CAZyme Information: MGYG000003811_01865

Basic Information

• Species: Corynebacterium amycolatum
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Mycobacteriales; Mycobacteriaceae; Corynebacterium; Corynebacterium amycolatum
• CAZyme ID: MGYG000003811_01865
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
329		35443.02	4.3271

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003811	2349574	MAG	Canada	North America

• Gene Location: Start: 3227; End: 4216 Strand: -

Full Sequence      

MKFLPLSATAVLKRRPGRATLASIVAVAPLTLGVIAPADAQPQDASAHSNPSAADSKGSL
DFLTESPSITDAPLVSDAQEPQGSDANGSSTNSEPSAESQSAENASSNSARTGFHMGPTG
VDVSKWQRPGGVALKWDEVAASGQKFAFIKATDGVEGDQKYFLEDSIAAAKAGLYVGSYH
KAHPDRSATAQADQYVEALQQRDEQISTDKTLPPVLDIELDNGLNPTQLQKWTKDFLERV
EEKTGETPMIYTYRWFWQNPMGNSTDFTDYPLWLAAYEDSAPTSLPGGWQSMTFWQRSST
GRIDGIPTIVDEDVFNGTEAELQQLAAAH

Enzyme Prediction     

No EC number prediction in MGYG000003811_01865.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	121	306	6.2e-50	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00599	GH25_muramidase	8.97e-58	120	315	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.
cd06412	GH25_CH-type	1.21e-56	120	322	3	199	CH-type (Chalaropsis-type) lysozymes represent one of four functionally-defined classes of peptidoglycan hydrolases (also referred to as endo-N-acetylmuramidases) that cleave bacterial cell wall peptidoglycans. CH-type lysozymes exhibit both lysozyme (acetylmuramidase) and diacetylmuramidase activity. The first member of this family to be described was a muramidase from the fungus Chalaropsis. However, a majority of the CH-type lysozymes are found in bacteriophages and Gram-positive bacteria such as Streptomyces and Clostridium. CH-type lysozymes have a single glycosyl hydrolase family 25 (GH25) domain with an unusual beta/alpha-barrel fold in which the last strand of the barrel is antiparallel to strands beta7 and beta1. Most CH-type lysozymes appear to lack the cell wall-binding domain found in other GH25 muramidases.
cd06524	GH25_YegX-like	2.70e-48	120	317	2	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.
pfam01183	Glyco_hydro_25	6.05e-45	121	306	1	180	Glycosyl hydrolases family 25.
cd06413	GH25_muramidase_1	7.35e-42	120	317	5	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QPR31460.1	5.50e-217	1	329	1	329
QQV00903.1	5.50e-217	1	329	1	329
QQB83339.1	5.50e-217	1	329	1	329
ASE57090.1	3.35e-216	1	329	1	321
QQU97309.1	3.74e-213	1	329	1	321

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JFX_A	9.19e-34	117	326	4	213	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
2X8R_A	7.00e-29	120	327	6	209	Thestructure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_B The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_C The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_D The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_E The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_F The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293]
6ZMV_A	1.01e-23	120	326	4	204	ChainA, muramidase [Trichobolus zukalii],6ZMV_B Chain B, muramidase [Trichobolus zukalii]
6ZM8_A	2.75e-22	120	326	4	205	ChainA, muramidase [Sodiomyces alcalophilus]
4KRU_A	3.17e-16	120	306	22	198	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	3.21e-32	117	326	81	290	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
Q8X7H0	2.23e-27	120	323	69	262	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
Q8FFY2	3.10e-27	120	323	69	262	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P76421	6.00e-27	120	323	69	262	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
D4ANU4	7.32e-26	143	326	51	232	N,O-diacetylmuramidase OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05911 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
0.002679	0.995154	0.000641	0.001067	0.000238	0.000189

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003811_01865.