Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P0A9J6 (RBSK_ECOLI)

Entry version 125 (17 Jun 2020)
Sequence version 1 (13 Aug 1987)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Ribokinase

Gene

rbsK

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

Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.UniRule annotation2 Publications

<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+UniRule annotation1 Publication1 Publication, Mn2+1 PublicationNote: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate (Probable). Also active with manganase (PubMed:16784868).UniRule annotation1 Publication1 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

Activated by a monovalent cation that binds near, but not in, the active site (PubMed:11786021). The most likely occupant of the site in vivo is potassium (PubMed:16784868, PubMed:11786021). Also activated by ammonium ion (PubMed:16784868). Ion binding induces a conformational change that may alter substrate affinity (Probable).UniRule annotation1 Publication2 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=0.213 mM for ATP1 Publication
  2. KM=0.279 mM for D-ribose1 Publication
  3. KM=1.41 mM for 2-deoxy-D-ribose1 Publication
  4. KM=32 mM for D-arabinose1 Publication
  5. KM=31.6 mM for D-xylose1 Publication
  6. KM=8.2 mM for D-fructose1 Publication
  7. KM=0.65 mM for ribose (at pH 6.2 in the presence of 0 mM inorganic phosphate)1 Publication
  8. KM=0.43 mM for ribose (at pH 6.2 in the presence of 0.5 mM inorganic phosphate)1 Publication
  9. KM=0.27 mM for ribose (at pH 6.2 in the presence of 1 mM inorganic phosphate)1 Publication
  10. KM=0.23 mM for ribose (at pH 6.2 in the presence of 5 mM inorganic phosphate)1 Publication
  11. KM=0.21 mM for ribose (at pH 6.2 in the presence of 20 mM inorganic phosphate)1 Publication
  1. Vmax=122 µmol/min/mg enzyme toward ATP1 Publication
  2. Vmax=81 µmol/min/mg enzyme toward D-ribose1 Publication
  3. Vmax=25 µmol/min/mg enzyme toward 2-deoxy-D-ribose1 Publication
  4. Vmax=0.6 µmol/min/mg enzyme toward D-arabinose1 Publication
  5. Vmax=0.86 µmol/min/mg enzyme toward D-xylose1 Publication
  6. Vmax=0.226 µmol/min/mg enzyme toward D-fructose1 Publication
  7. Vmax=7.6 pmol/min/mg enzyme (at pH 6.2 in the presence of 0 mM inorganic phosphate)1 Publication
  8. Vmax=32.0 pmol/min/mg enzyme (at pH 6.2 in the presence of 0.5 mM inorganic phosphate)1 Publication
  9. Vmax=59.6 pmol/min/mg enzyme (at pH 6.2 in the presence of 1 mM inorganic phosphate)1 Publication
  10. Vmax=139.4 pmol/min/mg enzyme (at pH 6.2 in the presence of 5 mM inorganic phosphate)1 Publication
  11. Vmax=172.4 pmol/min/mg enzyme (at pH 6.2 in the presence of 20 mM inorganic phosphate)1 Publication

pH dependencei

Optimum pH is 8-9.1 Publication

Temperature dependencei

Optimum temperature is 30-50 degrees Celsius.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: D-ribose degradation

This protein is involved in step 2 of the subpathway that synthesizes D-ribose 5-phosphate from beta-D-ribopyranose.UniRule annotation1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. D-ribose pyranase (rbsD), D-ribose pyranase (rbsD)
  2. Ribokinase (rbsK), Ribokinase (rbsK)
This subpathway is part of the pathway D-ribose degradation, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-ribose 5-phosphate from beta-D-ribopyranose, the pathway D-ribose degradation and in Carbohydrate 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 sitei143SubstrateUniRule annotation3 Publications1
Binding sitei187ATPUniRule annotation3 Publications1
<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 bindingi249PotassiumUniRule annotation1 Publication1
Metal bindingi251Potassium; via carbonyl oxygenUniRule annotation1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei255Proton acceptorUniRule annotation1 Publication1
Binding sitei255SubstrateUniRule annotation3 Publications1
Binding sitei279ATPUniRule annotation3 Publications1
Metal bindingi285Potassium; via carbonyl oxygenUniRule annotation1 Publication1
Metal bindingi288Potassium; via carbonyl oxygenUniRule annotation1 Publication1
Metal bindingi290Potassium; via carbonyl oxygenUniRule annotation1 Publication1
Metal bindingi294PotassiumUniRule annotation1 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 bindingi223 – 228ATPUniRule annotation3 Publications6
Nucleotide bindingi254 – 255ATPUniRule annotation2 Publications2

<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

  • ATP binding Source: UniProtKB-UniRule
  • metal ion binding Source: EcoCyc
  • ribokinase activity Source: EcoCyc
Complete GO annotation on QuickGO ...

GO - Biological processi

  • D-ribose catabolic process Source: EcoCyc
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 functionKinase, Transferase
Biological processCarbohydrate metabolism
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:RIBOKIN-MONOMER
ECOL316407:JW3731-MONOMER
MetaCyc:RIBOKIN-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.1.15 2026

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

More...UniPathwayi		UPA00916;UER00889

<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:
Ribokinase1 PublicationUniRule annotation (EC:2.7.1.15UniRule annotation2 Publications)
Short name:
RKUniRule annotation
<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:rbsK1 PublicationUniRule annotation
Ordered Locus Names:b3752, JW3731
<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

GO - Cellular componenti

Complete GO annotation on QuickGO ...

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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL5093

Drug and drug target database

More...DrugBanki		DB03909 Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate
DB01936 alpha-D-arabinofuranose
DB04444 Tetrafluoroaluminate Ion

<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_00000800971 – 309RibokinaseAdd BLAST309

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0A9J6

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

More...PaxDbi		P0A9J6

PRoteomics IDEntifications database

More...PRIDEi		P0A9J6

<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

Homodimer.

UniRule annotation1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4259582, 11 interactors

Database of interacting proteins

More...DIPi		DIP-36178N

Protein interaction database and analysis system

More...IntActi		P0A9J6, 3 interactors

STRING: functional protein association networks

More...STRINGi		511145.b3752

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P0A9J6

<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

1309
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		P0A9J6

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		P0A9J6

<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>Regioni14 – 16Substrate bindingUniRule annotation3 Publications3
Regioni42 – 46Substrate bindingUniRule annotation3 Publications5

<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 carbohydrate kinase PfkB family. Ribokinase subfamily.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4108RVA Bacteria
COG0524 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_027634_2_0_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0A9J6

KEGG Orthology (KO)

More...KOi		K00852

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0A9J6

Family and domain databases

Conserved Domains Database

More...CDDi		cd01174 ribokinase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.1190.20, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_01987 Ribokinase, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR002173 Carboh/pur_kinase_PfkB_CS
IPR011877 D_ribokin
IPR011611 PfkB_dom
IPR002139 Ribo/fructo_kinase
IPR029056 Ribokinase-like

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00294 PfkB, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00990 RIBOKINASE

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53613 SSF53613, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR02152 D_ribokin_bact, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00584 PFKB_KINASES_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%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.

P0A9J6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQNAGSLVVL GSINADHILN LQSFPTPGET VTGNHYQVAF GGKGANQAVA 
        60         70         80         90        100
AGRSGANIAF IACTGDDSIG ESVRQQLATD NIDITPVSVI KGESTGVALI 
       110        120        130        140        150
FVNGEGENVI GIHAGANAAL SPALVEAQRE RIANASALLM QLESPLESVM 
       160        170        180        190        200
AAAKIAHQNK TIVALNPAPA RELPDELLAL VDIITPNETE AEKLTGIRVE 
       210        220        230        240        250
NDEDAAKAAQ VLHEKGIRTV LITLGSRGVW ASVNGEGQRV PGFRVQAVDT 
       260        270        280        290        300
IAAGDTFNGA LITALLEEKP LPEAIRFAHA AAAIAVTRKG AQPSVPWREE 

IDAFLDRQR
Length:309
Mass (Da):32,291
Last modified:August 13, 1987 - 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:i753729B41E64060E
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M13169 Genomic DNA Translation: AAA51476.1
L10328 Genomic DNA Translation: AAA62105.1
U00096 Genomic DNA Translation: AAC76775.1
AP009048 Genomic DNA Translation: BAE77536.1

Protein sequence database of the Protein Information Resource

More...PIRi		A26305 KIECRB

NCBI Reference Sequences

More...RefSeqi		NP_418208.1, NC_000913.3
WP_001300603.1, NZ_STEB01000015.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76775; AAC76775; b3752
BAE77536; BAE77536; BAE77536

Database of genes from NCBI RefSeq genomes

More...GeneIDi		948260

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3731
eco:b3752

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.2948

<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
M13169 Genomic DNA Translation: AAA51476.1
L10328 Genomic DNA Translation: AAA62105.1
U00096 Genomic DNA Translation: AAC76775.1
AP009048 Genomic DNA Translation: BAE77536.1
PIRiA26305 KIECRB
RefSeqiNP_418208.1, NC_000913.3
WP_001300603.1, NZ_STEB01000015.1

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
1GQTX-ray2.34A/B/C/D1-309[»]
1RK2X-ray2.25A/B/C/D1-309[»]
1RKAX-ray2.30A1-309[»]
1RKDX-ray1.84A1-309[»]
1RKSX-ray2.40A1-309[»]
SMRiP0A9J6
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4259582, 11 interactors
DIPiDIP-36178N
IntActiP0A9J6, 3 interactors
STRINGi511145.b3752

Chemistry databases

BindingDBiP0A9J6
ChEMBLiCHEMBL5093
DrugBankiDB03909 Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate
DB01936 alpha-D-arabinofuranose
DB04444 Tetrafluoroaluminate Ion

Proteomic databases

jPOSTiP0A9J6
PaxDbiP0A9J6
PRIDEiP0A9J6

Genome annotation databases

EnsemblBacteriaiAAC76775; AAC76775; b3752
BAE77536; BAE77536; BAE77536
GeneIDi948260
KEGGiecj:JW3731
eco:b3752
PATRICifig|1411691.4.peg.2948

Organism-specific databases

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

More...EchoBASEi		EB0811

Phylogenomic databases

eggNOGiENOG4108RVA Bacteria
COG0524 LUCA
HOGENOMiCLU_027634_2_0_6
InParanoidiP0A9J6
KOiK00852
PhylomeDBiP0A9J6

Enzyme and pathway databases

UniPathwayiUPA00916;UER00889
BioCyciEcoCyc:RIBOKIN-MONOMER
ECOL316407:JW3731-MONOMER
MetaCyc:RIBOKIN-MONOMER
BRENDAi2.7.1.15 2026

Miscellaneous databases

EvolutionaryTraceiP0A9J6

Protein Ontology

More...PROi		PR:P0A9J6

Family and domain databases

CDDicd01174 ribokinase, 1 hit
Gene3Di3.40.1190.20, 1 hit
HAMAPiMF_01987 Ribokinase, 1 hit
InterProiView protein in InterPro
IPR002173 Carboh/pur_kinase_PfkB_CS
IPR011877 D_ribokin
IPR011611 PfkB_dom
IPR002139 Ribo/fructo_kinase
IPR029056 Ribokinase-like
PfamiView protein in Pfam
PF00294 PfkB, 1 hit
PRINTSiPR00990 RIBOKINASE
SUPFAMiSSF53613 SSF53613, 1 hit
TIGRFAMsiTIGR02152 D_ribokin_bact, 1 hit
PROSITEiView protein in PROSITE
PS00584 PFKB_KINASES_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 nameiRBSK_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: P0A9J6
Secondary accession number(s): P05054, Q2M870
<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: August 13, 1987
Last sequence update: August 13, 1987
Last modified: June 17, 2020
This is version 125 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again