CAZyme Information: MGYG000000215_00056

Basic Information

• Species: Prevotella stercorea
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella stercorea
• CAZyme ID: MGYG000000215_00056
• CAZy Family: GH25
• CAZyme Description: Lysozyme M1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
247		28951.34	8.0335

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000215	3117648	Isolate	China	Asia

• Gene Location: Start: 57037; End: 57780 Strand: -

Full Sequence      

MPLCLFYSNFAFMKRIFYIHIYIILGLFYSCPVFSQDNLVQCEDTCAHVHGIDLSHYQGE
VFWEVIGNNTKMAYVYLKATEGGDRIDHMYEQNIDLAHKYGLKVGSYHFFRPKTDLSKQL
ANFKTQCRPSQQDLIPMIDIEVKQGMSTEAFRDSVAKFLVMVEKAYHQKPLVYTGTNFYN
KYLVGVLDDYKLMIAQYSANEPILADDKDYMLWQYTGKGYIDGIKGYVDKSRFMGRHSLR
ELKYQRR

Enzyme Prediction     

No EC number prediction in MGYG000000215_00056.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	52	224	2.7e-44	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06413	GH25_muramidase_1	6.11e-53	49	235	3	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.
cd06524	GH25_YegX-like	1.54e-52	50	235	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.
cd00599	GH25_muramidase	1.21e-45	50	233	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.
cd06525	GH25_Lyc-like	2.23e-39	51	233	2	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	6.37e-39	49	229	63	249	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
VEH15347.1	6.77e-123	28	245	14	231
BCS86540.1	1.42e-115	19	245	7	232
EFC71701.2	3.32e-114	20	244	3	228
ALO48398.1	4.18e-112	21	247	5	231
QUB46591.1	1.03e-108	40	244	25	229

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	3.50e-19	48	233	19	207	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	1.83e-18	48	233	19	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]
5A6S_A	5.91e-16	53	231	26	199	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
2X8R_A	2.20e-09	49	218	4	187	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]
6ZMV_A	4.73e-08	49	236	2	205	ChainA, muramidase [Trichobolus zukalii],6ZMV_B Chain B, muramidase [Trichobolus zukalii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P76421	2.76e-31	49	235	67	256	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	5.43e-31	49	235	67	256	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	2.94e-30	49	235	67	256	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P26836	1.57e-21	48	233	8	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 SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.011248	0.987731	0.000419	0.000195	0.000178	0.000192

TMHMM  Annotations     

start	end
15	34