB8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1096.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70919; BAD70919; BAD70919.
GeneIDi3168967.
KEGGittj:TTHA1096.
PATRICi23957152. VBITheThe93045_1076.

Phylogenomic databases

eggNOGiENOG4107R2U. Bacteria.
COG1351. LUCA.
HOGENOMiHOG000021807.
KOiK03465.
OMAiGMTKREW.
PhylomeDBiQ5SJB8.

Enzyme and pathway databases

UniPathwayiUPA00575.

Family and domain databases

HAMAPiMF_01408. ThyX. 1 hit.
InterProiIPR003669. Thymidylate_synthase_ThyX.
[Graphical view]
PfamiPF02511. Thy1. 1 hit.
[Graphical view]
SUPFAMiSSF69796. SSF69796. 1 hit.
TIGRFAMsiTIGR02170. thyX. 1 hit.
PROSITEiPS51331. THYX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTHYX_THET8
AccessioniPrimary (citable) accession number: Q5SJB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: December 21, 2004
Last modified: November 2, 2016
This is version 61 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.