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CAZyme Information: MGYG000001338_02942

You are here: Home > Sequence: MGYG000001338_02942

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 Blautia_A wexlerae_A
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A wexlerae_A
CAZyme ID MGYG000001338_02942
CAZy Family GT35
CAZyme Description Glycogen phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
755 86115.66 5.2511
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001338 3930699 Isolate not provided not provided
Gene Location Start: 97519;  End: 99786  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT35 78 751 7.5e-221 0.9955489614243324

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK14986 PRK14986 0.0 26 755 43 814
glycogen phosphorylase; Provisional
COG0058 GlgP 0.0 4 753 14 750
Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985 PRK14985 0.0 43 749 56 794
maltodextrin phosphorylase; Provisional
TIGR02093 P_ylase 0.0 8 751 5 794
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 5 751 6 795
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBL21456.1 0.0 1 755 1 755
QCU01195.1 0.0 1 755 1 755
CBL27091.1 0.0 14 751 13 750
AEN95921.1 0.0 4 751 3 750
VCV23296.1 0.0 4 751 25 772

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4L22_A 0.0 6 750 10 756
Crystalstructure of putative glycogen phosphorylase from Streptococcus mutans [Streptococcus mutans UA159]
2C4M_A 4.74e-182 49 754 63 791
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 1.43e-171 45 749 58 792
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 1.43e-171 45 749 58 792
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]
2ECP_A 1.40e-168 45 749 58 792
TheCrystal Structure Of The E. Coli Maltodextrin Phosphorylase Complex [Escherichia coli],2ECP_B The Crystal Structure Of The E. Coli Maltodextrin Phosphorylase Complex [Escherichia coli]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P29849 0.0 1 751 1 751
Maltodextrin phosphorylase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=malP PE=3 SV=2
P39123 3.92e-184 38 753 53 796
Glycogen phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=glgP PE=2 SV=1
P00490 1.14e-170 45 749 59 793
Maltodextrin phosphorylase OS=Escherichia coli (strain K12) OX=83333 GN=malP PE=1 SV=7
O18751 6.70e-169 14 755 42 832
Glycogen phosphorylase, muscle form OS=Ovis aries OX=9940 GN=PYGM PE=2 SV=3
P79334 1.33e-168 14 755 42 832
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
1.000037 0.000003 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001338_02942.