Protein Family Models

This domain family includes a range of different proteins. Such as antifreeze proteins and flagellar FlgA proteins, and CpaB pilus proteins. [1]. 15146494. The emergence of catalytic and structural diversity within the beta-clip fold. Iyer LM, Aravind L;. Proteins. 2004;55:977-991. (from Pfam)

Date:

2024-10-16

NeuB is the prokaryotic N-acetylneuraminic acid (Neu5Ac) synthase. It catalyses the direct formation of Neu5Ac (the most common sialic acid) by condensation of phosphoenolpyruvate (PEP) and N-acetylmannosamine (ManNAc). This reaction has only been observed in prokaryotes; eukaryotes synthesise the 9-phosphate form, Neu5Ac-9-P, and utilise ManNAc-6-P instead of ManNAc. Such eukaryotic enzymes are not present in this family [1]. This family also contains SpsE spore coat polysaccharide biosynthesis proteins. [1]. 10873658. Molecular cloning and expression of the mouse N-acetylneuraminic acid 9-phosphate synthase which does not have deaminoneuraminic acid (KDN) 9-phosphate synthase activity. Nakata D, Close BE, Colley KJ, Matsuda T, Kitajima K;. Biochem Biophys Res Commun 2000;273:642-648. (from Pfam)

Date:

2024-10-16

This TIM alpha/beta barrel structure is found in xylose isomerase (Swiss:P19148) and in endonuclease IV (Swiss:P12638, EC:3.1.21.2). This domain is also found in the N termini of bacterial myo-inositol catabolism proteins. These are involved in the myo-inositol catabolism pathway, and is required for growth on myo-inositol in Rhizobium leguminosarum bv. viciae [1]. [1]. 11497462. Investigation of myo-inositol catabolism in Rhizobium leguminosarum bv. viciae and its effect on nodulation competitiveness. Fry J, Wood M, Poole PS;. Mol Plant Microbe Interact 2001;14:1016-1025. (from Pfam)

Date:

2024-10-16

CBS domains are small intracellular modules that pair together to form a stable globular domain [2]. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain [6]. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet [5]. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet [4]. CBS domain pairs from AMPK bind AMP or ATP [5]. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP [5]. Discovery and naming of the CBS domain. [1]. 9020585. The structure of a domain common to archaebacteria and the homocystinuria disease protein. Bateman A;. Trends Biochem Sci 1997;22:12-13. 3D Structure found as a sub-domain in TIM barrel of inosine-monophosphate dehydrogenase. [2]. 10200156. Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase. Zhang R, Evans G, Rotella FJ, Westbrook EM, Beno D, Huberman E, Joachimiak A, Collart FR;. Biochemistry 1999;38:4691-4700. Discovery of CBS domain. [3]. 9106071. CBS domains in ClC chloride channels implicated in myotonia and nephrolithiasis (kidney stones). Ponting CP;. J Mol Med 1997;75:160-163. [4]. 11524006. Regulation of human cystathionine beta-synthase by S-adenosyl-L-methionine: evidence for two catalytically active conformations involving an autoinhibitory domain in the C-terminal region. Janosik M, Kery V, Gaustadnes M, Macl. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16