beta-phosphoglucomutase. This 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 (2.4.1.8), trehalose (2.4.1.64) or trehalose-6-phosphate (2.4.1.216). 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. 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. 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. [Energy metabolism, Biosynthesis and degradation of polysaccharides]

beta-phosphoglucomutase family hydrolase. This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509).

glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.

beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM). Lactococcus lactis beta-PGM catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate as an intermediate. In the forward G6P-forming direction, this reaction links polysaccharide phosphorolysis to glycolysis, in the reverse direction, the reaction provides G1P for the biosynthesis of exo-polysaccharides. This subfamily belongs to the beta-phosphoglucomutase-like family whose other members include Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

Beta-phosphoglucomutase or related phosphatase, HAD superfamily [Carbohydrate transport and metabolism, General function prediction only].

Structureof Pentavalent Phosphorous Intermediate of an Enzyme Catalyzed Phosphoryl transfer Reaction observed on cocrystallization with Glucose 6-phosphate [Lactococcus lactis],1O08_A Structure of Pentavalent Phosphorous Intermediate of an Enzyme Catalyzed Phosphoryl transfer Reaction observed on cocrystallization with Glucose 1-phosphate [Lactococcus lactis],1Z4N_A Structure of beta-phosphoglucomutase with inhibitor bound alpha-galactose 1-phosphate cocrystallized with Fluoride [Lactococcus lactis],1Z4N_B Structure of beta-phosphoglucomutase with inhibitor bound alpha-galactose 1-phosphate cocrystallized with Fluoride [Lactococcus lactis],1Z4O_A Structure of beta-phosphoglucomutase with inhibitor bound alpha-galactose 1-phosphate [Lactococcus lactis],1Z4O_B Structure of beta-phosphoglucomutase with inhibitor bound alpha-galactose 1-phosphate [Lactococcus lactis],1ZOL_A native beta-PGM [Lactococcus lactis],2WF5_A Structure of Beta-Phosphoglucomutase inhibited with Glucose-6-phosphate and trifluoromagnesate [Lactococcus lactis],2WF6_A Structure of Beta-Phosphoglucomutase inhibited with Glucose-6-phosphate and Aluminium tetrafluoride [Lactococcus lactis],2WF7_A Structure of Beta-Phosphoglucomutase inhibited with Glucose-6- phosphonate and Aluminium tetrafluoride [Lactococcus lactis],2WF8_A Structure of Beta-Phosphoglucomutase inhibited with Glucose-6- phosphate, Glucose-1-phosphate and Beryllium trifluoride [Lactococcus lactis],2WF9_A Structure of Beta-Phosphoglucomutase inhibited with Glucose-6- phosphate, and Beryllium trifluoride, crystal form 2 [Lactococcus lactis],2WFA_A Structure of Beta-Phosphoglucomutase inhibited with Beryllium trifluoride, in an open conformation. [Lactococcus lactis],2WHE_A Structure of native Beta-Phosphoglucomutase in an open conformation without bound ligands. [Lactococcus lactis],3ZI4_A The structure of Beta-phosphoglucomutase Inhibited With Glucose-6-phosphate and Scandium Tetrafluoride [Lactococcus lactis],4C4R_A Structure of beta-phosphoglucomutase in complex with a phosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride [Lactococcus lactis],4C4S_A Structure of beta-phosphoglucomutase in complex with an alpha- fluorophosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride [Lactococcus lactis],4C4T_A Structure of beta-phosphoglucomutase in complex with a phosphonate analogue of beta-glucose-1-phosphate and aluminium tetrafluoride [Lactococcus lactis],6H8U_A Beta-phosphoglucomutase from Lactococcus lactis in an open conformer to 1.9 A. [Lactococcus lactis subsp. lactis Il1403],6H8V_A Beta-phosphoglucomutase from Lactococcus lactis in an open conformer in the P21 spacegroup to 1.8 A. [Lactococcus lactis subsp. lactis Il1403],6H8V_B Beta-phosphoglucomutase from Lactococcus lactis in an open conformer in the P21 spacegroup to 1.8 A. [Lactococcus lactis subsp. lactis Il1403],6H8W_A Beta-phosphoglucomutase from Lactococcus lactis in an open conformer complexed with aluminium tetrafluoride to 1.9 A. [Lactococcus lactis subsp. lactis Il1403],6H8X_A Beta-phosphoglucomutase from Lactococcus lactis in an open conformer complexed with magnesium trifluoride to 1.8 A. [Lactococcus lactis subsp. lactis Il1403],6H8X_B Beta-phosphoglucomutase from Lactococcus lactis in an open conformer complexed with magnesium trifluoride to 1.8 A. [Lactococcus lactis subsp. lactis Il1403],6H93_A Beta-phosphoglucomutase from Lactococcus lactis with inorganic phosphate bound in an open conformer to 1.8 A. [Lactococcus lactis subsp. lactis Il1403],6H93_B Beta-phosphoglucomutase from Lactococcus lactis with inorganic phosphate bound in an open conformer to 1.8 A. [Lactococcus lactis subsp. lactis Il1403],6QZG_A Beta-glucose 1,6-bisphosphonate bound to wild type beta-phosphoglucomutse in an open conformation. [Lactococcus lactis subsp. lactis Il1403],6QZG_B Beta-glucose 1,6-bisphosphonate bound to wild type beta-phosphoglucomutse in an open conformation. [Lactococcus lactis subsp. lactis Il1403],6YDL_A Substrate-free beta-phosphoglucomutase from Lactococcus lactis [Lactococcus lactis subsp. lactis Il1403],6YDM_A beta-phosphoglucomutase from Lactococcus lactis with citrate, tris and acetate bound [Lactococcus lactis subsp. lactis Il1403],6YDM_B beta-phosphoglucomutase from Lactococcus lactis with citrate, tris and acetate bound [Lactococcus lactis subsp. lactis Il1403]

R49Kvariant of beta-phosphoglucomutase from Lactococcus lactis in an open conformer to 1.6 A. [Lactococcus lactis subsp. lactis Il1403],6HDH_B R49K variant of beta-phosphoglucomutase from Lactococcus lactis in an open conformer to 1.6 A. [Lactococcus lactis subsp. lactis Il1403],6HDJ_A R49K variant of beta-phosphoglucomutase from Lactococcus lactis complexed aluminium tetrafluoride and beta-G6P to 1.2 A. [Lactococcus lactis subsp. lactis Il1403],6HDL_A R49K variant of beta-phosphoglucomutase from Lactococcus lactis complexed with magnesium trifluoride and beta-G6P to 1.2 A. [Lactococcus lactis subsp. lactis Il1403]

Structureof the D10N mutant of beta-phosphoglucomutase from Lactococcus lactis trapped with native reaction intermediate beta-glucose 1,6-bisphosphate to 2.2A resolution. [Lactococcus lactis],5OK1_A D10N variant of beta-phosphoglucomutase from Lactococcus lactis trapped with native beta-glucose 1,6-bisphosphate intermediate to 1.9A resolution. [Lactococcus lactis],5OK2_A Structure of the D10N mutant of beta-phosphoglucomutase from Lactococcus lactis inhibited with glucose 6-phosphate and tetrafluoroaluminate to 1.1A resolution. [Lactococcus lactis]

D10Nvariant of beta-phosphoglucomutase from Lactococcus lactis inhibited by a beryllium triflouride phosphoenzyme analogue to 1.3A resolution. [Lactococcus lactis]

T16Avariant of beta-phosphoglucomutase from Lactococcus lactis in an open conformer complexed with aluminium tetrafluoride to 1.9 A. [Lactococcus lactis subsp. lactis Il1403],6H8Z_A T16A variant of beta-phosphoglucomutase from Lactococcus lactis in an open conformer complexed with magnesium trifluoride to 1.6 A. [Lactococcus lactis subsp. lactis Il1403],6H94_A T16A variant of beta-phosphoglucomutase from Lactococcus lactis with phosphate and TRIS bound in an open conformer to 1.5 A. [Lactococcus lactis subsp. lactis Il1403]

Beta-phosphoglucomutase OS=Lactococcus lactis subsp. lactis (strain IL1403) OX=272623 GN=pgmB PE=1 SV=2

Beta-phosphoglucomutase OS=Bacillus subtilis (strain 168) OX=224308 GN=yvdM PE=1 SV=1

Alpha-galactosidase Mel36A OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=melA PE=1 SV=1

Beta-phosphoglucomutase OS=Escherichia coli (strain K12) OX=83333 GN=ycjU PE=1 SV=1

Alpha-galactosidase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=aga PE=3 SV=3