Glucan phosphorylase [Carbohydrate transport and metabolism].

alpha-glucan phosphorylases. This family consists of known phosphorylases, and homologs believed to share the function of using inorganic phosphate to cleave an alpha 1,4 linkage between the terminal glucose residue and the rest of the polymer (maltodextrin, glycogen, etc.). The name of the glucose storage polymer substrate, and therefore the name of this enzyme, depends on the chain lengths and branching patterns. A number of the members of this family have been shown to operate on small maltodextrins, as may be obtained by utilization of exogenous sources. This family represents a distinct clade from the related family modeled by TIGR02093/pfam00343.

proteins similar to glycogen phosphorylase. This family is most closely related to the oligosaccharide phosphorylase domain family and other unidentified sequences. Oligosaccharide phosphorylase catalyzes the breakdown of oligosaccharides into glucose-1-phosphate units. They are important allosteric enzymes in carbohydrate metabolism.

Protein of unknown function (DUF3417). This family of proteins are functionally uncharacterized. This protein is found in bacteria and archaea. Proteins in this family are typically between 145 to 860 amino acids in length. This protein is found associated with pfam00343. This protein has a conserved AYF sequence motif.

glycogen phosphorylase and similar proteins. This is a family of oligosaccharide phosphorylases. It includes yeast and mammalian glycogen phosphorylases, plant starch/glucan phosphorylase, as well as the maltodextrin phosphorylases of bacteria. The members of this family catalyze the breakdown of oligosaccharides into glucose-1-phosphate units. They are important allosteric enzymes in carbohydrate metabolism. The allosteric control mechanisms of yeast and mammalian members of this family are different from that of bacterial members. The members of this family belong to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.

Crystalstructure of putative glycogen phosphorylase from Streptococcus mutans [Streptococcus mutans UA159]

Structureof plastidial phosphorylase Pho1 from Barley [Hordeum vulgare subsp. vulgare],5LR8_B Structure of plastidial phosphorylase Pho1 from Barley [Hordeum vulgare subsp. vulgare],5LRA_A Plastidial phosphorylase PhoI from barley in complex with maltotetraose [Hordeum vulgare subsp. vulgare],5LRA_B Plastidial phosphorylase PhoI from barley in complex with maltotetraose [Hordeum vulgare subsp. vulgare],5LRB_A Plastidial phosphorylase from Barley in complex with acarbose [Hordeum vulgare subsp. vulgare],5LRB_B Plastidial phosphorylase from Barley in complex with acarbose [Hordeum vulgare subsp. vulgare]

Maltodextrin phosphorylase OS=Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C) OX=523849 GN=malP PE=1 SV=1

Glycogen phosphorylase OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) OX=233413 GN=glgP PE=3 SV=1

Glycogen phosphorylase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=glgP PE=1 SV=1

Glycogen phosphorylase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=glgP PE=3 SV=1

Glycogen phosphorylase OS=Aquifex aeolicus (strain VF5) OX=224324 GN=glgP PE=3 SV=1