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Q27541 (HPRT_CRIFA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 61. 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:HGPRT
OrganismCrithidia fasciculata
Taxonomic identifier5656 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeCrithidia

Protein attributes

Sequence length208 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 – 208208Hypoxanthine-guanine phosphoribosyltransferase
PRO_0000139595

Regions

Nucleotide binding122 – 1309GMP By similarity

Sites

Active site1261Proton acceptor By similarity
Metal binding1821Magnesium By similarity
Binding site631GMP By similarity
Binding site1541GMP By similarity
Binding site1821GMP; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q27541 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 7205B52781372EE1

FASTA20823,323
        10         20         30         40         50         60 
MSNAASPATS AAPVRHYPMS CRTLATQEQI WSATAKCAKQ IAEDYKQYNL SDENPLYLLC 

        70         80         90        100        110        120 
VLKGSFMFTA DLARFLCDEG VPVRIEFICA SSYGTDVKTS GEVRLLLDVR DPVENRHLLI 

       130        140        150        160        170        180 
VEDIVDSAIT LEYLKRFLQA KQPASLKTVV LLDKPSGRKV TLSVDYPVIT IPHAFVIGYG 

       190        200 
MDFAEAYREL RDVCVLKKEY YEKPASKL 

« Hide

References

[1]"Crithidia fasciculata: isolation, sequencing, and expression of the hypoxanthine-guanine phosphoribosyltransferase gene."
Jiang Y., Allen T.E., Carter D., Ray D.S., Ullman B.
Exp. Parasitol. 82:73-75(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U19968 Genomic DNA. Translation: AAB04164.1.

3D structure databases

ProteinModelPortalQ27541.
SMRQ27541. Positions 17-198.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_CRIFA
AccessionPrimary (citable) accession number: Q27541
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 61 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