CAZyme Information: MGYG000000550_02080

Basic Information

• Species: Lawsonibacter sp900545895
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; Lawsonibacter; Lawsonibacter sp900545895
• CAZyme ID: MGYG000000550_02080
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
302		33876.84	3.9685

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000550	2679456	MAG	China	Asia

• Gene Location: Start: 135; End: 1043 Strand: -

Full Sequence      

MIEELQAPRPRDDRPSPPRRGGGGWTGKLALVFSLLALAISCAVLYLTVFHKEPEPEYIT
YRDQQLLVVEGLDKNTYDPEAFTTDSQGWVQYEKDGQRAALGIDVSVYQGEIDWQAVAGS
GIDFAMIRVGYRGYSQGTLQLDERFQANMEGALEAGLDVGVYFFSQATTVAEAEEEADFV
LEAIRSYPIRYPVVFDWEYITTGQARTEGMDGQGITQCAAAFCELVSVAGYTPMVYFNQD
MGYLVYDLKSLDSSLFWLAEYDSKPDFYYDFDMWQYTHTGTVPGIEGSVDLNLAFRDFPI
SS

Enzyme Prediction     

No EC number prediction in MGYG000000550_02080.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	103	285	1.9e-43	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	4.56e-82	102	295	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	2.03e-34	102	294	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.
cd06413	GH25_muramidase_1	2.45e-29	102	292	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	4.19e-28	102	292	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.
pfam01183	Glyco_hydro_25	4.23e-27	103	285	1	180	Glycosyl hydrolases family 25.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCT06482.1	3.57e-76	69	298	88	319
QKN23542.1	2.78e-70	61	298	67	308
QKO29779.1	2.78e-70	61	298	67	308
ARP50725.1	2.78e-70	61	298	67	308
QNO18615.1	3.83e-68	61	298	60	299

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WWC_A	8.39e-12	103	293	272	466	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
3HMC_A	2.03e-11	103	292	8	177	Endolysinfrom Bacillus anthracis [Bacillus anthracis]
4KRU_A	1.19e-10	102	292	22	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
1JFX_A	1.39e-10	102	292	7	200	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
2WAG_A	2.66e-10	102	295	18	207	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P34020	5.77e-10	102	292	3	178	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	1.60e-09	102	292	84	277	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
0.999955	0.000020	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
29	51