Protein Family Models

This HMM describes a recurring sub-architecture, about 1500 amino acids long, with an SDR (short-chain alcohol reductase) at its C-terminus, in addition to a trio of domains shared by all type I polyketide synthases. While the actual function of member proteins is specific to the natural product made, this model is assigned family type equivalog_domain to elevate its precedence in automated annotation software and prevent the misapplication of even more generic annotation.

Date:

2024-04-14

KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human. (from Pfam)

Date:

2023-12-12

Date:

2023-12-12

This enzymatic domain is part of bacterial polyketide synthases and catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group [1]. [1]. 23790488. Structural and stereochemical analysis of a modular polyketide. synthase ketoreductase domain required for the generation of a. cis-alkene.. Bonnett SA, Whicher JR, Papireddy K, Florova G, Smith JL,. Reynolds KA;. Chem Biol. 2013;20:772-783. (from Pfam)

Date:

2024-04-03

The structure of beta-ketoacyl synthase is similar to that of the thiolase family (Pfam:PF00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. [1]. 9482715. Crystal structure of beta-ketoacyl-acyl carrier protein synthase. II from E.coli reveals the molecular architecture of condensing. enzymes.. Huang W, Jia J, Edwards P, Dehesh K, Schneider G, Lindqvist Y;. EMBO J 1998;17:1183-1191. (from Pfam)

Date:

2024-04-03

This family contains a wide variety of dehydrogenases. [1]. 9735295. The refined crystal structure of Drosophila lebanonensis alcohol. dehydrogenase at 1.9 A resolution.. Benach J, Atrian S, Gonzalez-Duarte R, Ladenstein R;. J Mol Biol 1998;282:383-399.. [2]. 10387002. Structure of tropinone reductase-II complexed with NADP+ and. pseudotropine at 1.9 A resolution: implication for. stereospecific substrate binding and catalysis.. Yamashita A, Kato H, Wakatsuki S, Tomizaki T, Nakatsu T,. Nakajima K, Hashimoto T, Yamada Y, Oda J;. Biochemistry 1999;38:7630-7637. (from Pfam)

Date:

2024-04-03

A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine. (from Pfam)

Date:

2023-12-12

The structure of beta-ketoacyl synthase is similar to that of the thiolase family (Pfam:PF00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine [1]. [1]. 9482715. Crystal structure of beta-ketoacyl-acyl carrier protein synthase. II from E.coli reveals the molecular architecture of condensing. enzymes.. Huang W, Jia J, Edwards P, Dehesh K, Schneider G, Lindqvist Y;. EMBO J 1998;17:1183-1191. (from Pfam)

Date:

2024-04-03

Date:

2023-12-12