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CAZyme Information: MGYG000000106_01685

You are here: Home > Sequence: MGYG000000106_01685

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 Enterococcus_D gallinarum
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus_D; Enterococcus_D gallinarum
CAZyme ID MGYG000000106_01685
CAZy Family GT35
CAZyme Description Glycogen phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
808 92312.01 4.9262
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000106 3151412 Isolate Canada North America
Gene Location Start: 261412;  End: 263838  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT35 92 793 1.2e-258 0.9955489614243324

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK14986 PRK14986 0.0 46 795 57 813
glycogen phosphorylase; Provisional
COG0058 GlgP 0.0 3 794 6 750
Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985 PRK14985 0.0 55 791 55 795
maltodextrin phosphorylase; Provisional
TIGR02093 P_ylase 0.0 12 792 3 794
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 7 792 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
AYY10389.1 0.0 1 808 1 808
QGR80985.1 0.0 1 808 1 808
QCT92343.1 0.0 1 808 1 808
QOG27153.1 0.0 1 808 1 808
AUJ85097.1 0.0 1 808 1 808

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5IKO_A 2.37e-219 25 803 50 842
Crystalstructure of human brain glycogen phosphorylase [Homo sapiens],5IKP_A Crystal structure of human brain glycogen phosphorylase bound to AMP [Homo sapiens]
1C50_A 5.69e-219 25 803 34 826
IdentificationAnd Structural Characterization Of A Novel Allosteric Binding Site Of Glycogen Phosphorylase B [Oryctolagus cuniculus]
1C8L_A 5.90e-219 25 803 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 5.90e-219 25 803 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]
3ZCQ_A 6.10e-219 25 803 47 839
Rabbitmuscle glycogen phosphorylase b in complex with N-(4- trifluoromethyl-benzoyl)-N-beta-D-glucopyranosyl urea determined at 2. 15 A resolution [Oryctolagus cuniculus],3ZCR_A Rabbit muscle glycogen phosphorylase b in complex with N-(4-tert- butyl-benzoyl)-N-beta-D-glucopyranosyl urea determined at 2.07 A resolution [Oryctolagus cuniculus],3ZCT_A Rabbit muscle glycogen phosphorylase b in complex with N-(2-naphthoyl) -N-beta-D-glucopyranosyl urea determined at 2.0 A resolution [Oryctolagus cuniculus],3ZCU_A Rabbit muscle glycogen phosphorylase b in complex with N-(pyridyl-2- carbonyl)-N-beta-D-glucopyranosyl urea determined at 2.05 A resolution [Oryctolagus cuniculus],3ZCV_A Rabbit muscle glycogen phosphorylase b in complex with N-(indol-2- carbonyl)-N-beta-D-glucopyranosyl urea determined at 1.8 A resolution [Oryctolagus cuniculus],4CTM_A Glucopyranosylidene-spiro-iminothiazolidinone, a New Bicyclic Ring System: Synthesis, Derivatization, and Evaluation as Glycogen Phosphorylase Inhibitors by Enzyme Kinetic and Crystallographic Methods [Oryctolagus cuniculus],4CTN_A Glucopyranosylidene-spiro-iminothiazolidinone, a New Bicyclic Ring System: Synthesis, Derivatization, and Evaluation as Glycogen Phosphorylase Inhibitors by Enzyme Kinetic and Crystallographic Methods [Oryctolagus cuniculus],4CTO_A Glucopyranosylidene-spiro-iminothiazolidinone, a New Bicyclic Ring System: Synthesis, Derivatization, and Evaluation as Glycogen Phosphorylase Inhibitors by Enzyme Kinetic and Crystallographic Methods [Oryctolagus cuniculus],4YI3_A Crystal structure of Gpb in complex with 4a [Oryctolagus cuniculus],4YI5_A Crystal structure of Gpb in complex with 4b [Oryctolagus cuniculus],4YUA_A Glycogen phosphorylase in complex with ellagic acid [Oryctolagus cuniculus],5JTT_A Crystal structure of GPb in complex with 8a [Oryctolagus cuniculus],5JTU_A Crystal structure of GPb in complex with 8b [Oryctolagus cuniculus],5LRD_A Crystal structure of Glycogen Phosphorylase b in complex with KS242 [Oryctolagus cuniculus],5MEM_A A potent fluorescent inhibitor of glycogen phosphorylase as a catalytic site probe. [Oryctolagus cuniculus],5O52_A Glycogen Phosphorylase b in complex with 33b [Oryctolagus cuniculus],5O54_A Glycogen Phosphorylase b in complex with 29a [Oryctolagus cuniculus],5O56_A Glycogen Phosphorylase b in complex with 29b [Oryctolagus cuniculus],5OWY_A Glycogen Phosphorylase in complex with KS252 [Oryctolagus cuniculus],5OWZ_A Glycogen Phosphorylase in complex with KS172 [Oryctolagus cuniculus],5OX1_A Glycogen Phosphorylase in complex with JLH270 [Oryctolagus cuniculus],5OX3_A Glycogen Phosphorylase in complex with SzB102v [Oryctolagus cuniculus],5OX4_A Glycogen Phosphorylase in complex with CK900 [Oryctolagus cuniculus],6F3J_A The crystal structure of Glycogen Phosphorylase in complex with 10a [Oryctolagus cuniculus],6F3L_A The crystal structure of Glycogen Phosphorylase in complex with 10b [Oryctolagus cuniculus],6F3R_A The crystal structure of Glycogen Phosphorylase in complex with 10c [Oryctolagus cuniculus],6F3S_A The crystal structure of Glycogen Phosphorylase in complex with 10d [Oryctolagus cuniculus],6F3U_A The crystal structure of Glycogen Phosphorylase in complex with 10h [Oryctolagus cuniculus],6QA6_A Glycogen Phosphorylase b in complex with 30 [Oryctolagus cuniculus],6QA7_A Glycogen Phosphorylase b in complex with 29 [Oryctolagus cuniculus],6QA8_A Glycogen Phosphorylase b in complex with 28 [Oryctolagus cuniculus],6R0H_A Glycogen Phosphorylase b in complex with 3 [Oryctolagus cuniculus],6R0I_A Glycogen Phosphorylase b in complex with 4 [Oryctolagus cuniculus],6S4H_A The crystal structure of glycogen phosphorylase in complex with 8 [Oryctolagus cuniculus],6S4K_A The crystal structure of glycogen phosphorylase in complex with 12 [Oryctolagus cuniculus],6S4O_A The crystal structure of glycogen phosphorylase in complex with 9 [Oryctolagus cuniculus],6S4P_A The crystal structure of glycogen phosphorylase in complex with 13 [Oryctolagus cuniculus],6S4R_A The crystal structure of glycogen phosphorylase in complex with 11 [Oryctolagus cuniculus],6S51_A The crystal structure of glycogen phosphorylase in complex with 10 [Oryctolagus cuniculus],6S52_A The crystal structure of glycogen phosphorylase in complex with 14 [Oryctolagus cuniculus],6YVE_AAA Chain AAA, Glycogen phosphorylase, muscle form [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 5.22e-278 3 795 5 797
Glycogen phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=glgP PE=2 SV=1
P0AC86 4.17e-234 25 795 36 813
Glycogen phosphorylase OS=Escherichia coli (strain K12) OX=83333 GN=glgP PE=3 SV=1
P0AC87 4.17e-234 25 795 36 813
Glycogen phosphorylase OS=Shigella flexneri OX=623 GN=glgP PE=3 SV=1
P73511 6.33e-234 23 801 46 835
Glycogen phosphorylase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=glgP PE=3 SV=1
Q9XTL9 2.85e-228 28 802 50 838
Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2

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
1.000060 0.000003 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000106_01685.