CAZyme Information: MGYG000001180_00904

Basic Information

• 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      

MKIKTWIAAIVFVAGIIAACFVYVNLRRSVKSVVVDEKMFPVRGMDLSSHNGEIDFSRIA
ADSIDFIMLKATEGTSFKDPRFHSNYLQARKSEIKAVGAYHFFRFDTDGEMQAINFLNSL
RGKTLDLPAVIDLEEWSNPSGIPTEEIVKRLRAMIECLHRNGHNVMFYTNKDGYERFLKG
RFDEYPLWICSFTDPPLDDGNDRWSLWQYSHQGWTEACNSEVDMNTFNGSHEEWLAWLKS
STF

Enzyme Prediction     

No EC number prediction in MGYG000001180_00904.

CAZyme Signature Domains

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

CDD Domains     

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     

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     

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     

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

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     

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