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P20712

- DRTS_PLACH

UniProt

P20712 - DRTS_PLACH

Protein

Bifunctional dihydrofolate reductase-thymidylate synthase

Gene
N/A
Organism
Plasmodium chabaudi
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    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.By similarity

    Catalytic activityi

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

    Pathwayi

    Sites

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

    Regions

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

    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 synthasePRO_0000186348Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

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

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni298 – 583286Thymidylate synthaseAdd
    BLAST

    Sequence similaritiesi

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

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti27 – 271G → S in AAB59201. (PubMed:7969277)Curated
    Sequence conflicti156 – 1561C → S in AAB59201. (PubMed:7969277)Curated
    Sequence conflicti164 – 1641I → V in AAB59201. (PubMed:7969277)Curated

    Natural variant

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

    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: October 1, 2014
    This is version 84 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