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P46103 (DRTS_PLAVN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 69. 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
OrganismPlasmodium vinckei
Taxonomic identifier5860 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Vinckeia)

Protein attributes

Sequence length182 AA.
Sequence statusFragment.
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.

Subunit structure

Homodimer By similarity.

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

Chain‹1 – ›182›182Bifunctional dihydrofolate reductase-thymidylate synthase
PRO_0000186350

Regions

Domain‹1 – ›182›182DHFR
Nucleotide binding25 – 317NADP By similarity
Nucleotide binding93 – 953NADP By similarity
Nucleotide binding114 – 1174NADP By similarity
Nucleotide binding155 – 1628NADP By similarity

Sites

Binding site401Substrate By similarity
Binding site1541Substrate; via carbonyl oxygen By similarity
Binding site1601Substrate By similarity
Binding site1751Substrate By similarity

Experimental info

Non-terminal residue11
Non-terminal residue1821

Sequences

Sequence LengthMass (Da)Tools
P46103 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 33CCD27441763198

FASTA18220,925
        10         20         30         40         50         60 
AICACCKVLN SNEKASCFSN KTFKGLGNAG GLPWKCNSVD MKHFVSVTSY VNENNYIRLK 

        70         80         90        100        110        120 
WKRDKYIKEN NVKVNTDGIP SIDKLQNIVV MGKTSWESIP SKFKPLENRI NIILSRTLKK 

       130        140        150        160        170        180 
ENLAKEYSNV IIIKSVDELF PILKCIKYYK CFIIGGASVY KEFLDRNLIK KIYFTRINNA 


YT 

« Hide

References

[1]"The dihydrofolate reductase domain of rodent malarias: point mutations and pyrimethamine resistance."
Cheng Q., Saul A.
Mol. Biochem. Parasitol. 65:361-363(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L28121 Genomic DNA. Translation: AAA29582.1.

3D structure databases

ProteinModelPortalP46103.
SMRP46103. Positions 1-181.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00077; UER00158.

Family and domain databases

Gene3D3.40.430.10. 1 hit.
InterProIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view]
PfamPF00186. DHFR_1. 1 hit.
[Graphical view]
PRINTSPR00070. DHFR.
SUPFAMSSF53597. SSF53597. 1 hit.
PROSITEPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDRTS_PLAVN
AccessionPrimary (citable) accession number: P46103
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 19, 2014
This is version 69 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