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Q27713

- DRTS_PLABA

UniProt

Q27713 - DRTS_PLABA

Protein

Bifunctional dihydrofolate reductase-thymidylate synthase

Gene
N/A
Organism
Plasmodium berghei (strain Anka)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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 sitei173 – 1731Substrate; via carbonyl oxygenBy similarity
    Binding sitei179 – 1791SubstrateBy similarity
    Binding sitei194 – 1941SubstrateBy similarity
    Binding sitei324 – 3241dUMPBy similarity
    Active sitei469 – 4691By similarity
    Binding sitei470 – 4701dUMPBy similarity
    Binding sitei500 – 5001dUMPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi36 – 427NADPBy similarity
    Nucleotide bindingi108 – 1103NADPBy similarity
    Nucleotide bindingi129 – 1324NADPBy similarity
    Nucleotide bindingi174 – 1818NADPBy similarity
    Nucleotide bindingi488 – 4925dUMPBy similarity
    Nucleotide bindingi530 – 5323dUMPBy 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 berghei (strain Anka)
    Taxonomic identifieri5823 [NCBI]
    Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Vinckeia)

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 587587Bifunctional dihydrofolate reductase-thymidylate synthasePRO_0000186347Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ27713.
    SMRiQ27713. Positions 1-238, 264-587.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 237229DHFRAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni301 – 587287Thymidylate 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.

    Q27713-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEDLSETFDI YAICACCKVL NDDEKVRCFN NKTFKGIGNA GVLPWKCNLI    50
    DMKYFSSVTS YINENNYIRL KWKRDKYMEK HNLKNNVELN TNIISSTNNL 100
    QNIVVMGKKS WESIPKKFKP LQNRINIILS RTLKKEDIVN ENNNENNNVI 150
    IIKSVDDLFP ILKCTKYYKC FIIGGSSVYK EFLDRNLIKK IYFTRINNSY 200
    NCDVLFPEIN ENLFKITSIS DVYYSNNTTL DFIIYSKTKE INPNEEVPNN 250
    TFLGVCDEQN KAFDDEDDYT YFSFNKNKEN IKKNSEHAHN FKIYNSIKYK 300
    NHPEYQYLNI IYDIIMHGNK QDDRTGVGVL SKFGYMMKFN LNEYFPLLTT 350
    KKLFIRGIIE ELLWFIRGET NGNTLLEKNV RIWEANGTRE FLDNRKLFHR 400
    EVNDLGPIYG FQWRHFGAEY TDMHDNYKDK GVDQLKNIIN LIKNDPTCRR 450
    IILCAWNVKN LDQMALPPCH ILCQFYVFDG KLSCIMYQRS CDLGLGVPFN 500
    IASYSIFTYM IAQVCNLQAA EFIHVLGNAH VYNNHIESLK IQLNRTPYPF 550
    PTLKLNPDIK NIEDFTISDF TVQNYVHHDK INMDMAA 587
    Length:587
    Mass (Da):68,932
    Last modified:November 1, 1996 - v1
    Checksum:i6E638C2B02FEC13A
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti110 – 1101S → N in pyrimethamine resistance.
    Natural varianti177 – 1771S → F in pyrimethamine resistance.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U12275 Genomic DNA. Translation: AAB60237.1.
    L28119 Genomic DNA. Translation: AAA29581.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U12275 Genomic DNA. Translation: AAB60237.1 .
    L28119 Genomic DNA. Translation: AAA29581.1 .

    3D structure databases

    ProteinModelPortali Q27713.
    SMRi Q27713. Positions 1-238, 264-587.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL3963.
    DrugBanki DB00440. Trimethoprim.

    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. "Mechanisms of pyrimethamine resistance in two different strains of Plasmodium berghei."
      van Dijk M.R., McConkey G.A., Vinkenoog R., Waters A.P., Janse C.J.
      Mol. Biochem. Parasitol. 68:167-171(1994) [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 12-201.

    Entry informationi

    Entry nameiDRTS_PLABA
    AccessioniPrimary (citable) accession number: Q27713
    Secondary accession number(s): Q27714
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 78 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