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GHMP kinase family

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GHMP kinases N terminal domain
crystal structure of the streptococcus pneumoniae phosphomevalonate kinase (pmk)
Identifiers
SymbolGHMP_kinases_N
PfamPF00288
Pfam clanCL0329
InterProIPR006204
PROSITEPDOC00545
SCOP21fwl / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
GHMP kinases C terminal
pyrococcus furiosus galactokinase in complex with galactose, adp and magnesium
Identifiers
SymbolGHMP_kinases_C
PfamPF08544
InterProIPR013750
PROSITEPDOC00545
SCOP21fwl / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

In molecular biology, the GHMP kinase family is a family of kinase enzymes. Members of this family include homoserine kinases EC 2.7.1.39, galactokinases EC 2.7.1.6, and mevalonate kinasesEC 2.7.1.36. These kinases make up the GHMP kinase superfamily of ATP-dependent enzymes.[1] These enzymes are involved in the biosynthesis of isoprenes and amino acids as well as in carbohydrate metabolism. These enzymes contain, in their N-terminal section, a conserved Gly/Ser-rich region which is probably involved in the binding of ATP.[2][3] The C-terminal domain of homoserine kinase has a central alpha-beta plait fold and an insertion of four helices, which, together with the N-terminal fold, creates a novel nucleotide binding fold.[4]

References

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  1. ^ Bork P, Sander C, Valencia A (January 1993). "Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases". Protein Sci. 2 (1): 31–40. doi:10.1002/pro.5560020104. PMC 2142297. PMID 8382990.
  2. ^ Tsay YH, Robinson GW (February 1991). "Cloning and characterization of ERG8, an essential gene of Saccharomyces cerevisiae that encodes phosphomevalonate kinase". Mol. Cell. Biol. 11 (2): 620–31. doi:10.1128/MCB.11.2.620. PMC 359713. PMID 1846667.
  3. ^ Lee M, Leustek T (December 1999). "Identification of the gene encoding homoserine kinase from Arabidopsis thaliana and characterization of the recombinant enzyme derived from the gene". Arch. Biochem. Biophys. 372 (1): 135–42. doi:10.1006/abbi.1999.1481. PMID 10562426.
  4. ^ Zhou T, Daugherty M, Grishin NV, Osterman AL, Zhang H (December 2000). "Structure and mechanism of homoserine kinase: prototype for the GHMP kinase superfamily". Structure. 8 (12): 1247–57. doi:10.1016/s0969-2126(00)00533-5. PMID 11188689.
This article incorporates text from the public domain Pfam and InterPro: IPR013750
This article incorporates text from the public domain Pfam and InterPro: IPR006204