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Entry version 127 (29 Sep 2021)
Sequence version 1 (01 Mar 2003)
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Protein

Purine nucleoside phosphorylase

Gene

PNP

Organism
Plasmodium falciparum (isolate 3D7)
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

As part of the purine salvage pathway, catalyzes 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 (PubMed:18957439, PubMed:14982926, PubMed:16131758, PubMed:19575810, PubMed:24416224, PubMed:29440412).

Preferentially acts on inosine and guanosine, and to a lesser extent on 2'-deoxyguanosine and guanosine (PubMed:14982926, PubMed:16131758, PubMed:19575810).

Also catalyzes the phosphorylation of S-methyl-5'-thioinosine (MTI) to hypoxanthine; MTI is produced by adenosine deaminase (ADA)-mediated breakdown of S-methyl-5'-thioadenosine (MTA), a major by-product of polyamine biosynthesis (PubMed:18957439, PubMed:14982926, PubMed:24416224).

Generates hypoxanthine from both the purine salvage pathway and from polyamine metabolism which is required for nucleic acids synthesis (PubMed:18957439, PubMed:14982926, PubMed:24416224).

Has no activity towards adenosine (By similarity).

By similarity6 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

Inhibited by Immucillin-H and 5'-methylthio-Immucillin-H (PubMed:14982926, PubMed:24416224). Inhibited by 5'-deaza-1'-aza-2c-deoxy-1'-(9-methylene)-Immucilin-G (DADMe-ImmG) (PubMed:29440412).3 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 1.7 sec(-1) with inosine as substrate (PubMed:14982926, PubMed:24416224). kcat is 2.63 sec(-1) with inosine as substrate (PubMed:29440412). kcat is 1.1 sec(-1) with guanosine as substrate (PubMed:19575810). kcat is 1.5 sec(-1) with 2'-deoxyinosine as substrate (PubMed:19575810). kcat is 1.1 sec(-1) with 2'-deoxyguanosine as substrate (PubMed:19575810). kcat is 1.5 sec(-1) with 5'-methylthioinosine as substrate (PubMed:14982926). kcat is 0.83 sec(-1) with 5'-methylthioinosine as substrate (PubMed:24416224).4 Publications
  1. KM=4.7 µM for inosine (at 25 degrees Celsius and pH 7.5)2 Publications
  2. KM=11 µM for inosine (at pH 7.4)1 Publication
  3. KM=7.6 µM for inosine (at 25 degrees Celsius and pH 7.4)1 Publication
  4. KM=2.2 µM for guanosine1 Publication
  5. KM=25.3 µM for 2'-deoxyinosine1 Publication
  6. KM=16.3 µM for 2'-deoxyguanosine1 Publication
  7. KM=16 µM for 5'-methylthioinosine (at 25 degrees Celsius and pH 7.5)1 Publication
  8. KM=8.8 µM for 5'-methylthioinosine (at pH 7.4)1 Publication

<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: purine nucleoside salvage

This protein is involved in the pathway purine nucleoside salvage, which is part of Purine metabolism.6 Publications
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 sitei7Purine nucleoside; shared with dimeric partnerCombined sources2 Publications1
Binding sitei45Phosphate; shared with dimeric partnerCombined sources2 Publications2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei206Proton donor1 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

GO - Biological processi

<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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.2.1, 4889
2.4.2.3, 4889

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-PFA-73614, Pyrimidine salvage
R-PFA-73621, Pyrimidine catabolism

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

More...
UniPathwayi
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 phosphorylase1 Publication (EC:2.4.2.16 Publications)
Alternative name(s):
PfPNP1 Publication
S-methyl-5'-thioinosine phosphorylase1 Publication (EC:2.4.2.443 Publications)
<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:PNP1 Publication
ORF Names:PF3D7_0513300Imported
<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>OrganismiPlasmodium falciparum (isolate 3D7)Imported
<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 identifieri36329 [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 lineageiEukaryotaSarAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)
<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
  • UP000001450 <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 5

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
PlasmoDB:PF3D7_0513300

<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

Severe growth defect in host erythrocytes which is rescued by the addition of exogenous purines (PubMed:18957439). Loss of purine nucleoside phosphorylase activity (PubMed:18957439).1 Publication

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>Mutagenesisi7H → A: Slight decrease in catalytic activity towards inosine and 5'-methylthioinosine. 1 Publication1
Mutagenesisi7H → F: 23-fold decrease in catalytic efficiency for inosine as substrate. Slight decrease in catalytic efficiency for 5'-methylthioinosine as substrate. 1 Publication1
Mutagenesisi7H → S: Slight decrease in catalytic activity towards inosine. Slight increase in catalytic activity towards 5'-methylthioinosine. 1 Publication1
Mutagenesisi45R → A: 1300-fold decrease in catalytic efficiency for inosine as substrate. Loss of catalytic activity towards 5'-methylthioinosine. 1 Publication1
Mutagenesisi47Y → A: 790-fold decrease in catalytic efficiency for inosine as substrate. 4000-fold decrease in catalytic efficiency for 5'-methylthioinosine as substrate. 1 Publication1
Mutagenesisi66V → A: No effect on catalytic activity towards inosine. Slight increase in catalytic efficiency with 5'-methylthioinosine as substrate. 1 Publication1
Mutagenesisi66V → F: 40-fold decrease in catalytic efficiency with inosine as substrate. Loss of catalytic activity towards 5'-methylthioinosine. 1 Publication1
Mutagenesisi66V → I: No effect on catalytic activity towards inosine or 5'-methylthioinosine; when associated with I-73. 20-fold decrease in catalytic efficiency with 5'-methylthioinosine as substrate and no effect on catalytic activity towards inosine; when associated with F-160. 170-fold decrease in catalytic efficiency with 5'-methylthioinosine as substrate and no effect on catalytic activity towards inosine; when associated with I-73 and F-160. 1 Publication1
Mutagenesisi66V → S: 8-fold decrease in catalytic efficiency with inosine as substrate. Slight increase in catalytic efficiency with 5'-methylthioinosine as substrate. 1 Publication1
Mutagenesisi73V → A: Slight decrease in catalytic efficiency with inosine or 5'-methylthioinosine as substrates. 1 Publication1
Mutagenesisi73V → F: Loss of catalytic activity towards inosine and 5'-methylthioinosine. 1 Publication1
Mutagenesisi73V → I: No effect on catalytic activity towards inosine or 5'-methylthioinosine; when associated with I-66. 20-fold decrease in catalytic efficiency with 5'-methylthioinosine as substrate and no effect on catalytic activity towards inosine; when associated with F-160. 170-fold decrease in catalytic efficiency with 5'-methylthioinosine as substrate and no effect on catalytic activity towards inosine; when associated with I-66 and F-160. 1 Publication1
Mutagenesisi73V → S: Slight decrease in catalytic efficiency with inosine as substrate. 8500-fold decrease in catalytic efficiency with 5'-methylthioinosine as substrate. 1 Publication1
Mutagenesisi160Y → A: 680-fold decrease in catalytic efficiency with inosine as substrate. 200-fold decrease in catalytic efficiency with 5'-methylthioinosine as substrate. 1 Publication1
Mutagenesisi160Y → F: No effect on catalytic activity towards inosine. 14-fold decrease in catalytic efficiency with 5'-methylthioinosine as substrate. 20-fold decrease in catalytic efficiency with 5'-methylthioinosine as substrate; when associated with I-66 or I-73. 170-fold decrease in catalytic efficiency with 5'-methylthioinosine as substrate and no effect on catalytic activity towards inosine; when associated with I-66 and I-73. 1 Publication1
Mutagenesisi181V → D: 4-fold decrease in catalytic efficiency with inosine as substrate. Reduced affinity for DADMe-ImmG inhibitor. 1 Publication1
Mutagenesisi183M → A: 20-fold decrease in affinity for inosine. Loss of catalytic activity towards 5'-methylthioinosine. 1 Publication1
Mutagenesisi183M → L: 17300-fold decrease in catalytic efficiency with inosine as substrate. Reduced affinity for DADMe-ImmG inhibitor. 1 Publication1
Mutagenesisi206D → A: 200-fold decrease in catalytic efficiency with inosine as substrate. Loss of catalytic activity towards 5'-methylthioinosine. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4523389

Drug and drug target database

More...
DrugBanki
DB03881, (2S,3R,4S,5S)-3,4-Dihydroxy-2-[(methylsulfanyl)methyl]-5-(4-oxo-4,5-dihydro-1H-pyrrolo[3,2-d]pyrimidin-7-yl)pyrrolidinium
DB11638, Artenimol

<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_00004518251 – 245Purine nucleoside phosphorylaseAdd BLAST245

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q8I3X4

PTM databases

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q8I3X4

<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 provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed during the parasite blood stage, including in trophozoites (at protein level).1 Publication

<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

Homohexamer; trimer of homodimers.

3 Publications1 Publication

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
Q8I3X4, 1 interactor

<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

1245
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

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SMRi
Q8I3X4

Database of comparative protein structure models

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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
Q8I3X4

<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>Regioni23 – 27Phosphate bindingCombined sources2 Publications2 Publications5
Regioni88 – 91Phosphate bindingCombined sources2 Publications3 Publications4
Regioni183 – 184Purine nucleoside bindingCombined sources2 Publications1 Publication2

<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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_068457_0_1_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q8I3X4

Identification of Orthologs from Complete Genome Data

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OMAi
MSDVFHL

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q8I3X4

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

Pfam protein domain database

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

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53167, SSF53167, 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.

Q8I3X4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDNLLRHLKI SKEQITPVVL VVGDPGRVDK IKVVCDSYVD LAYNREYKSV
60 70 80 90 100
ECHYKGQKFL CVSHGVGSAG CAVCFEELCQ NGAKVIIRAG SCGSLQPDLI
110 120 130 140 150
KRGDICICNA AVREDRVSHL LIHGDFPAVG DFDVYDTLNK CAQELNVPVF
160 170 180 190 200
NGISVSSDMY YPNKIIPSRL EDYSKANAAV VEMELATLMV IGTLRKVKTG
210 220 230 240
GILIVDGCPF KWDEGDFDNN LVPHQLENMI KIALGACAKL ATKYA
Length:245
Mass (Da):26,858
Last modified:March 1, 2003 - 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:i2159E9731C410A23
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AL844504 Genomic DNA Translation: CAD51497.1

NCBI Reference Sequences

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RefSeqi
XP_001351690.1, XM_001351654.1

Genome annotation databases

Ensembl protists genome annotation project

More...
EnsemblProtistsi
CAD51497; CAD51497; PF3D7_0513300

GeneDB pathogen genome database from Sanger Institute

More...
GeneDBi
PF3D7_0513300.1:pep

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
812947

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
pfa:PF3D7_0513300

<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
AL844504 Genomic DNA Translation: CAD51497.1
RefSeqiXP_001351690.1, XM_001351654.1

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
1NW4X-ray2.20A/B/C/D/E/F2-245[»]
1Q1GX-ray2.02A/B/C/D/E/F2-245[»]
1SQ6X-ray2.40A1-245[»]
2BSXX-ray2.00A1-245[»]
3ENZX-ray2.03A/B/C/D/E/F1-245[»]
3FOWX-ray2.80A/B2-245[»]
3PHCX-ray2.00A/B/C/D/E/F2-245[»]
6AQSX-ray1.57A1-245[»]
6AQUX-ray2.60A/B1-245[»]
SMRiQ8I3X4
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiQ8I3X4, 1 interactor

Chemistry databases

ChEMBLiCHEMBL4523389
DrugBankiDB03881, (2S,3R,4S,5S)-3,4-Dihydroxy-2-[(methylsulfanyl)methyl]-5-(4-oxo-4,5-dihydro-1H-pyrrolo[3,2-d]pyrimidin-7-yl)pyrrolidinium
DB11638, Artenimol

PTM databases

SwissPalmiQ8I3X4

Proteomic databases

PRIDEiQ8I3X4

Genome annotation databases

EnsemblProtistsiCAD51497; CAD51497; PF3D7_0513300
GeneDBiPF3D7_0513300.1:pep
GeneIDi812947
KEGGipfa:PF3D7_0513300

Organism-specific databases

VEuPathDBiPlasmoDB:PF3D7_0513300

Phylogenomic databases

HOGENOMiCLU_068457_0_1_1
InParanoidiQ8I3X4
OMAiMSDVFHL
PhylomeDBiQ8I3X4

Enzyme and pathway databases

UniPathwayiUPA00606
BRENDAi2.4.2.1, 4889
2.4.2.3, 4889
ReactomeiR-PFA-73614, Pyrimidine salvage
R-PFA-73621, Pyrimidine catabolism

Miscellaneous databases

EvolutionaryTraceiQ8I3X4

Family and domain databases

Gene3Di3.40.50.1580, 1 hit
InterProiView protein in InterPro
IPR000845, Nucleoside_phosphorylase_d
IPR035994, Nucleoside_phosphorylase_sf
PfamiView protein in Pfam
PF01048, PNP_UDP_1, 1 hit
SUPFAMiSSF53167, SSF53167, 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 nameiPNPH_PLAF7
<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: Q8I3X4
<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: February 10, 2021
Last sequence update: March 1, 2003
Last modified: September 29, 2021
This is version 127 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, 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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