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Q27783 (DRTS_TRYBB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismTrypanosoma brucei brucei
Taxonomic identifier5702 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

Protein attributes

Sequence length527 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP. HAMAP-Rule MF_00008

5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH. HAMAP-Rule MF_00008

Pathway

Pyrimidine metabolism; dTTP biosynthesis. HAMAP-Rule MF_00008

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. HAMAP-Rule MF_00008

Subunit structure

Homodimer By similarity. 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 – 527527Bifunctional dihydrofolate reductase-thymidylate synthase HAMAP-Rule MF_00008
PRO_0000186353

Regions

Domain28 – 238211DHFR
Nucleotide binding40 – 467NADP By similarity
Nucleotide binding84 – 863NADP By similarity
Nucleotide binding105 – 1084NADP By similarity
Nucleotide binding161 – 1688NADP By similarity
Nucleotide binding428 – 4325dUMP By similarity
Nucleotide binding470 – 4723dUMP By similarity
Region243 – 527285Thymidylate synthase HAMAP-Rule MF_00008

Sites

Active site4091 By similarity
Binding site321Substrate; via carbonyl oxygen By similarity
Binding site341NADP; via amide nitrogen and carbonyl oxygen By similarity
Binding site541Substrate By similarity
Binding site1601Substrate; via carbonyl oxygen By similarity
Binding site1661Substrate By similarity
Binding site1841Substrate By similarity
Binding site2631dUMP By similarity
Binding site4101dUMP By similarity
Binding site4401dUMP By similarity

Secondary structure

.................................... 527
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q27783 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 39982FC553BF7601

FASTA52758,805
        10         20         30         40         50         60 
MLSLTRILRK KIPVHELAGK ISRPPLRPFS VVVASDEKGG IGDGGTIPWE IPEDMQYFRR 

        70         80         90        100        110        120 
VTTNLRGKNV KPSPSKRNAV VMGRKTWDSL PPKFRPLSNR LNVVLSRSAT KEQLLAGIPD 

       130        140        150        160        170        180 
PIKRAEAAND VVAVNGGLED ALRMLVSKEH TSSIETVFCI GGGTIYKQAL CAPCVNVLQA 

       190        200        210        220        230        240 
IHRTVVRPAS NSCSVFFDIP AAGTKTPEGL ELVRESITDE RVSTGAGGKK YQFEKLVPRN 

       250        260        270        280        290        300 
SEEEQYLNLV GRIIDEGCTK CDRTGVGTRS LFGAQMRFSL RNNRLPLLTT KRVFWRGVCE 

       310        320        330        340        350        360 
ELLWFLRGET NAKLLSDKGI HIWDGNGSRA FLDSRGLTDY DEMDLGPVYG FQWRHFGADY 

       370        380        390        400        410        420 
ISCKVDSEGK GVDQIANIVK SLIENPDDRR MICTAWNPAA LPRMALPPCH MMAQFYVSNG 

       430        440        450        460        470        480 
ELSCMLYQRS CDMGLGVPFN IASYALLTFL MAKASGLRPG ELVHTLGDAH VYSNHVEPCR 

       490        500        510        520 
KQLKRVPRPF PFIVFKQDKE FLEDFQESDI EVIDYSPYPV ISMEMAV 

« Hide

References

[1]"Trypanosoma brucei dihydrofolate reductase-thymidylate synthase: gene isolation and expression and characterization of the enzyme."
Gamarro F., Yu P.L., Zhao J., Edman U., Greene P.J., Santi D.
Mol. Biochem. Parasitol. 72:11-22(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 427.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U20781 Genomic DNA. Translation: AAA91362.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QFXX-ray2.20A/B1-241[»]
3RG9X-ray2.00A/B1-240[»]
ProteinModelPortalQ27783.
SMRQ27783. Positions 11-521.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00077; UER00158.
UPA00575.

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...

Other

EvolutionaryTraceQ27783.

Entry information

Entry nameDRTS_TRYBB
AccessionPrimary (citable) accession number: Q27783
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 79 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways