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Q23695 (DRTS_CRIFA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismCrithidia fasciculata
Taxonomic identifier5656 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeCrithidia

Protein attributes

Sequence length515 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. 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 – 515515Bifunctional dihydrofolate reductase-thymidylate synthase HAMAP-Rule MF_00008
PRO_0000186343

Regions

Domain26 – 228203DHFR
Nucleotide binding38 – 447NADP By similarity
Nucleotide binding81 – 833NADP By similarity
Nucleotide binding101 – 1044NADP By similarity
Nucleotide binding155 – 1628NADP By similarity
Nucleotide binding416 – 4205dUMP By similarity
Nucleotide binding458 – 4603dUMP By similarity
Region233 – 515283Thymidylate synthase HAMAP-Rule MF_00008

Sites

Active site3951 By similarity
Binding site301Substrate; via carbonyl oxygen By similarity
Binding site321NADP; via amide nitrogen and carbonyl oxygen By similarity
Binding site1541Substrate; via carbonyl oxygen By similarity
Binding site1601Substrate By similarity
Binding site1781Substrate By similarity
Binding site2531dUMP By similarity
Binding site3961dUMP By similarity
Binding site4281dUMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q23695 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 8327DAB231535921

FASTA51558,294
        10         20         30         40         50         60 
MSRAAAKFKI PMPVTKADFA FPSLRAFSIV VAADQQHGIG DGETIPWTVP ETLAFFKDQT 

        70         80         90        100        110        120 
TLLRNKKPPT EKKRNAVVMG RKTWEVPLKF RPLKGRLNVV LSCRRPVDDL LAQLPEEKRA 

       130        140        150        160        170        180 
AAAADVVING GLKEALHLLA RPPYCSSIET AYCIGGARVY TEAMQSPCVE KLKEVYLTRV 

       190        200        210        220        230        240 
HTAPTCNRFY EFVRRRRARA AVDLESTSGV KVSDAAAHLS YEIMKYVPHN AEERQYLELI 

       250        260        270        280        290        300 
DRIMKTGLVK EDRTGVGTIS LFGAQMFSLR DNQLPLLTTK RVFWRGVCEE LIWFLRGETN 

       310        320        330        340        350        360 
AHVLADKDIH IWDGNGSREF LDSRGLTENK EMDLGPVYGF QWRHFGADYK GFDANYDEGV 

       370        380        390        400        410        420 
DQIKTIVETL KTNDRRLLVT AWNPCALHKM AVRPCHLLGQ FYVNTQTKEL SCMLYQRCCD 

       430        440        450        460        470        480 
MGLGVPFNIA SYALLTILIA KATGLRPGEL VHTLGTAHVY SNHVEALKEQ LQRVPVAFPV 

       490        500        510 
LVFKKEREFL EDYESTDMEV VDYVPYPPIK MEMAV 

« Hide

References

[1]"Structure, genomic organization and transcription of the bifunctional dihydrofolate reductase-thymidylate synthase gene from Crithidia fasciculata."
Hughes D.E., Shonekan O.A., Simpson L.
Mol. Biochem. Parasitol. 34:155-166(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M22852 Genomic DNA. Translation: AAA30318.1.

3D structure databases

ProteinModelPortalQ23695.
SMRQ23695. Positions 8-509.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00077; UER00158.

Family and domain databases

Gene3D3.30.572.10. 1 hit.
3.40.430.10. 1 hit.
HAMAPMF_00008. Thymidy_synth_bact.
InterProIPR024072. DHFR-like_dom.
IPR012262. DHFR-TS.
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. SSF55831. 1 hit.
TIGRFAMsTIGR03284. thym_sym. 1 hit.
PROSITEPS51330. DHFR_2. 1 hit.
PS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDRTS_CRIFA
AccessionPrimary (citable) accession number: Q23695
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 71 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

PATHWAY comments

Index of metabolic and biosynthesis pathways