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Q9WYT0 (THYX_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Thymidylate synthase ThyX
Short name=TS
Short name=TSase
EC=2.1.1.148
Gene names
Name:thyX
Synonyms:thy1
Ordered Locus Names:TM_0449
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga ›

Protein attributes

Sequence length220 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of dTMP and tetrahydrofolate from dUMP and methylenetetrahydrofolate. HAMAP-Rule MF_01408

Catalytic activity

5,10-methylenetetrahydrofolate + dUMP + NADPH = dTMP + tetrahydrofolate + NADP+. HAMAP-Rule MF_01408

Cofactor

Binds 1 FAD per subunit.

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the thymidylate synthase ThyX family.

Contains 1 thyX (flavin-dependent thymidylate synthase) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 220220Thymidylate synthase ThyX HAMAP-Rule MF_01408
PRO_0000175579

Regions

Domain1 – 208208ThyX
Motif78 – 8811ThyX motif HAMAP-Rule MF_01408

Secondary structure

1 ................................... 220
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9WYT0 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: E3B9712014185907

FASTA22026,004
        10         20         30         40         50         60 
MKIDILDKGF VELVDVMGND LSAVRAARVS FDMGLKDEER DRHLIEYLMK HGHETPFEHI 

        70         80         90        100        110        120 
VFTFHVKAPI FVARQWFRHR IASYNELSGR YSKLSYEFYI PSPERLEGYK TTIPPERVTE 

       130        140        150        160        170        180 
KISEIVDKAY RTYLELIESG VPREVARIVL PLNLYTRFFW TVNARSLMNF LNLRADSHAQ 

       190        200        210        220 
WEIQQYALAI ARIFKEKCPW TFEAFLKYAY KGDILKEVQV

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"Crystal structure of thy1, a thymidylate synthase complementing protein from Thermotoga maritima at 2.25 A resolution."
Kuhn P., Lesley S.A., Mathews I.I., Canaves J.M., Brinen L.S., Dai X., Deacon A.M., Elsliger M.-A., Eshaghi S., Floyd R., Godzik A., Grittini C., Grzechnik S.K., Guda C., Hodgson K.O., Jaroszewski L., Karlak C., Klock H.E. expand/collapse author list , Koesema E., Kovarik J.M., Kreusch A.T., McMullan D., McPhillips T.M., Miller M.A., Miller M., Morse A., Moy K., Ouyang J., Robb A., Rodrigues K., Selby T.L., Spraggon G., Stevens R.C., Taylor S.S., van den Bedem H., Velasquez J., Vincent J., Wang X., West B., Wolf G., Wooley J., Wilson I.A.
Proteins 49:142-145(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000512 Genomic DNA. Translation: AAD35532.1.
PIRB72375.
RefSeqNP_228259.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ9WYT0.
SMRQ9WYT0. Positions 1-220.
ModBaseSearch...

Protein-protein interaction databases

STRING243274.TM0449.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD35532; AAD35532; TM_0449.
GeneID897468.
KEGGtma:TM0449.
PATRIC23935783. VBITheMar51294_0455.

Phylogenomic databases

eggNOGCOG1351.
KOK03465.
OMADHGFIRV.
ProtClustDBPRK00847.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15758.
BRENDA2.1.1.148. 6331.
SABIO-RKQ9WYT0.

Family and domain databases

HAMAPMF_01408. ThyX.
InterProIPR003669. Thymidylate_synthase_ThyX.
[Graphical view]
PfamPF02511. Thy1. 1 hit.
[Graphical view]
SUPFAMSSF69796. Thy1. 1 hit.
TIGRFAMsTIGR02170. thyX. 1 hit.
PROSITEPS51331. THYX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9WYT0.

Entry information

Entry nameTHYX_THEMA
AccessionPrimary (citable) accession number: Q9WYT0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: November 1, 1999
Last modified: May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents