CAZyme Information: MGYG000000289_01465

Basic Information

• Species: Prevotella buccae
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella buccae
• CAZyme ID: MGYG000000289_01465
• CAZy Family: GH25
• CAZyme Description: Lysozyme M1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
230	MGYG000000289_21|CGC1	27139.03	8.4166

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000289	3001000	MAG	Sweden	Europe

• Gene Location: Start: 24900; End: 25592 Strand: -

Full Sequence      

MKKLLFFILYLFTATSLMAQVECEDTCSHIHGIDLSHYQGTVFWEAIGDNSKMAYVYLKA
TEGGNNIDSRYKENIDLAHKYGLKVGSYHFYRPKVEQEVQLRNFMTQCRPGDQDLIPMID
IETKSGLPTEEFCDSLFKFLRLVEKVYKQKPLIYTGTNFYNSYLSGKLDAYRLMIAQYTR
REPVLNDGRDFEMWQYTGKGHLNGINGYVDKSRFMRDHRLKEIRFRHRQD

Enzyme Prediction     

No EC number prediction in MGYG000000289_01465.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	33	205	2.2e-44	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06524	GH25_YegX-like	7.04e-54	31	214	1	192	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	1.93e-53	30	214	3	189	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	1.16e-48	31	214	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	4.08e-44	32	214	2	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	1.38e-39	30	210	63	249	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
QNT65928.1	3.40e-136	1	228	1	228
ALO48398.1	1.91e-129	1	228	1	231
AGB29159.1	7.77e-123	1	228	1	235
EFC71701.2	2.07e-122	1	227	1	230
VEH15347.1	6.67e-121	12	227	15	232

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	6.02e-25	30	214	16	206	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
4KRU_A	8.10e-23	29	214	19	207	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	5.70e-22	29	214	19	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]
5A6S_A	2.61e-21	28	224	19	210	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
1JFX_A	1.96e-18	28	214	3	202	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
P76421	7.40e-34	30	210	67	250	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8FFY2	1.04e-33	30	210	67	250	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	1.46e-33	30	210	67	250	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P26836	2.85e-27	28	214	7	196	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	3.54e-17	28	214	80	279	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
0.000278	0.999039	0.000203	0.000148	0.000141	0.000144

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000289_01465.