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P43152 (HPRT_LEIDO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 65. 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
OrganismLeishmania donovani
Taxonomic identifier5661 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the purine/pyrimidine phosphoribosyltransferase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 211211Hypoxanthine-guanine phosphoribosyltransferase
PRO_0000139593

Regions

Nucleotide binding125 – 1339GMP By similarity

Sites

Active site1291Proton acceptor By similarity
Metal binding1851Magnesium By similarity
Binding site661GMP By similarity
Binding site1571GMP By similarity
Binding site1851GMP; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
P43152 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 7802A85B00CA2190

FASTA21123,612
        10         20         30         40         50         60 
MSNSAKSPSG PVGDEGRRNY PMSAHTLVTQ EQVWAATAKC AKKIAEDYRS FKLTTDNPLY 

        70         80         90        100        110        120 
LLCVLKGSFI FTADLARFLA DEGVPVKVEF ICASSYGTGV ETSGQVRMLL DVRDSVENRH 

       130        140        150        160        170        180 
ILIVEDIVDS AITLQYLMRF MLAKKPASLK TVVLLDKPSG RKVEVLVDYP VITIPHAFVI 

       190        200        210 
GYGMDYAESY RELRDICVLK KEYYEKPESK V 

« Hide

References

[1]"Cloning and expression of the hypoxanthine-guanine phosphoribosyltransferase from Leishmania donovani."
Allen T.E., Hwang H.Y., Jardim A., Olafson R., Ullman B.
Mol. Biochem. Parasitol. 73:133-143(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: MHOM/SD/62/1S.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L25412 Genomic DNA. Translation: AAB00074.1.
RefSeqXP_003860615.1. XM_003860567.1.

3D structure databases

ProteinModelPortalP43152.
SMRP43152. Positions 20-201.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID13386422.
KEGGldo:LDBPK_210980.

Phylogenomic databases

KOK00760.

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_LEIDO
AccessionPrimary (citable) accession number: P43152
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 11, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways