Protein Family Models

This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilisation loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His [1]. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates [1]. [1]. 34059129. Polysaccharide utilization loci-driven enzyme discovery reveals BD-FAE: a bifunctional feruloyl and acetyl xylan esterase active on complex natural xylans. Hameleers L, Penttinen L, Ikonen M, Jaillot L, Faure R, Terrapon N, Deuss PJ, Hakulinen N, Master ER, Jurak E;. Biotechnol Biofuels. 2021;14:127. (from Pfam)

Date:

2024-10-16

This catalytic domain is found at the C terminal of acyl-CoA thioester hydrolases and bile acid-CoA:amino acid N-acetyltransferases (BAAT). [1]. 11694534. The peroxisome proliferator-induced cytosolic type I acyl-CoA thioesterase (CTE-I) is a serine-histidine-aspartic acid alpha /beta hydrolase. Huhtinen K, O'Byrne J, Lindquist PJ, Contreras JA, Alexson SE;. J Biol Chem. 2002;277:3424-3432. (from Pfam)

Date:

2024-10-16

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

The sequences found in this family are similar to PGAP1 (Swiss:Q765A7). This is an endoplasmic reticulum membrane protein with a catalytic serine containing motif that is conserved in a number of lipases. PGAP1 functions as a GPI inositol-deacylase; this deacylation is important for the efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi body [1]. This entry also includes Tgl2, a mitochondria protein that serves as a triacylglycerol lipase in budding yeasts [2]. [1]. 14734546. Inositol deacylation of glycosylphosphatidylinositol-anchored proteins is mediated by mammalian PGAP1 and yeast Bst1p. Tanaka S, Maeda Y, Tashima Y, Kinoshita T;. J Biol Chem. 2004;279:14256-14263. [2]. 19959834. The TGL2 gene of Saccharomyces cerevisiae encodes an active acylglycerol lipase located in the mitochondria. Ham HJ, Rho HJ, Shin SK, Yoon HJ;. J Biol Chem. 2010;285:3005-3013. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

Date:

2024-08-14

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