CAZyme Information: MGYG000004468_01764

Basic Information

• Species: Alistipes_A sp900539755
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes_A; Alistipes_A sp900539755
• CAZyme ID: MGYG000004468_01764
• CAZy Family: GH25
• CAZyme Description: Autolytic lysozyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
227	MGYG000004468_10|CGC1	26616.49	7.4305

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004468	2418771	MAG	Israel	Asia

• Gene Location: Start: 68701; End: 69384 Strand: +

Full Sequence      

MNISGCSWLRMLCLGVASLLMVSCERTADDFEVWGLDVSRHQKEVNWEKVLEHEQPNFVF
IKATEGTLIVDPTYEKHRAELEKTGVLWGAYHFFGHRTPGKEQARNFIKTAKLKHGNLIP
VLDIEWHRFMKDPKRSAREAKNFCREIKRYYGVNPIIYCSTNFYEKYLAETFPEDEYVLW
IADYRSCPPLKWQLWQHTDSHRIPGISGDVDRNVFAGSAEEFKKLIL

Enzyme Prediction     

No EC number prediction in MGYG000004468_01764.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	37	206	3.5e-50	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00599	GH25_muramidase	8.25e-57	34	215	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	1.00e-56	31	217	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	9.25e-56	35	217	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	3.43e-50	35	225	65	263	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
cd06525	GH25_Lyc-like	1.15e-41	35	215	2	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCG54743.1	1.27e-148	9	227	8	226
QGA24506.1	2.83e-115	14	227	11	224
AYD46598.1	1.81e-54	16	227	21	231
QEC73182.1	2.20e-52	33	223	37	225
AWM34133.1	2.88e-46	31	218	137	324

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	7.83e-37	29	223	12	214	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
2X8R_A	8.53e-17	33	225	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]
1JFX_A	3.57e-15	29	219	1	206	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
6ZMV_A	1.19e-09	35	225	4	203	ChainA, muramidase [Trichobolus zukalii],6ZMV_B Chain B, muramidase [Trichobolus zukalii]
6ZM8_A	3.10e-09	35	225	4	204	ChainA, muramidase [Sodiomyces alcalophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P76421	8.03e-36	26	226	60	265	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	1.13e-35	26	226	60	265	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	2.24e-35	31	226	65	265	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P25310	1.07e-14	25	219	71	283	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836	2.62e-13	35	215	11	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 LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000003	0.002611	0.997416	0.000001	0.000001	0.000001

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004468_01764.