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CAZyme Information: MGYG000002230_01028

You are here: Home > Sequence: MGYG000002230_01028

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 Ruminococcus sp900545125
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus; Ruminococcus sp900545125
CAZyme ID MGYG000002230_01028
CAZy Family GT35
CAZyme Description Maltodextrin phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
779 88740.82 4.9808
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002230 2337720 MAG United States North America
Gene Location Start: 41;  End: 2380  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT35 87 779 2.1e-243 0.9925816023738873

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK14986 PRK14986 0.0 27 779 43 810
glycogen phosphorylase; Provisional
COG0058 GlgP 0.0 6 779 9 748
Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985 PRK14985 0.0 28 778 37 795
maltodextrin phosphorylase; Provisional
TIGR02093 P_ylase 0.0 21 779 17 794
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 7 779 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
CBL18239.1 0.0 25 779 26 779
CBL34863.1 0.0 23 779 34 790
CBK96326.1 0.0 23 779 34 790
CCO05339.1 0.0 1 779 1 788
CBK95778.1 0.0 8 779 4 783

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2C4M_A 1.03e-259 32 779 40 788
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]
2GJ4_A 2.99e-209 28 779 43 816
Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2GM9_A 3.09e-209 28 779 43 816
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]
2FFR_A 3.09e-209 28 779 43 816
Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]
7O8E_A 3.62e-209 28 779 48 821
ChainA, 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
Q9XTL9 1.87e-215 14 779 41 828
Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2
Q8CI94 1.66e-210 28 779 55 828
Glycogen phosphorylase, brain form OS=Mus musculus OX=10090 GN=Pygb PE=1 SV=3
P79334 9.08e-210 52 779 81 828
Glycogen phosphorylase, muscle form OS=Bos taurus OX=9913 GN=PYGM PE=1 SV=3
O18751 3.62e-209 52 779 81 828
Glycogen phosphorylase, muscle form OS=Ovis aries OX=9940 GN=PYGM PE=2 SV=3
P53534 1.28e-208 28 779 55 828
Glycogen phosphorylase, brain form (Fragment) OS=Rattus norvegicus OX=10116 GN=Pygb 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
1.000069 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002230_01028.