CAZyme Information: MGYG000002747_00341

Basic Information

• Species: Collinsella sp900543025
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; Collinsella sp900543025
• CAZyme ID: MGYG000002747_00341
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
352	MGYG000002747_4|CGC1	38209.73	7.5313

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002747	2025294	MAG	Netherlands	Europe

• Gene Location: Start: 3914; End: 4972 Strand: +

Full Sequence      

MSMNGIDISNWQNGINLDVVPYDFIIAKATQGKTYVSPDCARQVEQARARGKLFGVYHYI
DGSGAIGEADFFIDNIKNWVGEGMLCLDWESNQNSAWGNEDYLRQVAQRVIDRTGIPPVI
YVQQSRMAQVKPIADALNCALWIAQYANMNATGYQDAPWNEGAYSCAIRQYSSCGRLSGY
SGNLDLNKAYMDAAAWKKYANPSGGASAPSPAPSKPSASAPSGSTLDLVYHIVTNDINGD
ARRDYCGSRYDDVQGFINDTHDASASTLAKWIRAGKYGNNPVRQTVIEACGGKYREAQDI
INGKGKQTTYVVKSGDTLSGIAAKFGTTYQAIAAKNGISNPNLIYPGQVLKI

Enzyme Prediction     

No EC number prediction in MGYG000002747_00341.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	6	179	3.2e-36	0.9887005649717514
CBM50	310	352	2.1e-16	0.95

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06417	GH25_LysA-like	4.15e-82	3	196	1	195	LysA is a cell wall endolysin produced by Lactobacillus fermentum, which degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. The N-terminal glycosyl hydrolase family 25 (GH25) domain of LysA has sequence similarity with other murein hydrolase catalytic domains while the C-terminal domain has sequence similarity with putative bacterial cell wall-binding SH3b domains. This domain family also includes LysL of Lactococcus lactis.
cd00599	GH25_muramidase	7.53e-36	5	189	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.
cd06525	GH25_Lyc-like	3.45e-25	4	188	1	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.
pfam01183	Glyco_hydro_25	4.41e-25	6	179	1	179	Glycosyl hydrolases family 25.
cd06413	GH25_muramidase_1	2.91e-19	5	190	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRT50187.1	1.46e-99	1	352	1	395
QRT50341.1	1.70e-91	1	352	1	345
QHJ76374.1	1.26e-87	3	350	1	374
CBK80688.1	1.18e-84	1	352	1	361
QHJ82694.1	1.70e-84	3	350	1	372

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JFX_A	1.96e-10	3	201	5	214	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
P25310	2.35e-09	3	201	82	291	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836	4.14e-09	2	188	8	195	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
Q49UX4	5.44e-06	308	352	86	129	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 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
1.000059	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002747_00341.