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CAZyme Information: MGYG000004359_00181

You are here: Home > Sequence: MGYG000004359_00181

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
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Anaerostipes;
CAZyme ID MGYG000004359_00181
CAZy Family GT35
CAZyme Description Glycogen phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
816 MGYG000004359_1|CGC2 94267.31 6.6209
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004359 2435549 MAG Israel Asia
Gene Location Start: 187488;  End: 189938  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT35 96 812 7.3e-252 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 16 816 21 814
glycogen phosphorylase; Provisional
COG0058 GlgP 0.0 19 812 16 748
Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985 PRK14985 0.0 62 810 56 794
maltodextrin phosphorylase; Provisional
TIGR02093 P_ylase 0.0 16 812 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 13 812 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
QCP35769.1 0.0 7 812 8 813
BCD36164.1 0.0 7 812 8 813
QMW70944.1 0.0 7 812 8 813
AQP40142.1 0.0 9 816 6 813
AYH39922.1 0.0 9 815 2 813

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1ABB_A 4.34e-234 3 816 9 822
ControlOf Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate [Oryctolagus cuniculus],1ABB_B Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate [Oryctolagus cuniculus],1ABB_C Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate [Oryctolagus cuniculus],1ABB_D Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate [Oryctolagus cuniculus]
1C50_A 4.63e-234 3 816 6 819
IdentificationAnd Structural Characterization Of A Novel Allosteric Binding Site Of Glycogen Phosphorylase B [Oryctolagus cuniculus]
1B4D_A 6.85e-234 3 816 18 831
AmidocarbamateInhibitor Of Glycogen Phosphorylase [Oryctolagus cuniculus],1BX3_A Effects Of Commonly Used Cryoprotectants On Glycogen Phosphorylase Activity And Structure [Oryctolagus cuniculus],1C8K_A Flavopiridol Inhibits Glycogen Phosphorylase By Binding At The Inhibitor Site [Oryctolagus cuniculus],1FS4_A Structures of glycogen phosphorylase-inhibitor complexes and the implications for structure-based drug design [Oryctolagus cuniculus],1FTQ_A Structures Of Glycogen Phosphorylase-Inhibitor Complexes And The Implications For Structure-Based Drug Design [Oryctolagus cuniculus],1FTW_A Structures Of Glycogen Phosphorylase-Inhibitor Complexes And The Implications For Structure-Based Drug Design [Oryctolagus cuniculus],1FTY_A Structures Of Glycogen Phosphorylase-Inhibitor Complexes And The Implications For Structure-Based Drug Design [Oryctolagus cuniculus],1FU4_A Structures Of Glycogen Phosphorylase-Inhibitor Complexes And The Implications For Structure-Based Drug Design [Oryctolagus cuniculus],1FU7_A Structures Of Glycogen Phosphorylase-Inhibitor Complexes And The Implications For Structure-Based Drug Design [Oryctolagus cuniculus],1FU8_A Structures Of Glycogen Phosphorylase-Inhibitor Complexes And The Implications For Structure-Based Drug Design [Oryctolagus cuniculus],1GFZ_A Flavopiridol Inhibits Glycogen Phosphorylase By Binding At The Inhibitor Site [Oryctolagus cuniculus],1GG8_A Design Of Inhibitors Of Glycogen Phosphorylase: A Study Of Alpha-And Beta-C-Glucosides And 1-Thio-Beta-D-Glucose Compounds [Oryctolagus cuniculus],1GGN_A Structures of glycogen phosphorylase-inhibitor complexes and the implications for structure-based drug design [Oryctolagus cuniculus],1GPB_A GLYCOGEN PHOSPHORYLASE B: DESCRIPTION OF THE PROTEIN STRUCTURE [Oryctolagus cuniculus],1H5U_A THE 1.76 A RESOLUTION CRYSTAL STRUCTURE OF GLYCOGEN PHOSPHORYLASE B COMPLEXED WITH GLUCOSE AND CP320626, A POTENTIAL ANTIDIABETIC DRUG [Oryctolagus cuniculus],1HLF_A Binding Of Glucopyranosylidene-spiro-thiohydantoin To Glycogen Phosphorylase B: Kinetic And Crystallographic Stud [Oryctolagus cuniculus],1K06_A Crystallographic Binding Study of 100 mM N-benzoyl-N'-beta-D-glucopyranosyl urea to glycogen phosphorylase b [Oryctolagus cuniculus],1K08_A Crystallographic Binding Study of 10 mM N-benzoyl-N'-beta-D-glucopyranosyl urea to glycogen phosphorylase b [Oryctolagus cuniculus],1KTI_A Binding Of 100 Mm N-Acetyl-N'-Beta-D-Glucopyranosyl Urea To Glycogen Phosphorylase B: Kinetic And Crystallographic Studies [Oryctolagus cuniculus],1P29_A Crystal Structure of glycogen phosphorylase b in complex with maltopentaose [Oryctolagus cuniculus],1P2B_A Crystal Structure of Glycogen Phosphorylase B in Complex with Maltoheptaose [Oryctolagus cuniculus],1P2D_A Crystal Structure of Glycogen Phosphorylase B in complex with Beta Cyclodextrin [Oryctolagus cuniculus],1P2G_A Crystal Structure of Glycogen Phosphorylase B in complex with Gamma Cyclodextrin [Oryctolagus cuniculus],1P4G_A Crystal structure of glycogen phosphorylase b in complex with C-(1-azido-alpha-D-glucopyranosyl)formamide [Oryctolagus cuniculus],1P4H_A Crystal structure of glycogen phosphorylase b in complex with C-(1-acetamido-alpha-D-glucopyranosyl) formamide [Oryctolagus cuniculus],1P4J_A Crystal structure of glycogen phosphorylase b in complex with C-(1-hydroxy-beta-D-glucopyranosyl)formamide [Oryctolagus cuniculus],1WUT_A Acyl Ureas as Human Liver Glycogen Phosphorylase Inhibitors for the Treatment of Type 2 Diabetes [Oryctolagus cuniculus],1WUY_A Crystallographic studies on acyl ureas, a new class of inhibitors of glycogen phosphorylase. Broad specificity of the allosteric site [Oryctolagus cuniculus],1WV0_A Crystallographic studies on acyl ureas, a new class of inhibitors of glycogen phosphorylase. Broad specificity of the allosteric site [Oryctolagus cuniculus],1WV1_A Crystallographic studies on acyl ureas, a new class of inhibitors of glycogenphosphorylase. Broad specificity of the allosteric site [Oryctolagus cuniculus],1WW2_A Crystallographic studies on two bioisosteric analogues, N-acetyl-beta-D-glucopyranosylamine and N-trifluoroacetyl-beta-D-glucopyranosylamine, potent inhibitors of muscle glycogen phosphorylase [Oryctolagus cuniculus],1WW3_A Crystallographic studies on two bioisosteric analogues, N-acetyl-beta-D-glucopyranosylamine and N-trifluoroacetyl-beta-D-glucopyranosylamine, potent inhibitors of muscle glycogen phosphorylase [Oryctolagus cuniculus],2GPB_A COMPARISON OF THE BINDING OF GLUCOSE AND GLUCOSE-1-PHOSPHATE DERIVATIVES TO T-STATE GLYCOGEN PHOSPHORYLASE B [Oryctolagus cuniculus],2IEG_A Crystal structure of rabbit muscle glycogen phosphorylase in complex with 3,4-dihydro-2-quinolone [Oryctolagus cuniculus],2IEG_B Crystal structure of rabbit muscle glycogen phosphorylase in complex with 3,4-dihydro-2-quinolone [Oryctolagus cuniculus],2IEI_A Crystal structure of rabbit muscle glycogen phosphorylase in complex with 3,4-dihydro-2-quinolone [Oryctolagus cuniculus],2IEI_B Crystal structure of rabbit muscle glycogen phosphorylase in complex with 3,4-dihydro-2-quinolone [Oryctolagus cuniculus],2PRI_A BINDING OF 2-DEOXY-GLUCOSE-6-PHOSPHATE TO GLYCOGEN PHOSPHORYLASE B [Oryctolagus cuniculus],2PRJ_A Binding of N-acetyl-beta-D-glucopyranosylamine to Glycogen Phosphorylase B [Oryctolagus cuniculus],2QN7_A Glycogen Phosphorylase b in complex with N-4-hydroxybenzoyl-N'-4-beta-D-glucopyranosyl urea [Oryctolagus cuniculus],2QN8_A Glycogen Phosphorylase b in complex with N-4-nitrobenzoyl-N'-beta-D-glucopyranosyl urea [Oryctolagus cuniculus],2QN9_A Glycogen Phosphorylase in complex with N-4-aminobenzoyl-N'-beta-D-glucopyranosyl urea [Oryctolagus cuniculus],2SKC_A Pyridoxal Phosphorylase B In Complex With Fluorophosphate, Glucose And Inosine-5'-Monophosphate [Oryctolagus cuniculus],2SKD_A Pyridoxal Phosphorylase B In Complex With Phosphate, Glucose And Inosine-5'-Monophosphate [Oryctolagus cuniculus],2SKE_A Pyridoxal Phosphorylase B In Complex With Phosphite, Glucose And Inosine-5'-monophosphate [Oryctolagus cuniculus],3GPB_A COMPARISON OF THE BINDING OF GLUCOSE AND GLUCOSE-1-PHOSPHATE DERIVATIVES TO T-STATE GLYCOGEN PHOSPHORYLASE B [Oryctolagus cuniculus],4GPB_A COMPARISON OF THE BINDING OF GLUCOSE AND GLUCOSE-1-PHOSPHATE DERIVATIVES TO T-STATE GLYCOGEN PHOSPHORYLASE B [Oryctolagus cuniculus],5GPB_A COMPARISON OF THE BINDING OF GLUCOSE AND GLUCOSE-1-PHOSPHATE DERIVATIVES TO T-STATE GLYCOGEN PHOSPHORYLASE B [Oryctolagus cuniculus],6GPB_A REFINED CRYSTAL STRUCTURE OF THE PHOSPHORYLASE-HEPTULOSE 2-PHOSPHATE-OLIGOSACCHARIDE-AMP COMPLEX [Oryctolagus cuniculus],7GPB_A STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY PHOSPHORYLATION AND AMP [Oryctolagus cuniculus],7GPB_B STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY PHOSPHORYLATION AND AMP [Oryctolagus cuniculus],7GPB_C STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY PHOSPHORYLATION AND AMP [Oryctolagus cuniculus],7GPB_D STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY PHOSPHORYLATION AND AMP [Oryctolagus cuniculus],8GPB_A STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY PHOSPHORYLATION AND AMP [Oryctolagus cuniculus],9GPB_A THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE [Oryctolagus cuniculus],9GPB_B THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE [Oryctolagus cuniculus],9GPB_C THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE [Oryctolagus cuniculus],9GPB_D THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE [Oryctolagus cuniculus]
1GPA_A 6.85e-234 3 816 18 831
STRUCTURALMECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY PHOSPHORYLATION AND AMP [Oryctolagus cuniculus],1GPA_B STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY PHOSPHORYLATION AND AMP [Oryctolagus cuniculus],1GPA_C STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY PHOSPHORYLATION AND AMP [Oryctolagus cuniculus],1GPA_D STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY PHOSPHORYLATION AND AMP [Oryctolagus cuniculus]
3ZCP_A 7.08e-234 3 816 19 832
Rabbitmuscle glycogen phosphorylase b in complex with N- cyclohexancarbonyl-N-beta-D-glucopyranosyl urea determined at 1.83 A resolution [Oryctolagus cuniculus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9WUB3 5.84e-235 3 816 19 832
Glycogen phosphorylase, muscle form OS=Mus musculus OX=10090 GN=Pygm PE=1 SV=3
P11217 1.33e-233 3 816 19 832
Glycogen phosphorylase, muscle form OS=Homo sapiens OX=9606 GN=PYGM PE=1 SV=6
P00489 7.76e-233 3 816 19 832
Glycogen phosphorylase, muscle form OS=Oryctolagus cuniculus OX=9986 GN=PYGM PE=1 SV=3
O18751 1.50e-232 3 816 19 832
Glycogen phosphorylase, muscle form OS=Ovis aries OX=9940 GN=PYGM PE=2 SV=3
P79334 1.50e-232 3 816 19 832
Glycogen phosphorylase, muscle form OS=Bos taurus OX=9913 GN=PYGM PE=1 SV=3

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
1.000083 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004359_00181.