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Q26997

- HGXR_TOXGO

UniProt

Q26997 - HGXR_TOXGO

Protein

Hypoxanthine-guanine-xanthine phosphoribosyltransferase

Gene

HPRT

Organism
Toxoplasma gondii
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to the N9 of hypoxanthine, guanine or xanthine.1 Publication

    Catalytic activityi

    IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate.
    GMP + diphosphate = guanine + 5-phospho-alpha-D-ribose 1-diphosphate.
    5-phospho-alpha-D-ribose 1-diphosphate + xanthine = (9-D-ribosylxanthine)-5'-phosphate + phosphate.

    Cofactori

    Binds 2 magnesium ions per subunit. The magnesium ions are essentially bound to the substrate and have few direct interactions with the protein.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei79 – 791GMP
    Active sitei150 – 1501Proton acceptor2 Publications
    Binding sitei178 – 1781GMP
    Metal bindingi206 – 2061Magnesium1 Publication
    Binding sitei206 – 2061GMP; via carbonyl oxygen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi146 – 1549GMP
    Nucleotide bindingi199 – 2002GMP

    GO - Molecular functioni

    1. hypoxanthine phosphoribosyltransferase activity Source: InterPro
    2. metal ion binding Source: UniProtKB-KW
    3. nucleotide binding Source: UniProtKB-KW

    GO - Biological processi

    1. GMP salvage Source: UniProtKB-UniPathway
    2. IMP salvage Source: UniProtKB-UniPathway
    3. purine ribonucleoside salvage Source: UniProtKB-KW
    4. XMP salvage Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Purine salvage

    Keywords - Ligandi

    Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    UniPathwayiUPA00591; UER00648.
    UPA00602; UER00658.
    UPA00909; UER00887.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hypoxanthine-guanine-xanthine phosphoribosyltransferase (EC:2.4.2.-)
    Short name:
    HGPRT
    Short name:
    HGXPRT
    Short name:
    HGXPRTase
    Gene namesi
    Name:HPRT
    OrganismiToxoplasma gondii
    Taxonomic identifieri5811 [NCBI]
    Taxonomic lineageiEukaryotaAlveolataApicomplexaConoidasidaCoccidiaEucoccidioridaEimeriorinaSarcocystidaeToxoplasma

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi150 – 1501D → A: Strongly reduced catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 230230Hypoxanthine-guanine-xanthine phosphoribosyltransferasePRO_0000139599Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer at low ionic strength and homotetramer at high ionic strength.2 Publications

    Structurei

    Secondary structure

    1
    230
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 83
    Beta strandi9 – 113
    Helixi29 – 313
    Turni36 – 416
    Beta strandi44 – 474
    Helixi49 – 6719
    Beta strandi72 – 787
    Turni79 – 813
    Helixi82 – 9817
    Beta strandi109 – 11911
    Beta strandi122 – 1309
    Helixi134 – 1374
    Beta strandi141 – 15212
    Helixi153 – 16311
    Beta strandi168 – 17811
    Beta strandi189 – 1957
    Beta strandi200 – 2023
    Turni208 – 2136
    Beta strandi215 – 2195
    Helixi222 – 2287

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DBRX-ray2.40A/B/C/D1-230[»]
    1FSGX-ray1.05A/C1-230[»]
    1QK3X-ray1.65A/B/C/D1-230[»]
    1QK4X-ray1.90A/B/C/D1-230[»]
    1QK5X-ray1.60A/B1-230[»]
    ProteinModelPortaliQ26997.
    SMRiQ26997. Positions 1-230.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ26997.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.2020. 1 hit.
    InterProiIPR005904. Hxn_phspho_trans.
    IPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    [Graphical view]
    PfamiPF00156. Pribosyltran. 1 hit.
    [Graphical view]
    SUPFAMiSSF53271. SSF53271. 1 hit.
    TIGRFAMsiTIGR01203. HGPRTase. 1 hit.
    PROSITEiPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q26997-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASKPIEDYG KGKGRIEPMY IPDNTFYNAD DFLVPPHCKP YIDKILLPGG    50
    LVKDRVEKLA YDIHRTYFGE ELHIICILKG SRGFFNLLID YLATIQKYSG 100
    RESSVPPFFE HYVRLKSYQN DNSTGQLTVL SDDLSIFRDK HVLIVEDIVD 150
    TGFTLTEFGE RLKAVGPKSM RIATLVEKRT DRSNSLKGDF VGFSIEDVWI 200
    VGCCYDFNEM FRDFDHVAVL SDAARKKFEK 230
    Length:230
    Mass (Da):26,386
    Last modified:November 1, 1996 - v1
    Checksum:iC3784254EF96361D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09219 mRNA. Translation: AAA57068.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09219 mRNA. Translation: AAA57068.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DBR X-ray 2.40 A/B/C/D 1-230 [» ]
    1FSG X-ray 1.05 A/C 1-230 [» ]
    1QK3 X-ray 1.65 A/B/C/D 1-230 [» ]
    1QK4 X-ray 1.90 A/B/C/D 1-230 [» ]
    1QK5 X-ray 1.60 A/B 1-230 [» ]
    ProteinModelPortali Q26997.
    SMRi Q26997. Positions 1-230.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00591 ; UER00648 .
    UPA00602 ; UER00658 .
    UPA00909 ; UER00887 .

    Miscellaneous databases

    EvolutionaryTracei Q26997.

    Family and domain databases

    Gene3Di 3.40.50.2020. 1 hit.
    InterProi IPR005904. Hxn_phspho_trans.
    IPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    [Graphical view ]
    Pfami PF00156. Pribosyltran. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53271. SSF53271. 1 hit.
    TIGRFAMsi TIGR01203. HGPRTase. 1 hit.
    PROSITEi PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and sequencing of a cDNA encoding the hypoxanthine-guanine phosphoribosyltransferase from Toxoplasma gondii."
      Vasanthakumar G., van Ginkel S., Parish G.
      Gene 147:153-154(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: RH.
    2. "Crystal structures of Toxoplasma gondii HGXPRTase reveal the catalytic role of a long flexible loop."
      Schumacher M.A., Carter D., Roos D.S., Ullman B., Brennan R.G.
      Nat. Struct. Biol. 3:881-887(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
    3. "Crystal structures of the Toxoplasma gondii hypoxanthine-guanine phosphoribosyltransferase-GMP and -IMP complexes: comparison of purine binding interactions with the XMP complex."
      Heroux A., White E.L., Ross L.J., Borhani D.W.
      Biochemistry 38:14485-14494(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
    4. "Crystal structure of Toxoplasma gondii hypoxanthine-guanine phosphoribosyltransferase with bound XMP, pyrophosphate and two Mg2+ ions: insights into the catalytic mechanism."
      Heroux A., White E.L., Ross L.J., Davis R.L., Borhani D.W.
      Biochemistry 38:14495-14506(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF MUTANT ALA-150 IN COMPLEX WITH XMP; PYROPHOSPHATE AND MAGNESIUM IONS, COFACTOR, CATALYTIC ACTIVITY, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF ASP-150.
    5. "Substrate deformation in a hypoxanthine-guanine phosphoribosyltransferase ternary complex: the structural basis for catalysis."
      Heroux A., White E.L., Ross L.J., Kuzin A.P., Borhani D.W.
      Structure 8:1309-1318(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) IN COMPLEX WITH MAGNESIUM; PHOSPHORIBOSYLPYROPHOSPHATE AND 9-DEAZAGUANINE, CATALYTIC ACTIVITY, ACTIVE SITE, FUNCTION.

    Entry informationi

    Entry nameiHGXR_TOXGO
    AccessioniPrimary (citable) accession number: Q26997
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 81 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    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