CAZyme Information: MGYG000002367_00670

Basic Information

• Species: Pediococcus pentosaceus
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Pediococcus; Pediococcus pentosaceus
• CAZyme ID: MGYG000002367_00670
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
257	MGYG000002367_6|CGC1	29911.32	10.4926

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002367	1751049	Isolate	China	Asia

• Gene Location: Start: 40963; End: 41736 Strand: +

Full Sequence      

MERKRHAKYRPKFNMRFVHHRRRIILGAFLLVVLLAVAGVWVVKNQQRGARLALAPYPVH
GCVIDQENGIIDFNSLQKQHISFVYLNATTGATYFDDSFNTNYSRIQSTDLKVGIVHNFS
FQKRPKAQLRFISQKVKSNTGQLPVVIRVSYYGDYNAKRVDWKKAGPDLADLVKLLANYY
GQAVLIKTTPAIKRQLDSTYIKQSKFWLEEPQIKKHNRRVQFVEYDAEQKFKNDHSDLEL
PVSYFNGSQKTWNEQTN

Enzyme Prediction     

No EC number prediction in MGYG000002367_00670.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	66	211	2.8e-23	0.807909604519774

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06419	GH25_muramidase_2	6.33e-95	53	245	2	190	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	1.32e-24	68	208	9	146	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.
cd06413	GH25_muramidase_1	6.27e-20	57	232	1	178	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.
COG3757	Acm	3.05e-11	50	254	54	262	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
cd06525	GH25_Lyc-like	4.54e-11	68	137	9	78	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
ARW20137.1	1.19e-184	1	257	1	257
AHA04808.1	2.40e-184	1	257	1	257
QYY85545.1	2.40e-184	1	257	1	257
AXR43204.1	4.85e-184	1	257	1	257
QDJ23965.1	6.89e-184	1	257	1	257

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	4.67e-15	57	189	14	146	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]

Swiss-Prot Hits     

has no Swissprot hit.

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
0.998545	0.001074	0.000057	0.000013	0.000005	0.000311

TMHMM  Annotations     

start	end
24	43