Structure for haloacid dehalogenase-like hydrolase domain containing 2

[| Sequence Details ]

[| Ideogram of HDHD2]

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
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).