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CAZyme Information: MGYG000003192_01647

You are here: Home > Sequence: MGYG000003192_01647

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 UBA5416 sp900539175
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UBA5416; UBA5416 sp900539175
CAZyme ID MGYG000003192_01647
CAZy Family GT35
CAZyme Description Glycogen phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
301 34854.53 5.0063
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003192 4033193 MAG United States North America
Gene Location Start: 3273;  End: 4178  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.1

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd04300 GT35_Glycogen_Phosphorylase 3.92e-166 12 301 1 288
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.
TIGR02093 P_ylase 2.11e-144 15 301 1 285
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]
pfam00343 Phosphorylase 3.48e-132 96 301 1 204
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.
COG0058 GlgP 3.90e-94 7 295 5 250
Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14986 PRK14986 2.54e-85 30 295 36 295
glycogen phosphorylase; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QOV19349.1 7.46e-192 1 301 1 301
QNM07938.1 6.63e-180 1 301 1 302
AWY99285.1 4.85e-177 1 301 1 301
CBL22715.1 1.04e-175 1 301 1 301
ASM70669.1 1.10e-175 1 301 1 301

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5IKO_A 1.10e-89 30 301 50 315
Crystalstructure of human brain glycogen phosphorylase [Homo sapiens],5IKP_A Crystal structure of human brain glycogen phosphorylase bound to AMP [Homo sapiens]
7P7D_A 6.52e-88 12 301 22 305
ChainA, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus]
5OX0_A 8.18e-88 12 301 29 312
GlycogenPhosphorylase in complex with CK898 [Oryctolagus cuniculus]
3CEH_A 8.78e-88 30 301 24 289
Humanliver glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE5688 [Homo sapiens],3CEH_B Human liver glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE5688 [Homo sapiens],3CEJ_A Human glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE2865 [Homo sapiens],3CEJ_B Human glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE2865 [Homo sapiens],3CEM_A Human glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE9423 [Homo sapiens],3CEM_B Human glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE9423 [Homo sapiens]
1Z8D_A 1.12e-87 12 301 29 312
ChainA, Glycogen phosphorylase, muscle form [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P53534 1.36e-89 30 301 47 312
Glycogen phosphorylase, brain form (Fragment) OS=Rattus norvegicus OX=10116 GN=Pygb PE=1 SV=3
Q0VCM4 3.35e-89 30 301 47 312
Glycogen phosphorylase, liver form OS=Bos taurus OX=9913 GN=PYGL PE=2 SV=1
Q5MIB5 4.68e-89 30 301 47 312
Glycogen phosphorylase, liver form OS=Ovis aries OX=9940 GN=PYGL PE=2 SV=3
P11216 5.69e-89 30 301 47 312
Glycogen phosphorylase, brain form OS=Homo sapiens OX=9606 GN=PYGB PE=1 SV=5
Q8CI94 7.97e-89 30 301 47 312
Glycogen phosphorylase, brain form OS=Mus musculus OX=10090 GN=Pygb 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
1.000059 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003192_01647.