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D9N170 (D9N170_PLAFA) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional dihydrofolate reductase-thymidylate synthase PIRNR PIRNR000389
Gene names
Name:DHFR-TS PDB 3QG2 PDB 3JSU
ORF Names:V1/S PDB 3QG2 PDB 3JSU
OrganismPlasmodium falciparum PDB 3QG2
Taxonomic identifier5833 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)

Protein attributes

Sequence length608 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 By similarity. PIRNR PIRNR000389

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. PIRNR PIRNR000389

Sequence similarities

In the C-terminal section; belongs to the thymidylate synthase family. PIRNR PIRNR000389

In the N-terminal section; belongs to the dihydrofolate reductase family. PIRNR PIRNR000389

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding44 – 452NADP PDB 3QG2
Nucleotide binding106 – 1083NADP PDB 3QG2
Nucleotide binding127 – 1304NADP PDB 3QG2 PDB 4DP3 PDB 4DPH
Nucleotide binding165 – 1728NADP PDB 3QG2 PDB 4DP3 PDB 4DPH
Region470 – 4712Phosphate binding
Region510 – 5112Phosphate binding

Sites

Active site4901 By similarity PIRSR PIRSR000389-1
Binding site161NADP; via amide nitrogen and carbonyl oxygen PDB 3QG2
Binding site401NADP; via carbonyl oxygen PDB 3QG2
Binding site1441NADP; via carbonyl oxygen PDB 3QG2
Binding site3451Phosphate

Sequences

Sequence LengthMass (Da)Tools
D9N170 [UniParc].

Last modified October 5, 2010. Version 1.
Checksum: 544ED69133C63613

FASTA60871,816
        10         20         30         40         50         60 
MMEQVCDVFD IYAICACCKV ESKNEGKKNE VFNNYTFRGL GNKGVLPWKC ISLDMKYFRA 

        70         80         90        100        110        120 
VTTYVNESKY EKLKYKRCKY LNKETVDNVN DMPNSKKLQN VVVMGRTNWE SIPKKFKPLS 

       130        140        150        160        170        180 
NRINVILSRT LKKEDFDEDV YIINKVEDLI VLLGKLNYYK CFILGGSVVY QEFLEKKLIK 

       190        200        210        220        230        240 
KIYFTRINST YECDVFFPEI NENEYQIISV SDVYTSNNTT LDFIIYKKTN NKMLNEQNCI 

       250        260        270        280        290        300 
KGEEKNNDMP LKNDDKDTCH MKKLTEFYKN VDKYKINYEN DDDDEEEDDF VYFNFNKEKE 

       310        320        330        340        350        360 
EKNKNSIHPN DFQIYNSLKY KYHPEYQYLN IIYDIMMNGN KQSDRTGVGV LSKFGYIMKF 

       370        380        390        400        410        420 
DLSQYFPLLT TKKLFLRGII EELLWFIRGE TNGNTLLNKN VRIWEANGTR EFLDNRKLFH 

       430        440        450        460        470        480 
REVNDLGPIY GFQWRHFGAE YTNMYDNYEN KGVDQLKNII NLIKNDPTSR RILLCAWNVK 

       490        500        510        520        530        540 
DLDQMALPPC HILCQFYVFD GKLSCIMYQR SCDLGLGVPF NIASYSIFTH MIAQVCNLQP 

       550        560        570        580        590        600 
AQFIHVLGNA HVYNNHIDSL KIQLNRIPYP FPTLKLNPDI KNIEDFTISD FTIQNYVHHE 


KISMDMAA 

« Hide

References

[1]"Trypanosomal dihydrofolate reductase reveals natural antifolate resistance."
Vanichtanankul J., Taweechai S., Yuvaniyama J., Vilaivan T., Chitnumsub P., Kamchonwongpaisan S., Yuthavong Y.
ACS Chem. Biol. 6:905-911(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH NADP.
[2]"Malarial dihydrofolate reductase as a paradigm for drug development against a resistance-compromised target."
Yuthavong Y., Tarnchompoo B., Vilaivan T., Chitnumsub P., Kamchonwongpaisan S., Charman S.A., McLennan D.N., White K.L., Vivas L., Bongard E., Thongphanchang C., Taweechai S., Vanichtanankul J., Rattanajak R., Arwon U., Fantauzzi P., Yuvaniyama J., Charman W.N., Matthews D.
Proc. Natl. Acad. Sci. U.S.A. 109:16823-16828(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) IN COMPLEX WITH NADP AND PHOSPHATE.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QG2X-ray2.30A/B1-608[»]
4DP3X-ray2.40A/B1-608[»]
4DPHX-ray2.38A/B1-608[»]
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...

Other

EvolutionaryTraceD9N170.

Entry information

Entry nameD9N170_PLAFA
AccessionPrimary (citable) accession number: D9N170
Entry history
Integrated into UniProtKB/TrEMBL: October 5, 2010
Last sequence update: October 5, 2010
Last modified: February 19, 2014
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)