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Protein

Thymidylate synthase ThyX

Gene

thyX

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the formation of dTMP and tetrahydrofolate from dUMP and methylenetetrahydrofolate.

Catalytic activityi

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

Cofactori

FADNote: Binds 1 FAD per subunit.

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-15758.
BRENDAi2.1.1.148. 2604.
SABIO-RKQ9WYT0.

Names & Taxonomyi

Protein namesi
Recommended name:
Thymidylate synthase ThyX (EC:2.1.1.148)
Short name:
TS
Short name:
TSase
Gene namesi
Name:thyX
Synonyms:thy1
Ordered Locus Names:TM_0449
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

Pathology & Biotechi

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 220220Thymidylate synthase ThyXPRO_0000175579Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

DIPiDIP-60076N.
STRINGi243274.TM0449.

Structurei

Secondary structure

1
220
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Turni6 – 83Combined sources
Beta strandi9 – 179Combined sources
Helixi20 – 289Combined sources
Helixi29 – 313Combined sources
Helixi39 – 5113Combined sources
Helixi55 – 595Combined sources
Beta strandi61 – 699Combined sources
Helixi70 – 767Combined sources
Beta strandi81 – 866Combined sources
Turni89 – 913Combined sources
Helixi103 – 1064Combined sources
Helixi115 – 13824Combined sources
Helixi143 – 1464Combined sources
Helixi147 – 1493Combined sources
Beta strandi154 – 16310Combined sources
Helixi164 – 17411Combined sources
Helixi181 – 19717Combined sources
Helixi199 – 20810Combined sources
Helixi214 – 2163Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KQ4X-ray2.25A/B/C/D1-220[»]
1O24X-ray2.00A/B/C/D1-220[»]
1O25X-ray2.40A/B/C/D1-220[»]
1O26X-ray1.60A/B/C/D1-220[»]
1O27X-ray2.30A/B/C/D1-220[»]
1O28X-ray2.10A/B/C/D1-220[»]
1O29X-ray2.00A/B/C/D1-220[»]
1O2AX-ray1.80A/B/C/D1-220[»]
1O2BX-ray2.45A/B/C/D1-220[»]
3G4AX-ray1.95A/B/C/D1-220[»]
3G4CX-ray2.05A/B/C/D1-220[»]
3N0BX-ray2.30A/B/C/D1-220[»]
3N0CX-ray2.30A/B/C/D1-220[»]
4GT9X-ray1.39A1-220[»]
4GTAX-ray1.50A1-220[»]
4GTBX-ray1.70A1-220[»]
4GTCX-ray1.97A/B/C/D1-220[»]
4GTDX-ray1.76A/B/C/D1-220[»]
4GTEX-ray1.89A/B/C/D1-220[»]
4GTFX-ray1.77A1-220[»]
4GTLX-ray2.17A/B/C/D1-220[»]
4KARX-ray2.03A/B/C/D1-220[»]
4KASX-ray1.85A/B/C/D1-220[»]
4KATX-ray2.14A/B/C/D1-220[»]
ProteinModelPortaliQ9WYT0.
SMRiQ9WYT0. Positions 1-220.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WYT0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 208208ThyXAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi78 – 8811ThyX motifAdd
BLAST

Sequence similaritiesi

Belongs to the thymidylate synthase ThyX family.Curated

Phylogenomic databases

eggNOGiENOG41087GE. Bacteria.
COG1351. LUCA.
InParanoidiQ9WYT0.
KOiK03465.
OMAiDAHAQYE.
OrthoDBiEOG661H77.

Family and domain databases

HAMAPiMF_01408. ThyX.
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.

Q9WYT0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIDILDKGF VELVDVMGND LSAVRAARVS FDMGLKDEER DRHLIEYLMK
60 70 80 90 100
HGHETPFEHI VFTFHVKAPI FVARQWFRHR IASYNELSGR YSKLSYEFYI
110 120 130 140 150
PSPERLEGYK TTIPPERVTE KISEIVDKAY RTYLELIESG VPREVARIVL
160 170 180 190 200
PLNLYTRFFW TVNARSLMNF LNLRADSHAQ WEIQQYALAI ARIFKEKCPW
210 220
TFEAFLKYAY KGDILKEVQV
Length:220
Mass (Da):26,004
Last modified:November 1, 1999 - v1
Checksum:iE3B9712014185907
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35532.1.
PIRiB72375.
RefSeqiNP_228259.1. NC_000853.1.
WP_004081517.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD35532; AAD35532; TM_0449.
GeneIDi897468.
KEGGitma:TM0449.
PATRICi23935783. VBITheMar51294_0455.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35532.1.
PIRiB72375.
RefSeqiNP_228259.1. NC_000853.1.
WP_004081517.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KQ4X-ray2.25A/B/C/D1-220[»]
1O24X-ray2.00A/B/C/D1-220[»]
1O25X-ray2.40A/B/C/D1-220[»]
1O26X-ray1.60A/B/C/D1-220[»]
1O27X-ray2.30A/B/C/D1-220[»]
1O28X-ray2.10A/B/C/D1-220[»]
1O29X-ray2.00A/B/C/D1-220[»]
1O2AX-ray1.80A/B/C/D1-220[»]
1O2BX-ray2.45A/B/C/D1-220[»]
3G4AX-ray1.95A/B/C/D1-220[»]
3G4CX-ray2.05A/B/C/D1-220[»]
3N0BX-ray2.30A/B/C/D1-220[»]
3N0CX-ray2.30A/B/C/D1-220[»]
4GT9X-ray1.39A1-220[»]
4GTAX-ray1.50A1-220[»]
4GTBX-ray1.70A1-220[»]
4GTCX-ray1.97A/B/C/D1-220[»]
4GTDX-ray1.76A/B/C/D1-220[»]
4GTEX-ray1.89A/B/C/D1-220[»]
4GTFX-ray1.77A1-220[»]
4GTLX-ray2.17A/B/C/D1-220[»]
4KARX-ray2.03A/B/C/D1-220[»]
4KASX-ray1.85A/B/C/D1-220[»]
4KATX-ray2.14A/B/C/D1-220[»]
ProteinModelPortaliQ9WYT0.
SMRiQ9WYT0. Positions 1-220.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60076N.
STRINGi243274.TM0449.

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD35532; AAD35532; TM_0449.
GeneIDi897468.
KEGGitma:TM0449.
PATRICi23935783. VBITheMar51294_0455.

Phylogenomic databases

eggNOGiENOG41087GE. Bacteria.
COG1351. LUCA.
InParanoidiQ9WYT0.
KOiK03465.
OMAiDAHAQYE.
OrthoDBiEOG661H77.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15758.
BRENDAi2.1.1.148. 2604.
SABIO-RKQ9WYT0.

Miscellaneous databases

EvolutionaryTraceiQ9WYT0.

Family and domain databases

HAMAPiMF_01408. ThyX.
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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).

Entry informationi

Entry nameiTHYX_THEMA
AccessioniPrimary (citable) accession number: Q9WYT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: November 1, 1999
Last modified: May 11, 2016
This is version 114 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.