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CAZyme Information: MGYG000000036_01245

You are here: Home > Sequence: MGYG000000036_01245

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 Pseudoruminococcus massiliensis
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Pseudoruminococcus; Pseudoruminococcus massiliensis
CAZyme ID MGYG000000036_01245
CAZy Family GH77
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1313 150055.09 4.8294
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000036 2411078 Isolate United Kingdom Europe
Gene Location Start: 321853;  End: 325794  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.25

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT35 596 1312 1.3e-255 0.9940652818991098
GH77 15 499 1.2e-167 0.9939271255060729

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00343 Phosphorylase 0.0 595 1312 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.
COG0058 GlgP 0.0 504 1312 5 748
Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14508 PRK14508 0.0 7 502 3 497
4-alpha-glucanotransferase; Provisional
pfam02446 Glyco_hydro_77 0.0 15 480 1 458
4-alpha-glucanotransferase. These enzymes EC:2.4.1.25 transfer a segment of a (1,4)-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or (1,4)-alpha-D-glucan.
cd04300 GT35_Glycogen_Phosphorylase 0.0 509 1312 1 795
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
CDZ24764.1 0.0 9 1312 4 1282
QCT06755.1 0.0 511 1310 2 782
CBK83088.1 0.0 7 1312 5 1258
QOR20895.1 0.0 7 1310 2 1253
QOR11554.1 0.0 7 1310 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 7.18e-247 540 1312 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]
3CEH_A 4.13e-216 540 1312 33 805
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]
1XOI_A 1.36e-215 540 1312 55 827
HumanLiver Glycogen Phosphorylase A complexed with Chloroindoloyl glycine amide [Homo sapiens],1XOI_B Human Liver Glycogen Phosphorylase A complexed with Chloroindoloyl glycine amide [Homo sapiens]
1FC0_A 1.36e-215 540 1312 55 827
HUMANLIVER GLYCOGEN PHOSPHORYLASE COMPLEXED WITH N-ACETYL-BETA-D-GLUCOPYRANOSYLAMINE [Homo sapiens],1FC0_B HUMAN LIVER GLYCOGEN PHOSPHORYLASE COMPLEXED WITH N-ACETYL-BETA-D-GLUCOPYRANOSYLAMINE [Homo sapiens],2ATI_A Glycogen Phosphorylase Inhibitors [Homo sapiens],2ATI_B Glycogen Phosphorylase Inhibitors [Homo sapiens]
1FA9_A 1.36e-215 540 1312 55 827
HUMANLIVER GLYCOGEN PHOSPHORYLASE A COMPLEXED WITH AMP [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9XTL9 1.15e-216 540 1310 56 826
Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2
Q9ET01 3.89e-216 526 1312 42 828
Glycogen phosphorylase, liver form OS=Mus musculus OX=10090 GN=Pygl PE=1 SV=4
P09811 4.27e-215 526 1312 42 828
Glycogen phosphorylase, liver form OS=Rattus norvegicus OX=10116 GN=Pygl PE=1 SV=5
P06737 7.69e-215 540 1312 56 828
Glycogen phosphorylase, liver form OS=Homo sapiens OX=9606 GN=PYGL PE=1 SV=4
Q0VCM4 2.44e-214 526 1312 42 828
Glycogen phosphorylase, liver form OS=Bos taurus OX=9913 GN=PYGL PE=2 SV=1

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
1.000001 0.000043 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000036_01245.