CAZyme Information: MGYG000000240_02311

Basic Information

• Species: Amedibacterium intestinale
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; Amedibacterium; Amedibacterium intestinale
• CAZyme ID: MGYG000000240_02311
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
344		38734.21	9.3819

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000240	2625986	Isolate	China	Asia

• Gene Location: Start: 381; End: 1415 Strand: -

Full Sequence      

MTLKFIDVASYQAGLDLSKIQTDGVVIKATEGTGYVNPYCDGFFQQGLKLGKVLGVYHFA
RNTSGNTPEKEAEYFIQHTKGYIGKAIPILDWEDKDAGDVGWAYQWLQIVEKAYGCKPWI
YMSEYIENSFNWKKVADAGYGLWIAKYRDNVVDKNWDMKDAGPIPSVKYWEFYAAWQWTS
SLVLDGWNGKLDGNIFYGNKDAWKKYVGKENQIKPQPPKPDNLKYKVNDSVNINGIYVSK
DSKEKLKPAISYGTITKIYPTSRNPYLIGNGTGFVNDECITGIHSSKVLKVGIKATPIKP
ISYDGVKLNSSVTKKSYKVIEIKGKRVVLGDGLNTAFHIDNLSY

Enzyme Prediction     

No EC number prediction in MGYG000000240_02311.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	6	186	4.5e-37	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06417	GH25_LysA-like	1.05e-52	3	203	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	1.04e-34	6	187	1	180	Glycosyl hydrolases family 25.
cd00599	GH25_muramidase	1.26e-32	4	196	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.
cd06525	GH25_Lyc-like	3.39e-22	4	196	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.
cd06412	GH25_CH-type	9.44e-19	6	193	4	198	CH-type (Chalaropsis-type) lysozymes represent one of four functionally-defined classes of peptidoglycan hydrolases (also referred to as endo-N-acetylmuramidases) that cleave bacterial cell wall peptidoglycans. CH-type lysozymes exhibit both lysozyme (acetylmuramidase) and diacetylmuramidase activity. The first member of this family to be described was a muramidase from the fungus Chalaropsis. However, a majority of the CH-type lysozymes are found in bacteriophages and Gram-positive bacteria such as Streptomyces and Clostridium. CH-type lysozymes have a single glycosyl hydrolase family 25 (GH25) domain with an unusual beta/alpha-barrel fold in which the last strand of the barrel is antiparallel to strands beta7 and beta1. Most CH-type lysozymes appear to lack the cell wall-binding domain found in other GH25 muramidases.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBK23905.1	4.97e-227	1	344	1	342
BBK61131.1	7.86e-221	1	344	1	339
BBK23875.1	3.65e-68	1	344	1	346
AAR59481.1	4.43e-63	1	237	5	244
QRG96708.1	3.39e-62	1	237	4	243

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	1.22e-13	3	210	16	220	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
6ZMV_A	7.47e-10	7	192	6	198	ChainA, muramidase [Trichobolus zukalii],6ZMV_B Chain B, muramidase [Trichobolus zukalii]
4KRT_A	2.43e-08	3	291	20	322	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]
4KRU_A	3.97e-07	3	196	20	207	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P76421	1.39e-09	2	207	66	265	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8X7H0	1.39e-09	2	207	66	265	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
Q8FFY2	3.41e-09	2	207	66	265	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P00721	1.63e-07	2	195	1	202	N,O-diacetylmuramidase OS=Chalaropsis sp. OX=36534 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
1.000056	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000240_02311.