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Protein

Ribokinase

Gene

rbsK

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 annotation

Catalytic activityi

ATP + D-ribose = ADP + D-ribose 5-phosphate.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: 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.UniRule annotation

Enzyme regulationi

Activated by a monovalent cation that binds near, but not in, the active site. The most likely occupant of the site in vivo is potassium. Ion binding induces a conformational change that may alter substrate affinity.UniRule annotation

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 annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. D-ribose pyranase (rbsD)
  2. 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
Binding sitei139SubstrateUniRule annotation1
Binding sitei183ATPUniRule annotation1
Metal bindingi236PotassiumUniRule annotation1
Metal bindingi238Potassium; via carbonyl oxygenUniRule annotation1
Active sitei242Proton acceptorUniRule annotation1
Binding sitei242SubstrateUniRule annotation1
Binding sitei266ATPUniRule annotation1
Metal bindingi272Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi275Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi277Potassium; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi210 – 215ATPUniRule annotation6
Nucleotide bindingi241 – 242ATPUniRule annotation2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

BioCyciBSUB:BSU35920-MONOMER.
UniPathwayiUPA00916; UER00889.

Names & Taxonomyi

Protein namesi
Recommended name:
RibokinaseUniRule annotation (EC:2.7.1.15UniRule annotation)
Short name:
RKUniRule annotation
Gene namesi
Name:rbsKUniRule annotation
Ordered Locus Names:BSU35920
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000800961 – 293RibokinaseAdd BLAST293

Proteomic databases

PaxDbiP36945.
PRIDEiP36945.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100019431.

Structurei

3D structure databases

ProteinModelPortaliP36945.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni11 – 13Substrate bindingUniRule annotation3
Regioni39 – 43Substrate bindingUniRule annotation5

Sequence similaritiesi

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108RVA. Bacteria.
COG0524. LUCA.
HOGENOMiHOG000235950.
InParanoidiP36945.
KOiK00852.
OMAiNAIIVYP.
PhylomeDBiP36945.

Family and domain databases

CDDicd01174. ribokinase. 1 hit.
Gene3Di3.40.1190.20. 1 hit.
HAMAPiMF_01987. Ribokinase. 1 hit.
InterProiIPR002173. Carboh/pur_kinase_PfkB_CS.
IPR011877. D_ribokin.
IPR011611. PfkB_dom.
IPR002139. Ribo/fructo_kinase.
IPR029056. Ribokinase-like.
[Graphical view]
PfamiPF00294. PfkB. 1 hit.
[Graphical view]
PRINTSiPR00990. RIBOKINASE.
SUPFAMiSSF53613. SSF53613. 1 hit.
TIGRFAMsiTIGR02152. D_ribokin_bact. 1 hit.
PROSITEiPS00584. PFKB_KINASES_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P36945-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRNICVIGSC SMDLVVTSDK RPKAGETVLG TSFQTVPGGK GANQAVAAAR
60 70 80 90 100
LGAQVFMVGK VGDDHYGTAI LNNLKANGVR TDYMEPVTHT ESGTAHIVLA
110 120 130 140 150
EGDNSIVVVK GANDDITPAY ALNALEQIEK VDMVLIQQEI PEETVDEVCK
160 170 180 190 200
YCHSHDIPII LNPAPARPLK QETIDHATYL TPNEHEASIL FPELTISEAL
210 220 230 240 250
ALYPAKLFIT EGKQGVRYSA GSKEVLIPSF PVEPVDTTGA GDTFNAAFAV
260 270 280 290
ALAEGKDIEA ALRFANRAAS LSVCSFGAQG GMPTRNEVEE LLS
Length:293
Mass (Da):31,138
Last modified:December 15, 1998 - v2
Checksum:iDCB69533E53253EE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti284 – 293TRNEVEELLS → DKK in CAA81049 (PubMed:7921236).Curated10

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z25798 Genomic DNA. Translation: CAA81049.1.
Z92953 Genomic DNA. Translation: CAB07465.1.
AL009126 Genomic DNA. Translation: CAB15609.1.
PIRiD69690.
RefSeqiNP_391473.1. NC_000964.3.
WP_009968280.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB15609; CAB15609; BSU35920.
GeneIDi936844.
KEGGibsu:BSU35920.
PATRICi18979204. VBIBacSub10457_3764.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z25798 Genomic DNA. Translation: CAA81049.1.
Z92953 Genomic DNA. Translation: CAB07465.1.
AL009126 Genomic DNA. Translation: CAB15609.1.
PIRiD69690.
RefSeqiNP_391473.1. NC_000964.3.
WP_009968280.1. NZ_JNCM01000034.1.

3D structure databases

ProteinModelPortaliP36945.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100019431.

Proteomic databases

PaxDbiP36945.
PRIDEiP36945.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15609; CAB15609; BSU35920.
GeneIDi936844.
KEGGibsu:BSU35920.
PATRICi18979204. VBIBacSub10457_3764.

Phylogenomic databases

eggNOGiENOG4108RVA. Bacteria.
COG0524. LUCA.
HOGENOMiHOG000235950.
InParanoidiP36945.
KOiK00852.
OMAiNAIIVYP.
PhylomeDBiP36945.

Enzyme and pathway databases

UniPathwayiUPA00916; UER00889.
BioCyciBSUB:BSU35920-MONOMER.

Family and domain databases

CDDicd01174. ribokinase. 1 hit.
Gene3Di3.40.1190.20. 1 hit.
HAMAPiMF_01987. Ribokinase. 1 hit.
InterProiIPR002173. Carboh/pur_kinase_PfkB_CS.
IPR011877. D_ribokin.
IPR011611. PfkB_dom.
IPR002139. Ribo/fructo_kinase.
IPR029056. Ribokinase-like.
[Graphical view]
PfamiPF00294. PfkB. 1 hit.
[Graphical view]
PRINTSiPR00990. RIBOKINASE.
SUPFAMiSSF53613. SSF53613. 1 hit.
TIGRFAMsiTIGR02152. D_ribokin_bact. 1 hit.
PROSITEiPS00584. PFKB_KINASES_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRBSK_BACSU
AccessioniPrimary (citable) accession number: P36945
Secondary accession number(s): P96733
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 15, 1998
Last modified: October 5, 2016
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.