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UniProtKB - Q26998 (UPP_TOXGO)

Entry version 103 (07 Apr 2021)
Sequence version 1 (01 Nov 1996)
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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>

<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>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

<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 PublicationNote: Binds 1 Mg2+ ion per subunit. The magnesium is bound as Mg-PRPP.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

<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

  1. KM=3.5 µM for uracil2 Publications
  2. KM=216 µM for 5-phospho-alpha-D-ribose 1-diphosphate (in the absence of GTP)2 Publications
  3. KM=37.4 µM for 5-phospho-alpha-D-ribose 1-diphosphate (in the presence of GTP)2 Publications
  1. Vmax=0.45 µmol/min/mg enzyme2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'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:
  1. Uracil phosphoribosyltransferase (uprt)
This subpathway is part of the pathway UMP biosynthesis via salvage pathway, which is itself part of Pyrimidine metabolism.
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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei59GTPCombined sources1 Publication1
Binding sitei68GTPCombined sources1 Publication1
Binding sitei1125-phospho-alpha-D-ribose 1-diphosphateCombined sources1 Publication1
Binding sitei129GTPCombined sources2 Publications1
Binding sitei1375-phospho-alpha-D-ribose 1-diphosphateCombined sources2 Publications1
Binding sitei158GTPCombined sources2 Publications1
Binding sitei1645-phospho-alpha-D-ribose 1-diphosphateCombined sources2 Publications1
Binding sitei229Uracil; via amide nitrogenCombined sources1 Publication1
Binding sitei2355-phospho-alpha-D-ribose 1-diphosphateCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi102 – 105GTPCombined sources1 Publication4

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionAllosteric enzyme, Glycosyltransferase, Transferase
LigandGTP-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%5Fand%5Ftaxonomy%5Fsection">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 Publications)
Short name:
UPRT
Short name:
UPRTase
Alternative name(s):
UMP pyrophosphorylase
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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>OrganismiToxoplasma gondii
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri5811 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Sar › Alveolata › Apicomplexa › Conoidasida › Coccidia › Eucoccidiorida › Eimeriorina › Sarcocystidae › Toxoplasma

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		ToxoDB:TGARI_312480
ToxoDB:TGCAST_312480
ToxoDB:TGCOUG_312480
ToxoDB:TGDOM2_312480
ToxoDB:TGFOU_312480
ToxoDB:TGGT1_312480
ToxoDB:TGMAS_312480
ToxoDB:TGME49_312480
ToxoDB:TGP89_312480
ToxoDB:TGPRC2_312480
ToxoDB:TGRH88_051740
ToxoDB:TGRUB_312480
ToxoDB:TGVAND_312480
ToxoDB:TGVEG_312480

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi59K → A: GTP-induced enzymatic activation is reduced 4-fold. 1 Publication1
Mutagenesisi68R → A: GTP-induced enzymatic activation is reduced 2-fold. 1 Publication1
Mutagenesisi128C → V: No effect on activity. Far less oxidation sensitive than wild-type. 1 Publication1
Mutagenesisi150K → A: GTP-induced enzymatic activation is reduced 4-fold. 1 Publication1
Mutagenesisi235D → A or N: No enzymatic activity. 1 Publication1

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001207831 – 244Uracil phosphoribosyltransferaseAdd BLAST244

<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%5Fsection">'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%5Fsection">'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

<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

1244
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q26998

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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 keyPosition(s)DescriptionActionsGraphical viewLength
<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>Regioni164 – 1725-phospho-alpha-D-ribose 1-diphosphate bindingCombined sources2 Publications9
Regioni234 – 236Uracil bindingCombined sources1 Publication3

<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

Identification of Orthologs from Complete Genome Data

More...OMAi		TYATRMP

Family and domain databases

Conserved Domains Database

More...CDDi		cd06223, PRTases_typeI, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.2020, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 basket
« Hide
        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
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links 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

<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...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BD3X-ray1.93A/B/C/D2-244[»]
1BD4X-ray2.20A/B/C/D2-244[»]
1JLRX-ray2.45A/B/C/D2-244[»]
1JLSX-ray2.50A/B/C/D2-244[»]
1UPFX-ray2.30A/B/C/D21-244[»]
1UPUX-ray2.50A/B/C/D21-244[»]
SMRiQ26998
ModBaseiSearch...
PDBe-KBiSearch...

Genome annotation databases

EnsemblProtistsiTGME49_312480-t26_1; TGME49_312480-t26_1; TGME49_312480

Organism-specific databases

VEuPathDBiToxoDB:TGARI_312480
ToxoDB:TGCAST_312480
ToxoDB:TGCOUG_312480
ToxoDB:TGDOM2_312480
ToxoDB:TGFOU_312480
ToxoDB:TGGT1_312480
ToxoDB:TGMAS_312480
ToxoDB:TGME49_312480
ToxoDB:TGP89_312480
ToxoDB:TGPRC2_312480
ToxoDB:TGRH88_051740
ToxoDB:TGRUB_312480
ToxoDB:TGVAND_312480
ToxoDB:TGVEG_312480

Phylogenomic databases

OMAiTYATRMP

Enzyme and pathway databases

UniPathwayiUPA00574;UER00636
BRENDAi2.4.2.9, 6411

Miscellaneous databases

EvolutionaryTraceiQ26998

Family and domain databases

CDDicd06223, PRTases_typeI, 1 hit
Gene3Di3.40.50.2020, 1 hit
InterProiView protein in InterPro
IPR000836, PRibTrfase_dom
IPR029057, PRTase-like
SUPFAMiSSF53271, SSF53271, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiUPP_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>AccessioniPrimary (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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 7, 2021
This is version 103 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 statusiReviewed (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 sequencing

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
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