CAZyme Information: MGYG000000189_00311

Basic Information

• Species: Coprococcus sp900066115
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Coprococcus; Coprococcus sp900066115
• CAZyme ID: MGYG000000189_00311
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
323		36639.17	4.4313

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000189	2889110	Isolate	China	Asia

• Gene Location: Start: 349998; End: 350969 Strand: -

Full Sequence      

MREADRRKQLAKRMKYAVCIGTGIVIGIIAGICIGIDYNKTTRSTPALYTEMEHGLELTP
GELANLIYDNYWNYIKKSYIIVGDDKETAQLYKISSKVARHNYDLERFQLDDNGYMSYSD
DKIKHAKLGIDVSSHQGSIDWETVKEAGIKFAMIRLGYRGYTQGGLALDDSYVTNIETAL
EAEMPVGVYFYTQAVSYDEGVEEAQYVLQNIADYKISYPVVIDTEKMEAEGARANDISNE
ERTDAIVGFCETIKDAGYTPMIYANRNWYAQNLDMDRLGDYQLWLAQYSNVPDFPYLFTG
WQYTSEGSVPGISGSVDIDVWMK

Enzyme Prediction     

No EC number prediction in MGYG000000189_00311.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	130	312	7e-49	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.12e-88	127	322	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	4.62e-43	129	321	2	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.
cd06413	GH25_muramidase_1	1.97e-33	129	320	5	188	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	1.19e-32	130	312	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	3.03e-29	129	319	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBK83179.1	2.04e-117	17	323	19	321
QWT52701.1	1.83e-102	5	322	3	323
QNL99368.1	4.03e-99	40	323	39	325
CBL26148.1	9.13e-68	12	323	4	303
QHI72152.1	2.54e-67	85	320	52	286

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	3.34e-14	129	319	22	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
2WAG_A	1.01e-13	129	321	18	206	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
4KRT_A	1.19e-13	129	319	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	6.50e-11	129	317	7	198	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
1OBA_A	8.66e-07	123	305	2	178	ChainA, Lysozyme [Streptococcus phage Cp1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P34020	2.89e-17	129	319	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	7.83e-10	129	317	84	275	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836	1.38e-09	129	319	11	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
Q8X7H0	7.22e-09	129	321	69	254	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P19386	8.36e-07	123	305	2	178	Lysozyme OS=Streptococcus phage Cp-9 OX=10749 GN=CPL9 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
0.998279	0.001469	0.000054	0.000012	0.000006	0.000204

TMHMM  Annotations     

start	end
16	38