CAZyme Information: MGYG000000223_02503

Basic Information

• Species: NSJ-61 sp003433845
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; NSJ-61; NSJ-61 sp003433845
• CAZyme ID: MGYG000000223_02503
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
357		40917.92	7.2048

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000223	4367631	Isolate	China	Asia

• Gene Location: Start: 93098; End: 94171 Strand: -

Full Sequence      

MTKLLGIDVSEHNGVINWDTIKKGGIEFAIIRSSYGHFVEDRQFRRNVKECERVHMPYGL
YHYSYVATDQEMREEASGFIRLCKSCKPSYPCFIDMEDADGWKASHHVSDAMNVKVCYYT
CSELEANGFYAGIYANLDWWNNHLNSSTLDRFDKWVAQWASVNTYTKPYQMWQFTSDGRV
DGYTGRLDMDYSFVDYEKLITSMGFNGYHKDGNKPENHPPITTHPARPRYSVGDKIAFKG
LWTQSNGGNWYPVKNLAIKEGIITKILYGTQHPYLINHNVGWANDDVVIHQESNRFKIGD
KVSFDGLWTQSNGGVYYPSSSLLVKQGRITSIAKGAKHPYLINENVGWAQESALHHI

Enzyme Prediction     

No EC number prediction in MGYG000000223_02503.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	7	182	1.6e-43	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.11e-71	6	193	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	2.36e-31	6	191	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.
cd06524	GH25_YegX-like	5.98e-23	5	191	1	191	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.
pfam01183	Glyco_hydro_25	4.93e-22	7	182	1	179	Glycosyl hydrolases family 25.
COG3757	Acm	4.65e-20	6	191	65	252	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
BCT44624.1	6.42e-174	3	357	2	355
QSI25415.1	2.78e-156	5	288	4	286
ANU70287.1	8.74e-153	5	288	4	286
QQR25843.1	8.74e-153	5	288	4	286
ASU17291.1	8.74e-153	5	288	4	286

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4JZ5_A	3.40e-15	4	190	23	210	High-resolutionstructure of catalytic domain of endolysin ply40 from bacteriophage P40 of Listeria monocytogenes [Listeria phage P40]
2WW5_A	5.95e-14	7	189	272	464	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae at 1.6 A resolution [Streptococcus pneumoniae R6],2WWD_A 3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment [Streptococcus pneumoniae R6]
2WWC_A	1.43e-13	7	189	272	464	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
1JFX_A	1.10e-10	6	188	7	198	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRU_A	2.36e-10	4	206	20	219	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25310	1.34e-09	6	188	84	275	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836	5.88e-07	4	254	9	259	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
1.000046	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000223_02503.