Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q04178 (HPRT_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hypoxanthine-guanine phosphoribosyltransferase

Short name=HGPRT
Short name=HGPRTase
EC=2.4.2.8
Alternative name(s):
Bypass of repression by adenine protein 6
Gene names
Name:HPT1
Synonyms:BRA6
Ordered Locus Names:YDR399W
ORF Names:D9509.18
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length221 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.12

Catalytic activity

IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate. Ref.12

GMP + diphosphate = guanine + 5-phospho-alpha-D-ribose 1-diphosphate. Ref.12

Cofactor

Magnesium. The magnesium ions are essentially bound to the substrate and have few direct interactions with the protein.

Enzyme regulation

Subject to feedback inhibition by GMP. Ref.12

Pathway

Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1.

Subunit structure

Dimer. Ref.4

Subcellular location

Cytoplasm. Nucleus Ref.9.

Miscellaneous

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

Sequence similarities

Belongs to the purine/pyrimidine phosphoribosyltransferase family.

Biophysicochemical properties

Kinetic parameters:

KM=23 µM for hypoxanthine Ref.3 Ref.4 Ref.5

KM=18 µM for guanine

KM=50 µM for phosphoribosylpyrophosphate

pH dependence:

Optimum pH is 8.5.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 221220Hypoxanthine-guanine phosphoribosyltransferase
PRO_0000257807

Regions

Nucleotide binding110 – 1189GMP
Nucleotide binding188 – 1947GMP

Sites

Active site1141Proton acceptor By similarity
Binding site851GMP
Binding site1591GMP

Amino acid modifications

Modified residue21N-acetylserine Ref.11

Secondary structure

................................... 221
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q04178 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 0D18A02BAF8F5390

FASTA22125,191
        10         20         30         40         50         60 
MSANDKQYIS YNNVHQLCQV SAERIKNFKP DLIIAIGGGG FIPARILRTF LKEPGVPTIR 

        70         80         90        100        110        120 
IFAIILSLYE DLNSVGSEVE EVGVKVSRTQ WIDYEQCKLD LVGKNVLIVD EVDDTRTTLH 

       130        140        150        160        170        180 
YALSELEKDA AEQAKAKGID TEKSPEMKTN FGIFVLHDKQ KPKKADLPAE MLNDKNRYFA 

       190        200        210        220 
AKTVPDKWYA YPWESTDIVF HTRMAIEQGN DIFIPEQEHK Q 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[10]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U32274 Genomic DNA. Translation: AAB64840.1.
BK006938 Genomic DNA. Translation: DAA12242.1.
PIRS69682.
RefSeqNP_010687.3. NM_001180707.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JKYX-ray2.30A/B2-214[»]
2JKZX-ray3.45A/B/C/D2-221[»]
2XBUX-ray1.80A/B1-221[»]
ProteinModelPortalQ04178.
SMRQ04178. Positions 5-214.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32460. 98 interactions.
DIPDIP-4318N.
IntActQ04178. 3 interactions.
MINTMINT-565941.
STRING4932.YDR399W.

Proteomic databases

MaxQBQ04178.
PaxDbQ04178.
PeptideAtlasQ04178.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR399W; YDR399W; YDR399W.
GeneID852008.
KEGGsce:YDR399W.

Organism-specific databases

CYGDYDR399w.
SGDS000002807. HPT1.

Phylogenomic databases

eggNOGCOG2236.
GeneTreeENSGT00390000007416.
HOGENOMHOG000170387.
KOK07101.
OMARTQWIDY.
OrthoDBEOG74J9MB.

Enzyme and pathway databases

BioCycMetaCyc:YDR399W-MONOMER.
YEAST:YDR399W-MONOMER.
SABIO-RKQ04178.
UniPathwayUPA00591; UER00648.

Gene expression databases

GenevestigatorQ04178.

Family and domain databases

Gene3D3.40.50.2020. 1 hit.
InterProIPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamPF00156. Pribosyltran. 1 hit.
[Graphical view]
SUPFAMSSF53271. SSF53271. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ04178.
NextBio970204.

Entry information

Entry nameHPRT_YEAST
AccessionPrimary (citable) accession number: Q04178
Secondary accession number(s): D6VT32
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways