Protein Family Models

The enzyme tetrahydromethanopterin S-methyltransferase EC:2.1.1.86 is composed of eight subunits [1]. The enzyme is a membrane- associated enzyme complex which catalyses an energy-conserving, sodium-ion-translocating step in methanogenesis from hydrogen and carbon dioxide [1]. [1]. 7737157. The energy conserving N5-methyltetrahydromethanopterin:coenzyme M methyltransferase complex from Methanobacterium thermoautotrophicum is composed of eight different subunits. Harms U, Weiss DS, Gartner P, Linder D, Thauer RK;. Eur J Biochem 1995;228:640-648. (from Pfam)

Date:

2024-10-16

This family includes a variety of pterin binding enzymes that all adopt a TIM barrel fold. The family includes dihydropteroate synthase EC:2.5.1.15 as well as a group methyltransferase enzymes including methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) Swiss:Q46389 that catalyses a key step in the Wood-Ljungdahl pathway of carbon dioxide fixation. It transfers the N5-methyl group from methyltetrahydrofolate (CH3-H4folate) to a cob(I)amide centre in another protein, the corrinoid iron-sulfur protein. MeTr is a member of a family of proteins that includes methionine synthase and methanogenic enzymes that activate the methyl group of methyltetra-hydromethano(or -sarcino)pterin [2]. [1]. 9187658. Crystal structure of the anti-bacterial sulfonamide drug target dihydropteroate synthase. Achari A, Somers DO, Champness JN, Bryant PK, Rosemond J, Stammers DK. Nat Struct Biol 1997;4:490-497. This paper shows similarity by sequence of DHPS and MetH enzymes. [2]. 10997901. Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase. Doukov T, Seravalli J, Stezowski JJ, Ragsdale SW;. Structure Fold Des 2000;8:817-830. (from Pfam)

Date:

2024-10-16

methyltetrahydrofolate cobalamin methyltransferase catalyzes the transfer of a methyl group from methyltetrahydrofolate to cobalamin and/or from methylcobalamin to tetrahydrofolate

Date:

2016-01-13

Date:

2020-10-26