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Q05763

- DRTS2_ARATH

UniProt

Q05763 - DRTS2_ARATH

Protein

Bifunctional dihydrofolate reductase-thymidylate synthase 2

Gene

THY-2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (26 Jun 2007)
      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 sitei69 – 691Substrate; via carbonyl oxygenBy similarity
    Binding sitei71 – 711NADP; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei91 – 911SubstrateBy similarity
    Binding sitei178 – 1781Substrate; via carbonyl oxygenBy similarity
    Binding sitei199 – 1991SubstrateBy similarity
    Binding sitei302 – 3021dUMPBy similarity
    Active sitei447 – 4471By similarity
    Binding sitei448 – 4481dUMPBy similarity
    Binding sitei478 – 4781dUMPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi77 – 837NADPBy similarity
    Nucleotide bindingi115 – 1173NADPBy similarity
    Nucleotide bindingi136 – 1394NADPBy similarity
    Nucleotide bindingi179 – 1868NADPBy similarity
    Nucleotide bindingi466 – 4705dUMPBy similarity
    Nucleotide bindingi508 – 5103dUMPBy 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:AT4G34570-MONOMER.
    UniPathwayiUPA00077; UER00158.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional dihydrofolate reductase-thymidylate synthase 2
    Short name:
    DHFR-TS 2
    Including the following 2 domains:
    Dihydrofolate reductase (EC:1.5.1.3)
    Thymidylate synthase (EC:2.1.1.45)
    Gene namesi
    Name:THY-2
    Ordered Locus Names:At4g34570
    ORF Names:T4L20.150
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G34570.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 565565Bifunctional dihydrofolate reductase-thymidylate synthase 2PRO_0000186356Add
    BLAST

    Proteomic databases

    PaxDbiQ05763.
    PRIDEiQ05763.

    Expressioni

    Gene expression databases

    GenevestigatoriQ05763.

    Interactioni

    Subunit structurei

    Heterodimer or homodimer.By similarity

    Protein-protein interaction databases

    STRINGi3702.AT4G34570.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ05763.
    SMRiQ05763. Positions 68-565.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini65 – 242178DHFRAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni245 – 28036HingeAdd
    BLAST
    Regioni281 – 565285Thymidylate 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.
    InParanoidiQ05763.
    KOiK13998.
    OMAiLTCMIAQ.
    PhylomeDBiQ05763.

    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.

    Q05763-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRCLQNSAKT LPLAFKSALL PLSQRWFCKF SPKPSSLTNI FKVSISTMAN    50
    TLNGNVIMTS KPQSTYQVVV AATKEMGIGK DGKLPWNLPT DLKFFKDLTL 100
    STSDSAKKNA VVMGRKTWES IPKKYRPLSG RLNVVLSRSS GFDIANTENV 150
    VTCSSIDSAL DLLAAPPFSL SIEKVFVIGG GDILREALNK PSCEAIHITE 200
    IDTSIDCDTF IPTVDTSAYQ PWCSSFPICE NGLRFSFTTH VRVKSSSAGE 250
    ASDESDGSKV LQVDWKKFSS VLPKMIFDRH EEYLYLNLVK EIISNGNLKD 300
    DRTGTGTLSK FGCQMKFNLR RNFPLLTTKR VFWRGVVEEL LWFISGSTNA 350
    KVLQEKGIRI WDGNASRAYL DGIGLTEREE GDLGPVYGFQ WRHFGAKYTD 400
    MHADYTGQGF DQLLDVINKI KNNPDDRRII MSAWNPSDLK LMALPPCHMF 450
    AQFYVANGEL SCQMYQRSAD MGLGVPFNIA SYSLLTCILA HVCDLVPGDF 500
    IHVIGDAHVY KNHVRPLQEQ LENPPKPFPV LKINPEKKDI DSFVADDFEL 550
    IGYDPHKKID MKMAV 565
    Length:565
    Mass (Da):63,209
    Last modified:June 26, 2007 - v2
    Checksum:iC442A1402A591DD9
    GO

    Sequence cautioni

    The sequence AAA32789.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAA18836.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAB80174.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L08594 Genomic DNA. Translation: AAA32789.1. Sequence problems.
    AL023094 Genomic DNA. Translation: CAA18836.1. Sequence problems.
    AL161585 Genomic DNA. Translation: CAB80174.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE86394.1.
    AK227728 mRNA. Translation: BAE99713.1.
    BT003159 mRNA. Translation: AAO24591.1.
    PIRiT05277.
    RefSeqiNP_195183.2. NM_119623.4.
    UniGeneiAt.31491.

    Genome annotation databases

    EnsemblPlantsiAT4G34570.1; AT4G34570.1; AT4G34570.
    GeneIDi829609.
    KEGGiath:AT4G34570.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L08594 Genomic DNA. Translation: AAA32789.1 . Sequence problems.
    AL023094 Genomic DNA. Translation: CAA18836.1 . Sequence problems.
    AL161585 Genomic DNA. Translation: CAB80174.1 . Sequence problems.
    CP002687 Genomic DNA. Translation: AEE86394.1 .
    AK227728 mRNA. Translation: BAE99713.1 .
    BT003159 mRNA. Translation: AAO24591.1 .
    PIRi T05277.
    RefSeqi NP_195183.2. NM_119623.4.
    UniGenei At.31491.

    3D structure databases

    ProteinModelPortali Q05763.
    SMRi Q05763. Positions 68-565.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT4G34570.1-P.

    Proteomic databases

    PaxDbi Q05763.
    PRIDEi Q05763.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G34570.1 ; AT4G34570.1 ; AT4G34570 .
    GeneIDi 829609.
    KEGGi ath:AT4G34570.

    Organism-specific databases

    TAIRi AT4G34570.

    Phylogenomic databases

    eggNOGi COG0262.
    HOGENOMi HOG000257901.
    InParanoidi Q05763.
    KOi K13998.
    OMAi LTCMIAQ.
    PhylomeDBi Q05763.

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00158 .
    BioCyci ARA:AT4G34570-MONOMER.

    Gene expression databases

    Genevestigatori Q05763.

    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. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      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. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
      , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
      Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "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] OF 48-565.
      Strain: cv. Columbia.

    Entry informationi

    Entry nameiDRTS2_ARATH
    AccessioniPrimary (citable) accession number: Q05763
    Secondary accession number(s): Q0WT35
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: June 26, 2007
    Last modified: October 1, 2014
    This is version 119 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