Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q07422 (DRTS_TOXGO)

Last modified November 4, 2008. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Bifunctional dihydrofolate reductase-thymidylate synthase
      Short name=DHFR-TS
Including the following 2 domains:
    1- Recommended name:
            Dihydrofolate reductase
              EC=1.5.1.3
    2- Recommended name:
            Thymidylate synthase
              EC=2.1.1.45
OrganismToxoplasma gondii
Taxonomic identifier5811 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaCoccidiaEucoccidioridaEimeriorinaSarcocystidaeToxoplasma

Protein attributes

Sequence length610 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH.

5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; tetrahydrofolate from dihydrofolate: step 1/1.

Miscellaneous

The reaction catalyzed by this enzyme represents an essential step for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP.

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.

Ontologies

Keywords

   Biological processNucleotide biosynthesis
One-carbon metabolism
   LigandNADP
   Molecular functionMethyltransferase
Oxidoreductase
Transferase
   Technical termMultifunctional enzyme

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 610610Bifunctional dihydrofolate reductase-thymidylate synthase
PRO_0000186352

Regions

Domain4 – 250247DHFR
Region322 – 610289Thymidylate synthase

Sites

Active site4891 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q07422-1 [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: 8454599] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: RH.

Cross-references

Sequence databases

L08489 Genomic DNA. Translation: AAB00163.1.
PIRA46005.

3D structure databases

HSSPHSSP built from PDB template 1HW3 based on UniProtKB P04818.
ModBaseSearch...

Family and domain databases

InterProIPR012262. DHFR-TS.
IPR001796. DHFR_reg.
IPR000398. Thymidylat_synth_C.
[Graphical view]
Gene3DG3DSA:3.30.572.10. Thymidylat_synth_C. 1 hit.
PANTHERPTHR11549:SF2. Thymidylat_synth_C. 1 hit.
PfamPF00186. DHFR_1. 1 hit.
PF00303. Thymidylat_synt. 1 hit.
[Graphical view]
PIRSFPIRSF000389. DHFR-TS. 1 hit.
PRINTSPR00070. DHFR.
PR00108. THYMDSNTHASE.
ProDomPD001180. Thymidylat_synth. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR03284. thym_sym. 1 hit.
PROSITEPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
PS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]
BLOCKSSearch...
ProtoNetSearch...

Other Resources

BindingDBQ07422.

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: November 4, 2008
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents