CAZyme Information: MGYG000003005_00830

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus
• CAZyme ID: MGYG000003005_00830
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
394	MGYG000003005_43|CGC1	44013.56	7.5854

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003005	2620760	MAG	United States	North America

• Gene Location: Start: 5795; End: 6979 Strand: +

Full Sequence      

MIKKYEFGDKSQLSPHFNVQEFKCKCGKKHEILIAEELIEKLEKLYSSLNCSKIIVTSGY
RCTNHDKNVGGIGTGQHTKGNAADICCYGQDGQPISSKTVCCKAQDIGFTGIANINEKYI
YTHVDVRTGSKWYGDETKGNSTVTSDFYSYFGFSKSNEPLMKGIDVSVHNGNIDWQKVKN
AGIQFAILRAGYGRELSQKDTRFEENYRNAKAAGIPVGAYWYSYAITPEEAQLEADVFLK
VIKGKQFEMPVYFDLEEKNQFDLGKEKVSAIMRAFLEKIEKAGYFVGLYGSASSLTTHTA
DGIKSRYTIWLAHWTNQTNYSGDYGIWQYSSEGKVNGISGNLDMDICYNDFPTIIKNKAM
NGFGKDTTPEPDTTSANVTVKIGNETYKGNLSKV

Enzyme Prediction     

No EC number prediction in MGYG000003005_00830.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	164	338	7.4e-50	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.13e-89	161	348	1	191	The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes.
cd00599	GH25_muramidase	1.54e-48	162	346	1	185	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	1.92e-34	162	345	1	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.
pfam01183	Glyco_hydro_25	3.60e-34	164	338	1	180	Glycosyl hydrolases family 25.
cd06524	GH25_YegX-like	3.61e-32	162	346	1	191	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QLI94930.1	8.88e-77	160	371	3	214
ADU27377.1	2.06e-76	161	389	3	229
AVQ96437.1	2.06e-76	161	389	3	229
QCN92678.1	2.06e-76	161	389	3	229
AYF41921.1	2.06e-76	161	389	3	229

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JFX_A	1.47e-17	161	343	5	198	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRU_A	8.79e-17	161	345	20	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	4.34e-16	161	345	20	205	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	2.68e-15	160	356	21	210	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
2WAG_A	3.65e-14	161	348	16	207	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P34020	1.61e-16	161	345	1	178	Autolytic lysozyme OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=lyc PE=1 SV=1
P25310	2.81e-16	161	343	82	275	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836	1.05e-13	157	345	5	194	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 OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000077	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003005_00830.