CAZyme Information: MGYG000000356_00868

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; VUNI01
• CAZyme ID: MGYG000000356_00868
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
491	MGYG000000356_6|CGC2	53324.74	4.0232

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000356	2991584	MAG	Sweden	Europe

• Gene Location: Start: 68680; End: 70155 Strand: +

Full Sequence      

MKKDRFDSLDDSTYGSRNIIRIIIAVVIIALVGAMLLAGFWMQKKKDQMGSVGELDTEQD
TKQQDTDDPETGSMGQETGAQVDASAILTASSAAENDQITLGIDVAKYQGTIDWSKVAAS
GIDFAMIRVGYRTQKTGEMCVDTNAKYNMQEAQANGIKIGVYFFSSAITEAEAKEEADWV
ADYISQYQITYPVAFDCEGFQDADSRQSGLDREKRTGLAAAFMDEIYQKGYTPMFYAASG
ELQDGADWNLDIIQNSYKIWVAQYPEVPYPDTASSSYTGTHAMWQYTNQGTIPGIGTTVD
LNVAYFGYDETAQAKDGAAPDAASADPEANMKFQDVSESVTAKESANLRNIPSQDTDSTV
ELTLNNGDVATRTGISESGWSRLLYNGATYYAVSSYLTTDLNYVAAGQEGSGSGDGLKTK
FTDCNDVVTAKIEVNLRTIPSVTNPDAVVAAVLTNGETVTRTGINEEFGWSRVDYNGQTL
YCISSYLTTAQ

Enzyme Prediction     

No EC number prediction in MGYG000000356_00868.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	103	295	6e-44	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.95e-68	102	305	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	6.16e-32	102	304	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.
pfam01183	Glyco_hydro_25	4.26e-28	103	295	1	180	Glycosyl hydrolases family 25.
cd06413	GH25_muramidase_1	6.57e-23	102	305	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.
cd06525	GH25_Lyc-like	7.86e-21	102	302	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
CBK93417.1	6.16e-219	17	488	5	482
ACR77025.1	7.13e-218	17	488	5	482
CBK89713.1	8.25e-217	17	488	5	482
ACR73526.1	8.37e-171	47	488	63	505
CBK74296.1	6.68e-161	58	491	77	522

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	7.19e-10	102	302	22	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	2.06e-09	102	302	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]
2WAG_A	2.85e-09	102	310	18	212	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
3HMC_A	3.87e-08	103	302	8	177	Endolysinfrom Bacillus anthracis [Bacillus anthracis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	5.97e-10	102	302	11	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2

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	0.000025	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
20	42