CAZyme Information: MGYG000003129_00886

Basic Information

• Species: Anaerococcus octavius
• Lineage: Bacteria; Firmicutes_A; Clostridia; Tissierellales; Peptoniphilaceae; Anaerococcus; Anaerococcus octavius
• CAZyme ID: MGYG000003129_00886
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
369	MGYG000003129_7|CGC1	42468.68	4.858

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003129	1715963	MAG	United States	North America

• Gene Location: Start: 93733; End: 94842 Strand: -

Full Sequence      

MDSFKIKWAGMGVALVVLFAKPVYAADVIKYDDSNLDQIFEENNIYYDKEAVEKRKSEFI
SDLNNAIAPDYEVEDVIISEELNVDDDGDVEKTVTKETSLIDKNPAPIYSKSPVYKKVVD
ISEHQDPDKIDYNEFANDIDGAILRTSITPADDLQIRKDYQIERHYKELNKRNVPVGFYH
YSRAINAAEALLEADYVYNIIKDKNVSLPVYIDIEDNKRQAKASIGEISEVAETFVKSMQ
AHGYVSGIYSYPWFANKYLTRDVKNKYNFWIADYDSKEFTKYNKSDFDSWQYTNKGKVNG
YSGNIDMSVLYKDYPYIIRGVSKKPINVLIDEILAGKWGVGSERQRRLAYAGYNYNIVQK
AVNQRLANL

Enzyme Prediction     

No EC number prediction in MGYG000003129_00886.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	119	300	8e-39	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	7.91e-47	116	311	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	7.13e-26	117	309	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	1.30e-23	117	307	1	181	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.
cd06523	GH25_PlyB-like	7.47e-21	117	308	1	175	PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) 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	8.93e-19	119	300	1	179	Glycosyl hydrolases family 25.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACV28608.1	7.90e-112	7	366	6	359
AZP03752.1	1.55e-50	119	368	6	267
QBE96747.1	4.30e-50	117	368	4	267
QBX31317.1	4.30e-50	117	368	4	267
AMC93674.1	6.04e-50	117	368	4	267

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	2.85e-13	116	311	269	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae at 1.6 A resolution [Streptococcus pneumoniae R6],2WWD_A 3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment [Streptococcus pneumoniae R6]
2WWC_A	6.80e-13	116	311	269	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
4FF5_A	9.38e-13	116	310	52	249	Structurebasis of a novel virulence factor GHIP a glycosyl hydrolase 25 of Streptococcus pneumoniae participating in host cell invasion [Streptococcus pneumoniae]
4JZ5_A	7.01e-08	118	320	25	222	High-resolutionstructure of catalytic domain of endolysin ply40 from bacteriophage P40 of Listeria monocytogenes [Listeria phage P40]
5A6S_A	3.01e-06	159	320	59	211	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P19385	3.52e-06	175	364	55	243	Lysozyme OS=Streptococcus phage Cp-7 OX=10748 GN=CPL7 PE=1 SV=2

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
0.000535	0.998751	0.000227	0.000157	0.000157	0.000154

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003129_00886.