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UniProtKB - P0A9M5 (XGPT_ECOLI)

Entry version 134 (25 May 2022)
Sequence version 1 (21 Jul 1986)
Previous versions | rss
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Protein

Xanthine-guanine phosphoribosyltransferase

Gene

gpt

Organism
Escherichia coli (strain K12)
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

Purine salvage pathway enzyme that catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of the 6-oxopurines guanine and xanthine to form the corresponding ribonucleotides GMP (guanosine 5'-monophosphate) and XMP (xanthosine 5'-monophosphate), with the release of PPi. To a lesser extent, also acts on hypoxanthine (PubMed:9100006, PubMed:3886014).

Does not ribophosphorylate adenine (PubMed:3886014).

2 Publications

Miscellaneous

E.coli cells express two distinct 6-oxopurine PRTases, with very different specificities for hypoxanthine, guanine, and xanthine. Salvage enzymes allow a more energy efficient synthesis of purine nucleoside monophosphates compared with the de novo pathway. The kinetic analysis suggests that E.coli HPRT is mainly responsible for the synthesis of IMP and that XGPRT primarily salvages guanine and xanthine.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 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

Inhibited by thioguanine, GMP and, to a lesser extent, by thioxanthine, azaxanthine and azaguanine (PubMed:3886014). Highly inhibited by nucleoside phosphonates, which are product analogs (PubMed:23927482).2 Publications

<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

kcat is 112.0 sec(-1) with guanine as substrate. kcat is 150.1 sec(-1) with xanthine as substrate. kcat is 54.8 sec(-1) with hypoxanthine as substrate (at pH 8.5).1 Publication
  1. KM=4.3 µM for guanine (at pH 8.5)1 Publication
  2. KM=30.5 µM for xanthine (at pH 8.5)1 Publication
  3. KM=90.8 µM for hypoxanthine (at pH 8.5)1 Publication
  4. KM=139 µM for 5-phospho-alpha-D-ribose 1-diphosphate (at pH 8.5)1 Publication
  5. KM=2.5 µM for guanine1 Publication
  6. KM=42 µM for xanthine1 Publication
  7. KM=182 µM for hypoxanthine1 Publication
  8. KM=38.5 µM for 5-phospho-alpha-D-ribose 1-diphosphate (with guanine as cosubstrate)1 Publication
  9. KM=100 µM for 5-phospho-alpha-D-ribose 1-diphosphate (with xanthine as cosubstrate)1 Publication

<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: GMP biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes GMP from guanine.1 Publication This subpathway is part of the pathway GMP biosynthesis via salvage pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes GMP from guanine, the pathway GMP biosynthesis via salvage pathway and in Purine metabolism.

Pathwayi: XMP biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes XMP from xanthine.1 Publication This subpathway is part of the pathway XMP biosynthesis via salvage pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes XMP from xanthine, the pathway XMP biosynthesis via salvage pathway and in Purine 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 sitei695-phospho-alpha-D-ribose 1-diphosphateCombined sources1 Publication1
Binding sitei69GMPCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi89Magnesium1 Publication1
Binding sitei92GuanineCombined sources1 Publication1
Binding sitei92XanthineCombined sources1 Publication1
Binding sitei135Guanine; via amide nitrogen and carbonyl oxygenCombined sources1 Publication1
Binding sitei135Xanthine; via amide nitrogen and carbonyl oxygenCombined 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 bindingi92 – 96GMPCombined sources1 Publication5
Nucleotide bindingi134 – 135GMPCombined sources1 Publication2

<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 functionGlycosyltransferase, Transferase
Biological processPurine salvage
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:GPT-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.4.2.22, 2026

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00602;UER00658
UPA00909;UER00887

<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:
Xanthine-guanine phosphoribosyltransferase3 Publications (EC:2.4.2.-2 Publications, EC:2.4.2.222 Publications)
Short name:
XGPRT1 Publication
Alternative name(s):
Xanthine phosphoribosyltransferase1 Publication
<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:gpt
Synonyms:gpp, gxu
Ordered Locus Names:b0238, JW0228
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

<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>Mutagenesisi59C → A: No effect on catalytic activity; increased stability. 1 Publication1
Mutagenesisi65 – 70HDNQRE → AAAAAA: No effect on affinity for xanthine and guanine substrates. However, the catalytic activity is highly reduced (200-fold when guanine is used as substrate) and the inhibition by GMP is also affected. 1 Publication6

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3988588

Drug and drug target database

More...DrugBanki		DB03942, Carboxylic PRPP
DB02377, Guanine
DB01972, Guanosine-5'-Monophosphate
DB02134, Xanthine

<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_00001396661 – 152Xanthine-guanine phosphoribosyltransferaseAdd BLAST152

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0A9M5

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P0A9M5

PRoteomics IDEntifications database

More...PRIDEi		P0A9M5

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P0A9M5

<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

Homotetramer.

2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4260989, 10 interactors

Protein interaction database and analysis system

More...IntActi		P0A9M5, 1 interactor

STRING: functional protein association networks

More...STRINGi		511145.b0238

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P0A9M5

<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

1152
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P0A9M5

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

More...SMRi		P0A9M5

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		P0A9M5

<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>Regioni37 – 385-phospho-alpha-D-ribose 1-diphosphate bindingCombined sources1 Publication2
Regioni88 – 965-phospho-alpha-D-ribose 1-diphosphate bindingCombined sources1 Publication9

<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 purine/pyrimidine phosphoribosyltransferase family. XGPT subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG2236, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_080904_3_0_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0A9M5

Identification of Orthologs from Complete Genome Data

More...OMAi		FHRDCRA

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0A9M5

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

HAMAP database of protein families

More...HAMAPi		MF_01903, XGPRT, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000836, PRibTrfase_dom
IPR029057, PRTase-like
IPR023747, Xanthine_Guanine_PRibTrfase

The PANTHER Classification System

More...PANTHERi		PTHR39563, PTHR39563, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00156, Pribosyltran, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53271, SSF53271, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00103, PUR_PYR_PR_TRANSFER, 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.

P0A9M5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSEKYIVTWD MLQIHARKLA SRLMPSEQWK GIIAVSRGGL VPGALLAREL 
        60         70         80         90        100
GIRHVDTVCI SSYDHDNQRE LKVLKRAEGD GEGFIVIDDL VDTGGTAVAI 
       110        120        130        140        150
REMYPKAHFV TIFAKPAGRP LVDDYVVDIP QDTWIEQPWD MGVVFVPPIS 

GR
Length:152
Mass (Da):16,971
Last modified:July 21, 1986 - 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:iF0AD813127E7200D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti122V → G in AAA23933 (PubMed:3540961).Curated1

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
X00221 Genomic DNA Translation: CAA25040.1
X00222 Genomic DNA Translation: CAA25041.1
M13422 Genomic DNA Translation: AAA23928.1
M12907 Genomic DNA Translation: AAA23932.1
M15035 Genomic DNA Translation: AAA23933.1
U70214 Genomic DNA Translation: AAB08658.1
U00096 Genomic DNA Translation: AAC73342.1
AP009048 Genomic DNA Translation: BAA77907.1
M10382 Genomic DNA Translation: AAA23931.1

Protein sequence database of the Protein Information Resource

More...PIRi		A00587, RTECGX

NCBI Reference Sequences

More...RefSeqi		NP_414773.1, NC_000913.3
WP_001291990.1, NZ_SSZK01000050.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC73342; AAC73342; b0238
BAA77907; BAA77907; BAA77907

Database of genes from NCBI RefSeq genomes

More...GeneIDi		66671444
944817

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW0228
eco:b0238

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.2045

<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
X00221 Genomic DNA Translation: CAA25040.1
X00222 Genomic DNA Translation: CAA25041.1
M13422 Genomic DNA Translation: AAA23928.1
M12907 Genomic DNA Translation: AAA23932.1
M15035 Genomic DNA Translation: AAA23933.1
U70214 Genomic DNA Translation: AAB08658.1
U00096 Genomic DNA Translation: AAC73342.1
AP009048 Genomic DNA Translation: BAA77907.1
M10382 Genomic DNA Translation: AAA23931.1
PIRiA00587, RTECGX
RefSeqiNP_414773.1, NC_000913.3
WP_001291990.1, NZ_SSZK01000050.1

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
1A95X-ray2.00A/B/C/D1-152[»]
1A96X-ray2.00A/B/C/D1-152[»]
1A97X-ray2.60A/B/C/D3-150[»]
1A98X-ray2.25A/B1-152[»]
1NULX-ray1.80A/B1-152[»]
4JITX-ray2.80A/B/C/D1-152[»]
4JLSX-ray2.20A/B/C/D/E/H/I/J1-152[»]
AlphaFoldDBiP0A9M5
SMRiP0A9M5
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4260989, 10 interactors
IntActiP0A9M5, 1 interactor
STRINGi511145.b0238

Chemistry databases

BindingDBiP0A9M5
ChEMBLiCHEMBL3988588
DrugBankiDB03942, Carboxylic PRPP
DB02377, Guanine
DB01972, Guanosine-5'-Monophosphate
DB02134, Xanthine

2D gel databases

SWISS-2DPAGEiP0A9M5

Proteomic databases

jPOSTiP0A9M5
PaxDbiP0A9M5
PRIDEiP0A9M5

Genome annotation databases

EnsemblBacteriaiAAC73342; AAC73342; b0238
BAA77907; BAA77907; BAA77907
GeneIDi66671444
944817
KEGGiecj:JW0228
eco:b0238
PATRICifig|1411691.4.peg.2045

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...EchoBASEi		EB0409

Phylogenomic databases

eggNOGiCOG2236, Bacteria
HOGENOMiCLU_080904_3_0_6
InParanoidiP0A9M5
OMAiFHRDCRA
PhylomeDBiP0A9M5

Enzyme and pathway databases

UniPathwayiUPA00602;UER00658
UPA00909;UER00887
BioCyciEcoCyc:GPT-MONOMER
BRENDAi2.4.2.22, 2026

Miscellaneous databases

EvolutionaryTraceiP0A9M5

Protein Ontology

More...PROi		PR:P0A9M5

Family and domain databases

CDDicd06223, PRTases_typeI, 1 hit
Gene3Di3.40.50.2020, 1 hit
HAMAPiMF_01903, XGPRT, 1 hit
InterProiView protein in InterPro
IPR000836, PRibTrfase_dom
IPR029057, PRTase-like
IPR023747, Xanthine_Guanine_PRibTrfase
PANTHERiPTHR39563, PTHR39563, 1 hit
PfamiView protein in Pfam
PF00156, Pribosyltran, 1 hit
SUPFAMiSSF53271, SSF53271, 1 hit
PROSITEiView protein in PROSITE
PS00103, PUR_PYR_PR_TRANSFER, 1 hit

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 nameiXGPT_ECOLI
<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: P0A9M5
Secondary accession number(s): P00501
<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: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 25, 2022
This is version 134 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)
Annotation programProkaryotic Protein Annotation Program

<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, Reference proteome

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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