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FGGY family of carbohydrate kinases, N-terminal domain
enterococcus casseliflavus glycerol kinase complexed with glycerol
Identifiers
SymbolFGGY_N
Pfam PF00370
Pfam clan CL0108
InterPro IPR018484
PROSITE PDOC00408
SCOP2 1gla / SCOPe / SUPFAM
CDD cd00366
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary
FGGY family of carbohydrate kinases, C-terminal domain
escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion
Identifiers
SymbolFGGY_C
Pfam PF02782
Pfam clan CL0108
InterPro IPR018485
PROSITE PDOC00408
SCOP2 1gla / SCOPe / SUPFAM
CDD cd00366
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

In molecular biology the FGGY carbohydrate kinase family is a family of evolutionarily related carbohydrate kinase enzymes. These enzymes include L-fuculokinase 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); D-ribulose kinase EC 2.7.1.47 (gene FGGY/YDR109c); [1] and L-xylulose kinase EC 2.7.1.53 (gene lyxK). These enzymes are proteins of from 480 to 520 amino acid residues.

These enzymes consist of two domains. The N-terminal and C-terminal domains both adopt a ribonuclease H-like fold and are structurally related to each other. [1] [2] [3]

References

  1. ^ a b Singh C, Glaab E, Linster C (2016). "Molecular Identification of D-Ribulokinase in Budding Yeast and Mammals". J. Biol. Chem. 292 (3): 1005–1028. doi: 10.1074/jbc.M116.760744. PMC  5247636. PMID  27909055.
  2. ^ Hurley JH, Faber HR, Worthylake D, Meadow ND, Roseman S, Pettigrew DW, Remington SJ (January 1993). "Structure of the regulatory complex of Escherichia coli IIIGlc with glycerol kinase". Science. 259 (5095): 673–7. Bibcode: 1993Sci...259..673H. doi: 10.1126/science.8430315. PMID  8430315. S2CID  20908371.
  3. ^ Ormo M, Bystrom CE, Remington SJ (November 1998). "Crystal structure of a complex of Escherichia coli glycerol kinase and an allosteric effector fructose 1,6-bisphosphate". Biochemistry. 37 (47): 16565–72. doi: 10.1021/bi981616s. PMID  9843423.
This article incorporates text from the public domain Pfam and InterPro: IPR018485
This article incorporates text from the public domain Pfam and InterPro: IPR018484