CAZyme Information: MGYG000000760_00424

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella
• CAZyme ID: MGYG000000760_00424
• CAZy Family: GH25
• CAZyme Description: Lysozyme M1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
235		27386.99	7.0047

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000760	2818339	MAG	Bangladesh	Asia

• Gene Location: Start: 141324; End: 142031 Strand: -

Full Sequence      

MIALFCLLAVHAQYFDVQCEDTCSHVHGIDLSHYQGEVFWETVGENTKNTYVYLKATEGG
DRIDPTYQTNIELAHRYGLKVGSYHFFRPKTNLTLQLQNFMTQCRPGDQDLIPMIDVETR
SGLSTEAFCDSLHKFLRMVEEAYQQKPLIYTGANFYDHNLSGQLDSYQIMIAQYTDREPV
LADGRDITMWQYTGKGRINGINTFVDKSRMMGRHGLREIRFRRNVTNTRKYTWIH

Enzyme Prediction     

No EC number prediction in MGYG000000760_00424.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	29	201	4.4e-46	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06524	GH25_YegX-like	3.03e-56	27	206	1	188	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.
cd06413	GH25_muramidase_1	2.27e-50	26	206	3	185	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	1.19e-49	27	206	1	182	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.
pfam01183	Glyco_hydro_25	2.18e-43	29	201	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	6.15e-43	28	206	2	180	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
EFC71701.2	8.83e-123	8	221	15	228
QNT65928.1	3.34e-119	1	222	8	226
BCS86540.1	1.32e-117	1	222	12	232
VEH15347.1	1.82e-117	5	222	15	231
QUB46591.1	1.12e-116	1	221	8	229

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	3.01e-21	26	202	16	195	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
4KRU_A	1.41e-17	25	202	19	199	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
1JFX_A	4.26e-17	24	212	3	204	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRT_A	6.24e-17	25	202	19	199	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]
5A6S_A	2.11e-14	24	208	19	199	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P76421	9.27e-33	26	206	67	250	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	1.83e-32	26	206	67	250	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	3.60e-32	26	206	67	250	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P26836	1.63e-21	24	202	7	188	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	7.12e-16	24	212	80	281	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000244	0.999100	0.000150	0.000160	0.000136	0.000139

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000760_00424.