CAZyme Information: MGYG000004041_01836

Basic Information

• Species: Ellagibacter isourolithinifaciens
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Eggerthellaceae; Ellagibacter; Ellagibacter isourolithinifaciens
• CAZyme ID: MGYG000004041_01836
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
364		39421.39	4.8255

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004041	2177939	MAG	United Kingdom	Europe

• Gene Location: Start: 3985; End: 5079 Strand: +

Full Sequence      

MSMNGIDISNWQAGMSLSAVSGSIGFVIVKATEGIGFVDKSCDKFYQEAKRLGKKLGFYH
FARQNDPVAEADFFYENTRNYFGEAIPVLDWEVDNDIAWVNKFVERIHDLTGVWPWVYAN
PWRFNQGTVNKNCGRWIAGYPKNGITDINYGKNNAIPSSYSVNGTICAWQFSSSVRLSGY
NGNLDGDIFYGDEAAWDKYADPKGAASSGDGGDDSDGGGSDSSSASGSGGVTPSGSTLDL
VYHIVTNNINGDARRDYCGSRYDEVQDFINYTHDASASTLAEWIKAGKYGNNPVRETVIE
ACGGKYQEAQDIINGKGKSTTYTVKSGDTLSGIAAKFGTTYQAIASKNGISNPNIIYAGQ
KLVI

Enzyme Prediction     

No EC number prediction in MGYG000004041_01836.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	6	179	4.2e-38	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06417	GH25_LysA-like	3.01e-52	3	196	1	195	LysA is a cell wall endolysin produced by Lactobacillus fermentum, which degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. The N-terminal glycosyl hydrolase family 25 (GH25) domain of LysA has sequence similarity with other murein hydrolase catalytic domains while the C-terminal domain has sequence similarity with putative bacterial cell wall-binding SH3b domains. This domain family also includes LysL of Lactococcus lactis.
cd00599	GH25_muramidase	3.41e-35	5	189	2	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	7.01e-30	4	189	1	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.
pfam01183	Glyco_hydro_25	1.80e-27	6	179	1	179	Glycosyl hydrolases family 25.
cd06524	GH25_YegX-like	1.59e-20	5	191	2	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBK80688.1	6.87e-69	1	362	1	359
QRT50341.1	3.19e-62	1	364	1	345
QRT50187.1	9.50e-61	1	362	1	393
QYC52388.1	8.16e-54	6	364	5	353
QOP65129.1	4.38e-53	1	362	1	337

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ZMV_A	6.12e-14	5	185	4	198	ChainA, muramidase [Trichobolus zukalii],6ZMV_B Chain B, muramidase [Trichobolus zukalii]
1JFX_A	2.50e-13	3	194	5	207	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
2X8R_A	5.59e-11	3	188	4	201	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]
2WAG_A	1.80e-09	3	199	16	216	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
2MKX_A	8.92e-08	317	364	2	48	Solutionstructure of LysM the peptidoglycan binding domain of autolysin AtlA from Enterococcus faecalis [Enterococcus faecalis V583]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P34020	1.91e-17	3	189	1	180	Autolytic lysozyme OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=lyc PE=1 SV=1
P25310	3.65e-12	3	194	82	284	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P00721	1.07e-11	3	132	2	152	N,O-diacetylmuramidase OS=Chalaropsis sp. OX=36534 PE=1 SV=1
Q49UX4	1.66e-10	320	364	86	129	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 PE=3 SV=1
P26836	4.35e-10	3	189	9	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 OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000045	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004041_01836.