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Protein

Ribose-phosphate pyrophosphokinase

Gene

prs

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

Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).UniRule annotation7 Publications

Miscellaneous

This enzyme uses a steady state ordered mechanism, where Mg2+ binds first, followed by Mg-ATP and lastly, ribose 5-phosphate.1 Publication

Caution

Although Mg2+ has been found in cristallography study, the positions do not correspond to the correct residues.1 Publication1 Publication

<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 ‘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+UniRule annotation1 Publication5 PublicationsNote: Binds 2 Mg2+ ions per subunit (Probable). Mn2+, Co2+ and Cd2+ are also accepted (PubMed:3009477, PubMed:2542328, PubMed:8679571, PubMed:9125530, PubMed:10954724).1 Publication5 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by inorganic phosphate (PubMed:3009477, PubMed:10954724). In addition to form a complex with ATP, Mg2+ also acts as a cofactor (PubMed:9125530). Strongly inhibited by ADP through competitive binding at the activation site and at a specific allosteric site (PubMed:3009477, PubMed:6290219,PubMed:9125530). Competitively inhibited by Ca2+ and ribose 1,5-bisphosphate (Rib-1,5-P2) (PubMed:2542328, PubMed:9125530). Less strongly inhibited by AMP, alpha,beta-methylene ATP (mATP), (2',3'-dialdehyde)-ATP (oATP) and 1-alpha,2-alpha,3-alpha-trihydroxy-4-beta-cyclopentanemethanol 5-phosphate (cRib-5-P) (PubMed:2542328, PubMed:7657655, PubMed:9125530).6 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

  1. KM=138 µM for Rib-5-P (at pH 8 and 37 degrees Celsius)1 Publication
  2. KM=230 µM for ATP (at pH 8 and 37 degrees Celsius)1 Publication
  3. KM=280 µM for Rib-5-P (at pH 8.5 and 37 degrees Celsius)1 Publication
  4. KM=300 µM for Rib-5-P (with 20 mM ATP at pH 8 and 37 degrees Celsius)1 Publication
  1. Vmax=129 µmol/min/mg enzyme toward Rib-5-P (at pH 8.5 and 37 degrees Celsius)1 Publication
  2. Vmax=143 µmol/min/mg enzyme toward ATP (at pH 8.5 and 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 9.7-9.8.1 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: 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I).UniRule annotation1 Publication
Proteins known to be involved in this subpathway in this organism are:
  1. Ribose-phosphate pyrophosphokinase (prs)
This subpathway is part of the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I), the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi131Magnesium 1UniRule annotation1
Metal bindingi170Magnesium 2UniRule annotation1
<p>This subsection of the ‘Function’ 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 sitei1941 Publication1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei196Ribose-5-phosphateUniRule annotation1
Binding sitei220Ribose-5-phosphateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi37 – 39ATPUniRule annotation3
Nucleotide bindingi96 – 97ATPUniRule annotation2

<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

  • 5-phosphoribose 1-diphosphate biosynthetic process Source: EcoCyc
  • nucleoside metabolic process Source: InterPro
  • nucleotide biosynthetic process Source: GO_Central
  • purine nucleotide biosynthetic process Source: GO_Central
  • ribonucleoside monophosphate biosynthetic process Source: UniProtKB-UniRule

<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, Kinase, Transferase
Biological processNucleotide biosynthesis
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:PRPPSYN-MONOMER
MetaCyc:PRPPSYN-MONOMER

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

More...
UniPathwayi
UPA00087;UER00172

<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:
Ribose-phosphate pyrophosphokinase1 PublicationUniRule annotation (EC:2.7.6.13 Publications4 Publications)
Short name:
RPPK1 PublicationUniRule annotation
Alternative name(s):
5-phospho-D-ribosyl alpha-1-diphosphateUniRule annotation
Phosphoribosyl diphosphate synthaseUniRule annotation
Phosphoribosyl pyrophosphate synthase1 PublicationUniRule annotation
Short name:
P-Rib-PP synthaseUniRule annotation
Short name:
PRPP synthaseUniRule annotation
Short name:
PRPPaseUniRule annotation
<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:prs1 PublicationUniRule annotation
Synonyms:prsA
Ordered Locus Names:b1207, JW1198
<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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
EG10774 prs

<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

Keywords - Cellular componenti

Cytoplasm

<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

Cells lacking this gene are unable to grow on nucleosides as purine source.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>Mutagenesisi220D → E: 4-fold decrease in the affinity binding for Rib-5-P in the presence of magnesium ions. In the presence of cobalt ions, it shows a 15-fold decrease in the affinity binding for Rib-5-P. 1 Publication1
Mutagenesisi220D → F: With magnesium or manganese ions, the affinity binding values for ATP and Rib-5-P are comparable to those of the wild-type. 1 Publication1
Mutagenesisi221D → A: The affinity binding for ATP is comparable to those of the wild-type, apart from a slight decrease in the presence of manganese ions. The affinity binding for Rib-5-P is greatly decreased in the presence of both manganese and cobalt ions but only about 2-fold in the presence of magnesium ions. 1 Publication1
Mutagenesisi224D → A: With magnesium or manganese ions, the affinity binding values for ATP and Rib-5-P are comparable to those of the wild-type. 1 Publication1
Mutagenesisi224D → S: With magnesium or manganese ions, the affinity binding values for ATP and Rib-5-P are comparable to those of the wild-type. 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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
<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_00001411342 – 315Ribose-phosphate pyrophosphokinaseAdd BLAST314

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P0A717

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0A717

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

More...
PaxDbi
P0A717

PRoteomics IDEntifications database

More...
PRIDEi
P0A717

<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.UniRule annotation

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
groLP0A6F52EBI-906827,EBI-543750

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4260813, 58 interactors

Database of interacting proteins

More...
DIPi
DIP-35839N

Protein interaction database and analysis system

More...
IntActi
P0A717, 155 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_1260

<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

1315
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4S2UX-ray2.71A2-315[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P0A717

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

More...
SMRi
P0A717

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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>Regioni224 – 228Ribose-5-phosphate bindingUniRule annotation5

<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 ribose-phosphate pyrophosphokinase family. Class I subfamily.1 PublicationUniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C5T Bacteria
COG0462 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000210452

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A717

KEGG Orthology (KO)

More...
KOi
K00948

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A717

Family and domain databases

Conserved Domains Database

More...
CDDi
cd06223 PRTases_typeI, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00583_B RibP_PPkinase_B, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000842 PRib_PP_synth_CS
IPR029099 Pribosyltran_N
IPR000836 PRibTrfase_dom
IPR029057 PRTase-like
IPR005946 Rib-P_diPkinase
IPR037515 Rib-P_diPkinase_bac

The PANTHER Classification System

More...
PANTHERi
PTHR10210 PTHR10210, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF14572 Pribosyl_synth, 1 hit
PF13793 Pribosyltran_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53271 SSF53271, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01251 ribP_PPkin, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00114 PRPP_SYNTHASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P0A717-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPDMKLFAGN ATPELAQRIA NRLYTSLGDA AVGRFSDGEV SVQINENVRG
60 70 80 90 100
GDIFIIQSTC APTNDNLMEL VVMVDALRRA SAGRITAVIP YFGYARQDRR
110 120 130 140 150
VRSARVPITA KVVADFLSSV GVDRVLTVDL HAEQIQGFFD VPVDNVFGSP
160 170 180 190 200
ILLEDMLQLN LDNPIVVSPD IGGVVRARAI AKLLNDTDMA IIDKRRPRAN
210 220 230 240 250
VSQVMHIIGD VAGRDCVLVD DMIDTGGTLC KAAEALKERG AKRVFAYATH
260 270 280 290 300
PIFSGNAANN LRNSVIDEVV VCDTIPLSDE IKSLPNVRTL TLSGMLAEAI
310
RRISNEESIS AMFEH
Length:315
Mass (Da):34,218
Last modified:January 23, 2007 - 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:i4D69B7D118F93720
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 conflicti127T → I in AAA24431 (PubMed:3009477).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti129D → A in mutant PRSA1; alters the binding of divalent cations, especially magnesium. Little alteration in the affinity for ribose 5-phosphate and 27-fold decrease of the affinity for ATP. Absence of inhibition by AMP. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M13174 Genomic DNA Translation: AAA24431.1
U00096 Genomic DNA Translation: AAC74291.1
AP009048 Genomic DNA Translation: BAA36065.1

Protein sequence database of the Protein Information Resource

More...
PIRi
D64867 KIECRY

NCBI Reference Sequences

More...
RefSeqi
NP_415725.1, NC_000913.3
WP_001298109.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC74291; AAC74291; b1207
BAA36065; BAA36065; BAA36065

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
945772

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW1198
eco:b1207

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|511145.12.peg.1255

<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
M13174 Genomic DNA Translation: AAA24431.1
U00096 Genomic DNA Translation: AAC74291.1
AP009048 Genomic DNA Translation: BAA36065.1
PIRiD64867 KIECRY
RefSeqiNP_415725.1, NC_000913.3
WP_001298109.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4S2UX-ray2.71A2-315[»]
ProteinModelPortaliP0A717
SMRiP0A717
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260813, 58 interactors
DIPiDIP-35839N
IntActiP0A717, 155 interactors
STRINGi316385.ECDH10B_1260

Proteomic databases

EPDiP0A717
jPOSTiP0A717
PaxDbiP0A717
PRIDEiP0A717

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74291; AAC74291; b1207
BAA36065; BAA36065; BAA36065
GeneIDi945772
KEGGiecj:JW1198
eco:b1207
PATRICifig|511145.12.peg.1255

Organism-specific databases

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

More...
EchoBASEi
EB0767
EcoGeneiEG10774 prs

Phylogenomic databases

eggNOGiENOG4105C5T Bacteria
COG0462 LUCA
HOGENOMiHOG000210452
InParanoidiP0A717
KOiK00948
PhylomeDBiP0A717

Enzyme and pathway databases

UniPathwayi
UPA00087;UER00172

BioCyciEcoCyc:PRPPSYN-MONOMER
MetaCyc:PRPPSYN-MONOMER

Miscellaneous databases

Protein Ontology

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PROi
PR:P0A717

Family and domain databases

CDDicd06223 PRTases_typeI, 1 hit
HAMAPiMF_00583_B RibP_PPkinase_B, 1 hit
InterProiView protein in InterPro
IPR000842 PRib_PP_synth_CS
IPR029099 Pribosyltran_N
IPR000836 PRibTrfase_dom
IPR029057 PRTase-like
IPR005946 Rib-P_diPkinase
IPR037515 Rib-P_diPkinase_bac
PANTHERiPTHR10210 PTHR10210, 1 hit
PfamiView protein in Pfam
PF14572 Pribosyl_synth, 1 hit
PF13793 Pribosyltran_N, 1 hit
SUPFAMiSSF53271 SSF53271, 1 hit
TIGRFAMsiTIGR01251 ribP_PPkin, 1 hit
PROSITEiView protein in PROSITE
PS00114 PRPP_SYNTHASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiKPRS_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: P0A717
Secondary accession number(s): P08330, P76828, P78058
<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: August 1, 1988
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 121 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, Direct protein sequencing, Reference proteome

Documents

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