CAZyme Information: MGYG000001097_00524

Basic Information

• Species: Prevotella pectinovora
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella pectinovora
• CAZyme ID: MGYG000001097_00524
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
398		44892.96	10.0326

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001097	3372203	MAG	China	Asia

• Gene Location: Start: 1774; End: 2970 Strand: -

Full Sequence      

MKISHLIIYALTALAIISCKDGKPIDTVTVYHGDYCYRGEMAHGKRNGYGVLSLKDSIVY
SGMWKDGKRCGYGTTTDSLGRRITALWHADTIVSGTREDSLGIYHGGFSEDLLADGHGTW
RNADGEFYTGQWTADRRNGFGCGVAENGKVKAGDWRKDRYRGEKMVHTADRIYGIDVSRY
QHEKGKKKFHLDWTKVRVIGLGSGRRSAGDINYRISFAYIKSTEGVTVRNRYFASDYVNA
KKRGIAVGAYHFFSTRSSAAAQAHFFLRHTALRVGDMPPVLDVEPSDAQIKQMGGPEVMF
RAIRTWLNIVRNATGTKPVLYVSQNFVNRYLSAAPDIKGNYPVWIARYGQYRPDVRLAFW
QLTPYGKVRGIQGDVDVNVFNGYKEQFAEFLHKETIKK

Enzyme Prediction     

No EC number prediction in MGYG000001097_00524.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	175	371	2.1e-41	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06524	GH25_YegX-like	1.31e-54	173	382	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.
cd06413	GH25_muramidase_1	8.25e-48	172	382	3	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.
cd00599	GH25_muramidase	2.67e-45	173	380	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.
COG3757	Acm	2.38e-36	158	391	51	264	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
cd06412	GH25_CH-type	3.91e-33	174	387	3	199	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
AGB29361.1	1.31e-147	11	391	27	407
ALO48884.1	1.32e-147	29	396	33	402
VEH15425.1	3.55e-124	39	393	21	377
BCS86499.1	1.58e-122	41	396	1	357
QVJ81333.1	7.34e-120	62	397	99	438

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	4.96e-23	172	394	16	220	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
1JFX_A	2.31e-22	172	382	5	204	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRU_A	1.56e-18	172	380	20	207	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	9.01e-18	172	380	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	2.47e-09	217	361	28	177	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	2.05e-34	172	395	67	271	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8X7H0	2.05e-34	172	395	67	271	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
Q8FFY2	5.54e-34	172	395	67	271	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P25310	1.58e-21	163	382	71	281	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000507	0.949608	0.049314	0.000199	0.000178	0.000179

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001097_00524.