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Q04178

- HPRT_YEAST

UniProt

Q04178 - HPRT_YEAST

Protein

Hypoxanthine-guanine phosphoribosyltransferase

Gene

HPT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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

    Magnesium. 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

    Pathwayi

    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

    1. guanine phosphoribosyltransferase activity Source: UniProtKB-EC
    2. hypoxanthine phosphoribosyltransferase activity Source: SGD
    3. metal ion binding Source: UniProtKB-KW
    4. nucleotide binding Source: UniProtKB-KW

    GO - Biological processi

    1. GMP salvage Source: SGD
    2. IMP salvage Source: SGD
    3. purine ribonucleoside salvage Source: UniProtKB-KW

    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: Chromosome IV

    Organism-specific databases

    CYGDiYDR399w.
    SGDiS000002807. HPT1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    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.

    Expressioni

    Gene expression databases

    GenevestigatoriQ04178.

    Interactioni

    Subunit structurei

    Dimer.2 Publications

    Protein-protein interaction databases

    BioGridi32460. 98 interactions.
    DIPiDIP-4318N.
    IntActiQ04178. 3 interactions.
    MINTiMINT-565941.
    STRINGi4932.YDR399W.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK07101.
    OMAiRTQWIDY.
    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

    MSANDKQYIS YNNVHQLCQV SAERIKNFKP DLIIAIGGGG FIPARILRTF    50
    LKEPGVPTIR IFAIILSLYE DLNSVGSEVE EVGVKVSRTQ WIDYEQCKLD 100
    LVGKNVLIVD EVDDTRTTLH YALSELEKDA AEQAKAKGID TEKSPEMKTN 150
    FGIFVLHDKQ KPKKADLPAE MLNDKNRYFA AKTVPDKWYA YPWESTDIVF 200
    HTRMAIEQGN DIFIPEQEHK Q 221
    Length:221
    Mass (Da):25,191
    Last modified:November 1, 1996 - v1
    Checksum:i0D18A02BAF8F5390
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U32274 Genomic DNA. Translation: AAB64840.1 .
    BK006938 Genomic DNA. Translation: DAA12242.1 .
    PIRi S69682.
    RefSeqi NP_010687.3. NM_001180707.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JKY X-ray 2.30 A/B 2-214 [» ]
    2JKZ X-ray 3.45 A/B/C/D 2-221 [» ]
    2XBU X-ray 1.80 A/B 1-221 [» ]
    ProteinModelPortali Q04178.
    SMRi Q04178. Positions 5-214.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32460. 98 interactions.
    DIPi DIP-4318N.
    IntActi Q04178. 3 interactions.
    MINTi MINT-565941.
    STRINGi 4932.YDR399W.

    Proteomic databases

    MaxQBi Q04178.
    PaxDbi Q04178.
    PeptideAtlasi Q04178.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR399W ; YDR399W ; YDR399W .
    GeneIDi 852008.
    KEGGi sce:YDR399W.

    Organism-specific databases

    CYGDi YDR399w.
    SGDi S000002807. HPT1.

    Phylogenomic databases

    eggNOGi COG2236.
    GeneTreei ENSGT00390000007416.
    HOGENOMi HOG000170387.
    KOi K07101.
    OMAi RTQWIDY.
    OrthoDBi EOG74J9MB.

    Enzyme and pathway databases

    UniPathwayi UPA00591 ; UER00648 .
    BioCyci MetaCyc:YDR399W-MONOMER.
    YEAST:YDR399W-MONOMER.
    SABIO-RK Q04178.

    Miscellaneous databases

    EvolutionaryTracei Q04178.
    NextBioi 970204.

    Gene expression databases

    Genevestigatori Q04178.

    Family and domain databases

    Gene3Di 3.40.50.2020. 1 hit.
    InterProi IPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    [Graphical view ]
    Pfami PF00156. Pribosyltran. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53271. SSF53271. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 103 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