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CAZyme Information: MGYG000003523_00568
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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-475 sp900769205 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-917; CAG-475; CAG-475 sp900769205 | |||||||||||
| CAZyme ID | MGYG000003523_00568 | |||||||||||
| CAZy Family | GT35 | |||||||||||
| CAZyme Description | Glycogen phosphorylase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 45; End: 884 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT35 | 2 | 274 | 1.8e-106 | 0.3857566765578635 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam00343 | Phosphorylase | 0.0 | 3 | 274 | 391 | 661 | 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 | 2.34e-169 | 3 | 274 | 524 | 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. |
| PRK14985 | PRK14985 | 1.91e-124 | 3 | 272 | 525 | 794 | maltodextrin phosphorylase; Provisional |
| COG0058 | GlgP | 3.86e-114 | 1 | 276 | 481 | 750 | Glucan phosphorylase [Carbohydrate transport and metabolism]. |
| PRK14986 | PRK14986 | 2.94e-108 | 3 | 277 | 539 | 813 | glycogen phosphorylase; Provisional |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QHQ60745.1 | 3.35e-115 | 3 | 277 | 530 | 803 |
| QOX62808.1 | 1.03e-114 | 3 | 277 | 534 | 809 |
| AVQ97458.1 | 5.68e-113 | 3 | 275 | 532 | 804 |
| AYF42955.1 | 5.68e-113 | 3 | 275 | 532 | 804 |
| QCN93713.1 | 5.68e-113 | 3 | 275 | 532 | 804 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2GJ4_A | 3.32e-90 | 3 | 275 | 546 | 817 | Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus] |
| 2GM9_A | 3.38e-90 | 3 | 275 | 546 | 817 | 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 | 3.38e-90 | 3 | 275 | 546 | 817 | Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus] |
| 1ABB_A | 3.57e-90 | 3 | 275 | 548 | 819 | 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 | 3.71e-90 | 3 | 275 | 545 | 816 | 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 |
|---|---|---|---|---|---|---|
| Q9XTL9 | 4.21e-98 | 1 | 275 | 556 | 829 | Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2 |
| P73511 | 6.67e-92 | 3 | 277 | 556 | 829 | Glycogen phosphorylase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=glgP PE=3 SV=1 |
| O18751 | 2.51e-89 | 3 | 275 | 558 | 829 | Glycogen phosphorylase, muscle form OS=Ovis aries OX=9940 GN=PYGM PE=2 SV=3 |
| P00489 | 2.56e-89 | 3 | 275 | 558 | 829 | Glycogen phosphorylase, muscle form OS=Oryctolagus cuniculus OX=9986 GN=PYGM PE=1 SV=3 |
| P79334 | 9.65e-89 | 3 | 275 | 558 | 829 | Glycogen phosphorylase, muscle form OS=Bos taurus OX=9913 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 |
|---|---|---|---|---|---|
| 1.000070 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |