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Q5HRP4 (HPRT_STAEQ) 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
Gene names
Name:hpt
Ordered Locus Names:SERP0149
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length179 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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 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
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processIMP salvage

Inferred from electronic annotation. Source: UniProtKB-UniPathway

purine ribonucleoside salvage

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionguanine phosphoribosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

hypoxanthine phosphoribosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 179179Hypoxanthine-guanine phosphoribosyltransferase
PRO_0000139619

Regions

Nucleotide binding98 – 10710IMP By similarity
Nucleotide binding157 – 1582IMP By similarity

Sites

Active site1021Proton acceptor By similarity
Metal binding1581Magnesium By similarity
Binding site1301IMP By similarity
Binding site1521IMP; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HRP4 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: F80B151862CEF3CA

FASTA17920,185
        10         20         30         40         50         60 
MHKDLKNVLL SEEDIQNICK EMGAIITEDY KDRPLVCVGI LKGSVMFMAD LIKRIDTHLS 

        70         80         90        100        110        120 
IDFMDVSSYH GGTESTGEVQ ILKDLGASIE NKDVLIIEDI LETGTTLKSI TELLQSRKVN 

       130        140        150        160        170 
SLEIATLLDK PNRRKADIEA KYVGKKIPDE FVVGYGLDYR ELYRNLPYIG TLKAEVYSK 

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35984 / RP62A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000029 Genomic DNA. Translation: AAW53518.1.
RefSeqYP_187745.1. NC_002976.3.

3D structure databases

ProteinModelPortalQ5HRP4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING176279.SERP0149.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW53518; AAW53518; SERP0149.
GeneID3240531.
KEGGser:SERP0149.
PATRIC19611155. VBIStaEpi130894_0140.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0634.
HOGENOMHOG000236520.
KOK00760.
OMAVDFMTVS.
OrthoDBEOG693GNP.

Enzyme and pathway databases

BioCycSEPI176279:GJJB-153-MONOMER.
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.
ProtoNetSearch...

Entry information

Entry nameHPRT_STAEQ
AccessionPrimary (citable) accession number: Q5HRP4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: February 15, 2005
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)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways