CAZyme Information: MGYG000001001_00669

Basic Information

• Species: Prevotella sp900540375
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900540375
• CAZyme ID: MGYG000001001_00669
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
299		34210.92	7.5944

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001001	3195691	MAG	China	Asia

• Gene Location: Start: 91617; End: 92516 Strand: +

Full Sequence      

MTTTVNPYHDHHGGGGFHDAHAHHHHHHSYQYYYIHHQISRFLHKSWLVLITIIALLFIG
FVLAAIYVPNFRDSLPNIDGFFSNGVKLTSALGRHGRMDYDGIDISHHQGVIDWNRVSRD
TCVKFVYIKATEGGDHIDSFYLKNIACARAAGIPVGTYHYLTSGSSIRQQFRLFYSIVNR
HHQDLVPMIDVEEEGVKGWSREVLTVKLDSMIQLLATHYHGTPIIYCYTRFFNERLYPRF
ASVPLFVSHFSSSEPPLFGNTKPLLWQHSDAGLIDGISTPVDLDVFSEGMRLDKLKLKH

Enzyme Prediction     

No EC number prediction in MGYG000001001_00669.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	103	277	1.9e-42	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06413	GH25_muramidase_1	8.15e-52	102	287	5	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	2.60e-51	102	286	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.
cd06524	GH25_YegX-like	1.79e-50	102	286	2	192	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.
cd06525	GH25_Lyc-like	4.28e-42	102	286	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.
pfam01183	Glyco_hydro_25	1.05e-37	103	277	1	180	Glycosyl hydrolases family 25.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALO48039.1	8.97e-70	94	298	45	249
QUB85048.1	9.57e-55	87	297	30	236
QUB71600.1	1.16e-54	97	297	31	231
AXV48434.1	1.07e-53	97	297	36	236
QUI94537.1	1.07e-53	97	297	36	236

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	5.73e-21	97	286	13	206	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
1JFX_A	9.31e-13	102	287	7	203	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
5JIP_A	7.14e-07	113	284	18	220	Crystalstructure of the Clostridium perfringens spore cortex lytic enzyme SleM [Clostridium perfringens],5JIP_B Crystal structure of the Clostridium perfringens spore cortex lytic enzyme SleM [Clostridium perfringens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P76421	1.22e-25	78	287	32	255	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	1.70e-25	102	287	69	255	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	8.91e-24	78	287	32	255	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P34020	2.21e-18	102	290	3	184	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	1.24e-11	102	287	84	280	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1

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
0.999988	0.000048	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
46	68