Protein Family Models

Date:

2024-08-14

This family now also contains the lysine 2-oxoglutarate reductases. [1]. 11354603. Lysine metabolism in higher plants.. Azevedo RA, Lea PJ;. Amino Acids 2001;20:261-279. (from Pfam)

Date:

2024-08-14

This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family Pfam:PF00389. [1]. 9126843. Crystal structure of a ternary complex of D-2-hydroxyisocaproate. dehydrogenase from Lactobacillus casei, NAD+ and. 2-oxoisocaproate at 1.9 A resolution.. Dengler U, Niefind K, Kiess M, Schomburg D;. J Mol Biol 1997;267:640-660. (from Pfam)

Date:

2024-08-14

This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyses the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyses the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate. Discusses the pentafunctional AROM multi-domain protein, which. possesses a shikimate 5-dehydrogenase enzyme. The AROM protein. catalyses steps two to six in the shikimate pathway in many. microbial eukaryotes.. [1]. 7556173. The molecular biology of multidomain proteins. Selected. examples.. Hawkins AR, Lamb HK;. Eur J Biochem 1995;232:7-18. (from Pfam)

Date:

2024-08-14

This family now also contains the lysine 2-oxoglutarate reductases. [1]. 11354603. Lysine metabolism in higher plants.. Azevedo RA, Lea PJ;. Amino Acids 2001;20:261-279. (from Pfam)

Date:

2024-08-14

This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain. [1]. 8805537. Protein-protein interactions in the pyruvate dehydrogenase. multienzyme complex: dihydrolipoamide dehydrogenase complexed. with the binding domain of dihydrolipoamide acetyltransferase.. Mande SS, Sarfaty S, Allen MD, Perham RN, Hol WG;. Structure 1996;4:277-286. (from Pfam)

Date:

2024-08-14

alanine dehydrogenase catalyzes the NAD(+)-dependent oxidative deamination of L-alanine to pyruvate, and the reverse reaction, the reductive amination of pyruvate; alanine dehydrogenase catalyzes the reversible oxidative deamination of L-alanine to pyruvate

Date:

2024-09-11

The family of known L-alanine dehydrogenases (EC 1.4.1.1) includes representatives from the Proteobacteria, Firmicutes, Cyanobacteria, and Actinobacteria, all with about 50 % identity or better. An outlier to this group in both sequence and gap pattern is the homolog from Helicobacter pylori, an epsilon division Proteobacteria, which must be considered a putative alanine dehydrogenase. In Mycobacterium smegmatis and M. tuberculosis, the enzyme doubles as a glycine dehydrogenase (1.4.1.10), running in the reverse direction (glyoxylate amination to glycine, with conversion of NADH to NAD+). Related proteins include saccharopine dehydrogenase and the N-terminal half of the NAD(P) transhydrogenase alpha subunit. All of these related proteins bind NAD and/or NADP.

Gene:

ald

Date:

2024-06-21