CAZyme Information: MGYG000001341_01011

Basic Information

• Species: Leuconostoc mesenteroides
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Leuconostoc; Leuconostoc mesenteroides
• CAZyme ID: MGYG000001341_01011
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
245	MGYG000001341_28|CGC5	27001.62	9.6169

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001341	1638558	Isolate	not provided	not provided

• Gene Location: Start: 307187; End: 307924 Strand: -

Full Sequence      

MENVFASASQYKTKKLLTFTSWLLILSGIVCSFTVWVFAKPVVTQTNTIPSGFSVQGVSV
NQTSNYVDFNNLVSNGVSFVYMRTTSGSSVMDGGYKSSFSRAKSAHLKVGTIHVYDASVT
AATQAQYYIDNVGNNIGELPIAISVTADQISTATSKQRLASLVQILASHYNHDMIIYTTP
NVQKKLSSTISKTKYWLIEDNTKNTDSKNLFIQYDEDQTIGSGLKAIKMPTTVFNGTQKQ
FEVYK

Enzyme Prediction     

No EC number prediction in MGYG000001341_01011.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	59	218	6.1e-27	0.9491525423728814

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06419	GH25_muramidase_2	3.59e-86	49	234	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	2.30e-26	56	197	1	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	4.72e-18	53	181	1	134	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	9.75e-14	39	237	47	256	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
pfam01183	Glyco_hydro_25	3.32e-11	67	181	10	130	Glycosyl hydrolases family 25.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ARR88607.1	8.31e-170	1	245	1	245
APE76272.1	3.39e-169	1	245	1	245
QHM58608.1	3.39e-169	1	245	1	245
ASR68445.1	3.39e-169	1	245	1	245
AWV37411.1	3.39e-169	1	245	1	245

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	1.63e-06	54	220	19	195	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	2.60e-06	54	220	19	195	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	2.99e-07	54	203	8	162	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
1.000028	0.000003	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
16	38