| Accession | TIGR01990 |
| Name | bPGM |
| Function | beta-phosphoglucomutase |
| Gene Symbol | pgmB |
| Trusted Cutoff | 189.40 |
| Domain Trusted Cutoff | 189.40 |
| Noise Cutoff | 146.10 |
| Domain Noise Cutoff | 146.10 |
| Isology Type | equivalog |
| EC Number | 5.4.2.6 |
| HMM Length | 187 |
| Mainrole Category | Energy metabolism |
| Subrole Category | Biosynthesis and degradation of polysaccharides |
| Gene Ontology Term | GO:0008801: beta-phosphoglucomutase activity molecular_function |
| | GO:0046352: disaccharide catabolic process biological_process |
| Author | Selengut J |
| Entry Date | Sep 24 2003 2:51PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | 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 [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]. |
| References | RN [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. |
