UniProtKB - P0A9J6 (RBSK_ECOLI)
Protein
Ribokinase
Gene
rbsK
Organism
Escherichia coli (strain K12)
Status
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
Catalytic activityi
- EC:2.7.1.15UniRule annotation3 Publications
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
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
Kineticsi
- KM=0.213 mM for ATP1 Publication
- KM=0.279 mM for D-ribose1 Publication
- KM=1.41 mM for 2-deoxy-D-ribose1 Publication
- KM=32 mM for D-arabinose1 Publication
- KM=31.6 mM for D-xylose1 Publication
- KM=8.2 mM for D-fructose1 Publication
- KM=0.65 mM for ribose (at pH 6.2 in the presence of 0 mM inorganic phosphate)1 Publication
- KM=0.43 mM for ribose (at pH 6.2 in the presence of 0.5 mM inorganic phosphate)1 Publication
- KM=0.27 mM for ribose (at pH 6.2 in the presence of 1 mM inorganic phosphate)1 Publication
- KM=0.23 mM for ribose (at pH 6.2 in the presence of 5 mM inorganic phosphate)1 Publication
- KM=0.21 mM for ribose (at pH 6.2 in the presence of 20 mM inorganic phosphate)1 Publication
- Vmax=122 µmol/min/mg enzyme toward ATP1 Publication
- Vmax=81 µmol/min/mg enzyme toward D-ribose1 Publication
- Vmax=25 µmol/min/mg enzyme toward 2-deoxy-D-ribose1 Publication
- Vmax=0.6 µmol/min/mg enzyme toward D-arabinose1 Publication
- Vmax=0.86 µmol/min/mg enzyme toward D-xylose1 Publication
- Vmax=0.226 µmol/min/mg enzyme toward D-fructose1 Publication
- Vmax=7.6 pmol/min/mg enzyme (at pH 6.2 in the presence of 0 mM inorganic phosphate)1 Publication
- Vmax=32.0 pmol/min/mg enzyme (at pH 6.2 in the presence of 0.5 mM inorganic phosphate)1 Publication
- Vmax=59.6 pmol/min/mg enzyme (at pH 6.2 in the presence of 1 mM inorganic phosphate)1 Publication
- Vmax=139.4 pmol/min/mg enzyme (at pH 6.2 in the presence of 5 mM inorganic phosphate)1 Publication
- 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
: D-ribose degradation Pathwayi
This protein is involved in step 2 of the subpathway that synthesizes D-ribose 5-phosphate from beta-D-ribopyranose.UniRule annotation1 PublicationProteins known to be involved in the 2 steps of the subpathway in this organism are:
- D-ribose pyranase (rbsD), D-ribose pyranase (rbsD)
- Ribokinase (rbsK), Ribokinase (rbsK)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 143 | SubstrateUniRule annotation3 Publications | 1 | |
Binding sitei | 187 | ATPUniRule annotation3 Publications | 1 | |
Metal bindingi | 249 | PotassiumUniRule annotation1 Publication | 1 | |
Metal bindingi | 251 | Potassium; via carbonyl oxygenUniRule annotation1 Publication | 1 | |
Active sitei | 255 | Proton acceptorUniRule annotation1 Publication | 1 | |
Binding sitei | 255 | SubstrateUniRule annotation3 Publications | 1 | |
Binding sitei | 279 | ATPUniRule annotation3 Publications | 1 | |
Metal bindingi | 285 | Potassium; via carbonyl oxygenUniRule annotation1 Publication | 1 | |
Metal bindingi | 288 | Potassium; via carbonyl oxygenUniRule annotation1 Publication | 1 | |
Metal bindingi | 290 | Potassium; via carbonyl oxygenUniRule annotation1 Publication | 1 | |
Metal bindingi | 294 | PotassiumUniRule annotation1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 223 – 228 | ATPUniRule annotation3 Publications | 6 | |
Nucleotide bindingi | 254 – 255 | ATPUniRule annotation2 Publications | 2 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-UniRule
- metal ion binding Source: EcoCyc
- ribokinase activity Source: EcoCyc
GO - Biological processi
- D-ribose catabolic process Source: EcoCyc
Keywordsi
Molecular function | Kinase, Transferase |
Biological process | Carbohydrate metabolism |
Ligand | ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium |
Enzyme and pathway databases
BioCyci | EcoCyc:RIBOKIN-MONOMER MetaCyc:RIBOKIN-MONOMER |
BRENDAi | 2.7.1.15, 2026 |
UniPathwayi | UPA00916;UER00889 |
Names & Taxonomyi
Protein namesi | Recommended name: Ribokinase1 PublicationUniRule annotation (EC:2.7.1.15UniRule annotation2 Publications)Short name: RKUniRule annotation |
Gene namesi | Name:rbsK1 PublicationUniRule annotation Ordered Locus Names:b3752, JW3731 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm UniRule annotationCurated
Cytosol
- cytosol Source: EcoCyc
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Chemistry databases
ChEMBLi | CHEMBL5093 |
DrugBanki | DB03909, Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate DB01936, alpha-D-arabinofuranose DB04444, Tetrafluoroaluminate Ion |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000080097 | 1 – 309 | RibokinaseAdd BLAST | 309 |
Proteomic databases
jPOSTi | P0A9J6 |
PaxDbi | P0A9J6 |
PRIDEi | P0A9J6 |
Interactioni
Subunit structurei
Homodimer.
UniRule annotation1 PublicationProtein-protein interaction databases
BioGRIDi | 4259582, 11 interactors |
DIPi | DIP-36178N |
IntActi | P0A9J6, 3 interactors |
STRINGi | 511145.b3752 |
Chemistry databases
BindingDBi | P0A9J6 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0A9J6 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A9J6 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 14 – 16 | Substrate bindingUniRule annotation3 Publications | 3 | |
Regioni | 42 – 46 | Substrate bindingUniRule annotation3 Publications | 5 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0524, Bacteria |
HOGENOMi | CLU_027634_2_0_6 |
InParanoidi | P0A9J6 |
PhylomeDBi | P0A9J6 |
Family and domain databases
CDDi | cd01174, ribokinase, 1 hit |
Gene3Di | 3.40.1190.20, 1 hit |
HAMAPi | MF_01987, Ribokinase, 1 hit |
InterProi | View protein in InterPro IPR002173, Carboh/pur_kinase_PfkB_CS IPR011877, D_ribokin IPR011611, PfkB_dom IPR002139, Ribo/fructo_kinase IPR029056, Ribokinase-like |
Pfami | View protein in Pfam PF00294, PfkB, 1 hit |
PRINTSi | PR00990, RIBOKINASE |
SUPFAMi | SSF53613, SSF53613, 1 hit |
TIGRFAMsi | TIGR02152, D_ribokin_bact, 1 hit |
PROSITEi | View protein in PROSITE PS00584, PFKB_KINASES_2, 1 hit |
i Sequence
Sequence statusi: Complete.
P0A9J6-1 [UniParc]FASTAAdd to basket
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
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 |
PIRi | A26305, KIECRB |
RefSeqi | NP_418208.1, NC_000913.3 WP_001300603.1, NZ_STEB01000015.1 |
Genome annotation databases
EnsemblBacteriai | AAC76775; AAC76775; b3752 BAE77536; BAE77536; BAE77536 |
GeneIDi | 948260 |
KEGGi | ecj:JW3731 eco:b3752 |
PATRICi | fig|1411691.4.peg.2948 |
Similar proteinsi
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 |
PIRi | A26305, KIECRB |
RefSeqi | NP_418208.1, NC_000913.3 WP_001300603.1, NZ_STEB01000015.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1GQT | X-ray | 2.34 | A/B/C/D | 1-309 | [»] | |
1RK2 | X-ray | 2.25 | A/B/C/D | 1-309 | [»] | |
1RKA | X-ray | 2.30 | A | 1-309 | [»] | |
1RKD | X-ray | 1.84 | A | 1-309 | [»] | |
1RKS | X-ray | 2.40 | A | 1-309 | [»] | |
SMRi | P0A9J6 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4259582, 11 interactors |
DIPi | DIP-36178N |
IntActi | P0A9J6, 3 interactors |
STRINGi | 511145.b3752 |
Chemistry databases
BindingDBi | P0A9J6 |
ChEMBLi | CHEMBL5093 |
DrugBanki | DB03909, Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate DB01936, alpha-D-arabinofuranose DB04444, Tetrafluoroaluminate Ion |
Proteomic databases
jPOSTi | P0A9J6 |
PaxDbi | P0A9J6 |
PRIDEi | P0A9J6 |
Genome annotation databases
EnsemblBacteriai | AAC76775; AAC76775; b3752 BAE77536; BAE77536; BAE77536 |
GeneIDi | 948260 |
KEGGi | ecj:JW3731 eco:b3752 |
PATRICi | fig|1411691.4.peg.2948 |
Organism-specific databases
EchoBASEi | EB0811 |
Phylogenomic databases
eggNOGi | COG0524, Bacteria |
HOGENOMi | CLU_027634_2_0_6 |
InParanoidi | P0A9J6 |
PhylomeDBi | P0A9J6 |
Enzyme and pathway databases
UniPathwayi | UPA00916;UER00889 |
BioCyci | EcoCyc:RIBOKIN-MONOMER MetaCyc:RIBOKIN-MONOMER |
BRENDAi | 2.7.1.15, 2026 |
Miscellaneous databases
EvolutionaryTracei | P0A9J6 |
PROi | PR:P0A9J6 |
Family and domain databases
CDDi | cd01174, ribokinase, 1 hit |
Gene3Di | 3.40.1190.20, 1 hit |
HAMAPi | MF_01987, Ribokinase, 1 hit |
InterProi | View protein in InterPro IPR002173, Carboh/pur_kinase_PfkB_CS IPR011877, D_ribokin IPR011611, PfkB_dom IPR002139, Ribo/fructo_kinase IPR029056, Ribokinase-like |
Pfami | View protein in Pfam PF00294, PfkB, 1 hit |
PRINTSi | PR00990, RIBOKINASE |
SUPFAMi | SSF53613, SSF53613, 1 hit |
TIGRFAMsi | TIGR02152, D_ribokin_bact, 1 hit |
PROSITEi | View protein in PROSITE PS00584, PFKB_KINASES_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | RBSK_ECOLI | |
Accessioni | P0A9J6Primary (citable) accession number: P0A9J6 Secondary accession number(s): P05054, Q2M870 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 13, 1987 |
Last sequence update: | August 13, 1987 | |
Last modified: | April 7, 2021 | |
This is version 130 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families