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P16126 (DRTS_LEIAM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 83. 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
OrganismLeishmania amazonensis
Taxonomic identifier5659 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

Protein attributes

Sequence length520 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 – 520520Bifunctional dihydrofolate reductase-thymidylate synthase HAMAP-Rule MF_00008
PRO_0000186344

Regions

Domain26 – 229204DHFR
Nucleotide binding38 – 447NADP By similarity
Nucleotide binding81 – 833NADP By similarity
Nucleotide binding102 – 1054NADP By similarity
Nucleotide binding157 – 1648NADP By similarity
Nucleotide binding421 – 4255dUMP By similarity
Nucleotide binding463 – 4653dUMP By similarity
Region234 – 520287Thymidylate synthase HAMAP-Rule MF_00008

Sites

Active site4001 By similarity
Binding site301Substrate; via carbonyl oxygen By similarity
Binding site321NADP; via amide nitrogen and carbonyl oxygen By similarity
Binding site521Substrate By similarity
Binding site1621Substrate By similarity
Binding site1801Substrate By similarity
Binding site2541dUMP By similarity
Binding site4011dUMP By similarity
Binding site4331dUMP By similarity

Sequences

Sequence LengthMass (Da)Tools
P16126 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: B59CEE0CC3CF7BED

FASTA52058,610
        10         20         30         40         50         60 
MSRAAAKFKI PMPVTKADFA FPSLRAFSIV VALDKQHGIG DGESIPWRVP EDMAFFKDQT 

        70         80         90        100        110        120 
TLLRNKKPPT DKKRNAVVMG RKTWESVPVK FRPLKGRLNV VLSSKATVEE LLAPLPEEKR 

       130        140        150        160        170        180 
AAAAQDIVVV NGGLAAAVRL LARPPYCSSI ETAYCVGGAQ VYADAMLSPC VEKLQEVYLT 

       190        200        210        220        230        240 
RIHTTAPACT RFFPFPPENA ATAWDLASSQ GRRKSAVDGL EFEICKYVPR NHEERQYLEL 

       250        260        270        280        290        300 
IDRIMKTGIA KEDRTGVGTL SLFGAQMRFS LRDNRLPLLT TKRVFWRGVC EELLWFLRGE 

       310        320        330        340        350        360 
TNAQLLADKD IHIWDGNGSR EFLDSRGLTE NTEMDLGPVY GFQWRHFGAE YRGLEANYDG 

       370        380        390        400        410        420 
EGVDQIKFIV ETIKANPNDR RLLFTAWNPC ALHKMALPPC HLLAQFYVNT EKSELSCMLY 

       430        440        450        460        470        480 
QRSCDMGLGV PFNIASYALL TILIAKATGL RPGELVHTLG DAHVYRSHID ALKAQLERVP 

       490        500        510        520 
HAFPTLVFKE ERQFLEDYEL MDMEVIDYVP HPPIKMEMAV 

« Hide

References

[1]"Sequence of the dihydrofolate reductase-thymidylate synthase (DHFR-TS) gene of Leishmania amazonensis."
Nelson K., Alonso G., Langer P.J., Beverley S.M.
Nucleic Acids Res. 18:2819-2819(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: MHOM/BR/77/LTB0016/C1S1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X51735 Genomic DNA. Translation: CAA36020.1.
PIRRDLNTZ. S15756.

3D structure databases

ProteinModelPortalP16126.
SMRP16126. Positions 8-514.
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.
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. 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_LEIAM
AccessionPrimary (citable) accession number: P16126
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: February 19, 2014
This is version 83 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