Structure for haloacid dehalogenase-like hydrolase domain containing 2: Difference between revisions
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| HYDROLASE: histidine biosynthesis bifunctional protein | | HYDROLASE: histidine biosynthesis bifunctional protein | ||
| HisB from Escherichia coli is a bifunctional enzyme catalyzing the sixth and eighth steps of l-histidine biosynthesis. The N-terminal domain (HisB-N) possesses histidinol phosphate phosphatase activity, and its crystal structure shows a single domain with fold similarity to the haloacid dehalogenase (HAD) enzyme family. (Pubmed) | | HisB from Escherichia coli is a bifunctional enzyme catalyzing the sixth and eighth steps of l-histidine biosynthesis. The N-terminal domain (HisB-N) possesses histidinol phosphate phosphatase activity, and its crystal structure shows a single domain with fold similarity to the haloacid dehalogenase (HAD) enzyme family. (Pubmed) | ||
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| HYDROLASE: phosphoserine phosphatase (psp) (in Methanococcus jannaschii) | |||
| D-Serine is a co-agonist of the N-methyl-D-aspartate subtype of glutamate receptors, a major neurotransmitter receptor family in mammalian nervous systems. D-Serine is converted from L-serine, 90% of which is the product of the enzyme phosphoserine phosphatase (PSP). PSP from M. jannaschii (MJ) shares significant sequence homology with human PSP. PSPs and P-type ATPases are members of the haloacid dehalogenase (HAD)-like hydrolase family, and all members share three conserved sequence motifs. PSP and P-type ATPases utilize a common mechanism that involves Mg(2+)-dependent phosphorylation and autodephosphorylation at an aspartyl side chain in the active site (Abstract from PBD). | |||
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Revision as of 06:18, 8 May 2007
Structure similarity Table (results from dali search)
number | PDB code | structural similarity (RMSD) (better if zero) | seuqence identity (%IDE) (better if 100%) | protein name | comments |
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2 | 1pw5 | 2.9 | 25 | STRUCTURAL GENOMICS, UNKNOWN FUNCTION, nagd protein, pu | Could be a hydrolase, not sure |
3 | 2hx1 | 4.7 | 23 | HYDROLASE: predicted sugar phosphatases of the had superfamily | The E. coli HAD phosphatases show high catalytic efficiency and affinity to a wide range of phosphorylated metabolites that are intermediates of various metabolic reactions. (pubmed) |
4 | 1o03 | 2.5 | 24 | ISOMERASE: beta-phosphoglucomutase (in lactococcus lactis) | Phosphoglucomutases catalyze the interconversion of D-glucose 1-phosphate and D-glucose 6-phosphate, a reaction central to energy metabolism in all cells and to the synthesis of cell wall polysaccharides in bacterial cells. Two classes of phosphoglucomutases (alpha-PGM and beta-PGM) are distinguished on the basis of their specificity for alpha- and beta-glucose-1-phosphate. beta-PGM is a member of the haloacid dehalogenase (HAD) superfamily, which includes the sarcoplasmic Ca(2+)-ATPase, phosphomannomutase, and phosphoserine phosphatase. beta-PGM is unusual among family members in that the common phosphoenzyme intermediate exists as a stable ground-state complex in this enzyme. Herein we report, for the first time, the three-dimensional structure of a beta-PGM and the first view of the true phosphoenzyme intermediate in the HAD superfamily. (Pubmed) |
22 | 2fpx | 3.3 | 20 | HYDROLASE: histidine biosynthesis bifunctional protein | HisB from Escherichia coli is a bifunctional enzyme catalyzing the sixth and eighth steps of l-histidine biosynthesis. The N-terminal domain (HisB-N) possesses histidinol phosphate phosphatase activity, and its crystal structure shows a single domain with fold similarity to the haloacid dehalogenase (HAD) enzyme family. (Pubmed) |
35 | 3.1 | 23 | HYDROLASE: phosphoserine phosphatase (psp) (in Methanococcus jannaschii) | D-Serine is a co-agonist of the N-methyl-D-aspartate subtype of glutamate receptors, a major neurotransmitter receptor family in mammalian nervous systems. D-Serine is converted from L-serine, 90% of which is the product of the enzyme phosphoserine phosphatase (PSP). PSP from M. jannaschii (MJ) shares significant sequence homology with human PSP. PSPs and P-type ATPases are members of the haloacid dehalogenase (HAD)-like hydrolase family, and all members share three conserved sequence motifs. PSP and P-type ATPases utilize a common mechanism that involves Mg(2+)-dependent phosphorylation and autodephosphorylation at an aspartyl side chain in the active site (Abstract from PBD). |