Protein Family Models

phosphopyruvate hydratase (enolase) catalyzes the reversible dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate as part of the glycolytic and gluconeogenesis pathways

Date:

2024-07-25

Enolase (phosphopyruvate hydratase, EC 4.2.1.11) is a widely distributed cytosolic enzyme with a critical role in glycolysis. In bacteria, it occurs in nearly every species. Enolases from multiple lineages have been reported to exhibit surface expression and to have virulence-related moonlighting functions, such as binding to fibrinogen or other host proteins.

Gene:

eno

Date:

2024-12-13

This domain appears at the C-terminus of many of the proteins that carry the MR_MLE_N Pfam:PF02746 domain. EC:4.2.1.40. (from Pfam)

Date:

2024-08-14

Methylaspartate ammonia-lyase EC:4.3.1.2 catalyses the second step of fermentation of glutamate. It is a homodimer. This family represents the C-terminal region of Methylaspartate ammonia-lyase and contains a TIM barrel fold similar to the Pfam:PF01188. This family represents the catalytic domain and contains a metal binding site [2]. [1]. 1420191. Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein. Goda SK, Minton NP, Botting NP, Gani D;. Biochemistry 1992;31:10747-10756. [2]. 11748244. The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step. Asuncion M, Blankenfeldt W, Barlow JN, Gani D, Naismith JH;. J Biol Chem 2002;277:8306-8311. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

Date:

2024-08-14

Enolase (phosphopyruvate hydratase, EC 4.2.1.11) is a ubiquitous cytosolic, Mg(2+)-dependent, octameric glycolytic enzyme. An extensive literature shows that in Staphylococcus aureus, Streptococcus pneumoniae, and a wide variety of other pathogens, closely related or not, enolase moonlights as a surface protein, despite the absence of a signal peptide or C-terminal anchoring sequence. As a (reportedly dimeric) surface protein in these pathogens, surface-exposed enolase exploits binding to host proteins, especially plasminogen, to promote infectious processes. This BlastRule identifies close homologs of specifically staphylococcal and streptococcal alpha-enolases shown to moonlight as virulence factors, displayed on the cell surface and interacting with host proteins in a manner that contributes to infection.

Gene:

eno

Date:

2023-07-15