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CAZyme Information: MGYG000002339_01963

You are here: Home > Sequence: MGYG000002339_01963

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Lacticaseibacillus saniviri
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lacticaseibacillus; Lacticaseibacillus saniviri
CAZyme ID MGYG000002339_01963
CAZy Family GT35
CAZyme Description Glycogen phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
802 MGYG000002339_57|CGC2 90074.18 5.7183
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002339 2435520 Isolate not provided not provided
Gene Location Start: 49773;  End: 52181  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT35 92 790 9.7e-248 0.9970326409495549

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK14986 PRK14986 0.0 39 792 53 812
glycogen phosphorylase; Provisional
COG0058 GlgP 0.0 2 792 3 750
Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985 PRK14985 0.0 1 788 1 794
maltodextrin phosphorylase; Provisional
TIGR02093 P_ylase 0.0 12 790 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 9 790 1 795
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QXG59129.1 0.0 1 800 1 799
QVI37339.1 0.0 1 800 1 799
QPB49158.1 0.0 1 800 1 799
ASY47944.1 0.0 1 800 1 799
QFG49474.1 0.0 1 800 1 799

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2C4M_A 4.07e-214 27 798 28 795
Starchphosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae],2C4M_B Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae],2C4M_C Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae],2C4M_D Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae]
2FFR_A 2.91e-213 27 793 35 819
Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]
1C8L_A 3.53e-213 27 801 46 838
SynergisticInhibition Of Glycogen Phosphorylase A By A Potential Antidiabetic Drug And Caffeine [Oryctolagus cuniculus],1LWN_A Crystal structure of rabbit muscle glycogen phosphorylase a in complex with a potential hypoglycaemic drug at 2.0 A resolution [Oryctolagus cuniculus],1LWO_A Crystal structure of rabbit muscle glycogen phosphorylase a in complex with a potential hypoglycaemic drug at 2.0 A resolution [Oryctolagus cuniculus],2GPA_A Allosteric Inhibition Of Glycogen Phosphorylase A By A Potential Antidiabetic Drug [Oryctolagus cuniculus],3AMV_A Allosteric Inhibition Of Glycogen Phosphorylase A By A Potential Antidiabetic Drug [Oryctolagus cuniculus]
1AXR_A 3.53e-213 27 801 46 838
CooperativityBetween Hydrogen-Bonding And Charge-Dipole Interactions In The Inhibition Of Beta-Glycosidases By Azolopyridines: Evidence From A Study With Glycogen Phosphorylase B [Oryctolagus cuniculus],1E1Y_A Flavopiridol inhibits glycogen phosphorylase by binding at the inhibitor site [Oryctolagus cuniculus],1GPY_A CRYSTALLOGRAPHIC BINDING STUDIES ON THE ALLOSTERIC INHIBITOR GLUCOSE-6-PHOSPHATE TO T STATE GLYCOGEN PHOSPHORYLASE B [Oryctolagus cuniculus],1PYG_A Structural Basis For The Activation Of Glycogen Phosphorylase B By Adenosine Monophosphate [Oryctolagus cuniculus],1PYG_B Structural Basis For The Activation Of Glycogen Phosphorylase B By Adenosine Monophosphate [Oryctolagus cuniculus],1PYG_C Structural Basis For The Activation Of Glycogen Phosphorylase B By Adenosine Monophosphate [Oryctolagus cuniculus],1PYG_D Structural Basis For The Activation Of Glycogen Phosphorylase B By Adenosine Monophosphate [Oryctolagus cuniculus],1UZU_A Glycogen Phosphorylase b in complex with indirubin-5'-sulphonate [Oryctolagus cuniculus],1XC7_A Binding of beta-D-glucopyranosyl bismethoxyphosphoramidate to glycogen phosphorylase b: Kinetic and crystallographic studies [Oryctolagus cuniculus],1XKX_A Kinetic and crystallographic studies on 2-(beta-D-glucopyranosyl)-5-methyl-1,3,4-oxadiazole,-benzothiazole, and-benzimidazole, inhibitors of muscle glycogen phosphorylase b. Evidence for a new binding site. [Oryctolagus cuniculus],1XL0_A Kinetic and crystallographic studies on 2-(beta-D-glucopyranosyl)-5-methyl-1,3,4-oxadiazole,-benzothiazole, and-benzimidazole, inhibitors of muscle glycogen phosphorylase b. Evidence for a new binding site. [Oryctolagus cuniculus],1XL1_A Kinetic and crystallographic studies on 2-(beta-D-glucopyranosyl)-5-methyl-1,3,4-oxadiazole,-benzothiazole, and-benzimidazole, inhibitors of muscle glycogen phosphorylase b. Evidence for a new binding site. [Oryctolagus cuniculus],1Z62_A Indirubin-3'-aminooxy-acetate inhibits glycogen phosphorylase by binding at the inhibitor and the allosteric site. Broad specificities of the two sites [Oryctolagus cuniculus],2AMV_A The Structure Of Glycogen Phosphorylase B With An Alkyl- Dihydropyridine-Dicarboxylic Acid [Oryctolagus cuniculus],2F3P_A Crystal Structure of the glycogen phosphorylase B / N-(beta-D-glucopyranosyl)oxamic acid complex [Oryctolagus cuniculus],2F3Q_A Crystal structure of the glycogen phosphorylase B / methyl-N-(beta-D-glucopyranosyl)oxamate complex [Oryctolagus cuniculus],2F3S_A Crystal Structure of the glycogen phosphorylase B / ethyl-N-(beta-D-glucopyranosyl)oxamate complex [Oryctolagus cuniculus],2F3U_A Crystal Structure of the glycogen phosphorylase B / N-(beta-D-glucopyranosyl)-N'-cyclopropyl oxalamide complex [Oryctolagus cuniculus],2FET_A Synthesis of C-D-Glycopyranosyl-Hydroquinones and-Benzoquinones. Inhibition of PTP1B. Inhibition of and binding to glycogen phosphorylase in the crystal [Oryctolagus cuniculus],2FF5_A Synthesis of C-D-Glycopyranosyl-Hydroquinones and-Benzoquinones. Inhibition of PTP1B. Inhibition of and binding to glycogen phosphorylase in the crystal [Oryctolagus cuniculus],3BD7_A Glycogen Phosphorylase complex with 1(-D-glucopyranosyl) thymine [Oryctolagus cuniculus],3BD8_A Glucogen Phosphorylase complex with 1(-D-glucopyranosyl) cytosine [Oryctolagus cuniculus],3BDA_A Glycogen Phosphorylase complex with 1(-D-glucopyranosyl) cyanuric acid [Oryctolagus cuniculus],5LRC_A Crystal structure of Glycogen Phosphorylase in complex with KS114 [Oryctolagus cuniculus],5LRE_A Crystal structure of Glycogen Phosphorylase b in complex with KS382 [Oryctolagus cuniculus],5LRF_A Crystal structure of Glycogen Phosphorylase b in complex with KS389 [Oryctolagus cuniculus],5O50_A Glycogen Phosphorylase b in complex with 33a [Oryctolagus cuniculus]
5OX0_A 3.64e-213 27 801 47 839
GlycogenPhosphorylase in complex with CK898 [Oryctolagus cuniculus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P39123 4.77e-259 6 792 6 796
Glycogen phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=glgP PE=2 SV=1
P0AC86 7.11e-217 48 792 57 812
Glycogen phosphorylase OS=Escherichia coli (strain K12) OX=83333 GN=glgP PE=3 SV=1
P0AC87 7.11e-217 48 792 57 812
Glycogen phosphorylase OS=Shigella flexneri OX=623 GN=glgP PE=3 SV=1
P73511 6.04e-213 27 799 48 835
Glycogen phosphorylase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=glgP PE=3 SV=1
Q9Z8N1 7.72e-213 2 790 11 814
Glycogen phosphorylase OS=Chlamydia pneumoniae OX=83558 GN=glgP PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000065 0.000010 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002339_01963.