Skip Header

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

Ribokinase

Gene

rbsK

Organism
Erwinia billingiae (strain Eb661)
Status
Unreviewed-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), 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
Binding sitei182ATPUniRule annotation1
Metal bindingi226PotassiumUniRule annotation1
Metal bindingi228Potassium; via carbonyl oxygenUniRule annotation1
Active sitei232Proton acceptorUniRule annotation1
Binding sitei232SubstrateUniRule annotation1
Metal bindingi264Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi267Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi269Potassium; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi200 – 205ATPUniRule annotation6
Nucleotide bindingi231 – 232ATPUniRule annotation2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

KinaseUniRule annotationSAAS annotationImported, Transferase

Keywords - Biological processi

Carbohydrate metabolismUniRule annotation

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotation, Metal-bindingUniRule annotation, Nucleotide-binding, PotassiumUniRule annotation

Enzyme and pathway databases

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:EbC_03290Imported
OrganismiErwinia billingiae (strain Eb661)Imported
Taxonomic identifieri634500 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesErwiniaceaeErwinia
Proteomesi
  • UP000008793 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi634500.EbC_03290.

Structurei

3D structure databases

ProteinModelPortaliD8MLX6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini21 – 275PfkBInterPro annotationAdd BLAST255

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni10 – 12Substrate bindingUniRule annotation3
Regioni38 – 42Substrate bindingUniRule annotation5

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108FK6. Bacteria.
ENOG410ZSV3. LUCA.
HOGENOMiHOG000235950.
KOiK00852.
OMAiFNPSPLQ.
OrthoDBiPOG091H05S4.

Family and domain databases

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.
PROSITEiPS00583. PFKB_KINASES_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D8MLX6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVYVTGNIA VDEIWSIPDI PTKGSSIHGN KTSQDIGGKG ANQAILLSRC
60 70 80 90 100
GIETTLVAAI GNDNNGKWIK EQMLAESLQL LPDTLFPCHS DTSIIFNSAD
110 120 130 140 150
GDNAIITTTT AADSLSLTGI TQALSAAQPG DVLLQQGNFS VEKTRGLFAF
160 170 180 190 200
AKARGMITVF NPSPVKAAFA ELWSLVDIAV LNQHEAALLK PEGVKTLVVT
210 220 230 240 250
HGSQGALLKA PDNEAFCRAI AVTAVDSTGA GDTFLAVMLA SALLRHTEID
260 270 280
KLALTHASQA AAITVSRAGT YSAFPSISEL TALLQN
Length:286
Mass (Da):29,943
Last modified:October 5, 2010 - v1
Checksum:iEEEC49063BA783CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FP236843 Genomic DNA. Translation: CAX57860.1.
RefSeqiWP_013200367.1. NC_014306.1.

Genome annotation databases

EnsemblBacteriaiCAX57860; CAX57860; EbC_03290.
KEGGiebi:EbC_03290.
PATRICi42303476. VBIErwBil95213_0600.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FP236843 Genomic DNA. Translation: CAX57860.1.
RefSeqiWP_013200367.1. NC_014306.1.

3D structure databases

ProteinModelPortaliD8MLX6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi634500.EbC_03290.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAX57860; CAX57860; EbC_03290.
KEGGiebi:EbC_03290.
PATRICi42303476. VBIErwBil95213_0600.

Phylogenomic databases

eggNOGiENOG4108FK6. Bacteria.
ENOG410ZSV3. LUCA.
HOGENOMiHOG000235950.
KOiK00852.
OMAiFNPSPLQ.
OrthoDBiPOG091H05S4.

Enzyme and pathway databases

UniPathwayiUPA00916; UER00889.

Family and domain databases

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.
PROSITEiPS00583. PFKB_KINASES_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiD8MLX6_ERWBE
AccessioniPrimary (citable) accession number: D8MLX6
Entry historyi
Integrated into UniProtKB/TrEMBL: October 5, 2010
Last sequence update: October 5, 2010
Last modified: November 30, 2016
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.