Protein Family Models

This entry represents the C-terminal domain of 2-methylcitrate dehydratase EC:4.2.1.79 (PrpD) that is required for propionate catabolism. It catalyses the third step of the 2-methylcitric acid cycle. This domain is related to the serine dehydratase beta chain. [1]. 11294638. In vitro conversion of propionate to pyruvate by Salmonella enterica enzymes: 2-methylcitrate dehydratase (PrpD) and aconitase Enzymes catalyze the conversion of 2-methylcitrate to 2-methylisocitrate. Horswill AR, Escalante-Semerena JC;. Biochemistry 2001;40:4703-4713. (from Pfam)

Date:

2024-10-16

This entry represents the N-terminal domain of 2-methylcitrate dehydratase EC:4.2.1.79 (PrpD) that is required for propionate catabolism. It catalyses the third step of the 2-methylcitric acid cycle [1]. This enzyme consists of two domains: a large domain with an all-helical fold and a smaller domain that folds into an alpha/beta domain [2]. Cis-aconitic acid decarboxylase (CAD) shares high identity with proteins of the MmgE/PrpD family [3,4]. Citrate/2-methylcitrate dehydratase from Bacillus subtilis is involved in the tricarboxylic acid (TCA) and methylcitric acid cycles as it has both 2-methylcitrate dehydratase and citrate dehydratase activities [5]. This entry represents the N-terminal domain of 2-methylcitrate dehydratase PrpD, which has an all-helical fold. [1]. 11294638. In vitro conversion of propionate to pyruvate by Salmonella enterica enzymes: 2-methylcitrate dehydratase (PrpD) and aconitase Enzymes catalyze the conversion of 2-methylcitrate to 2-methylisocitrate. Horswill AR, Escalante-Semerena JC;. Biochemistry 2001;40:4703-4713. [2]. 16934291. Three-dimensional structure of iminodisuccinate epimerase defines the fold of the MmgE/PrpD protein family. Lohkamp B, Bauerle B, Rieger PG, Schneider G;. J Mol Biol. 2006;362:555-566. [3]. 31548418. Crystal structure of cis-aconitate decarboxylase reveals the impact of naturally occurring human mutations on itaconate synthesis. Chen F, Lukat P, Iqbal AA, Saile K, Kaever V, van den Heuvel J, Blankenfeldt W, Bussow K, Pessler F;. Proc Natl Acad Sci U S A. 2019;116:20644-20654. [4]. 18584171. Cloning and functional characterization of the cis-aconitic acid decarboxylase. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

MmgE/PrpD family protein such as 2-methylcitrate dehydratase (PrpD), which catalyzes the stereospecific dehydration of (2S,3S)-2-methylcitrate to yield the cis isomer of 2-methyl-aconitate and could also catalyze the dehydration of citrate and the hydration of cis-aconitate

Date:

2018-03-22

Members of this family are bacterial proteins known or predicted to act as 2-methylcitrate dehydratase, an enzyme involved in the methylcitrate cycle of propionate catabolism. A related clade of archaeal proteins that may or may not be functionally equivalent is reserved for a future model and is excluded from this family. The PrpD enzyme of E. coli is responsible for the minor aconitase activity (AcnC) not accounted for by AcnA and AcnB.

Gene:

prpD

Date:

2024-06-21

Functions in propionate metabolism; involved in isomerization of (2S,3S)-methylcitrate to (2R,3S)-methylisocitrate; also encodes minor aconitase or dehydratase activity; aconitase C

Date:

2021-08-26