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P13100

- TYSY_PNECA

UniProt

P13100 - TYSY_PNECA

Protein

Thymidylate synthase

Gene

THYA

Organism
Pneumocystis carinii
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei173 – 1731

    GO - Molecular functioni

    1. thymidylate synthase activity Source: UniProtKB-EC

    GO - Biological processi

    1. dTMP biosynthetic process Source: InterPro
    2. dTTP biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Nucleotide biosynthesis

    Enzyme and pathway databases

    UniPathwayiUPA00575.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thymidylate synthase (EC:2.1.1.45)
    Short name:
    TS
    Short name:
    TSase
    Gene namesi
    Name:THYA
    OrganismiPneumocystis carinii
    Taxonomic identifieri4754 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaPneumocystidomycetesPneumocystidaceaePneumocystis

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 297297Thymidylate synthasePRO_0000140911Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    1
    297
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1916
    Beta strandi21 – 244
    Beta strandi28 – 369
    Beta strandi40 – 434
    Helixi45 – 473
    Beta strandi53 – 553
    Helixi59 – 7012
    Helixi76 – 805
    Turni81 – 833
    Helixi88 – 914
    Helixi93 – 986
    Helixi113 – 1197
    Helixi138 – 14811
    Beta strandi156 – 1583
    Turni162 – 1643
    Helixi165 – 1673
    Beta strandi168 – 1703
    Beta strandi173 – 1819
    Beta strandi191 – 20212
    Turni203 – 2053
    Helixi206 – 22419
    Beta strandi228 – 24215
    Helixi243 – 2508
    Helixi252 – 2543
    Beta strandi262 – 2654
    Helixi272 – 2743
    Helixi277 – 2793
    Beta strandi280 – 2845

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CI7X-ray2.60A/B1-297[»]
    1F28X-ray1.90A/B/C/D1-297[»]
    ProteinModelPortaliP13100.
    SMRiP13100. Positions 3-297.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13100.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thymidylate synthase family.Curated

    Family and domain databases

    Gene3Di3.30.572.10. 1 hit.
    HAMAPiMF_00008. Thymidy_synth_bact.
    InterProiIPR023451. Thymidate_synth/dCMP_Mease.
    IPR000398. Thymidylate_synthase.
    IPR020940. Thymidylate_synthase_AS.
    [Graphical view]
    PfamiPF00303. Thymidylat_synt. 1 hit.
    [Graphical view]
    PRINTSiPR00108. THYMDSNTHASE.
    SUPFAMiSSF55831. SSF55831. 1 hit.
    TIGRFAMsiTIGR03284. thym_sym. 1 hit.
    PROSITEiPS00091. THYMIDYLATE_SYNTHASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P13100-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVNAEEQQYL NLVQYIINHG EDRPDRTGTG TLSVFAPSPL KFSLRNKTFP    50
    LLTTKRVFIR GVIEELLWFI RGETDSLKLR EKNIHIWDAN GSREYLDSIG 100
    LTKRQEGDLG PIYGFQWRHF GAEYIDCKTN YIGQGVDQLA NIIQKIRTSP 150
    YDRRLILSAW NPADLEKMAL PPCHMFCQFY VHIPSNNHRP ELSCQLYQRS 200
    CDMGLGVPFN IASYALLTCM IAHVCDLDPG DFIHVMGDCH IYKDHIEALQ 250
    QQLTRSPRPF PTLSLNRSIT DIEDFTLDDF NIQNYHPYET IKMKMSI 297
    Length:297
    Mass (Da):34,362
    Last modified:January 1, 1990 - v1
    Checksum:i985F6F870EF2A7B2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25415 Genomic DNA. Translation: AAA33802.1.
    S77510 Genomic DNA. Translation: AAB34157.1.
    PIRiA33720. YXUNTP.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25415 Genomic DNA. Translation: AAA33802.1 .
    S77510 Genomic DNA. Translation: AAB34157.1 .
    PIRi A33720. YXUNTP.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CI7 X-ray 2.60 A/B 1-297 [» ]
    1F28 X-ray 1.90 A/B/C/D 1-297 [» ]
    ProteinModelPortali P13100.
    SMRi P13100. Positions 3-297.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P13100.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00575 .

    Miscellaneous databases

    EvolutionaryTracei P13100.

    Family and domain databases

    Gene3Di 3.30.572.10. 1 hit.
    HAMAPi MF_00008. Thymidy_synth_bact.
    InterProi IPR023451. Thymidate_synth/dCMP_Mease.
    IPR000398. Thymidylate_synthase.
    IPR020940. Thymidylate_synthase_AS.
    [Graphical view ]
    Pfami PF00303. Thymidylat_synt. 1 hit.
    [Graphical view ]
    PRINTSi PR00108. THYMDSNTHASE.
    SUPFAMi SSF55831. SSF55831. 1 hit.
    TIGRFAMsi TIGR03284. thym_sym. 1 hit.
    PROSITEi PS00091. THYMIDYLATE_SYNTHASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and expression of the Pneumocystis carinii thymidylate synthase gene."
      Edman U., Edman J.C., Lundgren B., Santi D.V.
      Proc. Natl. Acad. Sci. U.S.A. 86:6503-6507(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Polymorphism of the thymidylate synthase gene of Pneumocystis carinii from different host species."
      Mazars E., Odberg-Ferragut C., Dei-Cas E., Fourmaux M.N., Aliouat E.M., Brun-Pascaud M., Mougeot G., Camus D.
      J. Eukaryot. Microbiol. 42:26-32(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 112-210.
    3. "The structural mechanism for half-the-sites reactivity in an enzyme, thymidylate synthase, involves a relay of changes between subunits."
      Anderson A.C., O'Neil R.H., DeLano W.L., Stroud R.M.
      Biochemistry 38:13829-13836(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

    Entry informationi

    Entry nameiTYSY_PNECA
    AccessioniPrimary (citable) accession number: P13100
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 85 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3