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Q07422 (DRTS_TOXGO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional dihydrofolate reductase-thymidylate synthase

Short name=DHFR-TS

Including the following 2 domains:

  1. Dihydrofolate reductase
    EC=1.5.1.3
  2. Thymidylate synthase
    EC=2.1.1.45
OrganismToxoplasma gondii
Taxonomic identifier5811 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaConoidasidaCoccidiaEucoccidioridaEimeriorinaSarcocystidaeToxoplasma

Protein attributes

Sequence length610 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP By similarity. HAMAP-Rule MF_00008

Catalytic activity

5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH. HAMAP-Rule MF_00008

5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP. HAMAP-Rule MF_00008

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. HAMAP-Rule MF_00008

Sequence similarities

In the N-terminal section; belongs to the dihydrofolate reductase family.

In the C-terminal section; belongs to the thymidylate synthase family.

Contains 1 DHFR (dihydrofolate reductase) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 610610Bifunctional dihydrofolate reductase-thymidylate synthase HAMAP-Rule MF_00008
PRO_0000186352

Regions

Domain4 – 250247DHFR
Nucleotide binding16 – 227NADP By similarity
Nucleotide binding81 – 833NADP By similarity
Nucleotide binding102 – 1054NADP By similarity
Nucleotide binding152 – 1598NADP By similarity
Nucleotide binding509 – 5135dUMP By similarity
Nucleotide binding551 – 5533dUMP By similarity
Region322 – 610289Thymidylate synthase HAMAP-Rule MF_00008

Sites

Active site4891 By similarity
Binding site81Substrate; via carbonyl oxygen By similarity
Binding site101NADP; via amide nitrogen and carbonyl oxygen By similarity
Binding site311Substrate By similarity
Binding site1571Substrate By similarity
Binding site1721Substrate By similarity
Binding site3441dUMP By similarity
Binding site4901dUMP By similarity
Binding site5211dUMP By similarity

Secondary structure

....................................................................................... 610
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q07422 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: CFAF564416D04A29

FASTA61068,752
        10         20         30         40         50         60 
MQKPVCLVVA MTPKRGIGIN NGLPWPHLTT DFKHFSRVTK TTPEEASRLN GWLPRKFAKT 

        70         80         90        100        110        120 
GDSGLPSPSV GKRFNAVVMG RKTWESMPRK FRPLVDRLNI VVSSSLKEED IAAEKPQAEG 

       130        140        150        160        170        180 
QQRVRVCASL PAALSLLEEE YKDSVDQIFV VGGAGLYEAA LSLGVASHLY ITRVAREFPC 

       190        200        210        220        230        240 
DVFFPAFPGD DILSNKSTAA QAAAPAESVF VPFCPELGRE KDNEATYRPI FISKTFSDNG 

       250        260        270        280        290        300 
VPYDFVVLEK RRKTDDAATA EPSNAMSSLT STRETTPVHG LQAPSSAAAI APVLAWMDEE 

       310        320        330        340        350        360 
DRKKREQKEL IRAVPHVHFR GHEEFQYLDL IADIINNGRT MDDRTGVGVI SKFGCTMRYS 

       370        380        390        400        410        420 
LDQAFPLLTT KRVFWKGVLE ELLWFIRGDT NANHLSEKGV KIWDKNVTRE FLDSRNLPHR 

       430        440        450        460        470        480 
EVGDIGPGYG FQWRHFGAAY KDMHTDYTGQ GVDQLKNVIQ MLRTNPTDRR MLMTAWNPAA 

       490        500        510        520        530        540 
LDEMALPPCH LLCQFYVNDQ KELSCIMYQR SCDVGLGVPF NIASYSLLTL MVAHVCNLKP 

       550        560        570        580        590        600 
KEFIHFMGNT HVYTNHVEAL KEQLRREPRP FPIVNILNKE RIKEIDDFTA EDFEVVGYVP 

       610 
HGRIQMEMAV 

« Hide

References

[1]"Primary structure of the dihydrofolate reductase-thymidylate synthase gene from Toxoplasma gondii."
Roos D.S.
J. Biol. Chem. 268:6269-6280(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: RH.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L08489 Genomic DNA. Translation: AAB00163.1.
PIRA46005.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4ECKX-ray3.52A/B1-610[»]
4EILX-ray2.20A/B/C/D/E/F/G/H1-610[»]
ProteinModelPortalQ07422.
SMRQ07422. Positions 322-610.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ07422.
ChEMBLCHEMBL2425.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

OMALTCMIAQ.

Enzyme and pathway databases

UniPathwayUPA00077; UER00158.

Family and domain databases

Gene3D3.30.572.10. 1 hit.
3.40.430.10. 2 hits.
HAMAPMF_00008. Thymidy_synth_bact.
InterProIPR024072. DHFR-like_dom.
IPR012262. DHFR-TS.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
IPR023451. Thymidate_synth/dCMP_Mease.
IPR000398. Thymidylate_synthase.
IPR020940. Thymidylate_synthase_AS.
[Graphical view]
PfamPF00186. DHFR_1. 1 hit.
PF00303. Thymidylat_synt. 1 hit.
[Graphical view]
PIRSFPIRSF000389. DHFR-TS. 1 hit.
PRINTSPR00108. THYMDSNTHASE.
SUPFAMSSF53597. SSF53597. 2 hits.
SSF55831. SSF55831. 1 hit.
TIGRFAMsTIGR03284. thym_sym. 1 hit.
PROSITEPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
PS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDRTS_TOXGO
AccessionPrimary (citable) accession number: Q07422
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 14, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways