CAZyme Information: MGYG000002763_01721

Basic Information

• Species: Collinsella aerofaciens_J
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; Collinsella aerofaciens_J
• CAZyme ID: MGYG000002763_01721
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
342		37225.41	4.4832

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002763	2048046	MAG	Netherlands	Europe

• Gene Location: Start: 515; End: 1543 Strand: -

Full Sequence      

MNGIDISNWQNGINLAAVPFDFVICKATEGTHYVSPDCDRQIQQAIGLGKLVGVYHYVNG
GNAEAEAEYFYEHCKGYVGKAAFFIDWEDKGNKAWGDTSYLKAMAERLAELLGVSMDRIG
IYASKSVFPWNLTTAKTWVAQYADMKPTGYQDAPWNEGAYDCAIRQYSSCGRLDGWAGNL
DINKCYISRAEWEAMAGGSNGDPDSLIHGIDETPAADLAAKVLAGEFGDGDDRKHALGDR
YQEVQSLVNHILTASAEDLAAETWAGDYGNGSRRKAVLGPRYDEVMAVINGQAETEQVYV
VQSGDTLSGIASKYGTTYQDLAAKNGISNPNLIYPGMRLVVS

Enzyme Prediction     

No EC number prediction in MGYG000002763_01721.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	4	175	2.9e-33	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06417	GH25_LysA-like	1.38e-69	1	192	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.
pfam01183	Glyco_hydro_25	1.18e-26	4	176	1	180	Glycosyl hydrolases family 25.
cd00599	GH25_muramidase	1.35e-25	3	184	2	185	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	4.52e-25	2	184	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.
cd06414	GH25_LytC-like	2.35e-19	1	186	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRT50341.1	3.23e-86	1	339	3	343
QRT50187.1	8.37e-82	1	341	3	395
CBK80688.1	1.56e-73	1	341	3	361
QHJ76374.1	5.80e-71	1	336	1	263
QHJ82694.1	2.42e-69	1	334	1	315

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JFX_A	4.01e-11	1	196	5	213	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	4.99e-10	1	196	82	290	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
Q49UX4	2.68e-09	295	342	84	130	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
P26836	2.22e-08	1	184	9	195	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
Q8CMN2	1.20e-06	298	342	85	128	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=sle1 PE=3 SV=1
Q5HRU2	1.20e-06	298	342	85	128	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 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
1.000046	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002763_01721.