Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; | |||||||||||
CAZyme ID | MGYG000004682_00833 | |||||||||||
CAZy Family | GT35 | |||||||||||
CAZyme Description | Maltodextrin phosphorylase | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 160; End: 1692 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT35 | 1 | 509 | 1.2e-166 | 0.7255192878338279 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG0058 | GlgP | 0.0 | 1 | 509 | 244 | 748 | Glucan phosphorylase [Carbohydrate transport and metabolism]. |
TIGR02093 | P_ylase | 0.0 | 1 | 509 | 273 | 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] |
cd04300 | GT35_Glycogen_Phosphorylase | 0.0 | 1 | 509 | 276 | 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. |
pfam00343 | Phosphorylase | 0.0 | 1 | 509 | 192 | 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. |
PRK14985 | PRK14985 | 5.03e-157 | 17 | 507 | 294 | 794 | maltodextrin phosphorylase; Provisional |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ATP54275.1 | 0.0 | 1 | 510 | 246 | 755 |
AZH70366.1 | 0.0 | 1 | 510 | 255 | 764 |
QIA34016.1 | 0.0 | 1 | 510 | 246 | 755 |
AFA54837.1 | 0.0 | 1 | 510 | 246 | 755 |
QUC04926.1 | 3.97e-280 | 1 | 509 | 243 | 751 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4L22_A | 6.57e-225 | 1 | 508 | 247 | 756 | Crystalstructure of putative glycogen phosphorylase from Streptococcus mutans [Streptococcus mutans UA159] |
2C4M_A | 2.59e-131 | 3 | 509 | 267 | 788 | Starchphosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae],2C4M_B Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae],2C4M_C Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae],2C4M_D Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae] |
1E4O_A | 3.93e-119 | 17 | 507 | 291 | 792 | Phosphorylaserecognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question [Escherichia coli],1E4O_B Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question [Escherichia coli],1QM5_A Phosphorylase recognition and phosphorylysis of its oligosaccharide substrate: answers to a long outstanding question [Escherichia coli],1QM5_B Phosphorylase recognition and phosphorylysis of its oligosaccharide substrate: answers to a long outstanding question [Escherichia coli] |
1L5V_A | 3.93e-119 | 17 | 507 | 291 | 792 | CrystalStructure of the Maltodextrin Phosphorylase complexed with Glucose-1-phosphate [Escherichia coli],1L5V_B Crystal Structure of the Maltodextrin Phosphorylase complexed with Glucose-1-phosphate [Escherichia coli],1L5W_A Crystal Structure of the Maltodextrin Phosphorylase Complexed with the Products of the Enzymatic Reaction between Glucose-1-phosphate and Maltotetraose [Escherichia coli],1L5W_B Crystal Structure of the Maltodextrin Phosphorylase Complexed with the Products of the Enzymatic Reaction between Glucose-1-phosphate and Maltotetraose [Escherichia coli],1L6I_A Crystal Structure of the Maltodextrin Phosphorylase complexed with the products of the enzymatic reaction between glucose-1-phosphate and maltopentaose [Escherichia coli],1L6I_B Crystal Structure of the Maltodextrin Phosphorylase complexed with the products of the enzymatic reaction between glucose-1-phosphate and maltopentaose [Escherichia coli],2ASV_A Chain A, Maltodextrin phosphorylase [Escherichia coli],2ASV_B Chain B, Maltodextrin phosphorylase [Escherichia coli],2AV6_A Chain A, Maltodextrin phosphorylase [Escherichia coli],2AV6_B Chain B, Maltodextrin phosphorylase [Escherichia coli],2AW3_A X-Ray studies on maltodextrin phosphorylase complexes: recognition of substrates and cathalitic mechanism of phosphorylase family [Escherichia coli],2AW3_B X-Ray studies on maltodextrin phosphorylase complexes: recognition of substrates and cathalitic mechanism of phosphorylase family [Escherichia coli],2AZD_A Chain A, Maltodextrin phosphorylase [Escherichia coli],2AZD_B Chain B, Maltodextrin phosphorylase [Escherichia coli] |
7TM7_A | 6.72e-119 | 17 | 507 | 300 | 800 | ChainA, Alpha-1,4 glucan phosphorylase [Klebsiella pneumoniae subsp. pneumoniae HS11286],7TM7_B Chain B, Alpha-1,4 glucan phosphorylase [Klebsiella pneumoniae subsp. pneumoniae HS11286] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P29849 | 1.84e-235 | 1 | 510 | 243 | 752 | Maltodextrin phosphorylase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=malP PE=3 SV=2 |
P73511 | 1.67e-120 | 2 | 509 | 307 | 826 | Glycogen phosphorylase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=glgP PE=3 SV=1 |
Q9XTL9 | 1.61e-119 | 25 | 507 | 332 | 826 | Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2 |
P00490 | 2.20e-118 | 17 | 507 | 292 | 793 | Maltodextrin phosphorylase OS=Escherichia coli (strain K12) OX=83333 GN=malP PE=1 SV=7 |
P45180 | 6.52e-116 | 1 | 509 | 294 | 814 | Glycogen phosphorylase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=glgP PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000051 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.