Species | Ligilactobacillus agilis | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Ligilactobacillus; Ligilactobacillus agilis | |||||||||||
CAZyme ID | MGYG000002390_00347 | |||||||||||
CAZy Family | GT35 | |||||||||||
CAZyme Description | Glycogen phosphorylase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 138146; End: 140584 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT35 | 93 | 796 | 4.7e-260 | 0.9970326409495549 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
PRK14986 | PRK14986 | 0.0 | 40 | 798 | 49 | 813 | glycogen phosphorylase; Provisional |
COG0058 | GlgP | 0.0 | 2 | 796 | 3 | 749 | Glucan phosphorylase [Carbohydrate transport and metabolism]. |
PRK14985 | PRK14985 | 0.0 | 57 | 796 | 55 | 797 | maltodextrin phosphorylase; Provisional |
TIGR02093 | P_ylase | 0.0 | 12 | 795 | 1 | 794 | glycogen/starch/alpha-glucan phosphorylases. This family consists of phosphorylases. Members use phosphate to break alpha 1,4 linkages between pairs of glucose residues at the end of long glucose polymers, releasing alpha-D-glucose 1-phosphate. The nomenclature convention is to preface the name according to the natural substrate, as in glycogen phosphorylase, starch phosphorylase, maltodextrin phosphorylase, etc. Name differences among these substrates reflect differences in patterns of branching with alpha 1,6 linkages. Members include allosterically regulated and unregulated forms. A related family, TIGR02094, contains examples known to act well on particularly small alpha 1,4 glucans, as may be found after import from exogenous sources. [Energy metabolism, Biosynthesis and degradation of polysaccharides] |
cd04300 | GT35_Glycogen_Phosphorylase | 0.0 | 10 | 795 | 2 | 795 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ASR41255.1 | 0.0 | 1 | 812 | 1 | 812 |
AUJ31275.1 | 0.0 | 1 | 812 | 1 | 810 |
QIA89772.1 | 0.0 | 1 | 812 | 1 | 810 |
AWZ40467.1 | 0.0 | 1 | 812 | 1 | 810 |
AWZ38538.1 | 0.0 | 1 | 812 | 1 | 810 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1Z8D_A | 2.74e-215 | 24 | 796 | 41 | 829 | ChainA, Glycogen phosphorylase, muscle form [Homo sapiens] |
1E4O_A | 5.02e-215 | 59 | 796 | 57 | 795 | Phosphorylaserecognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question [Escherichia coli],1E4O_B Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question [Escherichia coli],1QM5_A Phosphorylase recognition and phosphorylysis of its oligosaccharide substrate: answers to a long outstanding question [Escherichia coli],1QM5_B Phosphorylase recognition and phosphorylysis of its oligosaccharide substrate: answers to a long outstanding question [Escherichia coli] |
1L5V_A | 1.00e-214 | 59 | 796 | 57 | 795 | CrystalStructure of the Maltodextrin Phosphorylase complexed with Glucose-1-phosphate [Escherichia coli],1L5V_B Crystal Structure of the Maltodextrin Phosphorylase complexed with Glucose-1-phosphate [Escherichia coli],1L5W_A Crystal Structure of the Maltodextrin Phosphorylase Complexed with the Products of the Enzymatic Reaction between Glucose-1-phosphate and Maltotetraose [Escherichia coli],1L5W_B Crystal Structure of the Maltodextrin Phosphorylase Complexed with the Products of the Enzymatic Reaction between Glucose-1-phosphate and Maltotetraose [Escherichia coli],1L6I_A Crystal Structure of the Maltodextrin Phosphorylase complexed with the products of the enzymatic reaction between glucose-1-phosphate and maltopentaose [Escherichia coli],1L6I_B Crystal Structure of the Maltodextrin Phosphorylase complexed with the products of the enzymatic reaction between glucose-1-phosphate and maltopentaose [Escherichia coli],2ASV_A Chain A, Maltodextrin phosphorylase [Escherichia coli],2ASV_B Chain B, Maltodextrin phosphorylase [Escherichia coli],2AV6_A Chain A, Maltodextrin phosphorylase [Escherichia coli],2AV6_B Chain B, Maltodextrin phosphorylase [Escherichia coli],2AW3_A X-Ray studies on maltodextrin phosphorylase complexes: recognition of substrates and cathalitic mechanism of phosphorylase family [Escherichia coli],2AW3_B X-Ray studies on maltodextrin phosphorylase complexes: recognition of substrates and cathalitic mechanism of phosphorylase family [Escherichia coli],2AZD_A Chain A, Maltodextrin phosphorylase [Escherichia coli],2AZD_B Chain B, Maltodextrin phosphorylase [Escherichia coli] |
2GJ4_A | 1.23e-214 | 24 | 796 | 29 | 817 | Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus] |
2GM9_A | 1.27e-214 | 24 | 796 | 29 | 817 | Structureof rabbit muscle glycogen phosphorylase in complex with thienopyrrole [Oryctolagus cuniculus],5MCB_A Glycogen phosphorylase in complex with chlorogenic acid. [Oryctolagus cuniculus],7ONF_A Chain A, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P39123 | 6.11e-265 | 4 | 796 | 4 | 795 | Glycogen phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=glgP PE=2 SV=1 |
P45180 | 1.24e-227 | 25 | 801 | 39 | 820 | Glycogen phosphorylase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=glgP PE=3 SV=1 |
P73511 | 4.91e-226 | 27 | 798 | 48 | 829 | Glycogen phosphorylase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=glgP PE=3 SV=1 |
P0AC87 | 5.24e-225 | 27 | 798 | 36 | 813 | Glycogen phosphorylase OS=Shigella flexneri OX=623 GN=glgP PE=3 SV=1 |
P0AC86 | 5.24e-225 | 27 | 798 | 36 | 813 | Glycogen phosphorylase OS=Escherichia coli (strain K12) OX=83333 GN=glgP PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000082 | 0.000003 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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