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phosphoenolpyruvate-utilizing N-terminal domain-containing protein
putative PEP-binding protein
This entry represents a TIM barrel domain found at the C terminus of a number of PEP (phosphoenolpyruvate)-utilising proteins. In PPDK (Pyruvate phosphate dikinase) this C-terminal domain has been shown to be a PEP-binding domain [1]. [1]. 18052212. Swiveling domain mechanism in pyruvate phosphate dikinase.. Lim K, Read RJ, Chen CC, Tempczyk A, Wei M, Ye D, Wu C,. Dunaway-Mariano D, Herzberg O;. Biochemistry. 2007;46:14845-14853. (from Pfam)
PEP-utilizing enzyme
This domain is a "swivelling" beta/beta/alpha domain which is thought to be mobile in all proteins known to contain it. [1]. 8610096. Swiveling-domain mechanism for enzymatic phosphotransfer between. remote reaction sites.. Herzberg O, Chen CC, Kapadia G, McGuire M, Carroll LJ, Noh SJ,. Dunaway-Mariano D;. Proc Natl Acad Sci U S A 1996;93:2652-2657. (from Pfam)
HPr family phosphocarrier protein
PTS sugar transporter subunit IIA
phosphoenolpyruvate--protein phosphotransferase
This HMM recognizes a distinct clade of phophoenolpyruvate (PEP)-dependent enzymes. Most members are known or deduced to function as the phosphoenolpyruvate-protein phosphotransferase (or enzyme I) of PTS sugar transport systems. However, some species with both a member of this family and a homolog of the phosphocarrier protein HPr lack a IIC component able to serve as a permease. An HPr homolog designated NPr has been implicated in the regulation of nitrogen assimilation, which demonstrates that not all phosphotransferase system components are associated directly with PTS transport.
multiphosphoryl transfer protein
multiphosphoryl transfer protein is a multifunctional protein that includes general (non sugar-specific) and sugar-specific components of the phosphoenolpyruvate-dependent sugar phosphotransferase system that catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane
fructose PTS transporter subunit IIA
4.A.2 The PTS Fructose-Mannitol (Fru) Family Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. The Fru family is a large and complex family which includes several sequenced fructose and mannitol-specific permeases as well as several putative PTS permeases of unknown specificities. The fructose permeases of this family phosphorylate fructose on the 1-position. Those of family 4.6 phosphorylate fructose on the 6-position. The Fru family PTS systems typically have 3 domains, IIA, IIB and IIC, which may be found as 1 or more proteins. The fructose and mannitol transporters form separate phylogenetic clusters in this family. This Hmm is specific for the IIA domain of the fructose PTS transporters. Also similar to the Enzyme IIA Fru subunits of the PTS, but included in TIGR01419 rather than this model, is enzyme IIA Ntr (nitrogen), also called PtsN, found in E. coli and other organisms, which may play a solely regulatory role.
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