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Q839B2 (HPRT_ENTFA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 75. 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:EF_0264
OrganismEnterococcus faecalis (strain ATCC 700802 / V583) [Reference proteome] [HAMAP]
Taxonomic identifier226185 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus

Protein attributes

Sequence length181 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 181181Hypoxanthine-guanine phosphoribosyltransferase
PRO_0000139603

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
Binding site1531IMP; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q839B2 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 835B70765C543114

FASTA18120,272
        10         20         30         40         50         60 
MIEKDIEKVL ISKEEILAKS AELGKQLTEE YQGKNPLVVG ILKGAVPFMA DLTREINTYL 

        70         80         90        100        110        120 
ELDFMDVSSY GNATVSSGEV KIVKDLDTNV EGRHILIVED IIDSGRTLAY LVDLFRYRKA 

       130        140        150        160        170        180 
ASVKIVTLLD KPEGRVVDIK ADYVGFDVPN EFVVGYGLDY AETYRNLPYI GVLKPEVYES 


N 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016830 Genomic DNA. Translation: AAO80129.1.
RefSeqNP_814058.1. NC_004668.1.

3D structure databases

ProteinModelPortalQ839B2.
SMRQ839B2. Positions 4-178.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226185.EF0264.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO80129; AAO80129; EF_0264.
GeneID1199155.
KEGGefa:EF0264.
PATRIC21850921. VBIEntFae7065_0242.

Phylogenomic databases

eggNOGCOG0634.
KOK00760.
OMARGMEPDF.
OrthoDBEOG693GNP.

Enzyme and pathway databases

BioCycEFAE226185:GHI1-244-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.
PROSITEPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHPRT_ENTFA
AccessionPrimary (citable) accession number: Q839B2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: June 1, 2003
Last modified: June 11, 2014
This is version 75 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