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CAZyme Information: MGYG000004714_02421

You are here: Home > Sequence: MGYG000004714_02421

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; Clostridiales; Clostridiaceae; Clostridium_X;
CAZyme ID MGYG000004714_02421
CAZy Family GT35
CAZyme Description Glycogen phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
280 31881.38 4.9501
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004714 2587994 MAG China Asia
Gene Location Start: 19;  End: 861  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004714_02421.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT35 2 272 8.8e-107 0.3827893175074184

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00343 Phosphorylase 5.56e-174 2 272 391 660
Carbohydrate phosphorylase. The members of this family catalyze the formation of glucose 1-phosphate from one of the following polyglucoses; glycogen, starch, glucan or maltodextrin.
cd04300 GT35_Glycogen_Phosphorylase 3.79e-164 2 272 524 794
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.
PRK14985 PRK14985 3.77e-119 2 271 525 794
maltodextrin phosphorylase; Provisional
COG0058 GlgP 2.11e-114 2 272 483 747
Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14986 PRK14986 1.83e-104 1 272 538 809
glycogen phosphorylase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AQM60034.1 4.00e-144 1 280 532 811
AQS12102.1 7.98e-144 2 280 533 811
AQS02500.1 7.98e-144 2 280 533 811
AQS16483.1 7.98e-144 2 280 533 811
AGX45323.1 7.98e-144 2 280 533 811

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2GJ4_A 1.05e-87 2 272 546 815
Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2GM9_A 1.07e-87 2 272 546 815
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 1.07e-87 2 272 546 815
Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]
1ABB_A 1.13e-87 2 272 548 817
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]
7O8E_A 1.17e-87 2 272 551 820
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
P39123 5.79e-100 1 272 522 793
Glycogen phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=glgP PE=2 SV=1
Q9WUB3 7.51e-88 2 272 558 827
Glycogen phosphorylase, muscle form OS=Mus musculus OX=10090 GN=Pygm PE=1 SV=3
P53534 1.92e-87 2 272 558 827
Glycogen phosphorylase, brain form (Fragment) OS=Rattus norvegicus OX=10116 GN=Pygb PE=1 SV=3
Q8CI94 2.09e-87 2 272 558 827
Glycogen phosphorylase, brain form OS=Mus musculus OX=10090 GN=Pygb PE=1 SV=3
P00489 8.01e-87 2 272 558 827
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
1.000067 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004714_02421.