CAZyme Information: MGYG000001927_00751

Basic Information

• Species: Prevotella sp900547005
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900547005
• CAZyme ID: MGYG000001927_00751
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
233	MGYG000001927_7|CGC1	27178.06	8.5392

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001927	2803818	MAG	Denmark	Europe

• Gene Location: Start: 61959; End: 62660 Strand: -

Full Sequence      

MNMKKIIILAAVIFSALCAKAQYTIQCEDTCNHVHGLDMSHYQGNVFWEAVGDNGRMFYV
YLKATEGGSNMDKRYEENIYMARRNGLKVGSYHFYRPRQPQEEQLRNFRAQCRPQDQDLI
PMIDVEVTSGLRASALCDSLQKFLILVEKEYQQKPLVYTYTNFYNKYLSGALDGYKLMVA
QYNDKEPVLNDEHDIFAWQYTGKGHINGVNGYVDKSRLLGRHTMREIRFIHKK

Enzyme Prediction     

No EC number prediction in MGYG000001927_00751.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	38	209	2e-43	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06413	GH25_muramidase_1	5.14e-54	34	220	3	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.
cd06525	GH25_Lyc-like	1.52e-46	36	214	2	180	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.
cd06524	GH25_YegX-like	3.53e-46	35	220	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.
cd00599	GH25_muramidase	1.96e-43	35	214	1	182	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	4.86e-40	38	209	2	180	Glycosyl hydrolases family 25.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKH87906.1	2.05e-121	1	233	1	235
QUB82002.1	4.29e-121	1	229	1	231
QUB79775.1	4.29e-121	1	229	1	231
AUI56122.1	4.29e-121	1	229	1	231
QUB59179.1	8.34e-121	1	233	1	235

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	1.70e-22	33	214	19	203	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
2WAG_A	1.05e-21	34	220	16	208	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
4KRT_A	1.17e-21	33	214	19	203	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	2.04e-14	34	220	5	204	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
5A6S_A	3.81e-14	38	216	26	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
P76421	4.88e-26	34	214	67	250	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	4.88e-26	34	214	67	250	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	6.83e-26	34	214	67	250	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P26836	4.38e-25	32	214	7	192	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	2.09e-13	24	220	73	281	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000533	0.982978	0.015729	0.000266	0.000237	0.000222

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001927_00751.