CAZyme Information: MGYG000000014_01877

Basic Information

• Species: Clostridium butyricum
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium butyricum
• CAZyme ID: MGYG000000014_01877
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
260	MGYG000000014_6|CGC3	29918.72	4.6892

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000014	4564499	Isolate	United Kingdom	Europe

• Gene Location: Start: 159708; End: 160490 Strand: +

Full Sequence      

MTCSYDIIVLKIKGGWDLLWFSLFNASKKYYITIFIVISLIVSFSAFNMITIDRNVQASY
INSRVKGINISNNDGNLDLSSVTQAGGKYVYLKATEGATFRDSYMDTYYNQCKDLGMKIG
VYHYLVNTSSPEEQAENFYNTISKYNWDLIPMLDTEVYFDGLEDYIKRFKVAFNKLSPLK
LGIYSYTSFIDKYLNNADSEIYEMPLWEANYNGKPWSSVGDNKFTNLVGHQYSTEKHISD
YIGDFNGDLNEFNEGCLINQ

Enzyme Prediction     

No EC number prediction in MGYG000000014_01877.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	68	238	9.1e-37	0.9774011299435028

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06525	GH25_Lyc-like	1.41e-82	66	252	1	184	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.
cd00599	GH25_muramidase	9.90e-37	66	252	1	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.
pfam01183	Glyco_hydro_25	6.05e-28	68	233	1	172	Glycosyl hydrolases family 25.
cd06524	GH25_YegX-like	7.70e-28	66	253	1	193	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.
COG3757	Acm	9.94e-24	65	255	63	256	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QJU45029.1	1.68e-177	18	260	1	243
QCJ03493.1	1.68e-177	18	260	1	243
QCJ07194.1	1.68e-177	18	260	1	243
ALS17706.1	1.68e-177	18	260	1	243
AOR94895.1	1.68e-177	18	260	1	243

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	8.40e-23	65	260	20	215	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	6.09e-22	65	260	20	215	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	3.38e-14	65	243	16	196	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
1JFX_A	1.09e-09	63	253	3	203	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
5A6S_A	5.09e-09	70	211	27	165	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	8.97e-28	65	258	1	186	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	1.16e-22	63	257	7	201	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	1.13e-08	63	253	80	280	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
1.000032	0.000015	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
30	52