CAZyme Information: MGYG000003018_01302

Basic Information

• Species: Alistipes_A sp900549685
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes_A; Alistipes_A sp900549685
• CAZyme ID: MGYG000003018_01302
• CAZy Family: GH25
• CAZyme Description: Lysozyme M1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
224	MGYG000003018_90|CGC1	26458.3	9.264

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003018	2600623	MAG	China	Asia

• Gene Location: Start: 2368; End: 3042 Strand: +

Full Sequence      

MRTFSYLICLSGLLLLAACGREKTPDDFEVWGLDVSRHQQNVNWEQVIAHERPDFVFIKA
TEGTKIVDPTYERHRRELEKAGVPWGAYHFFGHRTPGKEQARNFIKTAKLDKGNIIPVLD
IEKHRFMTDPKKSVREAKAFCDEIERYYGTPPIIYCSTNFYETYLAKDFKEGDYILWIAD
YRKCPPLRWQIWQHTDSHSIRGIRGKVDRNVFRGSREQFRKLIL

Enzyme Prediction     

No EC number prediction in MGYG000003018_01302.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	34	203	8.7e-51	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00599	GH25_muramidase	1.41e-58	31	212	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.
cd06413	GH25_muramidase_1	5.53e-57	28	214	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	2.00e-53	32	214	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.
COG3757	Acm	1.71e-47	24	222	57	263	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
pfam01183	Glyco_hydro_25	1.34e-41	34	203	2	180	Glycosyl hydrolases family 25.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGA24506.1	2.86e-128	1	224	1	224
BCG54743.1	7.05e-120	7	224	11	226
AYD46598.1	1.49e-52	22	224	30	231
QEC73182.1	1.16e-48	30	219	37	224
QEC57247.1	9.70e-48	25	224	51	255

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	6.42e-31	26	219	12	213	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
2X8R_A	2.99e-15	30	222	4	207	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]
3HMC_A	1.12e-14	33	216	8	183	Endolysinfrom Bacillus anthracis [Bacillus anthracis]
4JZ5_A	9.13e-13	33	210	26	210	High-resolutionstructure of catalytic domain of endolysin ply40 from bacteriophage P40 of Listeria monocytogenes [Listeria phage P40]
1JFX_A	1.60e-12	26	215	1	205	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8X7H0	5.20e-36	25	223	62	265	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P76421	7.32e-36	23	223	60	265	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	1.03e-35	23	223	60	265	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P26836	1.09e-14	32	213	11	197	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	1.95e-11	26	215	78	282	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000000	1.000033	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003018_01302.