CAZyme Information: MGYG000002705_02480

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS856
• CAZyme ID: MGYG000002705_02480
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
433	MGYG000002705_94|CGC1	46425.43	4.6702

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002705	2922707	MAG	Canada	North America

• Gene Location: Start: 974; End: 2275 Strand: -

Full Sequence      

MRRSSRYHKAAAAALAVCLTAALGGCGVNSLPADGWQIAPPTGEIYAGAEPFGPTTASST
EPGFPSMEETTTLPVSTEGTTTAATTTQRTSRKTTTTTKPIAVEDDPLWNREEESQEDTP
TVTLPNKTTTTTATTTTTASETTAEPTTGGTGTTAATTQVTSAATTTTTTTATTTGTPPQ
NGWYKADGKKYYYQNGKPVTGFYEIGGEYCAFDDDGVKLEAKVGIDVSTFQGSINWEQVK
EKVDFAIIRVGLRGWGTANIGKDARFEENIKGATAAGIDCGVYFFSQAITVAEAIEEANF
VLDAIKPYKLTYPVVIDMENPPDPEARTQAIKNNRRLLTDITLAFCETIRDAGYYPMVYS
GASWLNNNLYGSEIAQKYDIWVAHYGSKKPGHSGSIWQYSSSGRVDGITTNVDLNVSAKD
YAAIIREQGLNHL

Enzyme Prediction     

No EC number prediction in MGYG000002705_02480.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	225	408	1.9e-48	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	3.08e-86	222	417	1	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	8.27e-39	224	416	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	4.93e-31	225	408	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	7.53e-28	224	415	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	9.30e-25	224	418	5	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
ADL34306.1	9.80e-51	201	421	150	362
ABX43465.1	3.21e-50	214	422	416	622
AOZ96288.1	2.02e-49	217	421	159	362
CBL26148.1	1.39e-48	209	416	92	300
QYX28904.1	3.59e-48	209	416	76	283

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	1.79e-15	224	415	22	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	8.17e-15	224	415	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	2.28e-14	224	415	7	200	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4JZ5_A	3.67e-11	225	420	26	215	High-resolutionstructure of catalytic domain of endolysin ply40 from bacteriophage P40 of Listeria monocytogenes [Listeria phage P40]
5A6S_A	1.16e-09	226	426	26	210	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
P25310	3.72e-13	224	415	84	277	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836	1.49e-10	224	415	11	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P15057	8.21e-06	281	402	57	179	Lysozyme OS=Streptococcus phage Cp-1 OX=10747 GN=CPL1 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000011	1.000059	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002705_02480.