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P00494 (HPRT_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Gene names
Name:HPRT1
Synonyms:HPRT
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length218 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Catalytic activity

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

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

Cofactor

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

Pathway

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

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm.

Miscellaneous

The cell lines from which this sequence was cloned are revertants from mutants with no detectable enzyme activity. The phenotypic reversions are the result of overproduction of variant enzymes because of gene amplification. This variant sequence is expected to be very similar to the wild-type.

Sequence similarities

Belongs to the purine/pyrimidine phosphoribosyltransferase family.

Ontologies

Keywords
   Biological processPurine salvage
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
Nucleotide-binding
   Molecular functionGlycosyltransferase
Transferase
   PTMAcetylation
Gene Ontology (GO)
   Biological_processGMP catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

IMP metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

IMP salvage

Inferred from electronic annotation. Source: UniProtKB-UniPathway

guanine salvage

Inferred from sequence or structural similarity. Source: UniProtKB

hypoxanthine metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

hypoxanthine salvage

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of dopamine metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

protein homotetramerization

Inferred from sequence or structural similarity. Source: UniProtKB

purine nucleotide biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

purine ribonucleoside salvage

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionguanine phosphoribosyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

hypoxanthine phosphoribosyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

magnesium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 218217Hypoxanthine-guanine phosphoribosyltransferase
PRO_0000139584

Regions

Nucleotide binding134 – 1429GMP By similarity
Nucleotide binding186 – 1883GMP By similarity

Sites

Active site1381Proton acceptor By similarity
Metal binding1941Magnesium By similarity
Binding site691GMP By similarity
Binding site1661GMP By similarity
Binding site1941GMP; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1031N6-acetyllysine By similarity

Experimental info

Sequence conflict321L → M in AAP13884. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P00494 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 21DA6A26D92B7511

FASTA21824,644
        10         20         30         40         50         60 
MATRSPSVVI SDDEPGYDLD LFCIPNHYVE DLEKVFIPHG VIMDRTERLA RDVMKEMGGH 

        70         80         90        100        110        120 
HIVALCVLKG GYKFFADLLD YIKALNRNSD RSIPMTVDFI RLKSYCNDQS TGDIKVIGGD 

       130        140        150        160        170        180 
DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV KRYNLKMVKV ASLLVKRTSR SVGYRPDFVG 

       190        200        210 
FEIPDKFVVG YALDYNEYFR DLNHICVISE TGKAKYKA 

« Hide

References

[1]"Hypoxanthine-guanine phosphoribosyltransferase genes of mouse and Chinese hamster: construction and sequence analysis of cDNA recombinants."
Konecki D.S., Brennand J., Fuscoe J.C., Caskey C.T., Chinault A.C.
Nucleic Acids Res. 10:6763-6775(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The Chinese hamster HPRT gene: restriction map, sequence analysis, and multiplex PCR deletion screen."
Rossiter B.J.F., Fuscoe J.C., Muzny D.M., Fox M., Caskey C.T.
Genomics 9:247-256(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Analysis of X-ray-induced HPRT mutations in CHO cells: insertion and deletions."
Fuscoe J.C., Zimmerman L.J., Fekete A., Setzer R.W., Rossiter B.J.
Mutat. Res. 269:171-183(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J00060 mRNA. Translation: AAA36990.1.
X53073 expand/collapse EMBL AC list , X53074, X53075, X53076, X53077, X53078, X53079, X53080 Genomic DNA. Translation: CAA37247.1.
S46270 Genomic DNA. Translation: AAP13884.1.
PIRRTHYG. S14402.

3D structure databases

ProteinModelPortalP00494.
SMRP00494. Positions 5-218.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP00494.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG000242.

Enzyme and pathway databases

UniPathwayUPA00591; UER00648.

Family and domain databases

Gene3D3.40.50.2020. 1 hit.
InterProIPR005904. Hxn_phspho_trans.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamPF00156. Pribosyltran. 1 hit.
[Graphical view]
SUPFAMSSF53271. SSF53271. 1 hit.
TIGRFAMsTIGR01203. HGPRTase. 1 hit.
PROSITEPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHPRT_CRIGR
AccessionPrimary (citable) accession number: P00494
Secondary accession number(s): Q80XX0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways