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InterPro: IPR018483 Carbohydrate kinase, FGGY, conserved site

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3357 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession

IPR018483 Carb_kinase_FGGY_CS

Type

Conserved_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00445	FGGY_KINASES_2	2993
PROSITE pattern	PS00933	FGGY_KINASES_1	2310
Signatures in BioMart

InterPro Relationships Help

Found in

IPR000577 Carbohydrate kinase, FGGY
IPR005999 Glycerol kinase
IPR006000 Xylulokinase
IPR006002 Gluconate kinase
IPR013450 L-fuculokinase
IPR018484 Carbohydrate kinase, FGGY, N-terminal
IPR018485 Carbohydrate kinase, FGGY, C-terminal

GO Term annotation Help

Process

GO:0005975 carbohydrate metabolic process

Function

GO:0016773 phosphotransferase activity, alcohol group as acceptor

InterPro annotation

Entry Details in BioMart

Abstract

It has been shown [1] that four different type of carbohydrate kinases seem to be evolutionary related. These enzymes include L-fucolokinase (EC:2.7.1.51) (gene fucK); gluconokinase (EC:2.7.1.12) (gene gntK); glycerol kinase (EC:2.7.1.30) (gene glpK); xylulokinase (EC:2.7.1.17) (gene xylB); and L-xylulose kinase (EC:2.7.1.53) (gene lyxK). These enzymes are proteins of from 480 to 520 amino acid residues.

This entry represents conserved regions found in the central and C-terminal regions of these enzymes.

Structural links Help

PDB - click here

SCOP: c.55.1.4

CATH: 3.30.420.40

Database links Help

Enzyme: EC:2.7.1.30

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR018483

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P32189 Glycerol kinase

P32190 Glycerol kinase

P74260 Glycerol kinase

Q21944 Probable glycerol kinase

Q64516 Glycerol kinase

More proteins

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
IPR005999	Glycerol kinase
	SWISS-MODEL
	ModBase

Publications Open in usermanual
1.	Reizer A, Deutscher J, Saier MH Jr, Reizer J. Analysis of the gluconate (gnt) operon of Bacillus subtilis. Mol. Microbiol. 5 1081-9 1991 [PubMed: 1659648] http://dx.doi.org/10.1111/j.1365-2958.1991.tb01880.x

Additional Reading Open in usermanual
	Feese M, Pettigrew DW, Meadow ND, Roseman S, Remington SJ. Cation-promoted association of a regulatory and target protein is controlled by protein phosphorylation. Proc. Natl. Acad. Sci. U.S.A. 91 1994 3544-8 [PubMed: 8170944] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=8170944&action=stream&blobtype=pdf
	Yeh JI, Charrier V, Paulo J, Hou L, Darbon E, Claiborne A, Hol WG, Deutscher J. Structures of enterococcal glycerol kinase in the absence and presence of glycerol: correlation of conformation to substrate binding and a mechanism of activation by phosphorylation. Biochemistry 43 2004 362-73 [PubMed: 14717590] http://dx.doi.org/10.1021/bi034258o
	Feese MD, Faber HR, Bystrom CE, Pettigrew DW, Remington SJ. Glycerol kinase from Escherichia coli and an Ala65-->Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation. Structure 6 1998 1407-18 [PubMed: 9817843] http://dx.doi.org/10.1016/S0969-2126(98)00140-3
	Bystrom CE, Pettigrew DW, Branchaud BP, O'Brien P, Remington SJ. Crystal structures of Escherichia coli glycerol kinase variant S58-->W in complex with nonhydrolyzable ATP analogues reveal a putative active conformation of the enzyme as a result of domain motion. Biochemistry 38 1999 3508-18 [PubMed: 10090737] http://dx.doi.org/10.1021/bi982460z
	Ormo M, Bystrom CE, Remington SJ. Crystal structure of a complex of Escherichia coli glycerol kinase and an allosteric effector fructose 1,6-bisphosphate. Biochemistry 37 1998 16565-72 [PubMed: 9843423] http://dx.doi.org/10.1021/bi981616s

InterPro 23.1