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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

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
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.
SGDiS000002807. HPT1.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

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

Expressioni

Gene expression databases

GenevestigatoriQ04178.

Interactioni

Subunit structurei

Dimer.2 Publications

Protein-protein interaction databases

BioGridi32460. 99 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 – 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:October 31, 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. 99 interactions.
DIPiDIP-4318N.
IntActiQ04178. 3 interactions.
MINTiMINT-565941.
STRINGi4932.YDR399W.

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.
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.

Gene expression databases

GenevestigatoriQ04178.

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(1996) [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(1978) [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(1980) [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(1981) [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(1983) [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(1996) [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(2000) [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(2007) [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 30, 2006
Last sequence update: October 31, 1996
Last modified: January 6, 2015
This is version 106 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.