CAZyme Information: MGYG000000373_00447

Basic Information

• Species: UMGS1537 sp900761045
• Lineage: Bacteria; Firmicutes_A; Clostridia; UBA1212; UBA1255; UMGS1537; UMGS1537 sp900761045
• CAZyme ID: MGYG000000373_00447
• CAZy Family: GH25
• CAZyme Description: Lysozyme M1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
233		26796.59	6.3843

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000373	2809464	MAG	Sweden	Europe

• Gene Location: Start: 7055; End: 7756 Strand: +

Full Sequence      

MKKRRFLIHALFCIYLFILAALVRPIAGSYEVKGVDVARYQGEVDWSAFSEQGIAFAFIK
ATEGSSHVDMRFQENWEAVAKTSILAAPYHFLSYDSSGAAQAEHYITTVGKRRGMLPPAV
DVEFYGDYYDTPMEPHKAREILGDLLEALEKFYGAKPIIYATRSAYTLYIKDYFTDYPLW
IRGVYYPPFLDGIFSWTFWQYSDRGRLYGHEGVHIDLNVYRGTLDELQGLVIK

Enzyme Prediction     

No EC number prediction in MGYG000000373_00447.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	35	209	9.5e-45	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06413	GH25_muramidase_1	1.57e-82	30	222	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.
cd06524	GH25_YegX-like	2.13e-50	33	222	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	7.14e-50	33	220	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.
COG3757	Acm	5.50e-47	30	232	61	265	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
cd06412	GH25_CH-type	1.40e-37	32	227	1	199	CH-type (Chalaropsis-type) lysozymes represent one of four functionally-defined classes of peptidoglycan hydrolases (also referred to as endo-N-acetylmuramidases) that cleave bacterial cell wall peptidoglycans. CH-type lysozymes exhibit both lysozyme (acetylmuramidase) and diacetylmuramidase activity. The first member of this family to be described was a muramidase from the fungus Chalaropsis. However, a majority of the CH-type lysozymes are found in bacteriophages and Gram-positive bacteria such as Streptomyces and Clostridium. CH-type lysozymes have a single glycosyl hydrolase family 25 (GH25) domain with an unusual beta/alpha-barrel fold in which the last strand of the barrel is antiparallel to strands beta7 and beta1. Most CH-type lysozymes appear to lack the cell wall-binding domain found in other GH25 muramidases.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALU13329.1	4.06e-71	7	226	17	239
QCT71758.1	9.34e-70	7	225	17	238
ADO39003.1	2.66e-69	7	226	17	239
ARD65165.1	2.15e-68	7	226	17	239
QOW29174.1	2.73e-66	29	233	38	244

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	8.47e-66	30	233	14	219	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
1JFX_A	4.60e-24	32	230	5	212	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRU_A	6.44e-14	31	212	19	200	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	1.95e-13	31	212	19	200	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]
6ZM8_A	4.02e-11	31	230	1	204	ChainA, muramidase [Sodiomyces alcalophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8FFY2	9.43e-40	26	231	61	265	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P76421	5.23e-39	26	231	61	265	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8X7H0	1.14e-37	26	231	61	265	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P25310	5.69e-23	27	230	77	289	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836	5.12e-15	29	221	6	197	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
0.300095	0.692501	0.005463	0.000706	0.000476	0.000736

TMHMM  Annotations     

start	end
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