1,3-beta-galactosyl-N-acetylhexosamine phosphorylase. Members of this family are found in phylogenetically diverse bacteria, including Clostridium perfringens (in the Firmicutes), Bifidobacterium longum and Propionibacterium acnes (in the Actinobacteria), and Vibrio vulnificus (in the Proteobacteria), most of which occur as mammalian pathogens or commensals. The nominal activity, 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase (EC 2.4.1.211), varies somewhat from instance to instance in relative rates for closely related substrates. [Energy metabolism, Biosynthesis and degradation of polysaccharides]

Lacto-N-biose phosphorylase N-terminal TIM barrel domain. The gene which codes for this protein in gut-bacteria is located in a novel putative operon for galactose metabolism. The protein appears to be a carbohydrate-processing phosphorolytic enzyme (EC:2.4.1.211), unlike either glycoside hydrolases or glycoside lyase. Intestinal colonisation by bifidobacteria is important for human health, especially in pediatrics, because colonisation seems to prevent infection by some pathogenic bacteria that cause diarrhoea or other illnesses. The operon seems to be involved in intestinal colonisation by bifidobacteria mediated by metabolism of mucin sugars. In addition, it may also resolve the question of the nature of the bifidus factor in human milk as the lacto-N-biose structure found in milk oligosaccharides.

Lacto-N-biose phosphorylase central domain. The gene which codes for this protein in gut-bacteria is located in a novel putative operon for galactose metabolism. The protein appears to be a carbohydrate-processing phosphorolytic enzyme (EC:2.4.1.211), unlike either glycoside hydrolases or glycoside lyase. Intestinal colonisation by bifidobacteria is important for human health, especially in pediatrics, because colonisation seems to prevent infection by some pathogenic bacteria that cause diarrhoea or other illnesses. The operon seems to be involved in intestinal colonisation by bifidobacteria mediated by metabolism of mucin sugars. In addition, it may also resolve the question of the nature of the bifidus factor in human milk as the lacto-N-biose structure found in milk oligosaccharides.

Lacto-N-biose phosphorylase C-terminal domain. The gene which codes for this protein in gut-bacteria is located in a novel putative operon for galactose metabolism. The protein appears to be a carbohydrate-processing phosphorolytic enzyme (EC:2.4.1.211), unlike either glycoside hydrolases or glycoside lyase. Intestinal colonisation by bifidobacteria is important for human health, especially in pediatrics, because colonisation seems to prevent infection by some pathogenic bacteria that cause diarrhoea or other illnesses. The operon seems to be involved in intestinal colonisation by bifidobacteria mediated by metabolism of mucin sugars. In addition, it may also resolve the question of the nature of the bifidus factor in human milk as the lacto-N-biose structure found in milk oligosaccharides.

Type 1 glutamine amidotransferase (GATase1)-like domain. Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.

Crystalstructure of Galacto-N-Biose/Lacto-N-Biose I Phosphorylase C236Y Mutant [Bifidobacterium longum subsp. longum JCM 1217],3WFZ_B Crystal structure of Galacto-N-Biose/Lacto-N-Biose I Phosphorylase C236Y Mutant [Bifidobacterium longum subsp. longum JCM 1217],3WFZ_C Crystal structure of Galacto-N-Biose/Lacto-N-Biose I Phosphorylase C236Y Mutant [Bifidobacterium longum subsp. longum JCM 1217],3WFZ_D Crystal structure of Galacto-N-Biose/Lacto-N-Biose I Phosphorylase C236Y Mutant [Bifidobacterium longum subsp. longum JCM 1217]

Crystalstructure of Galacto-N-biose/Lacto-N-biose I phosphorylase [Bifidobacterium longum],2ZUS_B Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase [Bifidobacterium longum],2ZUS_C Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase [Bifidobacterium longum],2ZUS_D Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase [Bifidobacterium longum],2ZUT_A Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GalNAc [Bifidobacterium longum],2ZUT_B Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GalNAc [Bifidobacterium longum],2ZUT_C Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GalNAc [Bifidobacterium longum],2ZUT_D Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GalNAc [Bifidobacterium longum],2ZUU_A Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GlcNAc [Bifidobacterium longum],2ZUU_B Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GlcNAc [Bifidobacterium longum],2ZUU_C Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GlcNAc [Bifidobacterium longum],2ZUU_D Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GlcNAc [Bifidobacterium longum],2ZUV_A Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GlcNAc, Ethylene glycol, and nitrate [Bifidobacterium longum],2ZUV_B Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GlcNAc, Ethylene glycol, and nitrate [Bifidobacterium longum],2ZUW_A Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GlcNAc and sulfate [Bifidobacterium longum],2ZUW_B Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GlcNAc and sulfate [Bifidobacterium longum],2ZUW_C Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GlcNAc and sulfate [Bifidobacterium longum],2ZUW_D Crystal structure of Galacto-N-biose/Lacto-N-biose I phosphorylase in complex with GlcNAc and sulfate [Bifidobacterium longum]

1,3-beta-galactosyl-N-acetylhexosamine phosphorylase Cphy0577 OS=Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) OX=357809 GN=Cphy_0577 PE=1 SV=1

1,3-beta-galactosyl-N-acetylhexosamine phosphorylase Cphy3030 OS=Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) OX=357809 GN=Cphy_3030 PE=1 SV=1

1,3-beta-galactosyl-N-acetylhexosamine phosphorylase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=lnpA PE=1 SV=1

D-galactosyl-beta-1->4-L-rhamnose phosphorylase OS=Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) OX=357809 GN=Cphy_1920 PE=1 SV=1