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Q8DWM8 (HPRT_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 78. 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:SMU_14
OrganismStreptococcus mutans serotype c (strain ATCC 700610 / UA159) [Complete proteome] [HAMAP]
Taxonomic identifier210007 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length180 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 – 180180Hypoxanthine-guanine phosphoribosyltransferase
PRO_0000139622

Regions

Nucleotide binding99 – 10810IMP By similarity
Nucleotide binding158 – 1592IMP By similarity

Sites

Active site1031Proton acceptor By similarity
Metal binding1591Magnesium By similarity
Binding site1311IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DWM8 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: D7855D2A08683D56

FASTA18020,542
        10         20         30         40         50         60 
MLEQNIKKVL YSEEEIIVKT KELGAQLTKD YAGKNPLLVG VLKGSVPFMA ELMKHIDTHI 

        70         80         90        100        110        120 
EIDFMVVSSY HGGTTSSGEV KILKDVDTNI ENRDVIFIED IIDTGRTLKY LRDMFKYRQA 

       130        140        150        160        170        180 
NSVRIATLFD KPEGRVVDID ADYVCYKVPN EFIVGFGLDY AENYRNLPYV GVLKEDVYSK 

« Hide

References

[1]"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen."
Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.
Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014133 Genomic DNA. Translation: AAN57805.1.
RefSeqNP_720499.1. NC_004350.2.

3D structure databases

ProteinModelPortalQ8DWM8.
SMRQ8DWM8. Positions 4-178.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING210007.SMU.14.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN57805; AAN57805; SMU_14.
GeneID1027835.
KEGGsmu:SMU_14.
PATRIC19662275. VBIStrMut61772_0012.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0634.
KOK00760.
OMAEEDIAGK.
OrthoDBEOG693GNP.
PhylomeDBQ8DWM8.

Enzyme and pathway databases

BioCycSMUT210007:GC7Z-12-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_STRMU
AccessionPrimary (citable) accession number: Q8DWM8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 78 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