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P51820

- DRTS_SOYBN

UniProt

P51820 - DRTS_SOYBN

Protein

Bifunctional dihydrofolate reductase-thymidylate synthase

Gene
N/A
Organism
Glycine max (Soybean) (Glycine hispida)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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 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 sitei30 – 301Substrate; via carbonyl oxygenBy similarity
    Binding sitei32 – 321NADP; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei52 – 521SubstrateBy similarity
    Binding sitei139 – 1391Substrate; via carbonyl oxygenBy similarity
    Binding sitei160 – 1601SubstrateBy similarity
    Binding sitei267 – 2671dUMPBy similarity
    Active sitei412 – 4121By similarity
    Binding sitei413 – 4131dUMPBy similarity
    Binding sitei443 – 4431dUMPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi38 – 447NADPBy similarity
    Nucleotide bindingi76 – 783NADPBy similarity
    Nucleotide bindingi97 – 1004NADPBy similarity
    Nucleotide bindingi140 – 1478NADPBy similarity
    Nucleotide bindingi431 – 4355dUMPBy similarity
    Nucleotide bindingi473 – 4753dUMPBy 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

    BioCyciMetaCyc:MONOMER-9361.
    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)
    OrganismiGlycine max (Soybean) (Glycine hispida)
    Taxonomic identifieri3847 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeGlycineSoja
    ProteomesiUP000008827: Unplaced

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 530530Bifunctional dihydrofolate reductase-thymidylate synthasePRO_0000186359Add
    BLAST

    Expressioni

    Gene expression databases

    GenevestigatoriP51820.

    Structurei

    3D structure databases

    ProteinModelPortaliP51820.
    SMRiP51820. Positions 245-530.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 203178DHFRAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni206 – 530325Thymidylate 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

    KOiK13998.

    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.

    P51820-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPSDSSVISN GHSNGSVNPL PNLQRTYQVV VAATQDWGIG KDGKLPWRLP    50
    TDLKFFKEIT MKTSEPGKKN AIVMGRKTWE SIPLEYRPLS GRLNVVLTRS 100
    GSFDIATAEN VVICGSMSSA LELLAASPYS LSIEKVFVIG GGQIFREALN 150
    VPGCEAIHLT EIQSSIECDT FMPPVDFTIF RPWYSSFPKV ENNIRYSFTT 200
    YVRVRSSAAE SAGQNIDPLL DNNSESMKFE VKDFSFLPKM ISERHEEYLY 250
    LKLVQDIIAE GTTKGDRTGT GTLSKFGCQM RFNLRGNFPL LTTKKVFWRG 300
    VVEELLWFIS GSTNAKVLQE KGIHIWDGNA SREYLDGVGL TEREEGDLGP 350
    VYGFQWRHFG ARYTDMHHDY SGQGFDQLLD VINKIKRNPD DRRIILSAWN 400
    PVDLKLMALP PCHMFAQFYV AHGELSCQMY QRSADMGLGI PFNIASYALL 450
    TCMIAHVCDL IPGDFIHVIG DAHIYRNHVR PLQEQLHNQP KPFPTLKINP 500
    KKKDIDSFVA ADFKLIGYDP HQKIDMKLSV 530
    Length:530
    Mass (Da):59,745
    Last modified:October 1, 1996 - v1
    Checksum:iAFD710709FD5D820
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S78087 mRNA. Translation: AAB34317.1.
    PIRiS55683.
    RefSeqiNP_001238644.1. NM_001251715.1.
    UniGeneiGma.483.

    Genome annotation databases

    GeneIDi547833.
    KEGGigmx:547833.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S78087 mRNA. Translation: AAB34317.1 .
    PIRi S55683.
    RefSeqi NP_001238644.1. NM_001251715.1.
    UniGenei Gma.483.

    3D structure databases

    ProteinModelPortali P51820.
    SMRi P51820. Positions 245-530.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 547833.
    KEGGi gmx:547833.

    Phylogenomic databases

    KOi K13998.

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00158 .
    BioCyci MetaCyc:MONOMER-9361.

    Gene expression databases

    Genevestigatori P51820.

    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. "Cloning, nucleotide sequence and expression of the bifunctional dihydrofolate reductase-thymidylate synthase from Glycine max."
      Wang M., Ratnam S., Freisheim J.H.
      Biochim. Biophys. Acta 1261:325-336(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.

    Entry informationi

    Entry nameiDRTS_SOYBN
    AccessioniPrimary (citable) accession number: P51820
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    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)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

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

    External Data

    Dasty 3