CAZyme Information: MGYG000001042_01146

Basic Information

• Species: Prevotella sp000436595
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp000436595
• CAZyme ID: MGYG000001042_01146
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
298	MGYG000001042_45|CGC2	35518.57	9.7784

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001042	3438278	MAG	Denmark	Europe

• Gene Location: Start: 33882; End: 34778 Strand: -

Full Sequence      

MTTPNFKSMRNIHKTKSTKKRTATRKGWNRTSGNARNNRGGIHKLIGRYPRWAWWIGGLC
VVVFYVWIFYYIFVGPFGFRWRALYGDAKYPEGYEIRGIDISHHQGNIDWELLRNAMIEK
CPIRFILIKATEGTTIVDSKFKENFNNAREYGYIRGAYHFWSNKSSAREQAYFFLNNVFL
LKGDLPPVLDIENKPDTVSVEDFQRDVLTWLHIVEDRYHVKPIIYTYYKFKMKYLNDPVF
DDYPYWIAHYYVDKVEYAGEWKFWQHTDAGRLPGIKGYVDFNIYNGSYYDLRKLTIGN

Enzyme Prediction     

No EC number prediction in MGYG000001042_01146.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	99	275	1.1e-51	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06524	GH25_YegX-like	1.29e-74	97	286	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	2.66e-61	94	286	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	9.32e-55	97	284	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	9.52e-48	99	275	1	180	Glycosyl hydrolases family 25.
COG3757	Acm	1.90e-42	94	298	61	267	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
QNT67813.1	2.82e-154	48	298	24	274
ALO48669.1	6.37e-154	21	298	5	282
BCS86629.1	2.68e-149	48	298	37	287
QYR10351.1	2.85e-146	30	297	11	278
VEH15533.1	1.79e-144	48	297	34	283

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	2.96e-31	94	287	14	209	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
1JFX_A	4.71e-27	96	295	5	213	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRU_A	6.72e-24	96	298	20	227	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	5.50e-23	96	298	20	227	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]
5A6S_A	2.27e-22	91	293	16	210	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	3.12e-47	89	297	60	267	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P76421	1.73e-46	89	297	60	267	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8X7H0	1.35e-45	91	297	62	267	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P25310	1.31e-25	96	295	82	290	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836	2.12e-19	96	293	9	205	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
0.999938	0.000060	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
52	74