logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004153_02561

You are here: Home > Sequence: MGYG000004153_02561

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 UBA7102 sp900760085
Lineage Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; UBA1750; UBA7102; UBA7102 sp900760085
CAZyme ID MGYG000004153_02561
CAZy Family GH77
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1329 MGYG000004153_54|CGC1 151224.32 4.817
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004153 2844425 MAG United Kingdom Europe
Gene Location Start: 5229;  End: 9218  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.25

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT35 588 1329 7.1e-242 0.9940652818991098
GH77 9 488 7.2e-175 0.9898785425101214

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd04300 GT35_Glycogen_Phosphorylase 0.0 555 1329 53 795
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.
PRK14985 PRK14985 0.0 555 1328 59 795
maltodextrin phosphorylase; Provisional
TIGR02093 P_ylase 0.0 515 1329 8 794
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]
PRK14508 PRK14508 0.0 1 493 3 497
4-alpha-glucanotransferase; Provisional
pfam00343 Phosphorylase 0.0 587 1329 1 661
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CDZ24764.1 0.0 3 1329 4 1282
CBK83088.1 0.0 1 1329 5 1258
QCT06755.1 0.0 508 1327 7 782
SQH64588.1 0.0 1 1327 2 1253
QQB09653.1 0.0 1 1327 2 1253

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2C4M_A 5.14e-228 532 1329 37 788
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 3.22e-206 555 1327 69 814
Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]
2GM9_A 3.32e-206 555 1327 69 814
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 3.32e-206 555 1327 69 814
Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]
7O8E_A 3.90e-206 555 1327 74 819
ChainA, Glycogen phosphorylase, muscle form [Oryctolagus cuniculus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q0VCM4 5.35e-206 555 1329 81 828
Glycogen phosphorylase, liver form OS=Bos taurus OX=9913 GN=PYGL PE=2 SV=1
P11217 1.58e-205 555 1327 81 826
Glycogen phosphorylase, muscle form OS=Homo sapiens OX=9606 GN=PYGM PE=1 SV=6
Q5MIB5 2.09e-205 555 1329 81 828
Glycogen phosphorylase, liver form OS=Ovis aries OX=9940 GN=PYGL PE=2 SV=3
P00489 3.22e-205 555 1327 81 826
Glycogen phosphorylase, muscle form OS=Oryctolagus cuniculus OX=9986 GN=PYGM PE=1 SV=3
Q3B7M9 4.53e-205 555 1327 81 826
Glycogen phosphorylase, brain form OS=Bos taurus OX=9913 GN=PYGB PE=2 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
1.000048 0.000003 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004153_02561.