Protein Family Models

This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with Pfam:PF00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2. (from Pfam)

Date:

2024-08-14

This family contains alpha/beta hydrolase enzymes of diverse specificity. (from Pfam)

Date:

2024-08-14

Members of this family have serine hydrolase activity. They contain a conserved serine hydrolase motif, GXSXG/A, where the serine is a putative nucleophile [1]. This family has an alpha-beta hydrolase fold [2,3]. Eukaryotic members of this family have a conserved LXCXE motif, which binds to retinoblastomas. This motif is absent from prokaryotic members of this family [3]. [1]. 20080647. RBBP9: a tumor-associated serine hydrolase activity required for pancreatic neoplasia. Shields DJ, Niessen S, Murphy EA, Mielgo A, Desgrosellier JS, Lau SK, Barnes LA, Lesperance J, Bouvet M, Tarin D, Cravatt BF, Cheresh DA;. Proc Natl Acad Sci U S A. 2010;107:2189-2194. [2]. 15159570. Harvesting the high-hanging fruit: the structure of the YdeN gene product from Bacillus subtilis at 1.8 angstroms resolution. Janda I, Devedjiev Y, Cooper D, Chruszcz M, Derewenda U, Gabrys A, Minor W, Joachimiak A, Derewenda ZS;. Acta Crystallogr D Biol Crystallogr 2004;60:1101-1107. [3]. 19004028. Crystal structure of human retinoblastoma binding protein 9. Vorobiev SM, Su M, Seetharaman J, Huang YJ, Chen CX, Maglaqui M, Janjua H, Proudfoot M, Yakunin A, Xiao R, Acton TB, Montelione GT, Tong L;. Proteins. 2009;74:526-529. (from Pfam)

Date:

2024-10-16

This catalytic domain is found in a very wide range of enzymes. [1]. 1409539. The alpha/beta hydrolase fold. Ollis DL, Cheah E, Cygler M, Dijkstra B, Frolow F, Franken SM, Harel M, Remington SJ, Silman I, Schrag J, Sussman JL, Verschueren KHG, Goldman A;. Protein Eng 1992;5:197-211. (from Pfam)

Date:

2024-10-16

Fatty acid desaturases are enzymes that catalyse the insertion of a double bond at the delta position of fatty acids. There seem to be two distinct families of fatty acid desaturases which do not seem to be evolutionary related: Family 1 composed of Stearoyl-CoA desaturases (SCD) [1,2] and Family 2 composed of Bacterial fatty acid desaturases, Plant stearoyl-acyl-carrier-protein desaturase [3] and Cyanobacterial DesA [4]. Members of this entry are ER integral membrane proteins that share the same mushroom-shaped fold consisting of four transmembrane helices (TM1-TM4) which anchor them to the membrane, capped by a cytosolic domain containing a unique 9-10 histidine- coordinating di metal (di-iron) catalytic centre [5,6]. The structure of mouse stearoyl-CoA desaturase (SDC) revealed that TM2 and TM4 are longer than TM1 and TM3 and protrude into the cytosolic domain, providing three of the nine histidine residues that coordinate the two metal ions, while the other histidine residues are provided by the soluble domain in this enzyme [5]. [1]. 8861937. Crystal structure of delta9 stearoyl-acyl carrier protein desaturase from castor seed and its relationship to other di-iron proteins. Lindqvist Y, Huang W, Schneider G, Shanklin J;. EMBO J 1996;15:4081-4092. [2]. 2570068. Differentiation-induced gene expression in 3T3-L1 preadipocytes. A second differentially expressed gene encoding stearoyl-CoA desaturase. Kaestner KH, Ntambi JM, Kelly TJ Jr, Lane MD;. J Biol Chem. 1989;264:14755-14761. [3]. 2006187. Stearoyl-acyl-carrier-protein desaturase from higher plants is structurally unrelated to the animal and fungal homologs. Shanklin . TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16