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CAZyme Information: MGYG000000993_00260

You are here: Home > Sequence: MGYG000000993_00260

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 Haemophilus_D sp900756155
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Pasteurellaceae; Haemophilus_D; Haemophilus_D sp900756155
CAZyme ID MGYG000000993_00260
CAZy Family GH77
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1257 MGYG000000993_1|CGC2 144089.01 5.8928
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000993 1983283 MAG Denmark Europe
Gene Location Start: 275905;  End: 279678  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT35 580 1255 8.9e-221 0.9955489614243324
GH77 10 491 1.6e-160 0.9817813765182186

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00343 Phosphorylase 0.0 580 1254 1 660
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 0.0 510 1254 17 747
Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14508 PRK14508 0.0 1 497 2 497
4-alpha-glucanotransferase; Provisional
pfam02446 Glyco_hydro_77 0.0 10 477 1 460
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 0.0 505 1254 3 794
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
QOR06046.1 0.0 1 1257 1 1257
QOR11554.1 0.0 1 1257 1 1257
QOR13376.1 0.0 1 1257 1 1257
QOR20895.1 0.0 1 1257 1 1257
QOR24558.1 0.0 1 1257 1 1257

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4L22_A 0.0 506 1254 8 756
Crystalstructure of putative glycogen phosphorylase from Streptococcus mutans [Streptococcus mutans UA159]
6M6T_A 1.28e-219 4 499 5 499
ChainA, 4-alpha-glucanotransferase [Streptococcus agalactiae],6M6T_B Chain B, 4-alpha-glucanotransferase [Streptococcus agalactiae],6M6T_C Chain C, 4-alpha-glucanotransferase [Streptococcus agalactiae],6M6T_D Chain D, 4-alpha-glucanotransferase [Streptococcus agalactiae],6M6T_E Chain E, 4-alpha-glucanotransferase [Streptococcus agalactiae],6M6T_F Chain F, 4-alpha-glucanotransferase [Streptococcus agalactiae],6M6T_G Chain G, 4-alpha-glucanotransferase [Streptococcus agalactiae],6M6T_H Chain H, 4-alpha-glucanotransferase [Streptococcus agalactiae]
3CEH_A 6.65e-167 548 1256 58 806
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]
1FC0_A 1.97e-166 548 1256 80 828
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 1.97e-166 548 1256 80 828
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
P29849 0.0 503 1254 1 750
Maltodextrin phosphorylase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=malP PE=3 SV=2
P0A3Q0 4.02e-190 1 505 1 504
4-alpha-glucanotransferase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=malQ PE=3 SV=1
P0A3Q1 4.02e-190 1 505 1 504
4-alpha-glucanotransferase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=malQ PE=3 SV=1
Q9ET01 5.82e-167 548 1256 81 829
Glycogen phosphorylase, liver form OS=Mus musculus OX=10090 GN=Pygl PE=1 SV=4
P39123 1.33e-166 516 1253 22 792
Glycogen phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=glgP 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
0.999971 0.000071 0.000001 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000993_00260.