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Protein

Ribokinase

Gene

rbsK

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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. no protein annotated in this organism
  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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei146 – 1461SubstrateUniRule annotation
Binding sitei193 – 1931ATPUniRule annotation
Metal bindingi236 – 2361Magnesium; via carbonyl oxygenCombined sources
Metal bindingi236 – 2361PotassiumUniRule annotation
Binding sitei237 – 2371ADP; via carbonyl oxygenCombined sources
Metal bindingi238 – 2381Magnesium; via carbonyl oxygenCombined sources
Metal bindingi238 – 2381Potassium; via carbonyl oxygenUniRule annotation
Binding sitei241 – 2411ADP; via amide nitrogenCombined sources
Active sitei242 – 2421Proton acceptorUniRule annotation
Binding sitei242 – 2421SubstrateUniRule annotation
Metal bindingi276 – 2761Magnesium; via carbonyl oxygenCombined sources
Metal bindingi276 – 2761Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi279 – 2791Magnesium; via carbonyl oxygenCombined sources
Metal bindingi279 – 2791Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi281 – 2811Magnesium; via carbonyl oxygenCombined sources
Metal bindingi281 – 2811Potassium; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi210 – 2156ATPUniRule annotation
Nucleotide bindingi212 – 2154ADPCombined sources
Nucleotide bindingi241 – 2422ATPUniRule annotation
Nucleotide bindingi270 – 2734ADPCombined sources

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 annotationCombined sources, Metal-bindingUniRule annotationCombined sources, Nucleotide-binding, PotassiumUniRule annotation

Enzyme and pathway databases

BioCyciMTBRV:RV2436-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 annotationImported
Ordered Locus Names:Rv2436Imported
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)Imported
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

PTM / Processingi

Proteomic databases

PaxDbiP71913.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi83332.Rv2436.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GO6X-ray1.98A/B2-304[»]
3GO7X-ray2.50A/B2-304[»]
ProteinModelPortaliP71913.
SMRiP71913. Positions 13-285.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 288274PfkBInterPro annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni23 – 253Substrate bindingUniRule annotation
Regioni51 – 555Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0524. LUCA.
HOGENOMiHOG000235950.
KOiK00852.
OMAiANIVIIT.
PhylomeDBiP71913.

Family and domain databases

Gene3Di3.40.1190.20. 1 hit.
HAMAPiMF_01987. Ribokinase. 1 hit.
InterProiIPR011877. 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.

Sequencei

Sequence statusi: Complete.

P71913-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANASETNVG PMAPRVCVVG SVNMDLTFVV DALPRPGETV LAASLTRTPG
60 70 80 90 100
GKGANQAVAA ARAGAQVQFS GAFGDDPAAA QLRAHLRANA VGLDRTVTVP
110 120 130 140 150
GPSGTAIIVV DASAENTVLV APGANAHLTP VPSAVANCDV LLTQLEIPVA
160 170 180 190 200
TALAAARAAQ SADAVVMVNA SPAGQDRSSL QDLAAIADVV IANEHEANDW
210 220 230 240 250
PSPPTHFVIT LGVRGARYVG ADGVFEVPAP TVTPVDTAGA GDVFAGVLAA
260 270 280 290 300
NWPRNPGSPA ERLRALRRAC AAGALATLVS GVGDCAPAAA AIDAALRANR

HNGS
Length:304
Mass (Da):30,280
Last modified:February 1, 1997 - v1
Checksum:iD1990AADD9F1BA7A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP45228.1.
RefSeqiNP_216952.1. NC_000962.3.
WP_009936616.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP45228; CCP45228; Rv2436.
GeneIDi885671.
KEGGimtu:Rv2436.
mtv:RVBD_2436.
PATRICi18154013. VBIMycTub87468_2730.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP45228.1.
RefSeqiNP_216952.1. NC_000962.3.
WP_009936616.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GO6X-ray1.98A/B2-304[»]
3GO7X-ray2.50A/B2-304[»]
ProteinModelPortaliP71913.
SMRiP71913. Positions 13-285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2436.

Proteomic databases

PaxDbiP71913.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP45228; CCP45228; Rv2436.
GeneIDi885671.
KEGGimtu:Rv2436.
mtv:RVBD_2436.
PATRICi18154013. VBIMycTub87468_2730.

Phylogenomic databases

eggNOGiCOG0524. LUCA.
HOGENOMiHOG000235950.
KOiK00852.
OMAiANIVIIT.
PhylomeDBiP71913.

Enzyme and pathway databases

UniPathwayiUPA00916; UER00889.
BioCyciMTBRV:RV2436-MONOMER.

Family and domain databases

Gene3Di3.40.1190.20. 1 hit.
HAMAPiMF_01987. Ribokinase. 1 hit.
InterProiIPR011877. 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.
ProtoNetiSearch...

Entry informationi

Entry nameiP71913_MYCTU
AccessioniPrimary (citable) accession number: P71913
Secondary accession number(s): I6X491
Entry historyi
Integrated into UniProtKB/TrEMBL: February 1, 1997
Last sequence update: February 1, 1997
Last modified: September 7, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, 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.