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

Q3SZ18 (HPRT_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 68. 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

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 By similarity.

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
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGMP catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

GMP salvage

Inferred from Biological aspect of Ancestor. Source: RefGenome

IMP metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

IMP salvage

Inferred from Biological aspect of Ancestor. Source: RefGenome

adenine salvage

Inferred from Biological aspect of Ancestor. Source: RefGenome

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

cytosol

Inferred from Biological aspect of Ancestor. Source: RefGenome

   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_0000257812

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

Sequences

Sequence LengthMass (Da)Tools
Q3SZ18 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 761695098A5B6A20

FASTA21824,498
        10         20         30         40         50         60 
MAARSPSVVI SDDEPGYDLN LFCIPNHYAE DLEKVFIPHG LIMDRTERLA RDVMKEMGGH 

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

       130        140        150        160        170        180 
DLSTLTGKNV LIVEDIIDTG KTMQTLLALV KKHKPKMVKV ASLLMKRTPR SVGYKPDFVG 

       190        200        210 
FEIPDKFVVG YALDYNEYFR DLNHVCVISE TGKAKYKA 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC103248 mRNA. Translation: AAI03249.1.
RefSeqNP_001029207.1. NM_001034035.2.
UniGeneBt.49238.

3D structure databases

ProteinModelPortalQ3SZ18.
SMRQ3SZ18. Positions 5-218.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000053015.

Proteomic databases

PaxDbQ3SZ18.
PRIDEQ3SZ18.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000019547; ENSBTAP00000019547; ENSBTAG00000014685.
GeneID281229.
KEGGbta:281229.

Organism-specific databases

CTD3251.

Phylogenomic databases

eggNOGCOG0634.
GeneTreeENSGT00390000017323.
HOGENOMHOG000236521.
HOVERGENHBG000242.
KOK00760.
OMAAREIMKG.
OrthoDBEOG7673CK.
TreeFamTF313367.

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...

Other

NextBio20805276.

Entry information

Entry nameHPRT_BOVIN
AccessionPrimary (citable) accession number: Q3SZ18
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 68 of the entry and version 3 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