CAZyme Information: MGYG000001413_00822

Basic Information

• Species: Enorma massiliensis
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Enorma; Enorma massiliensis
• CAZyme ID: MGYG000001413_00822
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
500		55664.43	4.8345

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001413	2263023	Isolate	not provided	not provided

• Gene Location: Start: 973998; End: 975500 Strand: +

Full Sequence      

MKRRTFLAACATAIASTPAIAFAEETQAIDPADALNALGSNPSYEEFVDYAERYLTDMDD
PQHMSLGANNEPSTYAGSNPYWSSSNKGAKTFYDGNGNIWLSSAHKIVDVSSWQEDINWN
ATSQAVDGAVLRIGYGVGNTDRKFERNLSECRRLGVPYGVYFYSYAYDASFARREAQWLS
TLFSRYSIDRNTPVFYDLEQFEPWSGHYPPTSVSAYESIVDGFFSVLSANGFSSLHVYSY
RSYLTTGPLASAKIHSHVSWVAEYNPTLKYSISAASGVKGWQYTSTGSVPGISGHADISA
FNLSIRWTGGGYPYGFPDVYSWTPHAEDILWLKENGIAHGYGNGYFGTYDEVQREQMAAF
MYRVVGSPSYSPTGEDMARFPDVTSSTPHAKEIWWLGSTKIAEGYGDGSYGPYDPITREQ
MAAFLYRLAGFPDYEPSTEDAARFPDVNEATPHAKEIWWMGAQGLSSGYKDEGGIYGPFR
NILRLDMAAFLHRWHDMFGV

Enzyme Prediction     

No EC number prediction in MGYG000001413_00822.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	108	292	4.5e-33	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	8.56e-54	106	301	2	190	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	4.95e-25	106	301	1	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.
cd06523	GH25_PlyB-like	4.04e-24	106	300	1	176	PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) 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	1.42e-16	106	301	1	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.
pfam01183	Glyco_hydro_25	9.49e-15	108	292	1	180	Glycosyl hydrolases family 25.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QWT17570.1	2.05e-142	2	495	24	497
ATO39491.1	1.08e-99	86	493	62	470
AIZ16865.1	4.35e-98	90	493	63	467
ACS48426.1	9.57e-94	104	493	137	530
ACS46860.1	9.57e-94	104	493	137	530

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	2.50e-32	104	301	268	467	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	6.35e-32	104	301	268	467	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
1JFX_A	2.28e-08	108	304	8	205	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4FF5_A	1.72e-06	107	302	54	250	Structurebasis of a novel virulence factor GHIP a glycosyl hydrolase 25 of Streptococcus pneumoniae participating in host cell invasion [Streptococcus pneumoniae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25310	2.63e-07	108	304	85	282	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P22258	6.33e-07	296	435	9	151	Cell surface protein OS=Thermoanaerobacter kivui OX=2325 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as TAT

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000521	0.438526	0.000222	0.560201	0.000347	0.000165

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001413_00822.