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CAZyme Information: MGYG000000936_01250

You are here: Home > Sequence: MGYG000000936_01250

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 Collinsella sp900544235
Lineage Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; Collinsella sp900544235
CAZyme ID MGYG000000936_01250
CAZy Family GT35
CAZyme Description Glycogen phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
473 MGYG000000936_66|CGC1 53198.87 5.0439
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000936 2104086 MAG Germany Europe
Gene Location Start: 8691;  End: 10112  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT35 1 472 2.1e-153 0.6706231454005934

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0058 GlgP 0.0 1 472 277 748
Glucan phosphorylase [Carbohydrate transport and metabolism].
TIGR02093 P_ylase 0.0 1 472 310 794
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 1 472 313 795
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 1 472 229 661
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 2.18e-141 3 470 317 794
maltodextrin phosphorylase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QIA34016.1 0.0 1 473 283 755
ATP54275.1 0.0 1 473 283 755
AZH70366.1 0.0 1 473 292 764
AFA54837.1 0.0 1 473 283 755
QUC04926.1 2.94e-255 1 472 280 751

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4L22_A 1.53e-197 1 471 284 756
Crystalstructure of putative glycogen phosphorylase from Streptococcus mutans [Streptococcus mutans UA159]
2C4M_A 5.80e-120 1 472 302 788
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]
2GJ4_A 1.06e-107 1 470 333 814
Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2GM9_A 1.08e-107 1 470 333 814
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]
2FFR_A 1.08e-107 1 470 333 814
Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P29849 6.93e-210 1 473 280 752
Maltodextrin phosphorylase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=malP PE=3 SV=2
Q9XTL9 3.18e-112 1 470 345 826
Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2
P73511 7.02e-112 3 472 345 826
Glycogen phosphorylase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=glgP PE=3 SV=1
O18751 5.71e-108 1 470 345 826
Glycogen phosphorylase, muscle form OS=Ovis aries OX=9940 GN=PYGM PE=2 SV=3
P79334 5.71e-108 1 470 345 826
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
1.000062 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000936_01250.