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Protein

Flavin-dependent thymidylate synthase

Gene

thyX

Organism
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Status
Reviewed-Annotation score: Annotation score: 5 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 NAD(P)H and FADH2 as the reductant.1 Publication

Catalytic activityi

5,10-methylenetetrahydrofolate + dUMP + NADPH = dTMP + tetrahydrofolate + NADP+.1 Publication

Cofactori

FAD1 Publication1 PublicationNote: Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers.1 Publication

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 sitei50FAD; shared with neighboring subunitsCombined sources1 Publication1
Binding sitei147dUMP1 Publication1
Binding sitei169FADCombined sources1 Publication1
Active sitei174Involved in ionization of N3 of dUMP, leading to its activationUniRule annotation1
Binding sitei174dUMP; shared with dimeric partnerCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi71 – 74dUMP; shared with dimeric partnerCombined sources1 Publication4
Nucleotide bindingi74 – 76FADCombined sources1 Publication3
Nucleotide bindingi84 – 86dUMPCombined sources1 Publication3
Nucleotide bindingi163 – 165FAD; shared with neighboring subunitsCombined sources1 Publication3

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

BioCyciMetaCyc:MONOMER-15768.
UniPathwayiUPA00575.

Names & Taxonomyi

Protein namesi
Recommended name:
Flavin-dependent thymidylate synthase1 Publication (EC:2.1.1.1481 Publication)
Short name:
FDTSUniRule annotation
Alternative name(s):
FAD-dependent thymidylate synthaseUniRule annotation
Thymidylate synthase ThyX1 Publication
Short name:
TSUniRule annotation
Short name:
TSaseUniRule annotation
Gene namesi
Name:thyX1 Publication
Ordered Locus Names:HP_1533
OrganismiHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Taxonomic identifieri85962 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
Proteomesi
  • UP000000429 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi84S → A: Abolishes complementation when expressed in an E.coli thyA deletion mutant. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001755661 – 208Flavin-dependent thymidylate synthaseAdd BLAST208

Proteomic databases

PaxDbiO26061.
PRIDEiO26061.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

IntActiO26061. 12 interactors.
MINTiMINT-160429.
STRINGi85962.HP1533.

Structurei

Secondary structure

1208
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 8Combined sources7
Helixi12 – 22Combined sources11
Helixi25 – 27Combined sources3
Beta strandi30 – 32Combined sources3
Helixi33 – 43Combined sources11
Helixi46 – 54Combined sources9
Beta strandi56 – 65Combined sources10
Helixi66 – 72Combined sources7
Beta strandi77 – 82Combined sources6
Helixi85 – 88Combined sources4
Helixi89 – 92Combined sources4
Helixi103 – 109Combined sources7
Turni110 – 112Combined sources3
Helixi119 – 137Combined sources19
Helixi143 – 146Combined sources4
Helixi147 – 149Combined sources3
Beta strandi154 – 163Combined sources10
Helixi164 – 174Combined sources11
Helixi181 – 193Combined sources13
Turni196 – 198Combined sources3
Helixi199 – 201Combined sources3
Helixi203 – 205Combined sources3
Turni206 – 208Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AH5X-ray2.50A/B/C/D/E/F1-208[»]
ProteinModelPortaliO26061.
SMRiO26061.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO26061.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 208ThyXUniRule annotationAdd BLAST208

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi74 – 84ThyX motif1 PublicationAdd BLAST11

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG41087GE. Bacteria.
COG1351. LUCA.
KOiK03465.
OMAiCWQSFDK.

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.

O26061-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVICKHYTP LDIASQAIRT CWQSFEYSDD GGCKDKELIH RVGNIFRHSS
60 70 80 90 100
TLEHLYYNFE IKGLSRGALQ ELSRHRIASL SVKSSRYTLR ELKEVESFLP
110 120 130 140 150
LNETNLERAK EFLVFVDNEK VNAMSVLALE NLRILLSEHN IKNDLAKYAM
160 170 180 190 200
PESYKTHLAY SINARSLQNF LTLRSSNKAL KEMQDLAKAL FDALPGEHQY

LFEDCLKH
Length:208
Mass (Da):24,071
Last modified:July 11, 2001 - v2
Checksum:i88FF23ED4B26283C
GO

Sequence cautioni

The sequence AAD08571 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000511 Genomic DNA. Translation: AAD08571.1. Different initiation.
PIRiE64711.
RefSeqiNP_208323.1. NC_000915.1.
WP_000451918.1. NC_018939.1.

Genome annotation databases

EnsemblBacteriaiAAD08571; AAD08571; HP_1533.
GeneIDi899757.
KEGGiheo:C694_07940.
hpy:HP1533.
PATRICi20594487. VBIHelPyl33062_1611.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000511 Genomic DNA. Translation: AAD08571.1. Different initiation.
PIRiE64711.
RefSeqiNP_208323.1. NC_000915.1.
WP_000451918.1. NC_018939.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AH5X-ray2.50A/B/C/D/E/F1-208[»]
ProteinModelPortaliO26061.
SMRiO26061.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO26061. 12 interactors.
MINTiMINT-160429.
STRINGi85962.HP1533.

Proteomic databases

PaxDbiO26061.
PRIDEiO26061.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD08571; AAD08571; HP_1533.
GeneIDi899757.
KEGGiheo:C694_07940.
hpy:HP1533.
PATRICi20594487. VBIHelPyl33062_1611.

Phylogenomic databases

eggNOGiENOG41087GE. Bacteria.
COG1351. LUCA.
KOiK03465.
OMAiCWQSFDK.

Enzyme and pathway databases

UniPathwayiUPA00575.
BioCyciMetaCyc:MONOMER-15768.

Miscellaneous databases

EvolutionaryTraceiO26061.

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_HELPY
AccessioniPrimary (citable) accession number: O26061
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: July 11, 2001
Last modified: November 30, 2016
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

ThyX activity is mechanistically distinct from ThyA activity.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Helicobacter pylori
    Helicobacter pylori (strain 26695): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.