Protein Family Models

Date:

2024-08-14

This domain contains several repeats of the PQQ repeat. (from Pfam)

Date:

2024-08-14

The family represent a single repeat of a beta propeller. This propeller has been found in several enzymes which utilise pyrrolo-quinoline quinone as a prosthetic group. [1]. 7735834. The refined structure of the quinoprotein methanol dehydrogenase. from Methylobacterium extorquens at 1.94 A.. Ghosh M, Anthony C, Harlos K, Goodwin MG, Blake C;. Structure 1995;3:177-187.. [2]. 8676383. Determination of the gene sequence and the three-dimensional. structure at 2.4 angstroms resolution of methanol dehydrogenase. from Methylophilus W3A1.. Xia Z, Dai W, Zhang Y, White SA, Boyd GD, Mathews FS;. J Mol Biol 1996;259:480-501. (from Pfam)

Date:

2024-08-14

This protein family has a phylogenetic distribution very similar to that coenzyme PQQ biosynthesis enzymes, as shown by partial phylogenetic profiling. Genes in this family often are found adjacent to the PQQ biosynthesis genes themselves. An unusual, strained disulfide bond between adjacent Cys residues contributes to PQQ-binding, as does a Trp residue that is part of a PQQ enzyme repeat (see PF01011). Characterized members include the dehydrogenase subunit of a membrane-anchored, three subunit alcohol (ethanol) dehydrogenase of Gluconobacter suboxydans, a homodimeric ethanol dehydrogenase in Pseudomonas aeruginosa, and the large subunit of an alpha2/beta2 heterotetrameric methanol dehydrogenase in Methylobacterium extorquens.

Date:

2024-05-30

methanol/ethanol family PQQ-dependent dehydrogenase similar to Thauera butanivorans 1-butanol dehydrogenase (quinone) that catalyzes the oxidation of 1-butanol to 1-butanal and may function primarily in energy generation

Date:

2020-09-16