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

P09383 (HPRT_SCHMA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 74. 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
OrganismSchistosoma mansoni (Blood fluke)
Taxonomic identifier6183 [NCBI]
Taxonomic lineageEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

Protein attributes

Sequence length284 AA.
Sequence statusComplete.
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.

Sequence similarities

Belongs to the purine/pyrimidine phosphoribosyltransferase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 284284Hypoxanthine-guanine phosphoribosyltransferase
PRO_0000139594

Regions

Nucleotide binding194 – 2029GMP By similarity

Sites

Active site1981Proton acceptor By similarity
Metal binding2531Magnesium By similarity
Binding site1291GMP By similarity
Binding site2261GMP By similarity
Binding site2531GMP; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
P09383 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 5C2492D6ADFC6654

FASTA28431,854
        10         20         30         40         50         60 
MLTSLITSST TVTLTLSQIY YILDIACGFL ISVLVWMNSS VLDNGNHSNP QIRDMSSNMI 

        70         80         90        100        110        120 
KADCVVIEDS FRGFPTEYFC TSPRYDECLD YVLIPNGMIK DRLEKMSMDI VDYYEACNAT 

       130        140        150        160        170        180 
SITLMCVLKG GFKFLADLVD GLERTVRARG IVLPMSVEFV RVKSYVNDVS IHEPILTGLG 

       190        200        210        220        230        240 
DPSEYKDKNV LVVEDIIDTG KTITKLISHL DSLSTKSVKV ASLLVKRTSP RNDYRPDVGF 

       250        260        270        280 
EVPNRFVVGY ALDYNDNFRD LHHICVINEV GQKKFSVPCT SKPV 

« Hide

References

[1]"Analysis of cDNA encoding the hypoxanthine-guanine phosphoribosyltransferase (HGPRTase) of Schistosoma mansoni; a putative target for chemotherapy."
Craig S.P., McKerrow J.H., Newport G.N., Wang C.C.
Nucleic Acids Res. 16:7087-7101(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Puerto Rican.
[2]"Evidence for a class of very small introns in the gene for hypoxanthine-guanine phosphoribosyltransferase in Schistosoma mansoni."
Craig S.P., Muralidhar M.G., McKerrow J.H., Wang C.C.
Nucleic Acids Res. 17:1635-1647(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Puerto Rican.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07883 mRNA. Translation: CAA30730.1. Sequence problems.
X13531 expand/collapse EMBL AC list , X13532, X13533, X13534 Genomic DNA. Translation: CAA31885.1.
PIRS04278.
S09614.

3D structure databases

ProteinModelPortalP09383.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOGENOMHOG000236521.

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_SCHMA
AccessionPrimary (citable) accession number: P09383
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 11, 2014
This is version 74 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