CAZyme Information: MGYG000000532_01140

Basic Information

• Species: CAG-510 sp000434615
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-510; CAG-510 sp000434615
• CAZyme ID: MGYG000000532_01140
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
360		40688.25	4.3481

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000532	2771736	MAG	Fiji	Oceania

• Gene Location: Start: 67737; End: 68819 Strand: +

Full Sequence      

MKRKKKELLFYVITIASCLIAMTIVVIAALLIYDKIIEDKTAEKEQELAQQVAADPEVVS
YSQEEVDMMLADAIATTESSTRQQVSSEILDSLQASLESGTTMVESLRPIYKDKIVVVSN
KEYHFVPIDRSLKQSTLVQENLQVLENGELQYVENGEVVSHKGIDVSRYQGTIDWKKVAD
SGVEFAFVRVGVRGYGTEGKLTLDEKYKTNIEGASKAGIKVGVYFFSQAITEEEAKEEAD
LVLDAIAGLNVTYPIVYDVEKTGAKEGRMNQLTVEERTRMAHVFIDRIKEAGYTPMIYAN
MEMWSILINMSEFEDVDKWYAYYSPVVYFPYEYAIWQYSDTGTVPGITGDVDLNISFKEW

Enzyme Prediction     

No EC number prediction in MGYG000000532_01140.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	164	347	9.3e-48	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	3.24e-82	162	357	2	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	4.22e-41	162	355	1	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.
cd06413	GH25_muramidase_1	5.50e-37	162	354	4	187	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.
pfam01183	Glyco_hydro_25	7.00e-35	164	347	1	180	Glycosyl hydrolases family 25.
cd06524	GH25_YegX-like	1.12e-32	162	355	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNM03294.1	5.97e-113	2	360	20	380
ADL34306.1	1.99e-79	61	360	67	362
AOZ96288.1	5.60e-76	15	360	20	362
ABX43465.1	1.21e-66	94	360	357	621
ACR72973.1	1.94e-66	88	360	61	334

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	3.17e-16	162	354	21	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	1.43e-15	162	354	21	205	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]
2WAG_A	3.31e-15	162	357	17	207	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
1JFX_A	3.31e-13	162	354	6	200	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
5A6S_A	4.74e-09	165	360	26	205	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P34020	5.36e-16	162	354	2	178	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
P76421	5.38e-14	163	355	69	253	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	5.38e-14	163	355	69	253	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	7.31e-14	163	355	69	253	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P26836	4.78e-13	162	359	10	198	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
0.937379	0.036444	0.006373	0.000413	0.000183	0.019233

TMHMM  Annotations     

start	end
9	31