CAZyme Information: MGYG000001265_01088

Basic Information

• Species: Methylobacterium sp002778835
• Lineage: Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Beijerinckiaceae; Methylobacterium; Methylobacterium sp002778835
• CAZyme ID: MGYG000001265_01088
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
282		31445.7	9.4076

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001265	4213059	MAG	Italy	Europe

• Gene Location: Start: 3332; End: 4180 Strand: +

Full Sequence      

MSQTHARHAPARTFGALARKLAAAALLAGLAACASNNDFYPTKGDVKPHPGVAKAKRHPI
HGIDISKWQGPIDWASVRGAGTQFAFIKATEGGDHVDERFRENWDGAARAGVPRGAYHFV
FWCRSAREQVEWFKRNVPADPSALPPVLDVEWNGHSQKCPKRLPKAEALAMMRVMLAEME
AYTGKRPIIYTDITFHKDVLEGELPDYPHWLRSTAAEPEQRFANRQWMLWQFTSTGRVPG
VRGDVDRNAFYGTQAEWASFLATDCDPRVHGVLSRQGLCTGK

Enzyme Prediction     

No EC number prediction in MGYG000001265_01088.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	63	241	5.9e-52	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06413	GH25_muramidase_1	7.97e-111	59	252	2	191	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.
COG3757	Acm	1.99e-73	40	262	41	265	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
cd00599	GH25_muramidase	3.64e-58	61	250	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.
cd06524	GH25_YegX-like	7.45e-57	61	252	1	194	YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) catalytic domain that is similar in sequence to the CH-type (Chalaropsis-type) lysozymes of the GH25 family of endolysins.
pfam01183	Glyco_hydro_25	2.56e-49	63	241	1	180	Glycosyl hydrolases family 25.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AWN38180.1	9.41e-182	17	282	22	287
APT34108.1	2.86e-180	17	282	29	294
AWV14603.1	2.86e-180	17	282	29	294
AIQ93851.1	2.86e-180	17	282	29	294
ACB27463.1	5.77e-180	17	282	29	294

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	1.87e-40	49	264	5	220	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
1JFX_A	2.94e-34	60	255	5	207	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRU_A	3.56e-23	60	250	20	207	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	2.71e-22	60	250	20	207	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]
2X8R_A	1.60e-15	60	191	4	138	Thestructure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_B The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_C The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_D The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_E The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_F The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P76421	1.08e-34	58	261	65	265	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	1.08e-34	37	261	33	265	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	1.08e-34	58	261	65	265	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P25310	7.30e-33	52	255	74	284	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836	8.32e-20	60	250	9	196	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000526	0.031535	0.967851	0.000072	0.000018	0.000005

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001265_01088.