CAZyme Information: MGYG000003374_01664

Basic Information

• Species: Prevotella bivia
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella bivia
• CAZyme ID: MGYG000003374_01664
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
295	MGYG000003374_62|CGC1	34961.93	9.5254

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003374	2286602	MAG	United States	North America

• Gene Location: Start: 89224; End: 90111 Strand: +

Full Sequence      

MARETPFFVRRLKRFLKSLPLWGKWCWGITIGVFYCAIVYIYLVAPTGFRWRAIYGEPNY
PKGYNIRGIDVSRYQGNINWNRLRNALIDATPVRFIFIKSTQGDSYIDPKFRSNFFEAKE
NGFLRGVYHFWSNKVSARRQAYFFLAMVKLQPGDFPPVLDVENKPKDMTTEDFQQNILTW
LHIVEDRYHVKPIIYTYYKFKQQYLSDQRFDDYPYWIAHYYVNQMEYKGRWKIWQHTDAG
KLPGIKGYVDLNIYNGSYYDMQQMLIPEPAPIDSSAISDSTSYDSLGVQSPRDSA

Enzyme Prediction     

No EC number prediction in MGYG000003374_01664.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	69	245	2.1e-52	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06524	GH25_YegX-like	2.61e-76	67	256	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.
cd06413	GH25_muramidase_1	1.58e-58	64	256	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.
cd00599	GH25_muramidase	2.34e-55	67	254	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.
pfam01183	Glyco_hydro_25	1.90e-47	69	245	1	180	Glycosyl hydrolases family 25.
COG3757	Acm	7.64e-45	58	257	55	256	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBA30463.1	8.51e-155	7	286	2	287
AKU70014.1	2.05e-154	12	293	11	289
QUB85622.1	2.05e-154	12	293	11	289
ANR74160.1	1.40e-153	7	289	2	290
QUB44752.1	1.40e-153	7	289	2	290

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	1.34e-25	64	257	14	209	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
4KRU_A	1.24e-22	65	252	19	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	9.18e-22	65	252	19	205	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]
1JFX_A	5.02e-21	66	257	5	205	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
5A6S_A	3.75e-16	61	252	16	199	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8FFY2	2.97e-50	61	262	62	262	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P76421	2.34e-49	61	262	62	262	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8X7H0	9.24e-49	30	262	31	262	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P26836	2.33e-21	65	262	8	204	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	1.08e-19	66	257	82	282	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
1.000032	0.000006	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
21	43