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CAZyme Information: MGYG000001180_00904

You are here: Home > Sequence: MGYG000001180_00904

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 Muribaculum sp001701195
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Muribaculum; Muribaculum sp001701195
CAZyme ID MGYG000001180_00904
CAZy Family GH25
CAZyme Description Lysozyme M1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
243 MGYG000001180_15|CGC1 28046.83 5.8951
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001180 2921277 MAG Austria Europe
Gene Location Start: 2484;  End: 3215  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001180_00904.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH25 45 214 1.4e-42 0.9717514124293786

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06413 GH25_muramidase_1 1.91e-59 40 229 1 191
Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
cd00599 GH25_muramidase 1.67e-49 43 227 1 186
Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family of muramidases contains a glycosyl hydrolase family 25 (GH25) catalytic domain and is found in bacteria, fungi, slime molds, round worms, protozoans and bacteriophages. The bacteriophage members are referred to as endolysins which are involved in lysing the host cell at the end of the replication cycle to allow release of mature phage particles. Endolysins are typically modular enzymes consisting of a catalytically active domain that hydrolyzes the peptidoglycan cell wall and a cell wall-binding domain that anchors the protein to the cell wall. Endolysins generally have narrow substrate specificities with either intra-species or intra-genus bacteriolytic activity.
cd06524 GH25_YegX-like 4.74e-42 43 229 1 194
YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) catalytic domain that is similar in sequence to the CH-type (Chalaropsis-type) lysozymes of the GH25 family of endolysins.
cd06525 GH25_Lyc-like 4.81e-40 43 227 1 184
Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by the lyc gene. Lyc has a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
COG3757 Acm 7.72e-37 25 242 45 268
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QCD36459.1 5.09e-115 2 243 4 244
QQR08022.1 1.47e-104 1 243 11 252
ANU64613.1 1.47e-104 1 243 11 252
ASB37284.1 1.47e-104 1 243 11 252
QCD38842.1 1.79e-77 27 237 28 233

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2WAG_A 1.86e-39 40 233 14 212
TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
1JFX_A 1.53e-24 42 236 5 211
Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRU_A 3.02e-22 42 227 20 207
X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A 2.06e-21 42 227 20 207
X-raystructure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101],4KRT_B X-ray structure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
2X8R_A 8.39e-19 42 229 4 199
Thestructure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_B The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_C The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_D The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_E The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_F The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8X7H0 4.14e-28 28 238 52 265
Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
Q8FFY2 5.79e-28 28 233 52 260
Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P76421 8.11e-28 28 238 52 265
Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
P25310 3.77e-23 42 236 82 288
Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836 6.50e-19 42 227 9 196
Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2

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
0.737392 0.018104 0.243208 0.000094 0.000059 0.001147

TMHMM  Annotations      download full data without filtering help

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