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CAZyme Information: MGYG000001342_02081

You are here: Home > Sequence: MGYG000001342_02081

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 Streptococcus gordonii
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus; Streptococcus gordonii
CAZyme ID MGYG000001342_02081
CAZy Family GT35
CAZyme Description Maltodextrin phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
753 MGYG000001342_5|CGC8 85668.53 4.7913
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001342 2230611 Isolate not provided not provided
Gene Location Start: 526452;  End: 528713  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 2.5e-225 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 46 752 70 811
glycogen phosphorylase; Provisional
COG0058 GlgP 0.0 4 753 13 750
Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985 PRK14985 0.0 36 749 49 794
maltodextrin phosphorylase; Provisional
TIGR02093 P_ylase 0.0 7 751 4 794
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 12 751 12 795
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
ATF64425.1 0.0 1 753 1 753
SQG03166.1 0.0 1 753 1 753
VTT23509.1 0.0 1 753 1 753
AOS70591.1 0.0 1 753 1 753
ARC46529.1 0.0 1 753 1 753

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 7 750 11 756
Crystalstructure of putative glycogen phosphorylase from Streptococcus mutans [Streptococcus mutans UA159]
2C4M_A 2.72e-174 20 752 29 789
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 1.18e-169 27 753 41 796
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 1.18e-169 27 753 41 796
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 1.50e-169 14 753 33 804
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]

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 1 752 1 752
Maltodextrin phosphorylase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=malP PE=3 SV=2
P39123 1.01e-174 14 751 22 794
Glycogen phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=glgP PE=2 SV=1
P0AC86 1.86e-173 41 752 65 811
Glycogen phosphorylase OS=Escherichia coli (strain K12) OX=83333 GN=glgP PE=3 SV=1
P0AC87 1.86e-173 41 752 65 811
Glycogen phosphorylase OS=Shigella flexneri OX=623 GN=glgP PE=3 SV=1
Q9XTL9 8.47e-170 20 752 48 829
Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2

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
1.000042 0.000003 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001342_02081.