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InterPro: IPR018485 Carbohydrate kinase, FGGY, C-terminal

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Matches:

4899 proteins

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Accession

IPR018485 Carb_kinase_FGGY_C

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF02782	FGGY_C	4899
Signatures in BioMart

InterPro Relationships Help

Found in

IPR000577 Carbohydrate kinase, FGGY
IPR005929 L-ribulokinase
IPR005999 Glycerol kinase
IPR006000 Xylulokinase
IPR006002 Gluconate kinase
IPR006003 Carbohydrate kinase, FGGY-related
IPR013450 L-fuculokinase

Contains

IPR018483 Carbohydrate kinase, FGGY, conserved site

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 the C-terminal domain of these proteins. It adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain [2, 3].

Structural links Help

PDB - click here

SCOP: c.55.1.4

CATH: 3.30.420.40

Database links Help

Enzyme: EC:2.7.1

Pfam Clan: CL0108.12

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR018485

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A2AJL3 FGGY carbohydrate kinase domain-containing protein

O75191 Xylulose kinase

P30646 Uncharacterized sugar kinase R08D7.7

P32190 Glycerol kinase

P74260 Glycerol kinase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR006003	Carbohydrate kinase, FGGY-related
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
2.	Hurley JH, Faber HR, Worthylake D, Meadow ND, Roseman S, Pettigrew DW, Remington SJ. Structure of the regulatory complex of Escherichia coli IIIGlc with glycerol kinase. Science 259 673-7 1993 [PubMed: 8430315] http://www.sciencemag.org/cgi/content/abstract/259/5095/673
3.	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 16565-72 1998 [PubMed: 9843423] http://dx.doi.org/10.1021/bi981616s

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

InterPro 23.1