Species | [Candida] glabrata | |||||||||||
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Lineage | Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; [Candida] glabrata | |||||||||||
CAZyme ID | QHS65814.1 | |||||||||||
CAZy Family | GH47 | |||||||||||
CAZyme Description | Alpha-1,4 glucan phosphorylase [Source:UniProtKB/TrEMBL;Acc:A0A0W0CTB6] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 2.4.1.1:158 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT35 | 160 | 894 | 1.2e-271 | 0.9970326409495549 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
273967 | P_ylase | 0.0 | 71 | 893 | 1 | 793 | 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] |
340853 | GT35_Glycogen_Phosphorylase | 0.0 | 68 | 893 | 1 | 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. |
395272 | Phosphorylase | 0.0 | 161 | 894 | 1 | 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. |
184948 | PRK14986 | 0.0 | 94 | 898 | 44 | 814 | glycogen phosphorylase; Provisional |
223136 | GlgP | 0.0 | 63 | 896 | 5 | 750 | Glucan phosphorylase [Carbohydrate transport and metabolism]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 899 | 1 | 899 | |
0.0 | 1 | 899 | 1 | 899 | |
0.0 | 1 | 899 | 1 | 899 | |
0.0 | 1 | 899 | 1 | 899 | |
0.0 | 1 | 899 | 1 | 899 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
0.0 | 24 | 897 | 1 | 878 | Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. [Saccharomyces cerevisiae],1YGP_B Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. [Saccharomyces cerevisiae] |
|
2.59e-265 | 62 | 896 | 11 | 818 | Structure of rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus] |
|
2.68e-265 | 62 | 896 | 11 | 818 | Structure of 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] |
|
2.68e-265 | 62 | 896 | 11 | 818 | Crystallographic studies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus] |
|
4.20e-265 | 62 | 896 | 13 | 820 | Control Of 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
0.0 | 1 | 897 | 1 | 901 | Glycogen phosphorylase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=GPH1 PE=1 SV=4 |
|
8.33e-297 | 28 | 896 | 12 | 842 | Glycogen phosphorylase 1 OS=Dictyostelium discoideum OX=44689 GN=glpV PE=1 SV=3 |
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2.28e-282 | 62 | 898 | 109 | 911 | Glycogen phosphorylase 2 OS=Dictyostelium discoideum OX=44689 GN=glpD PE=1 SV=2 |
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9.67e-270 | 92 | 896 | 53 | 830 | Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2 |
|
1.89e-266 | 62 | 896 | 23 | 830 | Glycogen phosphorylase, muscle form OS=Mus musculus OX=10090 GN=Pygm PE=1 SV=3 |
Other | SP_Sec_SPI | CS Position |
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1.000061 | 0.000000 |
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