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P20712

- DRTS_PLACH

UniProt

P20712 - DRTS_PLACH

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Protein
Bifunctional dihydrofolate reductase-thymidylate synthase
Gene
N/A
Organism
Plasmodium chabaudi
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.UniRule annotation
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei51 – 511Substrate By similarity
Binding sitei165 – 1651Substrate; via carbonyl oxygen By similarity
Binding sitei171 – 1711Substrate By similarity
Binding sitei186 – 1861Substrate By similarity
Binding sitei320 – 3201dUMP By similarity
Active sitei465 – 4651 By similarity
Binding sitei466 – 4661dUMP By similarity
Binding sitei496 – 4961dUMP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi36 – 427NADP By similarity
Nucleotide bindingi104 – 1063NADP By similarity
Nucleotide bindingi125 – 1284NADP By similarity
Nucleotide bindingi166 – 1738NADP By similarity
Nucleotide bindingi484 – 4885dUMP By similarity
Nucleotide bindingi526 – 5283dUMP By similarity

GO - Molecular functioni

  1. dihydrofolate reductase activity Source: UniProtKB-EC
  2. thymidylate synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. dTMP biosynthetic process Source: InterPro
  2. glycine biosynthetic process Source: InterPro
  3. one-carbon metabolic process Source: UniProtKB-KW
  4. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Oxidoreductase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis, One-carbon metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional dihydrofolate reductase-thymidylate synthase
Short name:
DHFR-TS
Including the following 2 domains:
Dihydrofolate reductase (EC:1.5.1.3)
Thymidylate synthase (EC:2.1.1.45)
OrganismiPlasmodium chabaudi
Taxonomic identifieri5825 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Vinckeia)

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 583583Bifunctional dihydrofolate reductase-thymidylate synthaseUniRule annotation
PRO_0000186348Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP20712.
SMRiP20712. Positions 1-230, 260-583.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 229221DHFR
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni298 – 583286Thymidylate synthaseUniRule annotation
Add
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the dihydrofolate reductase family.
In the C-terminal section; belongs to the thymidylate synthase family.

Phylogenomic databases

HOGENOMiHOG000257901.

Family and domain databases

Gene3Di3.30.572.10. 1 hit.
3.40.430.10. 1 hit.
HAMAPiMF_00008. Thymidy_synth_bact.
InterProiIPR024072. 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]
PfamiPF00186. DHFR_1. 1 hit.
PF00303. Thymidylat_synt. 1 hit.
[Graphical view]
PIRSFiPIRSF000389. DHFR-TS. 1 hit.
PRINTSiPR00108. THYMDSNTHASE.
SUPFAMiSSF53597. SSF53597. 1 hit.
SSF55831. SSF55831. 1 hit.
TIGRFAMsiTIGR03284. thym_sym. 1 hit.
PROSITEiPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
PS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20712-1 [UniParc]FASTAAdd to Basket

« Hide

MEDISEIFDI YAICACCKVL NSNEKAGCFS NKTFKGLGNE GGLPWKCNSV    50
DMKHFSSVTS YVNETNYMRL KWKRDRYMEK NNVKLNTDGI PSVDKLQNIV 100
VMGKASWESI PSKFKPLQNR INIILSRTLK KEDLAKEYNN VIIINSVDDL 150
FPILKCIKYY KCFIIGGASV YKEFLDRNLI KKIYFTRINN AYTCDVLFPD 200
INEDLFKITS ISDVYSSNNT TLDFVIYSKT KEIHEEINPN DELFNNTFLG 250
VCDEKNTNFD DEDDYTYFSF NKHKDNIKKN SEHAHHFKIY NSIKYKHHPE 300
YQYLNIIYDI IMHGNKQDDR TGVGVLSKFG YMMKFNLSEY FPLLTTKKLF 350
VRGIIEELLW FIRGETNGNT LLEKNVRIWE ANGTREFLDN RKLFHREVND 400
LGPIYGFQWR HFGAEYTDMH ADYKDKGVDQ LKNIINLIKN DPTCRRIILC 450
AWNVKDLDQM ALPPCHILCQ FYVFDGKLSC IMYQRSCDLG LGVPFNIASY 500
SIFTYMIAQV CNLQPAEFIH VLGNAHVYNN HVESLKVQLN RTPYPFPTLK 550
LNPEIKNIED FTISDFTVQN YVHHDKISMD MAA 583
Length:583
Mass (Da):68,051
Last modified:February 1, 1991 - v1
Checksum:i4AA55E1C987E6FD7
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti106 – 1061S → I in pyrimethamine resistance.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271G → S in AAB59201. 1 Publication
Sequence conflicti156 – 1561C → S in AAB59201. 1 Publication
Sequence conflicti164 – 1641I → V in AAB59201. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M30834 Genomic DNA. Translation: AAA29587.1.
L28120 Genomic DNA. Translation: AAB59201.1.
PIRiA33484. RDZQTB.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M30834 Genomic DNA. Translation: AAA29587.1 .
L28120 Genomic DNA. Translation: AAB59201.1 .
PIRi A33484. RDZQTB.

3D structure databases

ProteinModelPortali P20712.
SMRi P20712. Positions 1-230, 260-583.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOGENOMi HOG000257901.

Enzyme and pathway databases

UniPathwayi UPA00077 ; UER00158 .

Family and domain databases

Gene3Di 3.30.572.10. 1 hit.
3.40.430.10. 1 hit.
HAMAPi MF_00008. Thymidy_synth_bact.
InterProi IPR024072. 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 ]
Pfami PF00186. DHFR_1. 1 hit.
PF00303. Thymidylat_synt. 1 hit.
[Graphical view ]
PIRSFi PIRSF000389. DHFR-TS. 1 hit.
PRINTSi PR00108. THYMDSNTHASE.
SUPFAMi SSF53597. SSF53597. 1 hit.
SSF55831. SSF55831. 1 hit.
TIGRFAMsi TIGR03284. thym_sym. 1 hit.
PROSITEi PS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
PS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Antifolate drug selection results in duplication and rearrangement of chromosome 7 in Plasmodium chabaudi."
    Cowman A.F., Lew A.M.
    Mol. Cell. Biol. 9:5182-5188(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "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] OF 12-193.

Entry informationi

Entry nameiDRTS_PLACH
AccessioniPrimary (citable) accession number: P20712
Secondary accession number(s): Q27715
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: February 19, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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