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CAZyme Information: MGYG000001765_01111

You are here: Home > Sequence: MGYG000001765_01111

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 CAG-448 sp000433415
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; CAG-448; CAG-448 sp000433415
CAZyme ID MGYG000001765_01111
CAZy Family GT35
CAZyme Description Glycogen phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
809 MGYG000001765_36|CGC1 92337.41 6.2801
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001765 2169338 MAG Denmark Europe
Gene Location Start: 1145;  End: 3574  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT35 95 804 9.3e-257 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 29 807 36 814
glycogen phosphorylase; Provisional
COG0058 GlgP 0.0 5 805 4 750
Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985 PRK14985 0.0 22 801 21 794
maltodextrin phosphorylase; Provisional
TIGR02093 P_ylase 0.0 23 803 10 794
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 11 803 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
AVQ97458.1 0.0 8 806 8 806
AYF42955.1 0.0 8 806 8 806
QCN93713.1 0.0 8 806 8 806
AYF40115.1 0.0 8 806 8 806
ADU27514.1 0.0 8 806 45 843

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2GJ4_A 1.36e-232 29 808 35 821
Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2GM9_A 1.41e-232 29 808 35 821
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]
7O8E_A 1.66e-232 29 808 40 826
ChainA, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus]
1ABB_A 2.20e-232 29 808 37 823
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 2.35e-232 29 808 34 820
IdentificationAnd Structural Characterization Of A Novel Allosteric Binding Site Of Glycogen Phosphorylase B [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 1.30e-247 23 806 21 797
Glycogen phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=glgP PE=2 SV=1
P45180 1.52e-241 10 807 22 818
Glycogen phosphorylase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=glgP PE=3 SV=1
P0AC86 5.37e-235 29 807 36 814
Glycogen phosphorylase OS=Escherichia coli (strain K12) OX=83333 GN=glgP PE=3 SV=1
P0AC87 5.37e-235 29 807 36 814
Glycogen phosphorylase OS=Shigella flexneri OX=623 GN=glgP PE=3 SV=1
P00489 1.39e-231 29 808 47 833
Glycogen phosphorylase, muscle form OS=Oryctolagus cuniculus OX=9986 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
1.000047 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001765_01111.