CAZyme Information: MGYG000004129_00932

Basic Information

• Species: Acutalibacter sp000435395
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Acutalibacter; Acutalibacter sp000435395
• CAZyme ID: MGYG000004129_00932
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
305		33769.56	3.9502

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004129	2343469	MAG	United Kingdom	Europe

• Gene Location: Start: 3016; End: 3933 Strand: -

Full Sequence      

MASRHSKQQQQKVNPVLLATSAAVALVVVMVVVAISLAGGGGQGQEEESSGTGVPEGMVL
VNDLYEGQRLVPDFDMDLNQYDTEKFVEENGFIRYQDGKAVAGVDVSEHQGTIDWQQVKD
AGFEYAILRVAYRGMTEGGLNVDSTFEQNYQGATAAGLKVGVYFFSQAITQEEAREEAQY
VLDTLDGRELDYPVVFDWEIPIPSEQLPAEDLRAYDISGEVVTAMAKAFCQEIQSNGYTP
CVYTNKSMAYNTFNLEELKDFSLWYAEYQPAPSLYYHFQMWQYSASGTVPGIAGSADLNI
CFEPY

Enzyme Prediction     

No EC number prediction in MGYG000004129_00932.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	104	292	2.9e-48	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.73e-81	103	302	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	4.99e-40	103	300	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	1.56e-38	104	292	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	6.48e-37	103	299	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	5.01e-32	100	299	2	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQR31702.1	2.16e-97	54	305	49	299
ANU54365.1	2.16e-97	54	305	49	299
ASB42415.1	2.16e-97	54	305	49	299
QNO18615.1	7.37e-88	50	305	45	299
QKN23542.1	9.62e-72	59	305	61	308

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A6S_A	3.68e-11	105	305	26	205	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
1JFX_A	1.22e-09	97	299	1	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
P34020	2.09e-20	103	299	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
P26836	2.76e-15	103	299	11	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
Q8X7H0	1.47e-11	101	300	67	253	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P25310	1.32e-08	97	299	78	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
0.993146	0.006136	0.000049	0.000033	0.000022	0.000644

TMHMM  Annotations     

start	end
13	35