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InterPro: IPR006000 Xylulokinase

Protein matchesHelp
UniProtKB
Matches:
700 proteins
AccessionHelp IPR006000 Xylulokinase
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR000577 Carbohydrate kinase, FGGY
Contains IPR018483 Carbohydrate kinase, FGGY, conserved site
IPR018484 Carbohydrate kinase, FGGY, N-terminal
IPR018485 Carbohydrate kinase, FGGY, C-terminal
GO Term annotationHelp
Process GO:0005997 xylulose metabolic process
Function GO:0004856 xylulokinase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

The ability to metabolise xylose, one of the most abundant sugars in nature, is dependent on its conversion to xylulose-5-phosphate, which then enters the non-oxidative pentose phosphate pathway [1]. Xylulose-5-phosphate is produced from xylose by the sequential action of two enzymes; xylose isomerase, which converts xylose to xylulose, and xylulokinase, which subsequently phosphorylates xylulose.

This entry represents bacterial xylulokinase. In addition to its role in xylose metabolism this enzyme may also have a biosynthetic role. 1-deoxy-D-xylulose 5-phosphate serves as a precursor for the biosynthesis of the vitamins thiamine and pyridoxal and for the formation of isopentenyl pyrophosphate and dimethylallyl pyrophosphate via the nonmevalonate pathway of terpenoid biosynthesis. Xylulokinase catalyses the phosphorylation of 1-deoxy-D-xylulose at the hydroxy group of C-5 [2]. This reaction therefore constitutes a potential salvage pathway for the generation of 1-deoxy-D-xylulose 5-phosphate from exogenous or endogenous 1-deoxy-D-xylulose as starting material for the biosynthesis of terpenoids, thiamine and pyridoxal.

Database linksHelp
Enzyme: EC:2.7.1.17

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR006000 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P09099 Xylulose kinase

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Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR018483 Carbohydrate kinase, FGGY, conserved site
IPR018485 Carbohydrate kinase, FGGY, C-terminal
IPR000577 Carbohydrate kinase, FGGY
IPR018484 Carbohydrate kinase, FGGY, N-terminal
IPR006000 Xylulokinase
PDB Chain
ModBase

PublicationsHelp
1. Di Luccio E, Petschacher B, Voegtli J, Chou HT, Stahlberg H, Nidetzky B, Wilson DK.
Structural and kinetic studies of induced fit in xylulose kinase from Escherichia coli.
J. Mol. Biol. 365 783-98 2007 [PubMed: 17123542]
http://dx.doi.org/10.1016/j.jmb.2006.10.068
2. Wungsintaweekul J, Herz S, Hecht S, Eisenreich W, Feicht R, Rohdich F, Bacher A, Zenk MH.
Phosphorylation of 1-deoxy-D-xylulose by D-xylulokinase of Escherichia coli.
Eur. J. Biochem. 268 310-6 2001 [PubMed: 11168365]
http://dx.doi.org/10.1046/j.1432-1033.2001.01875.x

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InterPro 23.1