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InterPro: IPR000577 Carbohydrate kinase, FGGY

Protein matchesHelp
UniProtKB
Matches:
5689 proteins
AccessionHelp IPR000577 Carb_kinase_FGGY
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Children IPR005929 L-ribulokinase
IPR005999 Glycerol kinase
IPR006000 Xylulokinase
IPR006002 Gluconate kinase
IPR006003 Carbohydrate kinase, FGGY-related
IPR013449 Rhamnulokinase
IPR013450 L-fuculokinase
Contains IPR018483 Carbohydrate kinase, FGGY, conserved site
IPR018484 Carbohydrate kinase, FGGY, N-terminal
IPR018485 Carbohydrate kinase, FGGY, C-terminal
GO Term annotationHelp
Process GO:0005975 carbohydrate metabolic process
Function GO:0016773 phosphotransferase activity, alcohol group as acceptor
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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.

Structural linksHelp
SCOP: c.55.1.4
CATH: 3.30.420.40
Database linksHelp
PDBe-motif: PS00445 , PS00933
Enzyme: EC:2.7.1
PROSITE doc: PDOC00408
PANDIT: PF00370 , PF02782
Blocks: IPB000577

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR000577 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
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

PublicationsHelp
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 ReadingHelp
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
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InterPro 23.1