Species | ||||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; UBA4372; | |||||||||||
CAZyme ID | MGYG000003470_00678 | |||||||||||
CAZy Family | GT35 | |||||||||||
CAZyme Description | Glycogen phosphorylase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1113; End: 2201 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd04299 | GT35_Glycogen_Phosphorylase-like | 5.57e-154 | 1 | 306 | 469 | 772 | proteins similar to glycogen phosphorylase. This family is most closely related to the oligosaccharide phosphorylase domain family and other unidentified sequences. Oligosaccharide phosphorylase catalyzes the breakdown of oligosaccharides into glucose-1-phosphate units. They are important allosteric enzymes in carbohydrate metabolism. |
TIGR02094 | more_P_ylases | 5.48e-128 | 4 | 220 | 385 | 601 | alpha-glucan phosphorylases. This family consists of known phosphorylases, and homologs believed to share the function of using inorganic phosphate to cleave an alpha 1,4 linkage between the terminal glucose residue and the rest of the polymer (maltodextrin, glycogen, etc.). The name of the glucose storage polymer substrate, and therefore the name of this enzyme, depends on the chain lengths and branching patterns. A number of the members of this family have been shown to operate on small maltodextrins, as may be obtained by utilization of exogenous sources. This family represents a distinct clade from the related family modeled by TIGR02093/pfam00343. |
COG0058 | GlgP | 1.62e-78 | 4 | 228 | 483 | 711 | Glucan phosphorylase [Carbohydrate transport and metabolism]. |
cd04300 | GT35_Glycogen_Phosphorylase | 6.60e-11 | 3 | 131 | 523 | 661 | 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. |
PRK14986 | PRK14986 | 4.65e-07 | 4 | 131 | 539 | 676 | glycogen phosphorylase; Provisional |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QDO70152.1 | 5.25e-203 | 1 | 362 | 492 | 853 |
QQT79696.1 | 1.05e-202 | 1 | 362 | 492 | 853 |
ASM67067.1 | 1.05e-202 | 1 | 362 | 492 | 853 |
QRP58421.1 | 1.05e-202 | 1 | 362 | 492 | 853 |
QUT91861.1 | 2.99e-202 | 1 | 362 | 492 | 853 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2FFR_A | 1.53e-09 | 4 | 131 | 546 | 683 | Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus] |
2GM9_A | 1.53e-09 | 4 | 131 | 546 | 683 | 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] |
2GJ4_A | 1.53e-09 | 4 | 131 | 546 | 683 | Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus] |
3ZCQ_A | 1.54e-09 | 4 | 131 | 558 | 695 | Rabbitmuscle glycogen phosphorylase b in complex with N-(4- trifluoromethyl-benzoyl)-N-beta-D-glucopyranosyl urea determined at 2. 15 A resolution [Oryctolagus cuniculus],3ZCR_A Rabbit muscle glycogen phosphorylase b in complex with N-(4-tert- butyl-benzoyl)-N-beta-D-glucopyranosyl urea determined at 2.07 A resolution [Oryctolagus cuniculus],3ZCT_A Rabbit muscle glycogen phosphorylase b in complex with N-(2-naphthoyl) -N-beta-D-glucopyranosyl urea determined at 2.0 A resolution [Oryctolagus cuniculus],3ZCU_A Rabbit muscle glycogen phosphorylase b in complex with N-(pyridyl-2- carbonyl)-N-beta-D-glucopyranosyl urea determined at 2.05 A resolution [Oryctolagus cuniculus],3ZCV_A Rabbit muscle glycogen phosphorylase b in complex with N-(indol-2- carbonyl)-N-beta-D-glucopyranosyl urea determined at 1.8 A resolution [Oryctolagus cuniculus],4CTM_A Glucopyranosylidene-spiro-iminothiazolidinone, a New Bicyclic Ring System: Synthesis, Derivatization, and Evaluation as Glycogen Phosphorylase Inhibitors by Enzyme Kinetic and Crystallographic Methods [Oryctolagus cuniculus],4CTN_A Glucopyranosylidene-spiro-iminothiazolidinone, a New Bicyclic Ring System: Synthesis, Derivatization, and Evaluation as Glycogen Phosphorylase Inhibitors by Enzyme Kinetic and Crystallographic Methods [Oryctolagus cuniculus],4CTO_A Glucopyranosylidene-spiro-iminothiazolidinone, a New Bicyclic Ring System: Synthesis, Derivatization, and Evaluation as Glycogen Phosphorylase Inhibitors by Enzyme Kinetic and Crystallographic Methods [Oryctolagus cuniculus],4YI3_A Crystal structure of Gpb in complex with 4a [Oryctolagus cuniculus],4YI5_A Crystal structure of Gpb in complex with 4b [Oryctolagus cuniculus],4YUA_A Glycogen phosphorylase in complex with ellagic acid [Oryctolagus cuniculus],5JTT_A Crystal structure of GPb in complex with 8a [Oryctolagus cuniculus],5JTU_A Crystal structure of GPb in complex with 8b [Oryctolagus cuniculus],5LRD_A Crystal structure of Glycogen Phosphorylase b in complex with KS242 [Oryctolagus cuniculus],5MEM_A A potent fluorescent inhibitor of glycogen phosphorylase as a catalytic site probe. [Oryctolagus cuniculus],5O52_A Glycogen Phosphorylase b in complex with 33b [Oryctolagus cuniculus],5O54_A Glycogen Phosphorylase b in complex with 29a [Oryctolagus cuniculus],5O56_A Glycogen Phosphorylase b in complex with 29b [Oryctolagus cuniculus],5OWY_A Glycogen Phosphorylase in complex with KS252 [Oryctolagus cuniculus],5OWZ_A Glycogen Phosphorylase in complex with KS172 [Oryctolagus cuniculus],5OX1_A Glycogen Phosphorylase in complex with JLH270 [Oryctolagus cuniculus],5OX3_A Glycogen Phosphorylase in complex with SzB102v [Oryctolagus cuniculus],5OX4_A Glycogen Phosphorylase in complex with CK900 [Oryctolagus cuniculus],6F3J_A The crystal structure of Glycogen Phosphorylase in complex with 10a [Oryctolagus cuniculus],6F3L_A The crystal structure of Glycogen Phosphorylase in complex with 10b [Oryctolagus cuniculus],6F3R_A The crystal structure of Glycogen Phosphorylase in complex with 10c [Oryctolagus cuniculus],6F3S_A The crystal structure of Glycogen Phosphorylase in complex with 10d [Oryctolagus cuniculus],6F3U_A The crystal structure of Glycogen Phosphorylase in complex with 10h [Oryctolagus cuniculus],6QA6_A Glycogen Phosphorylase b in complex with 30 [Oryctolagus cuniculus],6QA7_A Glycogen Phosphorylase b in complex with 29 [Oryctolagus cuniculus],6QA8_A Glycogen Phosphorylase b in complex with 28 [Oryctolagus cuniculus],6R0H_A Glycogen Phosphorylase b in complex with 3 [Oryctolagus cuniculus],6R0I_A Glycogen Phosphorylase b in complex with 4 [Oryctolagus cuniculus],6S4H_A The crystal structure of glycogen phosphorylase in complex with 8 [Oryctolagus cuniculus],6S4K_A The crystal structure of glycogen phosphorylase in complex with 12 [Oryctolagus cuniculus],6S4O_A The crystal structure of glycogen phosphorylase in complex with 9 [Oryctolagus cuniculus],6S4P_A The crystal structure of glycogen phosphorylase in complex with 13 [Oryctolagus cuniculus],6S4R_A The crystal structure of glycogen phosphorylase in complex with 11 [Oryctolagus cuniculus],6S51_A The crystal structure of glycogen phosphorylase in complex with 10 [Oryctolagus cuniculus],6S52_A The crystal structure of glycogen phosphorylase in complex with 14 [Oryctolagus cuniculus],6YVE_AAA Chain AAA, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus] |
3ZCP_A | 1.54e-09 | 4 | 131 | 558 | 695 | Rabbitmuscle glycogen phosphorylase b in complex with N- cyclohexancarbonyl-N-beta-D-glucopyranosyl urea determined at 1.83 A resolution [Oryctolagus cuniculus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q9YGA7 | 4.26e-86 | 1 | 361 | 476 | 825 | Maltodextrin phosphorylase OS=Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C) OX=523849 GN=malP PE=1 SV=1 |
O66932 | 7.87e-68 | 4 | 221 | 473 | 687 | Glycogen phosphorylase OS=Aquifex aeolicus (strain VF5) OX=224324 GN=glgP PE=3 SV=1 |
Q7U078 | 1.99e-56 | 5 | 360 | 506 | 861 | Glycogen phosphorylase OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) OX=233413 GN=glgP PE=3 SV=1 |
P9WMW1 | 7.11e-56 | 5 | 360 | 506 | 861 | Glycogen phosphorylase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=glgP PE=1 SV=1 |
P9WMW0 | 7.11e-56 | 5 | 360 | 506 | 861 | Glycogen phosphorylase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=glgP PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
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1.000069 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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