CAZyme Information: MGYG000004509_00853

Basic Information

• Lineage: Bacteria; Firmicutes; Bacilli; RF39; UBA660; RUG11198
• CAZyme ID: MGYG000004509_00853
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
354	MGYG000004509_6|CGC1	41487.26	9.285

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004509	1456179	MAG	Israel	Asia

• Gene Location: Start: 7389; End: 8453 Strand: -

Full Sequence      

MKGIDISSYQGTVNFQKIKNSEYQFVIIRLGYGDNILSQDDKKLQYNLTKCMEYNIPYAF
YLVSYAKNFTGKESVDSEIEHTKRLIKSTTPFCIFYDMEVDSIKYLGKNTLTNQAIKYCD
YFKNQGYQVGIYANKDWYTNYLDYDKLKSKNYKIWLAHYGIEKPSLECDLWQYTDKGKVE
GIYENTVDLNIMYKNLLLDTSNASTNKQIEELVQEVIEGKWGNGEERKNKLIRSGYPYEE
IQKKVNEKLNSNLRKEIEYKVKKGDTLSKIASLYHMTYQELANYNHLSNPNQIYPNQIIK
IPNQTLNSKYYQVKKGDTLSKIAKENNTTVEKLVKINNIKNPNLIYVGQKIRIS

Enzyme Prediction     

No EC number prediction in MGYG000004509_00853.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	4	182	3.1e-36	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.65e-56	1	193	1	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	1.37e-29	2	192	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.
cd06525	GH25_Lyc-like	7.61e-24	2	190	1	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.
cd06523	GH25_PlyB-like	2.00e-21	4	190	3	175	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.
pfam01183	Glyco_hydro_25	5.30e-20	4	182	1	180	Glycosyl hydrolases family 25.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CED93768.1	6.58e-51	2	251	4	253
QJA08433.1	4.60e-49	2	251	4	252
QEK16471.1	2.77e-46	3	353	5	325
QHJ73726.1	1.78e-42	4	301	5	309
QHJ73661.1	2.49e-42	4	301	5	309

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	2.69e-15	1	202	20	217	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4JZ5_A	4.53e-15	4	197	26	217	High-resolutionstructure of catalytic domain of endolysin ply40 from bacteriophage P40 of Listeria monocytogenes [Listeria phage P40]
4KRT_A	1.10e-14	1	202	20	217	X-raystructure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101],4KRT_B X-ray structure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
3HMC_A	2.90e-09	4	195	8	182	Endolysinfrom Bacillus anthracis [Bacillus anthracis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q37896	2.87e-13	160	354	67	263	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
P07540	5.71e-12	258	354	162	258	Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1
P11187	5.71e-12	258	354	162	258	Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 PE=1 SV=1
P34020	7.87e-12	1	198	1	186	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
Q49UX4	1.46e-11	259	354	29	130	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 PE=3 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
1.000087	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004509_00853.