CAZyme Information: MGYG000002925_01164

Basic Information

• Species: CAG-877 sp900548695
• Lineage: Bacteria; Firmicutes; Bacilli; RF39; UBA660; CAG-877; CAG-877 sp900548695
• CAZyme ID: MGYG000002925_01164
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
314		35240.44	7.1389

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002925	1410926	MAG	United States	North America

• Gene Location: Start: 22422; End: 23366 Strand: +

Full Sequence      

MLKGIDISHHQNGINIANLDVDFVICKATEGVGYVDECCDKFYQQAKKAGKKLGVYHFAR
PDLGNSAEAEANWFIKNIKGYINEAILILDWESGNLNNPNWVKAFCDKVKNETGVKPIVY
MSASPANSFDWSPVVKGDYGLWIASYGSNNGQANKAPVSSKWPFYCMWQYTSRGRINGYN
GNLDLNYFYGTKEAWDKYANGSAPAQDSKADQVLYPGSKVQFYGCQIDDIKTVGDKTTFY
SDNYGVWLPITSWYRVGEKGERYINQISSKGNWLMNDSIYTVKSVSKNPDRAVINVEGKD
YNVLSSSLYEVSNS

Enzyme Prediction     

No EC number prediction in MGYG000002925_01164.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	5	178	1.4e-49	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06417	GH25_LysA-like	6.18e-66	2	195	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	1.01e-47	3	188	1	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	3.19e-42	5	178	1	179	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	5.06e-41	3	188	1	184	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.
COG3757	Acm	4.37e-35	3	204	64	269	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AQY30476.1	1.42e-66	1	242	1	240
QWW15615.1	1.34e-65	2	233	6	239
CAD7757511.1	1.60e-65	1	242	1	240
AAR59481.1	3.88e-65	2	233	7	240
QCT71926.1	5.97e-65	1	201	1	204

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JFX_A	6.93e-21	2	203	5	217	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
2WAG_A	2.72e-20	2	198	16	216	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
4JZ5_A	2.03e-19	1	186	22	210	High-resolutionstructure of catalytic domain of endolysin ply40 from bacteriophage P40 of Listeria monocytogenes [Listeria phage P40]
5A6S_A	8.31e-18	1	269	21	272	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
5JIP_A	2.80e-11	4	264	16	290	Crystalstructure of the Clostridium perfringens spore cortex lytic enzyme SleM [Clostridium perfringens],5JIP_B Crystal structure of the Clostridium perfringens spore cortex lytic enzyme SleM [Clostridium perfringens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25310	1.50e-19	2	203	82	294	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
Q8X7H0	2.48e-14	2	201	67	267	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P76421	3.39e-14	2	201	67	267	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	4.62e-14	2	201	67	267	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P34020	5.76e-14	2	188	1	180	Autolytic lysozyme OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=lyc PE=1 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
1.000053	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002925_01164.