CAZyme Information: MGYG000000417_02487

Basic Information

• Species: Acetatifactor sp900755865
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Acetatifactor; Acetatifactor sp900755865
• CAZyme ID: MGYG000000417_02487
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
364	MGYG000000417_57|CGC1	41196.45	4.3362

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000417	2910146	MAG	Sweden	Europe

• Gene Location: Start: 5737; End: 6831 Strand: -

Full Sequence      

MRLPDDYEEHSSMTPMMVMSIVLVTLLVGVILVVVLLMNNKTRTPVQNTQQSQSFSSPVI
EREKSQTDLAGGDKLTPDDLDFWDMYPPKESATPLPEESVEKEPEKTTDPATDGKHTRVT
YSNGEEEWVLISPYLPKNEYDFTKLVCQSDVMKYYVDGKQASYSGVDISKLQDYVDFGKV
KKAGIDFVMLRVGARGYGTGQLILDDYFSDNLKRATDAGLNVGAYFFSQAITKEEAVEEA
NMVLQNLGEYKISYPIAFDMEKIENDKARTDSLSRGEKTEIAKAFMDTISAAGYKTILYG
NKEWLLKQIDMSKLTAYDVWYAEQSDIPDYPYQFTMWQYSTVGTVDGIAGYVNRNISFID
YSEK

Enzyme Prediction     

No EC number prediction in MGYG000000417_02487.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	166	348	2.5e-42	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	2.70e-73	165	358	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	2.73e-32	165	356	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.
pfam01183	Glyco_hydro_25	3.15e-24	166	348	1	180	Glycosyl hydrolases family 25.
cd06413	GH25_muramidase_1	1.06e-21	165	355	5	187	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	1.13e-17	165	355	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
QNM01196.1	1.18e-156	1	364	1	373
QEK18217.1	1.00e-64	135	358	73	298
QCT06482.1	4.78e-64	120	361	76	319
BBF45127.1	2.37e-63	137	361	54	280
QRO38911.1	5.03e-62	135	361	60	288

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JFX_A	4.19e-06	165	355	7	200	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
P76421	7.37e-08	161	356	63	253	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8X7H0	9.89e-08	161	356	63	253	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
Q8FFY2	1.33e-07	161	356	63	253	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX 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
1.000084	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
15	37