dihydroxyacetone kinase subunit DhaK is the dihydroxyacetone binding subunit of dihydroxyacetone kinase, which catalyzes the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone via a phosphoryl group transfer from DhaL-ATP
dihydroxyacetone kinase, DhaK subunit; Two types of dihydroxyacetone kinase (glycerone kinase) ...
1-352
0e+00
dihydroxyacetone kinase, DhaK subunit; Two types of dihydroxyacetone kinase (glycerone kinase) are described. In yeast and a few bacteria, e.g. Citrobacter freundii, the enzyme is a single chain that uses ATP as phosphoryl donor and is designated EC 2.7.1.29. By contract, E. coli and many other bacterial species have a multisubunit form (EC 2.7.1.-) with a phosphoprotein donor related to PTS transport proteins. This family represents the DhaK subunit of the latter type of dihydroxyacetone kinase, but it specifically excludes the DhaK paralog DhaK2 (TIGR02362) found in the same operon as DhaK and DhaK in the Firmicutes.
Pssm-ID: 274098 Cd Length: 329 Bit Score: 507.66 E-value: 0e+00
universal stress protein Rv2623 and similar proteins, USP repeat 2; Mycobacterium tuberculosis ...
7-74
9.11e-03
universal stress protein Rv2623 and similar proteins, USP repeat 2; Mycobacterium tuberculosis universal stress protein Rv2623 regulates mycobacterial growth in vitro and in vivo and is required for the entry of the tubercle bacillus into the chronic phase of infection in the host. In addition, Rv2623 binds ATP and the growth-regulatory attribute of this USP is dependent on its ATP-binding activity. Rv2623 is thought to function as an ATP-dependent signaling intermediate in a pathway that promotes persistent infection. The universal stress protein Usp is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. Usp enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. The crystal structure of Haemophilus influenzae Usp reveals an alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, which binds ATP, although Usp lacks ATP-binding activity.
Pssm-ID: 467507 [Multi-domain] Cd Length: 133 Bit Score: 35.95 E-value: 9.11e-03
dihydroxyacetone kinase, DhaK subunit; Two types of dihydroxyacetone kinase (glycerone kinase) ...
1-352
0e+00
dihydroxyacetone kinase, DhaK subunit; Two types of dihydroxyacetone kinase (glycerone kinase) are described. In yeast and a few bacteria, e.g. Citrobacter freundii, the enzyme is a single chain that uses ATP as phosphoryl donor and is designated EC 2.7.1.29. By contract, E. coli and many other bacterial species have a multisubunit form (EC 2.7.1.-) with a phosphoprotein donor related to PTS transport proteins. This family represents the DhaK subunit of the latter type of dihydroxyacetone kinase, but it specifically excludes the DhaK paralog DhaK2 (TIGR02362) found in the same operon as DhaK and DhaK in the Firmicutes.
Pssm-ID: 274098 Cd Length: 329 Bit Score: 507.66 E-value: 0e+00
dihydroxyacetone kinase, ATP-dependent; This family consists of examples of the form of ...
2-354
5.21e-82
dihydroxyacetone kinase, ATP-dependent; This family consists of examples of the form of dihydroxyacetone kinase (also called glycerone kinase) that uses ATP (2.7.1.29) as the phosphate donor, rather than a phosphoprotein as in E. coli. This form is composed of a single chain with separable domains homologous to the K and L subunits of the E. coli enzyme, and is found in yeasts and other eukaryotes and in some bacteria, including Citrobacter freundii. The member from tomato has been shown to phosphorylate dihydroxyacetone, 3,4-dihydroxy-2-butanone, and some other aldoses and ketoses ().
Pssm-ID: 274097 [Multi-domain] Cd Length: 574 Bit Score: 260.39 E-value: 5.21e-82
universal stress protein Rv2623 and similar proteins, USP repeat 2; Mycobacterium tuberculosis ...
7-74
9.11e-03
universal stress protein Rv2623 and similar proteins, USP repeat 2; Mycobacterium tuberculosis universal stress protein Rv2623 regulates mycobacterial growth in vitro and in vivo and is required for the entry of the tubercle bacillus into the chronic phase of infection in the host. In addition, Rv2623 binds ATP and the growth-regulatory attribute of this USP is dependent on its ATP-binding activity. Rv2623 is thought to function as an ATP-dependent signaling intermediate in a pathway that promotes persistent infection. The universal stress protein Usp is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. Usp enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. The crystal structure of Haemophilus influenzae Usp reveals an alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, which binds ATP, although Usp lacks ATP-binding activity.
Pssm-ID: 467507 [Multi-domain] Cd Length: 133 Bit Score: 35.95 E-value: 9.11e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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