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Q26997

- HGXR_TOXGO

UniProt

Q26997 - HGXR_TOXGO

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Protein
Hypoxanthine-guanine-xanthine phosphoribosyltransferase
Gene
HPRT
Organism
Toxoplasma gondii
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to the N9 of hypoxanthine, guanine or xanthine.1 Publication

Catalytic activityi

IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate.2 Publications
GMP + diphosphate = guanine + 5-phospho-alpha-D-ribose 1-diphosphate.2 Publications
5-phospho-alpha-D-ribose 1-diphosphate + xanthine = (9-D-ribosylxanthine)-5'-phosphate + phosphate.2 Publications

Cofactori

Binds 2 magnesium ions per subunit. The magnesium ions are essentially bound to the substrate and have few direct interactions with the protein.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei79 – 791GMP
Active sitei150 – 1501Proton acceptor2 Publications
Binding sitei178 – 1781GMP
Metal bindingi206 – 2061Magnesium
Binding sitei206 – 2061GMP; via carbonyl oxygen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi146 – 1549GMP
Nucleotide bindingi199 – 2002GMP

GO - Molecular functioni

  1. hypoxanthine phosphoribosyltransferase activity Source: InterPro
  2. metal ion binding Source: UniProtKB-KW
  3. nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  1. GMP salvage Source: UniProtKB-UniPathway
  2. IMP salvage Source: UniProtKB-UniPathway
  3. XMP salvage Source: UniProtKB-UniPathway
  4. purine ribonucleoside salvage Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine salvage

Keywords - Ligandi

Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00591; UER00648.
UPA00602; UER00658.
UPA00909; UER00887.

Names & Taxonomyi

Protein namesi
Recommended name:
Hypoxanthine-guanine-xanthine phosphoribosyltransferase (EC:2.4.2.-)
Short name:
HGPRT
Short name:
HGXPRT
Short name:
HGXPRTase
Gene namesi
Name:HPRT
OrganismiToxoplasma gondii
Taxonomic identifieri5811 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaConoidasidaCoccidiaEucoccidioridaEimeriorinaSarcocystidaeToxoplasma

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi150 – 1501D → A: Strongly reduced catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 230230Hypoxanthine-guanine-xanthine phosphoribosyltransferase
PRO_0000139599Add
BLAST

Interactioni

Subunit structurei

Homodimer at low ionic strength and homotetramer at high ionic strength.1 Publication

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83
Beta strandi9 – 113
Helixi29 – 313
Turni36 – 416
Beta strandi44 – 474
Helixi49 – 6719
Beta strandi72 – 787
Turni79 – 813
Helixi82 – 9817
Beta strandi109 – 11911
Beta strandi122 – 1309
Helixi134 – 1374
Beta strandi141 – 15212
Helixi153 – 16311
Beta strandi168 – 17811
Beta strandi189 – 1957
Beta strandi200 – 2023
Turni208 – 2136
Beta strandi215 – 2195
Helixi222 – 2287

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DBRX-ray2.40A/B/C/D1-230[»]
1FSGX-ray1.05A/C1-230[»]
1QK3X-ray1.65A/B/C/D1-230[»]
1QK4X-ray1.90A/B/C/D1-230[»]
1QK5X-ray1.60A/B1-230[»]
ProteinModelPortaliQ26997.
SMRiQ26997. Positions 1-230.

Miscellaneous databases

EvolutionaryTraceiQ26997.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
InterProiIPR005904. Hxn_phspho_trans.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamiPF00156. Pribosyltran. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR01203. HGPRTase. 1 hit.
PROSITEiPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q26997-1 [UniParc]FASTAAdd to Basket

« Hide

MASKPIEDYG KGKGRIEPMY IPDNTFYNAD DFLVPPHCKP YIDKILLPGG    50
LVKDRVEKLA YDIHRTYFGE ELHIICILKG SRGFFNLLID YLATIQKYSG 100
RESSVPPFFE HYVRLKSYQN DNSTGQLTVL SDDLSIFRDK HVLIVEDIVD 150
TGFTLTEFGE RLKAVGPKSM RIATLVEKRT DRSNSLKGDF VGFSIEDVWI 200
VGCCYDFNEM FRDFDHVAVL SDAARKKFEK 230
Length:230
Mass (Da):26,386
Last modified:November 1, 1996 - v1
Checksum:iC3784254EF96361D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U09219 mRNA. Translation: AAA57068.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U09219 mRNA. Translation: AAA57068.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DBR X-ray 2.40 A/B/C/D 1-230 [» ]
1FSG X-ray 1.05 A/C 1-230 [» ]
1QK3 X-ray 1.65 A/B/C/D 1-230 [» ]
1QK4 X-ray 1.90 A/B/C/D 1-230 [» ]
1QK5 X-ray 1.60 A/B 1-230 [» ]
ProteinModelPortali Q26997.
SMRi Q26997. Positions 1-230.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00591 ; UER00648 .
UPA00602 ; UER00658 .
UPA00909 ; UER00887 .

Miscellaneous databases

EvolutionaryTracei Q26997.

Family and domain databases

Gene3Di 3.40.50.2020. 1 hit.
InterProi IPR005904. Hxn_phspho_trans.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view ]
Pfami PF00156. Pribosyltran. 1 hit.
[Graphical view ]
SUPFAMi SSF53271. SSF53271. 1 hit.
TIGRFAMsi TIGR01203. HGPRTase. 1 hit.
PROSITEi PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Isolation and sequencing of a cDNA encoding the hypoxanthine-guanine phosphoribosyltransferase from Toxoplasma gondii."
    Vasanthakumar G., van Ginkel S., Parish G.
    Gene 147:153-154(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: RH.
  2. "Crystal structures of Toxoplasma gondii HGXPRTase reveal the catalytic role of a long flexible loop."
    Schumacher M.A., Carter D., Roos D.S., Ullman B., Brennan R.G.
    Nat. Struct. Biol. 3:881-887(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  3. "Crystal structures of the Toxoplasma gondii hypoxanthine-guanine phosphoribosyltransferase-GMP and -IMP complexes: comparison of purine binding interactions with the XMP complex."
    Heroux A., White E.L., Ross L.J., Borhani D.W.
    Biochemistry 38:14485-14494(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
  4. "Crystal structure of Toxoplasma gondii hypoxanthine-guanine phosphoribosyltransferase with bound XMP, pyrophosphate and two Mg2+ ions: insights into the catalytic mechanism."
    Heroux A., White E.L., Ross L.J., Davis R.L., Borhani D.W.
    Biochemistry 38:14495-14506(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF MUTANT ALA-150 IN COMPLEX WITH XMP; PYROPHOSPHATE AND MAGNESIUM IONS, COFACTOR, CATALYTIC ACTIVITY, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF ASP-150.
  5. "Substrate deformation in a hypoxanthine-guanine phosphoribosyltransferase ternary complex: the structural basis for catalysis."
    Heroux A., White E.L., Ross L.J., Kuzin A.P., Borhani D.W.
    Structure 8:1309-1318(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) IN COMPLEX WITH MAGNESIUM; PHOSPHORIBOSYLPYROPHOSPHATE AND 9-DEAZAGUANINE, CATALYTIC ACTIVITY, ACTIVE SITE, FUNCTION.

Entry informationi

Entry nameiHGXR_TOXGO
AccessioniPrimary (citable) accession number: Q26997
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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