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Q05762

- DRTS1_ARATH

UniProt

Q05762 - DRTS1_ARATH

Protein

Bifunctional dihydrofolate reductase-thymidylate synthase 1

Gene

THY-1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (27 May 2002)
      Previous versions | rss
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    Functioni

    Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Can play two different roles depending on the source of dihydrofolate: de novo synthesis of tetrahydrofolate or recycling of the dihydrofolate released as one of the end products of the TS catalyzed reaction. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP.

    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 sitei25 – 251Substrate; via carbonyl oxygenBy similarity
    Binding sitei27 – 271NADP; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei47 – 471SubstrateBy similarity
    Binding sitei134 – 1341Substrate; via carbonyl oxygenBy similarity
    Binding sitei155 – 1551SubstrateBy similarity
    Binding sitei256 – 2561dUMPBy similarity
    Active sitei401 – 4011By similarity
    Binding sitei402 – 4021dUMPBy similarity
    Binding sitei432 – 4321dUMPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi33 – 397NADPBy similarity
    Nucleotide bindingi71 – 733NADPBy similarity
    Nucleotide bindingi92 – 954NADPBy similarity
    Nucleotide bindingi135 – 1428NADPBy similarity
    Nucleotide bindingi420 – 4245dUMPBy similarity
    Nucleotide bindingi462 – 4643dUMPBy similarity

    GO - Molecular functioni

    1. dihydrofolate reductase activity Source: TAIR
    2. thymidylate synthase activity Source: TAIR

    GO - Biological processi

    1. 10-formyltetrahydrofolate biosynthetic process Source: TAIR
    2. dTMP biosynthetic process Source: InterPro
    3. glycine biosynthetic process Source: InterPro
    4. one-carbon metabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Methyltransferase, Oxidoreductase, Transferase

    Keywords - Biological processi

    Nucleotide biosynthesis, One-carbon metabolism

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciARA:AT2G16370-MONOMER.
    UniPathwayiUPA00077; UER00158.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional dihydrofolate reductase-thymidylate synthase 1
    Short name:
    DHFR-TS 1
    Including the following 2 domains:
    Dihydrofolate reductase (EC:1.5.1.3)
    Thymidylate synthase (EC:2.1.1.45)
    Gene namesi
    Name:THY-1
    Ordered Locus Names:At2g16370
    ORF Names:F16F14.13
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 2

    Organism-specific databases

    TAIRiAT2G16370.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: TAIR

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 519518Bifunctional dihydrofolate reductase-thymidylate synthase 1PRO_0000186355Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ05762.
    PRIDEiQ05762.

    Expressioni

    Gene expression databases

    GenevestigatoriQ05762.

    Interactioni

    Subunit structurei

    Heterodimer or homodimer.By similarity

    Protein-protein interaction databases

    BioGridi1492. 1 interaction.
    IntActiQ05762. 1 interaction.
    STRINGi3702.AT2G16370.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ05762.
    SMRiQ05762. Positions 24-519.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 198178DHFRAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni201 – 23434HingeAdd
    BLAST
    Regioni235 – 519285Thymidylate 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

    eggNOGiCOG0262.
    HOGENOMiHOG000257901.
    InParanoidiQ05762.
    KOiK13998.
    OMAiVESNIRH.
    PhylomeDBiQ05762.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q05762-1 [UniParc]FASTAAdd to Basket

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    MATTTLNDSV TTTLASEPQR TYQVVVAATK EMGIGKDGKL PWNLPTDLKF    50
    FKDITLTTSD SSKKNAVVMG RKTWESIPIK YRPLSGRLNV VLTRSGGFDI 100
    ANTENVVTCS SVDSALDLLA APPYCLSIER VFVIGGGDIL REALNRPSCD 150
    AIHLTEIDTS VDCDTFIPAI DTSVYQPWSS SFPVTENGLR FCFTTFVRVK 200
    SSADESSDES NGSQSLQFDG KKFLFLPKMV FDQHEEFLYL NMVEDIISNG 250
    NVKNDRTGTG TLSKFGCQMK FNLRRSFPLL TTKRVFWRGV VEELLWFISG 300
    STNAKVLQEK GIHIWDGNAS REYLDGIGLT EREEGDLGPV YGFQWRHFGA 350
    KYTDMHADYT GQGFDQLVDV IDKIKNNPDD RRIIMSAWNP SDLKLMALPP 400
    CHMFAQFYVA EGELSCQMYQ RSADMGLGVP FNIASYSLLT CMLAHVCDLV 450
    PGDFIHVLGD AHVYKTHVRP LQEQLLNLPK PFPVMKINPE KKQIDSFVAS 500
    DFDLTGYDPH KKIEMKMAV 519
    Length:519
    Mass (Da):58,143
    Last modified:May 27, 2002 - v2
    Checksum:iB5EB36A3A936580F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti120 – 1201A → R in AAA32788. (PubMed:8374616)Curated
    Sequence conflicti478 – 4781L → P in AAA32788. (PubMed:8374616)Curated
    Sequence conflicti485 – 4851M → L in AAA32788. (PubMed:8374616)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L08593 mRNA. Translation: AAA32788.1.
    AC007047 Genomic DNA. Translation: AAD22302.1.
    CP002685 Genomic DNA. Translation: AEC06489.1.
    AY063968 mRNA. Translation: AAL36324.1.
    AY114032 mRNA. Translation: AAM45080.1.
    PIRiE84539.
    RefSeqiNP_179230.1. NM_127191.3.
    UniGeneiAt.27124.

    Genome annotation databases

    EnsemblPlantsiAT2G16370.1; AT2G16370.1; AT2G16370.
    GeneIDi816134.
    KEGGiath:AT2G16370.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L08593 mRNA. Translation: AAA32788.1 .
    AC007047 Genomic DNA. Translation: AAD22302.1 .
    CP002685 Genomic DNA. Translation: AEC06489.1 .
    AY063968 mRNA. Translation: AAL36324.1 .
    AY114032 mRNA. Translation: AAM45080.1 .
    PIRi E84539.
    RefSeqi NP_179230.1. NM_127191.3.
    UniGenei At.27124.

    3D structure databases

    ProteinModelPortali Q05762.
    SMRi Q05762. Positions 24-519.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 1492. 1 interaction.
    IntActi Q05762. 1 interaction.
    STRINGi 3702.AT2G16370.1-P.

    Proteomic databases

    PaxDbi Q05762.
    PRIDEi Q05762.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT2G16370.1 ; AT2G16370.1 ; AT2G16370 .
    GeneIDi 816134.
    KEGGi ath:AT2G16370.

    Organism-specific databases

    TAIRi AT2G16370.

    Phylogenomic databases

    eggNOGi COG0262.
    HOGENOMi HOG000257901.
    InParanoidi Q05762.
    KOi K13998.
    OMAi VESNIRH.
    PhylomeDBi Q05762.

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00158 .
    BioCyci ARA:AT2G16370-MONOMER.

    Miscellaneous databases

    PROi Q05762.

    Gene expression databases

    Genevestigatori Q05762.

    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. "The origin of the bifunctional dihydrofolate reductase-thymidylate synthase isogenes of Arabidopsis thaliana."
      Lazar G., Zhang H., Goodman H.M.
      Plant J. 3:657-668(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Landsberg erecta.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDRTS1_ARATH
    AccessioniPrimary (citable) accession number: Q05762
    Secondary accession number(s): Q9SIW4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: May 27, 2002
    Last modified: October 1, 2014
    This is version 121 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3