HMM Summary Page: TIGR01990

Gene SymbolpgmB
Trusted Cutoff189.40
Domain Trusted Cutoff189.40
Noise Cutoff146.10
Domain Noise Cutoff146.10
Isology Typeequivalog
EC Number5.4.2.6
HMM Length187
Mainrole CategoryEnergy metabolism
Subrole CategoryBiosynthesis and degradation of polysaccharides
Gene Ontology TermGO:0008801: beta-phosphoglucomutase activity molecular_function
GO:0046352: disaccharide catabolic process biological_process
AuthorSelengut J
Entry DateSep 24 2003 2:51PM
Last ModifiedFeb 14 2011 3:27PM
CommentThis model represents the beta-phosphoglucomutase enzyme which catalyzes the interconverison of beta-D-glucose-1-phosphate and beta-D-glucose-6-phosphate. The 6-phosphate is capable of non-enzymatic anomerization (alpha <-> beta) while the 1-phosphate is not. A separate enzyme is responsible for the isomerization of the alpha anomers. Beta-D-glucose-1-phosphate results from the phosphorylysis of maltose (, trehalose ( or trehalose-6-phosphate ( Alternatively, these reactions can be run in the synthetic direction to create the disaccharides. All sequenced genomes which contain a member of this family also appear to contain at least one putative maltose or trehalose phosphorylase. Three species, Lactococcus, Enterococcus and Neisseria appear to contain a pair of paralogous beta-PGM's. Beta-phosphoglucomutase is a member of the haloacid dehalogenase superfamily of hydrolase enzymes. These enzymes are characterized by a series of three catalytic motifs positioned within an alpha-beta (Rossman) fold [1]. beta-PGM contains an inserted alpha helical domain in between the first and second conserved motifs and thus is a member of subfamily IA of the superfamily [2,3]. The third catalytic motif comes in three variants, the third of which, containing a conserved DD or ED, is the only one found here as well as in several other related enzymes (TIGR01509). The enzyme from L. lactis has been extensively characterized including a remarkable crystal structure which traps the pentacoordinate transition state [4].
ReferencesRN [1] RM PMID: 7966317 RT Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search. RA Koonin EV, Tatusov RL. RL J Mol Biol 1994 Nov 18;244(1):125-32 RN [2] RM PMID: 11601995 RT MDP-1 is a new and distinct member of the haloacid dehalogenase family of aspartate-dependent phosphohydrolases. RA Selengut, JD RL Biochemistry 2001 Oct 23;40(42):12704-11 RN [3] RM PMID: 10956028 RT The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification wi thin the HAD enzyme superfamily. RA Morais MC, Zhang W, Baker AS, Zhang G, Dunaway-Mariano D, Allen KN. RL Biochemistry 2000 Aug 29;39(34):10385-96 RN [4] RM PMID: 12637673 RT The pentacovalent phosphorus intermediate of a phosphoryl transfer reaction. RA Lahiri SD, Zhang G, Dunaway-Mariano D, Allen KN. RL Science. 2003 Mar 28;299(5615):2067-71. Epub 2003 Mar 13.