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Q27828 (DRTS_PARTE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 79. 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:
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
Gene names
ORF Names:GSPATT00019973001
OrganismParamecium tetraurelia [Reference proteome]
Taxonomic identifier5888 [NCBI]
Taxonomic lineageEukaryota › Alveolata › Ciliophora › Intramacronucleata › Oligohymenophorea › Peniculida › Parameciidae › Paramecium

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

Catalytic activity

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

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

Pathway

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

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 – 462462Bifunctional dihydrofolate reductase-thymidylate synthase
PRO_0000186346

Regions

Domain6 – 165160DHFR
Nucleotide binding18 – 247NADP By similarity
Nucleotide binding49 – 513NADP By similarity
Nucleotide binding68 – 714NADP By similarity
Nucleotide binding102 – 1098NADP By similarity
Nucleotide binding364 – 3685dUMP By similarity
Nucleotide binding406 – 4083dUMP By similarity
Region180 – 462283Thymidylate synthase

Sites

Active site3451 By similarity
Binding site101Substrate; via carbonyl oxygen By similarity
Binding site121NADP; via amide nitrogen and carbonyl oxygen By similarity
Binding site321Substrate By similarity
Binding site1011Substrate; via carbonyl oxygen By similarity
Binding site1221Substrate By similarity
Binding site2001dUMP By similarity
Binding site3461dUMP By similarity
Binding site3761dUMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q27828 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C8C9B3A12BBD5C72

FASTA46253,201
        10         20         30         40         50         60 
MTTNKTFSMV LAMTLNGGIG YQNRLPWKLK EDLQRFKKIT TGGIVIMGRK TFESMNSKPL 

        70         80         90        100        110        120 
PNRVNVVISK NMKSSNEVQV FPRIEDALQF YNTSHQKLYL IGGKRIFEEG LATDKCSDVH 

       130        140        150        160        170        180 
LTRIGVETKC DVYLNKNIFS TFQVNKTSQT KSENGINYDY QHLINKNSHE QSYIDEEHQE 

       190        200        210        220        230        240 
NQYLDMITKI MKEGVSKDDR TGVGTMSIFG QTMRFNLAQS FPLLTTKKVF FRGVVEELLW 

       250        260        270        280        290        300 
FLRGNTNGKL LLDKGVKIWE GNGTREYLDT IGLQHRQEHD LGPVYGFQWR HFGAKYKDCQ 

       310        320        330        340        350        360 
TDYSNQGVDQ VKEIIQLLKN NPDSRRIILS AWNPIDLKQM ALPPCHVMSQ FFVANGKLSC 

       370        380        390        400        410        420 
MMYQRSCDFG LGIPFNIASY ALLTYMLAKE CNLNLGEFVH VLGDTHIYSN HVEALKKQIE 

       430        440        450        460 
RVPYPFPLLK IKGNKSLFDY TYEDFELVGY NAHDKIEMKM AV

« Hide

References

« Hide 'large scale' references
[1]"Cloning and molecular analysis of the bifunctional dihydrofolate reductase-thymidylate synthase gene in the ciliated protozoan Paramecium tetraurelia."
Schlichtherle I.M., van Houten J.L., Roos D.S.
Mol. Gen. Genet. 250:665-673(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Stock 51.
[2]"Global trends of whole-genome duplications revealed by the ciliate Paramecium tetraurelia."
Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M., Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A., Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R. expand/collapse author list , Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F., Le Mouel A., Lepere G., Malinsky S., Nowacki M., Nowak J.K., Plattner H., Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M., Weissenbach J., Scarpelli C., Schaechter V., Sperling L., Meyer E., Cohen J., Wincker P.
Nature 444:171-178(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Stock d4-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U03885 Genomic DNA. Translation: AAC47025.1.
CT868563 Genomic DNA. Translation: CAK86280.1.
PIRS65570.
RefSeqXP_001453677.1. XM_001453640.1.

3D structure databases

ProteinModelPortalQ27828.
SMRQ27828. Positions 138-462.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5039462.
KEGGptm:GSPATT00019973001.

Phylogenomic databases

KOK13998.
ProtClustDBPTZ00164.

Enzyme and pathway databases

UniPathwayUPA00077; UER00158.

Family and domain databases

Gene3D3.30.572.10. 1 hit.
3.40.430.10. 1 hit.
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. 1 hit.
SSF55831. Thymidylat_synth_C. 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_PARTE
AccessionPrimary (citable) accession number: Q27828
Secondary accession number(s): A0DTB3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 3, 2013
This is version 79 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

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