CAZyme Information: MGYG000003731_00644

Basic Information

• Species: Prevotella amnii
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella amnii
• CAZyme ID: MGYG000003731_00644
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
255	MGYG000003731_18|CGC1	30218.83	10.3949

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003731	1790835	MAG	Canada	North America

• Gene Location: Start: 17184; End: 17951 Strand: -

Full Sequence      

MKRKKKKNSIRTTSIIAFWIAITALLFIISKKTWQQYSYPTKSSSWPFKDLTSGEYATCF
DGIDISRHQGKIHWQEIKDNTSLTFVYVKATEGSSIKDPYYNENIRQARRQGLKVGSYHF
LTSYTTMKRQATLFLNTIDTQWQDLLPMVDIEEDGTKQWKRKTIQKNLAKFISIIKKKTG
KAPIIYTSEKYYLKNLYPEFNKYHLFIANYTKEPSLKDAQYDIWQSSKHARVHGVWNWTD
INHLRKGITLKKIYW

Enzyme Prediction     

No EC number prediction in MGYG000003731_00644.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	63	235	1.5e-48	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06413	GH25_muramidase_1	2.82e-44	62	242	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.
cd06524	GH25_YegX-like	1.12e-43	62	235	2	183	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.
cd00599	GH25_muramidase	2.10e-43	62	242	2	184	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	7.82e-41	62	242	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.
COG3757	Acm	3.32e-35	62	242	65	251	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
AXV48472.1	3.96e-95	1	250	2	254
QUB88840.1	1.21e-94	24	250	30	256
QUI94578.1	1.66e-94	24	250	29	255
QUB93449.1	2.43e-94	24	250	30	256
AEA21016.1	3.15e-94	24	250	59	285

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	1.56e-24	62	234	18	193	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
4KRU_A	2.97e-19	62	248	22	211	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	1.58e-18	62	248	22	211	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]
5A6S_A	1.72e-10	64	244	26	201	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
1JFX_A	1.92e-09	62	120	7	64	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
Q8FFY2	4.82e-31	62	242	69	252	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P76421	9.48e-31	62	242	69	252	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8X7H0	1.86e-30	62	242	69	252	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P26836	1.24e-19	54	248	3	200	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	1.94e-08	62	120	84	141	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm 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
0.980345	0.019159	0.000165	0.000053	0.000038	0.000262

TMHMM  Annotations     

start	end
13	30