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

Cofactori

Mg2+1 PublicationNote: 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 – 2061Magnesium1 Publication
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
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-KW
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 phosphoribosyltransferasePRO_0000139599Add
BLAST

Interactioni

Subunit structurei

Homodimer at low ionic strength and homotetramer at high ionic strength.2 Publications

Structurei

Secondary structure

1
230
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83Combined sources
Beta strandi9 – 113Combined sources
Helixi29 – 313Combined sources
Turni36 – 416Combined sources
Beta strandi44 – 474Combined sources
Helixi49 – 6719Combined sources
Beta strandi72 – 787Combined sources
Turni79 – 813Combined sources
Helixi82 – 9817Combined sources
Beta strandi109 – 11911Combined sources
Beta strandi122 – 1309Combined sources
Helixi134 – 1374Combined sources
Beta strandi141 – 15212Combined sources
Helixi153 – 16311Combined sources
Beta strandi168 – 17811Combined sources
Beta strandi189 – 1957Combined sources
Beta strandi200 – 2023Combined sources
Turni208 – 2136Combined sources
Beta strandi215 – 2195Combined sources
Helixi222 – 2287Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

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

        10         20         30         40         50
MASKPIEDYG KGKGRIEPMY IPDNTFYNAD DFLVPPHCKP YIDKILLPGG
60 70 80 90 100
LVKDRVEKLA YDIHRTYFGE ELHIICILKG SRGFFNLLID YLATIQKYSG
110 120 130 140 150
RESSVPPFFE HYVRLKSYQN DNSTGQLTVL SDDLSIFRDK HVLIVEDIVD
160 170 180 190 200
TGFTLTEFGE RLKAVGPKSM RIATLVEKRT DRSNSLKGDF VGFSIEDVWI
210 220 230
VGCCYDFNEM FRDFDHVAVL SDAARKKFEK
Length:230
Mass (Da):26,386
Last modified:November 1, 1996 - v1
Checksum:iC3784254EF96361D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09219 mRNA. Translation: AAA57068.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09219 mRNA. Translation: AAA57068.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 83 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