InterPro : IPR005935

Name  Diphosphomevalonate/phosphomevalonate decarboxylase Short Name  Mev_decarb
Type  Family Description  This group of enzymes belongs to the GHMP kinase domain superfamily. GHMP kinases are a unique class of ATP-dependent enzymes (the abbreviation of which refers to the original members: galactokinase, homoserine kinase, mevalonate kinase, and phosphomevalonate kinase) []. Enzymes belonging to this superfamily contain three well-conserved motifs, the second of which has the typical sequence Pro-X-X-X-Gly-Leu-X-Ser-Ser-Ala and is involved in ATP binding []. The phosphate binding loop in GHMP kinases is distinct from the classical P-loops found in many ATP/GTP binding proteins. The bound ADP molecule adopts a rare syn conformation and is in the opposite orientation from those bound to the P-loop-containing proteins []. GHMP kinases display a distinctly bilobal appearance with their N-terminal subdomains dominated by a mixed beta-sheet flanked on one side by alpha-helices and their C-terminal subdomains containing a four stranded anti-parallel beta-sheet [, , , ]. Diphosphomevalonate decarboxylase (mevalonate pyrophosphate decarboxylase, () catalyzes the decarboxylation of mevalonate pyrophosphate to isopentyl pyrophosphate (IPP) [], the last step in the synthesis of IPP in the mevalonate pathway. In archaea, an alternate pathway involves decarboxylation of mevalonate monophosphate instead of diphosphomevalonate []. Mevalonate is a key intermediate in the biosynthesis of sterols and non-sterol isoprenes in the mevalonate pathway. In mammals, the majority of mevalonate is converted into cholesterol.ATP + (R)-5-diphosphomevalonate = ADP + phosphate + isopentenyl diphosphate + CO2 The classical mevalonate (MVA) pathway involves decarboxylation of mevalonate diphosphate, while an alternate pathway involves decarboxylation of mevalonate monophosphate. The enzyme responsible is known as phosphomevalonate decarboxylase [].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



1 Child Features

Id Name Short Name Type
IPR029765 Diphosphomevalonate decarboxylase Mev_diP_decarb Family

4 Contains

Id Name Short Name Type
IPR020568 Ribosomal protein S5 domain 2-type fold Ribosomal_S5_D2-typ_fold Domain
IPR013750 GHMP kinase, C-terminal domain GHMP_kinase_C_dom Domain
IPR006204 GHMP kinase N-terminal domain GHMP_kinase_N_dom Domain
IPR014721 Ribosomal protein S5 domain 2-type fold, subgroup Ribosomal_S5_D2-typ_fold_subgr Domain

0 Found In

0 Parent Features

7 Publications

First Author Title Year Journal Volume Pages
Zhou T Structure and mechanism of homoserine kinase: prototype for the GHMP kinase superfamily. 2000 Structure 8 1247-57
Wada T Crystal structure of 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase, an enzyme in the non-mevalonate pathway of isoprenoid synthesis. 2003 J Biol Chem 278 30022-7
Bork P Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases. 1993 Protein Sci 2 31-40
Romanowski MJ Crystal structure of the Streptococcus pneumoniae phosphomevalonate kinase, a member of the GHMP kinase superfamily. 2002 Proteins 47 568-71
Thoden JB Molecular structure of galactokinase. 2003 J Biol Chem 278 33305-11
Dhe-Paganon S Mechanism of mevalonate pyrophosphate decarboxylase: evidence for a carbocationic transition state. 1994 Biochemistry 33 13355-62
Vannice JC Identification in Haloferax volcanii of phosphomevalonate decarboxylase and isopentenyl phosphate kinase as catalysts of the terminal enzyme reactions in an archaeal alternate mevalonate pathway. 2014 J Bacteriol 196 1055-63

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)