CAZyme Information: MGYG000002140_00724

Basic Information

• Species: CAG-510 sp900551115
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-510; CAG-510 sp900551115
• CAZyme ID: MGYG000002140_00724
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
370		41253.44	4.1453

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002140	3321781	MAG	United States	North America

• Gene Location: Start: 44534; End: 45646 Strand: +

Full Sequence      

MKLPEEFDEQPKMGMGVVRMIIGVTLFIAAILVFVLIMNNKNNKPGGNNGSQAALSGTDN
SETGTNPGADASQTGTIEPGTLTPDDFDFWDMYPEETPAPLPEESGEKEEAVASDPATDG
KHTLVVGADGKEEWVLISPYLPKHEYDYTKLVCQSNLMKYYEDGRQVSYVGTDISKYQDY
VDFVKLKKAGIDFVMLRVGARGYGTGQLMLDEYFSDNIKRASDAGLEIGLYFFSQAVTEE
EAVEEANLVLENIGEYEITYPIAIDMELIAGDTSRIENLTRAEKTDISKKFLETIKEAGY
KPILYGNKEWLLKKIDLSKLTAYDIWLSQPGDLPDYPYKFSMWQYSNTAVIDGIAGYANL
NISFIDYSEK

Enzyme Prediction     

No EC number prediction in MGYG000002140_00724.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	173	354	6.7e-41	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	3.02e-59	171	364	3	191	The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes.
cd00599	GH25_muramidase	2.71e-27	171	362	2	185	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	3.31e-21	173	354	2	180	Glycosyl hydrolases family 25.
cd06413	GH25_muramidase_1	6.32e-20	171	361	5	187	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	3.61e-15	171	361	2	182	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
QNM01196.1	7.38e-157	77	370	76	373
QEK18217.1	2.96e-62	141	364	73	298
ACR72973.1	1.11e-61	125	368	88	335
ABX43465.1	1.44e-61	127	369	381	623
BBF45127.1	2.49e-61	143	367	54	280

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5JIP_A	1.47e-08	162	361	7	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
P26836	8.30e-09	171	361	11	194	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
1.000056	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
15	37