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CAZyme Information: MGYG000003014_00341

You are here: Home > Sequence: MGYG000003014_00341

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 Actinomyces graevenitzii
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Actinomyces; Actinomyces graevenitzii
CAZyme ID MGYG000003014_00341
CAZy Family GT35
CAZyme Description Maltodextrin phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
789 89575.07 4.7631
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003014 1770918 MAG United States North America
Gene Location Start: 34317;  End: 36686  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT35 88 784 1.2e-253 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 36 784 48 811
glycogen phosphorylase; Provisional
COG0058 GlgP 0.0 3 784 7 749
Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985 PRK14985 0.0 21 784 26 797
maltodextrin phosphorylase; Provisional
TIGR02093 P_ylase 0.0 9 783 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 7 783 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BAV85068.1 0.0 1 789 22 809
QQQ58633.1 0.0 1 789 1 788
QQC40174.1 0.0 1 789 1 788
AMD99458.1 0.0 1 789 1 788
QLF53919.1 0.0 1 789 1 788

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2C4M_A 0.0 9 787 13 792
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]
3CEH_A 5.00e-215 24 784 24 806
Humanliver glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE5688 [Homo sapiens],3CEH_B Human liver glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE5688 [Homo sapiens],3CEJ_A Human glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE2865 [Homo sapiens],3CEJ_B Human glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE2865 [Homo sapiens],3CEM_A Human glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE9423 [Homo sapiens],3CEM_B Human glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE9423 [Homo sapiens]
1XOI_A 1.15e-214 24 784 46 828
HumanLiver Glycogen Phosphorylase A complexed with Chloroindoloyl glycine amide [Homo sapiens],1XOI_B Human Liver Glycogen Phosphorylase A complexed with Chloroindoloyl glycine amide [Homo sapiens]
1L5V_A 1.32e-214 25 784 30 795
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]
1FC0_A 1.63e-214 24 784 46 828
HUMANLIVER GLYCOGEN PHOSPHORYLASE COMPLEXED WITH N-ACETYL-BETA-D-GLUCOPYRANOSYLAMINE [Homo sapiens],1FC0_B HUMAN LIVER GLYCOGEN PHOSPHORYLASE COMPLEXED WITH N-ACETYL-BETA-D-GLUCOPYRANOSYLAMINE [Homo sapiens],2ATI_A Glycogen Phosphorylase Inhibitors [Homo sapiens],2ATI_B Glycogen Phosphorylase Inhibitors [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P73511 1.73e-214 3 784 27 827
Glycogen phosphorylase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=glgP PE=3 SV=1
P09811 1.79e-214 24 784 47 829
Glycogen phosphorylase, liver form OS=Rattus norvegicus OX=10116 GN=Pygl PE=1 SV=5
Q9ET01 2.53e-214 24 784 47 829
Glycogen phosphorylase, liver form OS=Mus musculus OX=10090 GN=Pygl PE=1 SV=4
P06737 9.18e-214 24 784 47 829
Glycogen phosphorylase, liver form OS=Homo sapiens OX=9606 GN=PYGL PE=1 SV=4
Q0VCM4 1.47e-213 24 788 47 833
Glycogen phosphorylase, liver form OS=Bos taurus OX=9913 GN=PYGL PE=2 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
1.000026 0.000005 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003014_00341.