CAZyme Information: MGYG000001540_01063

Basic Information

• Species: Corynebacterium provencense
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Mycobacteriales; Mycobacteriaceae; Corynebacterium; Corynebacterium provencense
• CAZyme ID: MGYG000001540_01063
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
404	MGYG000001540_1|CGC4	42749.27	3.9808

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001540	3078120	Isolate	not provided	not provided

• Gene Location: Start: 1128167; End: 1129381 Strand: +

Full Sequence      

MRSLPWRRHARTTTPARLTATVLMGSAAAVAALVATDVLPVPSWALDGIDVASHQHPGGA
AIDWDAVAASGQSFAFIKATEGTGYTNPYFSSDSAKAAAAGITPGSYHYAKPEIDARTQA
RYYAAQLATGVSPSLPPTLDLEETGGLGPTELQNWVREWIDEIKTLTGRDPIIYTYYSFW
VGQMGNTTEFSEYPLWLAYYNSSLPDQIPGGWDEVTFWQYSGSGSVDGVITDVDLNTYYG
TDEELQALTGTAESGTTVGDATEALKPIQDAAVDEAETTNAVQHSAAVLGLPVLNIPLST
DLLVNLLGLVAGEVSPEVVLQTALNSGFDYQTSQTITDAGTETRDADITLPQGRISELVS
TVLGDGNGTVTLQGVLRVLNEFGAQDYITNLAGHVNGSAYSPAG

Enzyme Prediction     

No EC number prediction in MGYG000001540_01063.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	49	229	1.6e-53	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00599	GH25_muramidase	2.70e-63	48	238	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	8.41e-56	48	245	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	7.41e-51	48	240	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	2.58e-49	49	229	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	2.08e-40	48	238	2	184	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
AWT27325.1	9.24e-288	1	404	1	404
AGP29806.1	1.58e-227	1	404	5	406
AEK38235.1	2.00e-220	1	391	5	396
AHW65540.1	1.64e-174	1	392	1	431
QQC46823.1	3.36e-164	1	387	1	388

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JFX_A	5.73e-33	46	248	5	212	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
6ZMV_A	2.38e-29	45	248	1	203	ChainA, muramidase [Trichobolus zukalii],6ZMV_B Chain B, muramidase [Trichobolus zukalii]
2X8R_A	3.07e-23	46	221	4	185	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]
6ZM8_A	4.05e-23	63	248	15	204	ChainA, muramidase [Sodiomyces alcalophilus]
4KRU_A	1.45e-20	46	238	20	207	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
Q8X7H0	1.69e-32	43	247	64	263	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P76421	3.27e-32	43	247	64	263	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
P25310	7.47e-32	40	248	76	289	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
Q8FFY2	1.22e-31	43	246	64	262	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P00721	1.31e-23	46	228	2	193	N,O-diacetylmuramidase OS=Chalaropsis sp. OX=36534 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
0.050507	0.948151	0.000443	0.000404	0.000251	0.000229

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001540_01063.