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CAZyme Information: MGYG000000406_01453

You are here: Home > Sequence: MGYG000000406_01453

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 UBA10677 sp003533505
Lineage Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-552; UBA10677; UBA10677 sp003533505
CAZyme ID MGYG000000406_01453
CAZy Family GT35
CAZyme Description Glycogen phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
808 MGYG000000406_14|CGC1 91520.35 6.2666
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000406 1936952 MAG Sweden Europe
Gene Location Start: 9630;  End: 12056  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT35 92 800 1.5e-258 0.9985163204747775

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK14986 PRK14986 0.0 8 802 17 813
glycogen phosphorylase; Provisional
COG0058 GlgP 0.0 6 801 7 750
Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985 PRK14985 0.0 12 800 14 797
maltodextrin phosphorylase; Provisional
TIGR02093 P_ylase 0.0 12 799 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 9 799 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
CAB1239238.1 8.03e-317 7 804 9 802
QEY35301.1 3.55e-316 7 802 9 799
ANU55021.1 1.66e-314 7 802 9 800
ASB41745.1 1.66e-314 7 802 9 800
QQR31011.1 1.66e-314 7 802 9 800

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2FFR_A 2.18e-231 27 801 35 818
Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]
2GJ4_A 2.99e-231 27 801 35 818
Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2GM9_A 3.09e-231 27 801 35 818
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 3.64e-231 27 801 40 823
ChainA, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus]
1ABB_A 4.82e-231 27 801 37 820
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P73511 1.02e-251 8 808 29 835
Glycogen phosphorylase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=glgP PE=3 SV=1
P39123 4.22e-251 7 802 7 797
Glycogen phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=glgP PE=2 SV=1
Q9XTL9 3.80e-234 33 801 53 830
Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2
P45180 5.08e-234 2 802 16 817
Glycogen phosphorylase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=glgP PE=3 SV=1
Q9CN90 5.22e-233 2 802 16 817
Glycogen phosphorylase OS=Pasteurella multocida (strain Pm70) OX=272843 GN=glgP PE=3 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
1.000073 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000406_01453.