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UniProtKB - P45563 (XAPA_ECOLI)

Entry version 146 (16 Oct 2019)
Sequence version 2 (01 Nov 1997)
Previous versions | rss
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Protein

Purine nucleoside phosphorylase 2

Gene

xapA

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

The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. This protein can degrade all purine nucleosides including xanthosine, inosine and guanosine, but cannot cleave adenosine, deoxyadenosine or hypoxanthine arabinoside. Has a preference for the neutral over the monoanionic form of xanthosine.4 Publications

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Rapidly inactivated by p-chloromercuriphenylsulfonic acid (p-CMB). Dithiothreitol incubation restores the activity.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=51 µM for xanthosine (at pH 7.0)1 Publication
  2. KM=72 µM for xanthosine (at 25 degrees Celsius and pH 7.1)1 Publication
  3. KM=110 µM for guanosine (at pH 7.0)1 Publication
  4. KM=155 µM for guanosine (at 25 degrees Celsius and pH 7.1)1 Publication
  5. KM=963 µM for inosine (at 25 degrees Celsius and pH 7.1)1 Publication
  6. KM=340 µM for inosine (at 25 degrees Celsius and pH 7.0)1 Publication
  7. KM=62 µM for 2'-deoxyinosine (at 25 degrees Celsius and pH 7.0)1 Publication
  8. KM=600 µM for 5'-deoxyinosine (at 25 degrees Celsius and pH 7.0)1 Publication
  9. KM=2600 µM for 2',3'-dideoxyinosine (at 25 degrees Celsius and pH 7.0)1 Publication
  10. KM=44 µM for 2'-deoxyguanosine (at 25 degrees Celsius and pH 7.0)1 Publication
  11. KM=3.3 µM for hypoxanthine (at 25 degrees Celsius and pH 7.0)1 Publication
  12. KM=4.1 µM for guanine (at 25 degrees Celsius and pH 7.0)1 Publication
  13. KM=760 µM for phosphate (at 25 degrees Celsius and pH 7.0)1 Publication
  14. KM=59 µM for alpha-D-ribose 1-phosphate (at 25 degrees Celsius and pH 7.0)1 Publication
  15. KM=58 µM for alpha-D-2'-deoxyribose 1-phosphate (at 25 degrees Celsius and pH 7.0)1 Publication
  1. Vmax=8.7 µmol/min/mg enzyme with xanthosine as substrate (at 25 degrees Celsius and pH 7.1)1 Publication
  2. Vmax=14.2 µmol/min/mg enzyme with guanosine as substrate (at 25 degrees Celsius and pH 7.1)1 Publication
  3. Vmax=11.9 µmol/min/mg enzyme with inosine as substrate (at 25 degrees Celsius and pH 7.1)1 Publication

pH dependencei

Optimum pH is 6.5-7.5 with guanosine as substrate. At pH higher than 7.5, there is a marked reduction in reaction rate and a steep drop at pH higher than 9. Below pH 6.5, there is a dramatic decrease in activity reaching virtually zero at pH 6.0. With xanthosine as substrate, the pH optimum is 5.8-7.2. In the reverse reaction with guanine or xanthine as substrates, the pH optimum is 6.5-8.0. The pH dependence of inosine cleavage does not vary between pH 6 and 8. Maximal activity with inosine as substrate is observed at pH 6.6.2 Publications

Temperature dependencei

The half-life at 45 degrees Celsius between pH 5 and 8 is 5 to 9 minutes.2 Publications

<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: xanthosine degradation

This protein is involved in the pathway xanthosine degradation, which is part of Purine metabolism.
View all proteins of this organism that are known to be involved in the pathway xanthosine degradation and in Purine metabolism.

Pathwayi: purine nucleoside salvage

This protein is involved in the pathway purine nucleoside salvage, which is part of Purine metabolism.
View all proteins of this organism that are known to be involved in the pathway purine nucleoside salvage and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei65PhosphateCombined sources1 Publication1
Binding sitei117Phosphate; via amide nitrogenCombined sources1 Publication1
Binding sitei197Purine nucleoside1 Publication1
Binding sitei216PhosphateCombined sources1 Publication1
Binding sitei239Purine nucleoside1 Publication1

<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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:XANTHOSINEPHOSPHORY-MONOMER
ECOL316407:JW2398-MONOMER
MetaCyc:XANTHOSINEPHOSPHORY-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.4.2.1 2026

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

More...UniPathwayi		UPA00119
UPA00606

<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:
Purine nucleoside phosphorylase 2 (EC:2.4.2.16 Publications)
Alternative name(s):
Inosine-guanosine phosphorylase
Purine nucleoside phosphorylase II
Short name:
PNP II
Xanthosine phosphorylase
<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:xapA
Synonyms:pndA
Ordered Locus Names:b2407, JW2398
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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

Organism-specific databases

Escherichia coli strain K12 genome database

More...EcoGenei		EG20250 xapA

<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

GO - Cellular componenti

Complete GO annotation on QuickGO ...

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Does not grow on xanthosine. Slightly increases inosine productivity compared to wild-type (5.6 g/l of inosine versus 4.6 g/l, respectively, from 40 g/l of glucose).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Mutagenesisi191Y → L: No detectable activity with xanthosine as substrate, but largely retains its activity against other substrates, namely inosine and guanosine, although with altered affinities, higher and lower respectively, and clearly reduced maximal velocities for both. 1 Publication1
Mutagenesisi239N → D: Catalyzes the phosphorolysis of adenosine with moderate efficiency, and essentially has lost all activity against the 6-oxo-purine substrates xanthosine, inosine and guanosine. 1 Publication1

Chemistry databases

Drug and drug target database

More...DrugBanki		DB02377 Guanine
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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001845551 – 277Purine nucleoside phosphorylase 2Add BLAST277

Proteomic databases

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

More...PaxDbi		P45563

PRoteomics IDEntifications database

More...PRIDEi		P45563

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By xanthosine and to a lesser extent by deoxyinosine. Full expression requires XapR-xanthosine DNA-binding transcriptional activator.3 Publications

<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

Hexamer. Dimer of trimers.

2 Publications

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4260565, 18 interactors

Protein interaction database and analysis system

More...IntActi		P45563, 4 interactors

STRING: functional protein association networks

More...STRINGi		511145.b2407

<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

1277
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		P45563

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		P45563

<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>Regioni85 – 87Phosphate 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 PNP/MTAP phosphorylase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4107U5R Bacteria
COG0005 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000045183

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P45563

KEGG Orthology (KO)

More...KOi		K03815

Database for complete collections of gene phylogenies

More...PhylomeDBi		P45563

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.1580, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000845 Nucleoside_phosphorylase_d
IPR035994 Nucleoside_phosphorylase_sf
IPR011268 Purine_phosphorylase
IPR018099 Purine_phosphorylase-2_CS
IPR010943 Xanthosine_phosphorylase

The PANTHER Classification System

More...PANTHERi		PTHR11904 PTHR11904, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01048 PNP_UDP_1, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000477 PurNPase, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53167 SSF53167, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01697 PNPH-PUNA-XAPA, 1 hit
TIGR01699 XAPA, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS01240 PNP_MTAP_2, 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>. 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_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.

P45563-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSQVQFSHNP LFCIDIIKTY KPDFTPRVAF ILGSGLGALA DQIENAVAIS 
        60         70         80         90        100
YEKLPGFPVS TVHGHAGELV LGHLQGVPVV CMKGRGHFYE GRGMTIMTDA 
       110        120        130        140        150
IRTFKLLGCE LLFCTNAAGS LRPEVGAGSL VALKDHINTM PGTPMVGLND 
       160        170        180        190        200
DRFGERFFSL ANAYDAEYRA LLQKVAKEEG FPLTEGVFVS YPGPNFETAA 
       210        220        230        240        250
EIRMMQIIGG DVVGMSVVPE VISARHCDLK VVAVSAITNM AEGLSDVKLS 
       260        270 
HAQTLAAAEL SKQNFINLIC GFLRKIA
Length:277
Mass (Da):29,835
Last modified:November 1, 1997 - v2
<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:iDD26545755C08F8B
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAA52049 differs from that shown. Reason: Frameshift.Curated

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 conflicti144P → A in CAA52049 (PubMed:7559336).Curated1
Sequence conflicti261S → H in CAA52049 (PubMed:7559336).Curated1
Sequence conflicti265F → L in CAA52049 (PubMed:7559336).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
X73828 Genomic DNA Translation: CAA52049.1 Frameshift.
U00096 Genomic DNA Translation: AAC75460.1
AP009048 Genomic DNA Translation: BAA16275.1

Protein sequence database of the Protein Information Resource

More...PIRi		F65014

NCBI Reference Sequences

More...RefSeqi		NP_416902.1, NC_000913.3
WP_000084573.1, NZ_STEB01000039.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC75460; AAC75460; b2407
BAA16275; BAA16275; BAA16275

Database of genes from NCBI RefSeq genomes

More...GeneIDi		946878

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW2398
eco:b2407

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.4325

<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
X73828 Genomic DNA Translation: CAA52049.1 Frameshift.
U00096 Genomic DNA Translation: AAC75460.1
AP009048 Genomic DNA Translation: BAA16275.1
PIRiF65014
RefSeqiNP_416902.1, NC_000913.3
WP_000084573.1, NZ_STEB01000039.1

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
1YQQX-ray2.60A/B/C1-277[»]
1YQUX-ray3.10A/B/C1-277[»]
1YR3X-ray3.20A/B/C/D/E/F1-277[»]
SMRiP45563
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4260565, 18 interactors
IntActiP45563, 4 interactors
STRINGi511145.b2407

Chemistry databases

DrugBankiDB02377 Guanine
DB02134 Xanthine

Proteomic databases

PaxDbiP45563
PRIDEiP45563

Genome annotation databases

EnsemblBacteriaiAAC75460; AAC75460; b2407
BAA16275; BAA16275; BAA16275
GeneIDi946878
KEGGiecj:JW2398
eco:b2407
PATRICifig|1411691.4.peg.4325

Organism-specific databases

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

More...EchoBASEi		EB4152
EcoGeneiEG20250 xapA

Phylogenomic databases

eggNOGiENOG4107U5R Bacteria
COG0005 LUCA
HOGENOMiHOG000045183
InParanoidiP45563
KOiK03815
PhylomeDBiP45563

Enzyme and pathway databases

UniPathwayiUPA00119
UPA00606
BioCyciEcoCyc:XANTHOSINEPHOSPHORY-MONOMER
ECOL316407:JW2398-MONOMER
MetaCyc:XANTHOSINEPHOSPHORY-MONOMER
BRENDAi2.4.2.1 2026

Miscellaneous databases

EvolutionaryTraceiP45563

Protein Ontology

More...PROi		PR:P45563

Family and domain databases

Gene3Di3.40.50.1580, 1 hit
InterProiView protein in InterPro
IPR000845 Nucleoside_phosphorylase_d
IPR035994 Nucleoside_phosphorylase_sf
IPR011268 Purine_phosphorylase
IPR018099 Purine_phosphorylase-2_CS
IPR010943 Xanthosine_phosphorylase
PANTHERiPTHR11904 PTHR11904, 1 hit
PfamiView protein in Pfam
PF01048 PNP_UDP_1, 1 hit
PIRSFiPIRSF000477 PurNPase, 1 hit
SUPFAMiSSF53167 SSF53167, 1 hit
TIGRFAMsiTIGR01697 PNPH-PUNA-XAPA, 1 hit
TIGR01699 XAPA, 1 hit
PROSITEiView protein in PROSITE
PS01240 PNP_MTAP_2, 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 nameiXAPA_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: P45563
Secondary accession number(s): P77325
<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 historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: October 16, 2019
This is version 146 of the entry and version 2 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, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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