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CAZyme Information: MGYG000003783_00408

You are here: Home > Sequence: MGYG000003783_00408

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 Anaerosacchariphilus sp002160765
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Anaerosacchariphilus; Anaerosacchariphilus sp002160765
CAZyme ID MGYG000003783_00408
CAZy Family GH25
CAZyme Description Lysozyme M1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
255 MGYG000003783_16|CGC1 29607.24 4.8553
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003783 3019490 MAG Canada North America
Gene Location Start: 5675;  End: 6442  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003783_00408.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH25 51 225 7.4e-48 0.9887005649717514

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06413 GH25_muramidase_1 1.09e-103 46 240 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 2.79e-56 49 238 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.
COG3757 Acm 7.51e-55 33 244 45 259
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
cd06524 GH25_YegX-like 3.36e-47 49 240 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.
pfam01183 Glyco_hydro_25 2.11e-42 51 225 1 179
Glycosyl hydrolases family 25.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCI60136.1 2.56e-110 26 253 22 249
QRP39332.1 7.03e-94 11 248 9 245
ASN98838.1 7.03e-94 11 248 9 245
QJU19847.1 2.01e-93 11 248 9 245
QIX89794.1 2.85e-93 7 245 2 242

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2WAG_A 7.31e-90 44 248 12 216
TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
1JFX_A 4.32e-22 48 249 5 213
Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRU_A 1.19e-12 48 246 20 213
X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A 3.29e-12 48 246 20 213
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]
4JZ5_A 3.12e-06 41 236 16 210
High-resolutionstructure of catalytic domain of endolysin ply40 from bacteriophage P40 of Listeria monocytogenes [Listeria phage P40]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8X7H0 4.01e-38 46 244 65 260
Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
Q8FFY2 4.36e-37 46 244 65 260
Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P76421 6.13e-37 46 244 65 260
Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
P25310 9.58e-21 48 249 82 290
Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836 1.72e-11 42 246 3 201
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
1.000040 0.000002 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

start end
13 35