CAZyme Information: MGYG000004431_02484

Basic Information

• Species: COE1 sp001916965
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; COE1; COE1 sp001916965
• CAZyme ID: MGYG000004431_02484
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
428	MGYG000004431_33|CGC2	47415.39	3.9053

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004431	3494954	MAG	Israel	Asia

• Gene Location: Start: 31568; End: 32854 Strand: +

Full Sequence      

MDSKIKRLTILAMLGSMVLVAAVIVVFNYERFVSTGSTAKQEQTTETEGALEEDGMVKGA
DLSAFLQDETFFDHEKNTYEKAMEDGTQTESDTDVTLLATSVEKDIRIKVVDAEGKTVEG
YPFVLSVGDLGNYQDTDEDGMIYISGVRPGEYEITLADAGEYTCTSPSLDVRVKAMVSYM
PIEDISYLIRSESEVDASIEDTESDEVDGDDSQYTALLDTDSQDKPIELGIDVSKWNGEI
DWDVVKAEGVDYAIIRCGYRGSSSGWLIEDPYFWQNLQNAKKAGVKVGIYFFSQATTMVE
AVEEASMVVTLLGGETLDYPVFIDTEGAGGNGRADGLDADTRTMVCESFCRTIENAGYRA
GVYASCNWYRNNLHAEDLDAYKIWLAEYRQTPQYEGRYDMWQYTSSGSVAGIEGRVDLNV
SYIQSYAN

Enzyme Prediction     

No EC number prediction in MGYG000004431_02484.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	231	412	5.5e-46	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	3.00e-83	230	422	3	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	6.92e-43	230	420	2	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.
pfam01183	Glyco_hydro_25	1.66e-32	231	412	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	3.20e-30	230	419	2	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.
cd06413	GH25_muramidase_1	1.88e-27	226	422	2	190	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
QNM02113.1	2.65e-129	1	422	1	431
QNM02116.1	9.40e-71	229	423	908	1100
ADL34064.1	3.31e-66	75	420	67	484
CBK74089.1	7.66e-66	228	421	324	516
AOZ95561.1	1.17e-65	226	422	1018	1213

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	6.76e-18	230	419	22	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
2WW5_A	1.01e-17	231	422	272	468	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	2.42e-17	231	422	272	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
4KRT_A	3.80e-17	230	419	22	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]
1JFX_A	2.44e-11	230	419	7	200	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	2.75e-15	230	419	11	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	1.87e-14	230	419	3	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
P25310	3.30e-10	230	419	84	277	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 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
0.798323	0.190934	0.002674	0.001652	0.000833	0.005599

TMHMM  Annotations     

start	end
7	29