Protein Family Models

This entry includes a domain found in the central region of the acyltransferase domain (AT) from fungal type I fatty acid synthase (FAS, such as FAS1 from yeast) and mycobacteria, which have secondary-structure elements and sequence homology [1-5]. Mycobacterial fatty acid synthase (FAS) complex is an homohexameric multifunctional enzyme that catalyses the synthesis of fatty acid precursors of mycolic acids, the major components of the cell wall in Mycobacteria and play an important role in pathogenicity [6]. Paper describing PDB structure 2pff. [1]. 17448991. The crystal structure of yeast fatty acid synthase, a cellular machine with eight active sites working together. Lomakin IB, Xiong Y, Steitz TA;. Cell. 2007;129:319-332. Paper describing PDB structure 2uv8. [2]. 17431182. Structural basis for substrate delivery by acyl carrier protein in the yeast fatty acid synthase. Leibundgut M, Jenni S, Frick C, Ban N;. Science. 2007;316:288-290. Paper describing PDB structure 6jsh. [3]. 31509190. Modulation of fatty acid synthase by ATR checkpoint kinase Rad3. Qiu S, Liu S, Zaoti ZF, Wang X, Cai G;. J Mol Cell Biol. 2019;11:1098-1100. Paper describing PDB structure 6u5t. [4]. 31506493. Electron cryomicroscopy observation of acyl carrier protein translocation in type I fungal fatty acid synthase. Lou JW, Iyer KR, Hasan SMN, Cowen LE, Mazhab-Jafari MT;. Sci Rep. 2019;9:12987. Paper describing PDB structure 6wc7. [5]. 32471977. Steric occlusion regulates proximal interactions of acyl carrier protein domain in fungal fatty acid synthase. Lou JW, Mazhab-Jafari MT;. Commun Biol. 2020;3:274. [6]. 23291528. 7.5-A cryo-em structure of th. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

This is the acyl carrier domain (ACP) found in fatty acid synthase subunit alpha (FAS2) EC:2.3.1.86 .The fungal type I fatty acid synthase (FAS) is a 2.6 MDa multienzyme complex, catalyzing all necessary steps for the synthesis of long acyl chains. To be catalytically competent, the FAS must be activated by a posttranslational modification of the central acyl carrier domain (ACP) by an intrinsic phosphopantetheine transferase (PPT) [1]. [1]. 17431182. Structural basis for substrate delivery by acyl carrier protein in the yeast fatty acid synthase. Leibundgut M, Jenni S, Frick C, Ban N;. Science. 2007;316:288-290. [2]. 18725634. Inhibition of the fungal fatty acid synthase type I multienzyme complex. Johansson P, Wiltschi B, Kumari P, Kessler B, Vonrhein C, Vonck J, Oesterhelt D, Grininger M;. Proc Natl Acad Sci U S A. 2008;105:12803-12808. [3]. 19679086. Multimeric options for the auto-activation of the Saccharomyces cerevisiae FAS type I megasynthase. Johansson P, Mulinacci B, Koestler C, Vollrath R, Oesterhelt D, Grininger M;. Structure. 2009;17:1063-1074. (from Pfam)

Date:

2024-10-16

This is the N-terminal domain of DNA polymerase beta present in Homo sapiens. DNA polymerase beta is a repair enzyme that has a key role in the base excision repair of simple DNA lesions [1]. [1]. 16615916. Magnesium-induced assembly of a complete DNA polymerase catalytic complex. Batra VK, Beard WA, Shock DD, Krahn JM, Pedersen LC, Wilson SH;. Structure. 2006;14:757-766. (from Pfam)

Date:

2024-10-16

This domain has been identified in fungi and bacteria. It is found in fatty acid synthase beta subunit from fungi, including Fas1 from yeasts and aflB from Aspergillus parasiticus. This is an inserted helical domain, whose function is not clear, and is found together with the MaoC-like domain (Pfam:PF01575) and the acyltransferase domain (Pfam:PF00698) [1]. Fas1 is a fatty acid synthetase that catalyses the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH [2]. AflB is part of the gene cluster that mediates the biosynthesis of aflatoxins [3]. [1]. 9693066. Cloning of the fatty acid synthetase beta subunit from fission yeast, coexpression with the alpha subunit, and purification of the intact multifunctional enzyme complex. Niwa H, Katayama E, Yanagida M, Morikawa K;. Protein Expr Purif 1998;13:403-413. [2]. 3528750. The pentafunctional FAS1 gene of yeast: its nucleotide sequence and order of the catalytic domains. Schweizer M, Roberts LM, Holtke HJ, Takabayashi K, Hollerer E, Hoffmann B, Muller G, Kottig H, Schweizer E;. Mol Gen Genet. 1986;203:479-486. [3]. 15006741. Clustered pathway genes in aflatoxin biosynthesis. Yu J, Chang PK, Ehrlich KC, Cary JW, Bhatnagar D, Cleveland TE, Payne GA, Linz JE, Woloshuk CP, Bennett JW;. Appl Environ Microbiol. 2004;70:1253-1262. (from Pfam)

Date:

2024-10-16

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:

2024-10-16

The maoC gene is part of a operon with maoA which is involved in the synthesis of monoamine oxidase [1]. The MaoC protein is found to share similarity with a wide variety of enzymes; estradiol 17 beta-dehydrogenase 4, peroxisomal hydratase-dehydrogenase-epimerase, fatty acid synthase beta subunit. Several bacterial proteins that are composed solely of this domain have (R)-specific enoyl-CoA hydratase activity [2]. This domain is also present in the NodN nodulation protein N. [1]. 8647101. A monoamine-regulated Klebsiella aerogenes operon containing the monoamine oxidase structural gene (maoA) and the maoC gene. Sugino H, Sasaki M, Azakami H, Yamashita M, Murooka Y. J Bacteriol 1992;174:2485-2492. [2]. 9457873. Expression and characterization of (R)-specific enoyl coenzyme A hydratase involved in polyhydroxyalkanoate biosynthesis by Aeromonas caviae. Fukui T, Shiomi N, Doi Y;. J Bacteriol. 1998;180:667-673. (from Pfam)

Date:

2024-10-16

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:

2024-10-16

Date:

2024-08-14