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CAZyme Information: MGYG000000395_00241
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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-217 sp900547275 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; CAG-217; CAG-217 sp900547275 | |||||||||||
| CAZyme ID | MGYG000000395_00241 | |||||||||||
| CAZy Family | GT35 | |||||||||||
| CAZyme Description | Maltodextrin phosphorylase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 229186; End: 231936 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT35 | 94 | 796 | 1.3e-259 | 0.9970326409495549 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK14985 | PRK14985 | 0.0 | 22 | 797 | 21 | 797 | maltodextrin phosphorylase; Provisional |
| TIGR02093 | P_ylase | 0.0 | 14 | 796 | 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] |
| COG0058 | GlgP | 0.0 | 2 | 798 | 1 | 750 | Glucan phosphorylase [Carbohydrate transport and metabolism]. |
| pfam00343 | Phosphorylase | 0.0 | 95 | 795 | 1 | 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. |
| PRK14986 | PRK14986 | 0.0 | 4 | 801 | 11 | 815 | glycogen phosphorylase; Provisional |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BCI59382.1 | 0.0 | 1 | 799 | 3 | 803 |
| CAB1239238.1 | 0.0 | 7 | 805 | 7 | 806 |
| QKO30335.1 | 0.0 | 6 | 799 | 6 | 800 |
| ARP49466.1 | 0.0 | 6 | 799 | 6 | 800 |
| QKN23059.1 | 0.0 | 6 | 799 | 6 | 800 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1Z8D_A | 6.59e-239 | 6 | 805 | 24 | 837 | ChainA, Glycogen phosphorylase, muscle form [Homo sapiens] |
| 2GM9_A | 3.01e-238 | 6 | 805 | 12 | 825 | 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 | 3.01e-238 | 6 | 805 | 12 | 825 | Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus] |
| 7O8E_A | 3.55e-238 | 6 | 805 | 17 | 830 | ChainA, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus] |
| 1ABB_A | 4.70e-238 | 6 | 805 | 14 | 827 | 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 |
|---|---|---|---|---|---|---|
| P79334 | 1.13e-239 | 6 | 805 | 24 | 837 | Glycogen phosphorylase, muscle form OS=Bos taurus OX=9913 GN=PYGM PE=1 SV=3 |
| O18751 | 2.26e-239 | 6 | 805 | 24 | 837 | Glycogen phosphorylase, muscle form OS=Ovis aries OX=9940 GN=PYGM PE=2 SV=3 |
| Q3B7M9 | 3.30e-239 | 7 | 804 | 25 | 836 | Glycogen phosphorylase, brain form OS=Bos taurus OX=9913 GN=PYGB PE=2 SV=3 |
| P11217 | 4.51e-239 | 6 | 805 | 24 | 837 | Glycogen phosphorylase, muscle form OS=Homo sapiens OX=9606 GN=PYGM PE=1 SV=6 |
| Q9WUB3 | 3.61e-238 | 6 | 805 | 24 | 837 | Glycogen phosphorylase, muscle form OS=Mus musculus OX=10090 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 |
|---|---|---|---|---|---|
| 1.000048 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |