CAZyme Information: MGYG000000250_01000

Basic Information

• Species: TF01-11 sp001414325
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; TF01-11; TF01-11 sp001414325
• CAZyme ID: MGYG000000250_01000
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
317	MGYG000000250_2|CGC3	35020.23	9.2071

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000250	3613289	Isolate	China	Asia

• Gene Location: Start: 290724; End: 291677 Strand: +

Full Sequence      

MSQKFGIDVSHWQGSFDFARAKSKEGVEFAIIKAGGADAGLYKDSQFEANYKKCEKCGLP
KGAYFYGNARSVADAKKEAEYFLSLIKGKRYEYPVFYDVEGSMITKNDRNTLTQIVKAFC
SAIEAAGYWVGIYSSESFFNSEMNDGELTRYSHWVARWGKNKPAPASGAETQIWQFGGET
NLIRSNKINGQSCDQDYCYVDFPAKIKAAGLNGYAKGGSSTSAPVKKSNEEIASEVIAGK
WGNGAERQKLLSQAGYDYSAIQGIVNKKLSPSRKSVDEIAREVIHGDWGNGSDRKKRITS
AGYDYSAVQKRVNELLK

Enzyme Prediction     

No EC number prediction in MGYG000000250_01000.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	7	178	1.1e-43	0.9548022598870056

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	3.21e-75	4	199	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	3.14e-34	6	179	2	171	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	1.01e-26	7	176	1	171	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	8.79e-25	6	197	2	183	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.
cd06524	GH25_YegX-like	6.22e-22	5	176	1	174	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QHB22110.1	2.38e-191	1	270	1	269
QEI32774.1	2.38e-191	1	270	1	269
ACR75820.1	2.04e-82	1	266	1	263
ARP51107.1	1.23e-75	6	269	5	264
ARP49658.1	1.56e-67	6	269	5	262

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JFX_A	2.38e-17	6	192	7	206	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRU_A	4.57e-12	6	163	22	175	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	1.31e-11	6	163	22	175	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]
3HMC_A	1.28e-09	7	176	8	162	Endolysinfrom Bacillus anthracis [Bacillus anthracis]
4CVD_A	2.64e-06	232	270	4	42	ChainA, LYSOZYME [Streptococcus phage CP-7]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25310	4.27e-16	6	192	84	283	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836	4.66e-12	6	174	11	170	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P19385	1.31e-09	7	267	9	243	Lysozyme OS=Streptococcus phage Cp-7 OX=10748 GN=CPL7 PE=1 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
1.000072	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000250_01000.