UniProtKB - Q26998 (UPP_TOXGO)
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- BLAST
>sp|Q26998|UPP_TOXGO Uracil phosphoribosyltransferase OS=Toxoplasma gondii OX=5811 GN=uprt PE=1 SV=1 MAQVPASGKLLVDPRYSTNDQEESILQDIITRFPNVVLMKQTAQLRAMMTIIRDKETPKE EFVFYADRLIRLLIEEALNELPFEKKEVTTPLDVSYHGVSFYSKICGVSIVRAGESMESG LRAVCRGCRIGKILIQRDETTAEPKLIYEKLPADIRDRWVMLLDPMCATAGSVCKAIEVL LRLGVKEERIIFVNILAAPQGIERVFKEYPKVRMVTAAVDICLNSRYYIVPGIGDFGDRY FGTM
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Protein
Uracil phosphoribosyltransferase
Gene
uprt
Organism
Toxoplasma gondii
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Expression, purification, and characterization of uracil phosphoribosyltransferase from Toxoplasma gondii."
Carter D., Donald R.G.K., Roos D., Ullman B.
Mol. Biochem. Parasitol. 87:137-144(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-6, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- diphosphateEC:2.4.2.92 Publications
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.1"Expression, purification, and characterization of uracil phosphoribosyltransferase from Toxoplasma gondii."
Carter D., Donald R.G.K., Roos D., Ullman B.
Mol. Biochem. Parasitol. 87:137-144(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-6, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY. - Ref.3"The structural mechanism of GTP stabilized oligomerization and catalytic activation of the Toxoplasma gondii uracil phosphoribosyltransferase."
Schumacher M.A., Bashor C.J., Song M.H., Otsu K., Zhu S., Parry R.J., Ullman B., Brennan R.G.
Proc. Natl. Acad. Sci. U.S.A. 99:78-83(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF MUTANT VAL-128 IN COMPLEXES WITH URACIL; SUBSTRATE ANALOG AND GTP, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF LYS-59; ARG-68; LYS-150 AND ASP-235, CATALYTIC ACTIVITY.
Manual assertion based on experiment ini
- Ref.1"Expression, purification, and characterization of uracil phosphoribosyltransferase from Toxoplasma gondii."
Carter D., Donald R.G.K., Roos D., Ullman B.
Mol. Biochem. Parasitol. 87:137-144(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-6, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY. - Ref.3"The structural mechanism of GTP stabilized oligomerization and catalytic activation of the Toxoplasma gondii uracil phosphoribosyltransferase."
Schumacher M.A., Bashor C.J., Song M.H., Otsu K., Zhu S., Parry R.J., Ullman B., Brennan R.G.
Proc. Natl. Acad. Sci. U.S.A. 99:78-83(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF MUTANT VAL-128 IN COMPLEXES WITH URACIL; SUBSTRATE ANALOG AND GTP, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF LYS-59; ARG-68; LYS-150 AND ASP-235, CATALYTIC ACTIVITY.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
diphosphate- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
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+UMP- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
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=5-phospho-α-D-ribose 1-diphosphate- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
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+uracil- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
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<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
Mg2+1 Publication
Manual assertion based on experiment ini
- Ref.3"The structural mechanism of GTP stabilized oligomerization and catalytic activation of the Toxoplasma gondii uracil phosphoribosyltransferase."
Schumacher M.A., Bashor C.J., Song M.H., Otsu K., Zhu S., Parry R.J., Ullman B., Brennan R.G.
Proc. Natl. Acad. Sci. U.S.A. 99:78-83(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF MUTANT VAL-128 IN COMPLEXES WITH URACIL; SUBSTRATE ANALOG AND GTP, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF LYS-59; ARG-68; LYS-150 AND ASP-235, CATALYTIC ACTIVITY.
Manual assertion based on experiment ini
- Ref.3"The structural mechanism of GTP stabilized oligomerization and catalytic activation of the Toxoplasma gondii uracil phosphoribosyltransferase."
Schumacher M.A., Bashor C.J., Song M.H., Otsu K., Zhu S., Parry R.J., Ullman B., Brennan R.G.
Proc. Natl. Acad. Sci. U.S.A. 99:78-83(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF MUTANT VAL-128 IN COMPLEXES WITH URACIL; SUBSTRATE ANALOG AND GTP, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF LYS-59; ARG-68; LYS-150 AND ASP-235, CATALYTIC ACTIVITY.
<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Allosterically activated by GTP. Binding of GTP leads to 5-time activation of the enzyme.1 Publication
Manual assertion based on experiment ini
- Ref.3"The structural mechanism of GTP stabilized oligomerization and catalytic activation of the Toxoplasma gondii uracil phosphoribosyltransferase."
Schumacher M.A., Bashor C.J., Song M.H., Otsu K., Zhu S., Parry R.J., Ullman B., Brennan R.G.
Proc. Natl. Acad. Sci. U.S.A. 99:78-83(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF MUTANT VAL-128 IN COMPLEXES WITH URACIL; SUBSTRATE ANALOG AND GTP, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF LYS-59; ARG-68; LYS-150 AND ASP-235, CATALYTIC ACTIVITY.
<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=3.5 µM for uracil2 Publications
Manual assertion based on experiment ini
- Ref.1"Expression, purification, and characterization of uracil phosphoribosyltransferase from Toxoplasma gondii."
Carter D., Donald R.G.K., Roos D., Ullman B.
Mol. Biochem. Parasitol. 87:137-144(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-6, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY. - Ref.3"The structural mechanism of GTP stabilized oligomerization and catalytic activation of the Toxoplasma gondii uracil phosphoribosyltransferase."
Schumacher M.A., Bashor C.J., Song M.H., Otsu K., Zhu S., Parry R.J., Ullman B., Brennan R.G.
Proc. Natl. Acad. Sci. U.S.A. 99:78-83(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF MUTANT VAL-128 IN COMPLEXES WITH URACIL; SUBSTRATE ANALOG AND GTP, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF LYS-59; ARG-68; LYS-150 AND ASP-235, CATALYTIC ACTIVITY.
- KM=216 µM for 5-phospho-alpha-D-ribose 1-diphosphate (in the absence of GTP)2 Publications
Manual assertion based on experiment ini
- Ref.1"Expression, purification, and characterization of uracil phosphoribosyltransferase from Toxoplasma gondii."
Carter D., Donald R.G.K., Roos D., Ullman B.
Mol. Biochem. Parasitol. 87:137-144(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-6, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY. - Ref.3"The structural mechanism of GTP stabilized oligomerization and catalytic activation of the Toxoplasma gondii uracil phosphoribosyltransferase."
Schumacher M.A., Bashor C.J., Song M.H., Otsu K., Zhu S., Parry R.J., Ullman B., Brennan R.G.
Proc. Natl. Acad. Sci. U.S.A. 99:78-83(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF MUTANT VAL-128 IN COMPLEXES WITH URACIL; SUBSTRATE ANALOG AND GTP, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF LYS-59; ARG-68; LYS-150 AND ASP-235, CATALYTIC ACTIVITY.
- KM=37.4 µM for 5-phospho-alpha-D-ribose 1-diphosphate (in the presence of GTP)2 Publications
Manual assertion based on experiment ini
- Ref.1"Expression, purification, and characterization of uracil phosphoribosyltransferase from Toxoplasma gondii."
Carter D., Donald R.G.K., Roos D., Ullman B.
Mol. Biochem. Parasitol. 87:137-144(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-6, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY. - Ref.3"The structural mechanism of GTP stabilized oligomerization and catalytic activation of the Toxoplasma gondii uracil phosphoribosyltransferase."
Schumacher M.A., Bashor C.J., Song M.H., Otsu K., Zhu S., Parry R.J., Ullman B., Brennan R.G.
Proc. Natl. Acad. Sci. U.S.A. 99:78-83(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF MUTANT VAL-128 IN COMPLEXES WITH URACIL; SUBSTRATE ANALOG AND GTP, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF LYS-59; ARG-68; LYS-150 AND ASP-235, CATALYTIC ACTIVITY.
- Vmax=0.45 µmol/min/mg enzyme2 Publications
Manual assertion based on experiment ini
- Ref.1"Expression, purification, and characterization of uracil phosphoribosyltransferase from Toxoplasma gondii."
Carter D., Donald R.G.K., Roos D., Ullman B.
Mol. Biochem. Parasitol. 87:137-144(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-6, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY. - Ref.3"The structural mechanism of GTP stabilized oligomerization and catalytic activation of the Toxoplasma gondii uracil phosphoribosyltransferase."
Schumacher M.A., Bashor C.J., Song M.H., Otsu K., Zhu S., Parry R.J., Ullman B., Brennan R.G.
Proc. Natl. Acad. Sci. U.S.A. 99:78-83(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF MUTANT VAL-128 IN COMPLEXES WITH URACIL; SUBSTRATE ANALOG AND GTP, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF LYS-59; ARG-68; LYS-150 AND ASP-235, CATALYTIC ACTIVITY.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: UMP biosynthesis via salvage pathway
This protein is involved in step 1 of the subpathway that synthesizes UMP from uracil.Proteins known to be involved in this subpathway in this organism are:
- Uracil phosphoribosyltransferase (uprt)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes UMP from uracil, the pathway UMP biosynthesis via salvage pathway and in Pyrimidine metabolism.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 59 | GTPCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Binding sitei | 68 | GTPCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Binding sitei | 112 | 5-phospho-alpha-D-ribose 1-diphosphateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Binding sitei | 129 | GTPCombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 137 | 5-phospho-alpha-D-ribose 1-diphosphateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 158 | GTPCombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 164 | 5-phospho-alpha-D-ribose 1-diphosphateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 229 | Uracil; via amide nitrogenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Binding sitei | 235 | 5-phospho-alpha-D-ribose 1-diphosphateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 102 – 105 | GTPCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 4 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- GTP binding Source: UniProtKB-KW
- uracil phosphoribosyltransferase activity Source: UniProtKB-EC
GO - Biological processi
- UMP salvage Source: UniProtKB-UniPathway
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Allosteric enzyme, Glycosyltransferase, Transferase |
| Ligand | GTP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.4.2.9 6411 |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00574;UER00636 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Uracil phosphoribosyltransferase (EC:2.4.2.92 PublicationsManual assertion based on experiment ini
Short name: UPRT Short name: UPRTase Alternative name(s): UMP pyrophosphorylase |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:uprt |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Toxoplasma gondii |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 5811 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Alveolata › Apicomplexa › Conoidasida › Coccidia › Eucoccidiorida › Eimeriorina › Sarcocystidae › Toxoplasma |
<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 59 | K → A: GTP-induced enzymatic activation is reduced 4-fold. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 68 | R → A: GTP-induced enzymatic activation is reduced 2-fold. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 128 | C → V: No effect on activity. Far less oxidation sensitive than wild-type. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 150 | K → A: GTP-induced enzymatic activation is reduced 4-fold. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 235 | D → A or N: No enzymatic activity. 1 Publication Manual assertion based on experiment ini
| 1 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000120783 | 1 – 244 | Uracil phosphoribosyltransferaseAdd BLAST | 244 |
Proteomic databases
PRoteomics IDEntifications database More...PRIDEi | Q26998 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Monomer. Forms homodimers in presence of substrates and homotetramers in the presence of GTP.2 Publications
Manual assertion based on experiment ini
- Ref.1"Expression, purification, and characterization of uracil phosphoribosyltransferase from Toxoplasma gondii."
Carter D., Donald R.G.K., Roos D., Ullman B.
Mol. Biochem. Parasitol. 87:137-144(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-6, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY. - Ref.3"The structural mechanism of GTP stabilized oligomerization and catalytic activation of the Toxoplasma gondii uracil phosphoribosyltransferase."
Schumacher M.A., Bashor C.J., Song M.H., Otsu K., Zhu S., Parry R.J., Ullman B., Brennan R.G.
Proc. Natl. Acad. Sci. U.S.A. 99:78-83(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF MUTANT VAL-128 IN COMPLEXES WITH URACIL; SUBSTRATE ANALOG AND GTP, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF LYS-59; ARG-68; LYS-150 AND ASP-235, CATALYTIC ACTIVITY.
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 14 – 16 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 22 – 32 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| Beta strandi | 36 – 38 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 43 – 53 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| Helixi | 59 – 78 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 20 | |
| Beta strandi | 83 – 89 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 91 – 93 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 95 – 101 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 105 – 111 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Turni | 112 – 114 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 115 – 124 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 130 – 137 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 139 – 141 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 144 – 150 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 155 – 157 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 158 – 163 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 165 – 169 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 171 – 183 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| Helixi | 187 – 189 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 190 – 197 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 199 – 208 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 212 – 219 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 221 – 223 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 229 – 231 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 236 – 241 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q26998 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q26998 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q26998 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 164 – 172 | 5-phospho-alpha-D-ribose 1-diphosphate bindingCombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 9 | |
| Regioni | 234 – 236 | Uracil bindingCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 3 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the UPRTase family.Curated
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG4203 Eukaryota COG0035 LUCA |
Identification of Orthologs from Complete Genome Data More...OMAi | RICGYEI |
Family and domain databases
Conserved Domains Database More...CDDi | cd06223 PRTases_typeI, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000836 PRibTrfase_dom IPR029057 PRTase-like |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF53271 SSF53271, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
Q26998-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MAQVPASGKL LVDPRYSTND QEESILQDII TRFPNVVLMK QTAQLRAMMT
60 70 80 90 100
IIRDKETPKE EFVFYADRLI RLLIEEALNE LPFEKKEVTT PLDVSYHGVS
110 120 130 140 150
FYSKICGVSI VRAGESMESG LRAVCRGCRI GKILIQRDET TAEPKLIYEK
160 170 180 190 200
LPADIRDRWV MLLDPMCATA GSVCKAIEVL LRLGVKEERI IFVNILAAPQ
210 220 230 240
GIERVFKEYP KVRMVTAAVD ICLNSRYYIV PGIGDFGDRY FGTM
Length:244
Mass (Da):27,646
Last modified:November 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i1810CC234B2CE60F
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | U10246 Genomic DNA Translation: AAB60213.1 |
Genome annotation databases
Ensembl protists genome annotation project More...EnsemblProtistsi | TGME49_312480-t26_1; TGME49_312480-t26_1; TGME49_312480 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q26998 | Putative uracil phosphoribosyltransferase FUR1 | 244 | UniRef100_Q26998 | |||
| Putative uracil phosphoribosyltransferase FUR1 | 244 | |||||
| Putative uracil phosphoribosyltransferase FUR1 | 244 | |||||
| Putative uracil phosphoribosyltransferase FUR1 | 244 | |||||
| Putative uracil phosphoribosyltransferase FUR1 | 244 | |||||
| +9 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q26998 | Putative uracil phosphoribosyltransferase FUR1 | 244 | UniRef90_Q26998 | |||
| Putative uracil phosphoribosyltransferase FUR1 | 244 | |||||
| Putative uracil phosphoribosyltransferase FUR1 | 244 | |||||
| Putative uracil phosphoribosyltransferase FUR1 | 244 | |||||
| Putative uracil phosphoribosyltransferase FUR1 | 244 | |||||
| +12 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q26998 | Putative uracil phosphoribosyltransferase FUR1 | 244 | UniRef50_Q26998 | |||
| Putative uracil phosphoribosyltransferase FUR1 | 244 | |||||
| Putative uracil phosphoribosyltransferase FUR1 | 244 | |||||
| Putative uracil phosphoribosyltransferase FUR1 | 244 | |||||
| Putative uracil phosphoribosyltransferase FUR1 | 244 | |||||
| +21 | ||||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U10246 Genomic DNA Translation: AAB60213.1 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1BD3 | X-ray | 1.93 | A/B/C/D | 2-244 | [»] | |
| 1BD4 | X-ray | 2.20 | A/B/C/D | 2-244 | [»] | |
| 1JLR | X-ray | 2.45 | A/B/C/D | 2-244 | [»] | |
| 1JLS | X-ray | 2.50 | A/B/C/D | 2-244 | [»] | |
| 1UPF | X-ray | 2.30 | A/B/C/D | 21-244 | [»] | |
| 1UPU | X-ray | 2.50 | A/B/C/D | 21-244 | [»] | |
| ProteinModelPortali | Q26998 | |||||
| SMRi | Q26998 | |||||
| ModBasei | Search... | |||||
| MobiDBi | Search... | |||||
Proteomic databases
| PRIDEi | Q26998 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
| EnsemblProtistsi | TGME49_312480-t26_1; TGME49_312480-t26_1; TGME49_312480 |
Phylogenomic databases
| eggNOGi | KOG4203 Eukaryota COG0035 LUCA |
| OMAi | RICGYEI |
Enzyme and pathway databases
| UniPathwayi | UPA00574;UER00636 |
| BRENDAi | 2.4.2.9 6411 |
Miscellaneous databases
| EvolutionaryTracei | Q26998 |
Family and domain databases
| CDDi | cd06223 PRTases_typeI, 1 hit |
| InterProi | View protein in InterPro IPR000836 PRibTrfase_dom IPR029057 PRTase-like |
| SUPFAMi | SSF53271 SSF53271, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | UPP_TOXGO | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q26998Primary (citable) accession number: Q26998 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
| Last sequence update: | November 1, 1996 | |
| Last modified: | December 5, 2018 | |
| This is version 93 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - PATHWAY comments
Index of metabolic and biosynthesis pathways
