Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Hypoxanthine-guanine phosphoribosyltransferase

Gene

HPT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway.7 Publications

Catalytic activityi

IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate.1 Publication
GMP + diphosphate = guanine + 5-phospho-alpha-D-ribose 1-diphosphate.1 Publication

Cofactori

Mg2+Note: The magnesium ions are essentially bound to the substrate and have few direct interactions with the protein.

Enzyme regulationi

Subject to feedback inhibition by GMP.1 Publication

Kineticsi

  1. KM=23 µM for hypoxanthine3 Publications
  2. KM=18 µM for guanine3 Publications
  3. KM=50 µM for phosphoribosylpyrophosphate3 Publications

    pH dependencei

    Optimum pH is 8.5.3 Publications

    Pathway:iIMP biosynthesis via salvage pathway

    This protein is involved in step 1 of the subpathway that synthesizes IMP from hypoxanthine.
    Proteins known to be involved in this subpathway in this organism are:
    1. Hypoxanthine-guanine phosphoribosyltransferase (HPT1)
    This subpathway is part of the pathway IMP biosynthesis via salvage pathway, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes IMP from hypoxanthine, the pathway IMP biosynthesis via salvage pathway and in Purine metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei85 – 851GMP1 Publication
    Active sitei114 – 1141Proton acceptorBy similarity
    Binding sitei159 – 1591GMP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi110 – 1189GMP1 Publication
    Nucleotide bindingi188 – 1947GMP1 Publication

    GO - Molecular functioni

    GO - Biological processi

    • GMP salvage Source: SGD
    • IMP salvage Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Purine salvage

    Keywords - Ligandi

    Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:YDR399W-MONOMER.
    YEAST:YDR399W-MONOMER.
    SABIO-RKQ04178.
    UniPathwayiUPA00591; UER00648.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hypoxanthine-guanine phosphoribosyltransferase (EC:2.4.2.8)
    Short name:
    HGPRT
    Short name:
    HGPRTase
    Alternative name(s):
    Bypass of repression by adenine protein 6
    Gene namesi
    Name:HPT1
    Synonyms:BRA6
    Ordered Locus Names:YDR399W
    ORF Names:D9509.18
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311 Componenti: Chromosome IV

    Organism-specific databases

    CYGDiYDR399w.
    EuPathDBiFungiDB:YDR399W.
    SGDiS000002807. HPT1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 221220Hypoxanthine-guanine phosphoribosyltransferasePRO_0000257807Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ04178.
    PaxDbiQ04178.
    PeptideAtlasiQ04178.

    Interactioni

    Subunit structurei

    Dimer.2 Publications

    Protein-protein interaction databases

    BioGridi32460. 97 interactions.
    DIPiDIP-4318N.
    IntActiQ04178. 3 interactions.
    MINTiMINT-565941.

    Structurei

    Secondary structure

    1
    221
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 83Combined sources
    Helixi11 – 2515Combined sources
    Turni26 – 283Combined sources
    Beta strandi31 – 366Combined sources
    Helixi37 – 5115Combined sources
    Beta strandi60 – 6910Combined sources
    Beta strandi85 – 906Combined sources
    Helixi94 – 974Combined sources
    Beta strandi105 – 11612Combined sources
    Helixi117 – 13620Combined sources
    Turni141 – 1433Combined sources
    Helixi145 – 1473Combined sources
    Beta strandi150 – 15910Combined sources
    Helixi169 – 1724Combined sources
    Turni175 – 1773Combined sources
    Beta strandi178 – 1847Combined sources
    Beta strandi188 – 1903Combined sources
    Helixi192 – 1943Combined sources
    Helixi198 – 20811Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JKYX-ray2.30A/B2-214[»]
    2JKZX-ray3.45A/B/C/D2-221[»]
    2XBUX-ray1.80A/B1-221[»]
    ProteinModelPortaliQ04178.
    SMRiQ04178. Positions 5-214.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ04178.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2236.
    GeneTreeiENSGT00390000007416.
    HOGENOMiHOG000170387.
    InParanoidiQ04178.
    KOiK07101.
    OMAiNNVHQLC.
    OrthoDBiEOG74J9MB.

    Family and domain databases

    Gene3Di3.40.50.2020. 1 hit.
    InterProiIPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    [Graphical view]
    PfamiPF00156. Pribosyltran. 1 hit.
    [Graphical view]
    SUPFAMiSSF53271. SSF53271. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q04178-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSANDKQYIS YNNVHQLCQV SAERIKNFKP DLIIAIGGGG FIPARILRTF
    60 70 80 90 100
    LKEPGVPTIR IFAIILSLYE DLNSVGSEVE EVGVKVSRTQ WIDYEQCKLD
    110 120 130 140 150
    LVGKNVLIVD EVDDTRTTLH YALSELEKDA AEQAKAKGID TEKSPEMKTN
    160 170 180 190 200
    FGIFVLHDKQ KPKKADLPAE MLNDKNRYFA AKTVPDKWYA YPWESTDIVF
    210 220
    HTRMAIEQGN DIFIPEQEHK Q
    Length:221
    Mass (Da):25,191
    Last modified:November 1, 1996 - v1
    Checksum:i0D18A02BAF8F5390
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U32274 Genomic DNA. Translation: AAB64840.1.
    BK006938 Genomic DNA. Translation: DAA12242.1.
    PIRiS69682.
    RefSeqiNP_010687.3. NM_001180707.3.

    Genome annotation databases

    EnsemblFungiiYDR399W; YDR399W; YDR399W.
    GeneIDi852008.
    KEGGisce:YDR399W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U32274 Genomic DNA. Translation: AAB64840.1.
    BK006938 Genomic DNA. Translation: DAA12242.1.
    PIRiS69682.
    RefSeqiNP_010687.3. NM_001180707.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JKYX-ray2.30A/B2-214[»]
    2JKZX-ray3.45A/B/C/D2-221[»]
    2XBUX-ray1.80A/B1-221[»]
    ProteinModelPortaliQ04178.
    SMRiQ04178. Positions 5-214.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi32460. 97 interactions.
    DIPiDIP-4318N.
    IntActiQ04178. 3 interactions.
    MINTiMINT-565941.

    Proteomic databases

    MaxQBiQ04178.
    PaxDbiQ04178.
    PeptideAtlasiQ04178.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYDR399W; YDR399W; YDR399W.
    GeneIDi852008.
    KEGGisce:YDR399W.

    Organism-specific databases

    CYGDiYDR399w.
    EuPathDBiFungiDB:YDR399W.
    SGDiS000002807. HPT1.

    Phylogenomic databases

    eggNOGiCOG2236.
    GeneTreeiENSGT00390000007416.
    HOGENOMiHOG000170387.
    InParanoidiQ04178.
    KOiK07101.
    OMAiNNVHQLC.
    OrthoDBiEOG74J9MB.

    Enzyme and pathway databases

    UniPathwayiUPA00591; UER00648.
    BioCyciMetaCyc:YDR399W-MONOMER.
    YEAST:YDR399W-MONOMER.
    SABIO-RKQ04178.

    Miscellaneous databases

    EvolutionaryTraceiQ04178.
    NextBioi970204.
    PROiQ04178.

    Family and domain databases

    Gene3Di3.40.50.2020. 1 hit.
    InterProiIPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    [Graphical view]
    PfamiPF00156. Pribosyltran. 1 hit.
    [Graphical view]
    SUPFAMiSSF53271. SSF53271. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "Purification and characterization of the hypoxanthine-guanine phosphoribosyltransferase from Saccharomyces cerevisiae."
      Schmidt R., Wiegand H., Reichert U.
      Eur. J. Biochem. 93:355-361(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    4. "Purification and characterization of hypoxanthine-guanine phosphoribosyltransferase from Saccharomyces cerevisiae."
      Nussbaum R.L., Caskey C.T.
      Biochemistry 20:4584-4590(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
    5. "Studies of the kinetic mechanism of hypoxanthine-guanine phosphoribosyltransferase from yeast."
      Ali L.Z., Sloan D.L.
      J. Biol. Chem. 257:1149-1155(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    6. "Adenine phosphoribosyltransferase mutants in Saccharomyces cerevisiae."
      Woods R.A., Roberts D.G., Stein D.S., Filpula D.
      J. Gen. Microbiol. 130:2629-2637(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "The isolation and characterization of Saccharomyces cerevisiae mutants that constitutively express purine biosynthetic genes."
      Guetsova M.L., Lecoq K., Daignan-Fornier B.
      Genetics 147:383-397(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Transcriptional regulation of the yeast gmp synthesis pathway by its end products."
      Escobar-Henriques M., Daignan-Fornier B.
      J. Biol. Chem. 276:1523-1530(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    12. "Lethal accumulation of guanylic nucleotides in Saccharomyces cerevisiae HPT1-deregulated mutants."
      Breton A., Pinson B., Coulpier F., Giraud M.F., Dautant A., Daignan-Fornier B.
      Genetics 178:815-824(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND GMP, CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION.

    Entry informationi

    Entry nameiHPRT_YEAST
    AccessioniPrimary (citable) accession number: Q04178
    Secondary accession number(s): D6VT32
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2006
    Last sequence update: November 1, 1996
    Last modified: July 22, 2015
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 36500 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    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
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.