Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
phosphoenolpyruvate-utilizing N-terminal domain-containing protein
PTS system fructose IIA component
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
dihydroxyacetone kinase phosphoryl donor subunit DhaM
DhaM becomes phosphorylated by phosphoenolpyruvate (PEP) and then serves as the donor for the phosphorylation of dihydroxyacetone (also known as glycerone). This HMM represents the longer form with an HPr-like central domain and EI-like C-terminal domain as seen in E. coli. DhaM is unrelated to ATP-dependent types of dihydroxyacetone kinase.
PTS-dependent dihydroxyacetone kinase phosphotransferase subunit DhaM
PTS-dependent dihydroxyacetone kinase phosphotransferase subunit DhaM is a component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone
DhaM becomes phosphorylated by phosphoenolpyruvate (PEP) and then serves as the donor for the phosphorylation of dihydroxyacetone (also known as glycerone). This HMM describes a region of sequence similar to the EIIA component of PTS-type sugar transporters, which also perform PEP-dependent phosphorylation of substrates. In some bacterial species, such as E. coli, DhaM is longer, with an HPr-like central domain and EI-like C-terminal domain. DhaM is unrelated to ATP-dependent types of dihydroxyacetone kinase.
The HPr family are bacterial proteins (or domains of proteins) which function in phosphoryl transfer system (PTS) systems. They include energy-coupling components which catalyze sugar uptake via a group translocation mechanism. The functions of most of these proteins are not known, but they presumably function in PTS-related regulatory capacities. All seed members are stand-alone HPr proteins, although the model also recognizes HPr domains of PTS fusion proteins. This family includes the related NPr protein.
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on