CAZyme Information: MGYG000003452_01581

Basic Information

• Species: Bifidobacterium ruminantium
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium ruminantium
• CAZyme ID: MGYG000003452_01581
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
414	MGYG000003452_16|CGC2	45087.59	9.7309

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003452	2217592	MAG	Fiji	Oceania

• Gene Location: Start: 78818; End: 80062 Strand: +

Full Sequence      

MRKHKPPWLKRFRLAVTGVVMAITMAVAPAAMADLNGYDVSGYQAPDITQVAPADFAIVK
VNQGWYINSSWGQQASGAVNTGKELGLYDYASGMDATTEADNFVNHITGYVGKAMLVLDW
EPYQNAAWGNSNWVRTWVYRVHARTGVWPVVYCSKGFVGQIPADVRAKCMLWAAQYANNY
ATGYQDSPWLAGSQGEGMLQYTSTGYLNGRGPLDLDKFFGDRTAWRKIACGERAGCSTTG
GSTGTPTIHVEKRTTNTTDLNAMATAVIRGDYGNGADRQARLGDNYQAVMNIVNSRLSSS
AYSGPTTVTRTKTRTYVVRSGDTVSAIAERTGLKPASAWRVPSGNINRIYVGQTITYYGS
STVSTPSTTYYGSSTHVVSSGESLWKIYGAGWYAAAQRNGLRPPYTIYPGQRLR

Enzyme Prediction     

No EC number prediction in MGYG000003452_01581.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	39	209	1.6e-31	0.9830508474576272

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06417	GH25_LysA-like	1.32e-88	35	225	1	195	LysA is a cell wall endolysin produced by Lactobacillus fermentum, which degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. The N-terminal glycosyl hydrolase family 25 (GH25) domain of LysA has sequence similarity with other murein hydrolase catalytic domains while the C-terminal domain has sequence similarity with putative bacterial cell wall-binding SH3b domains. This domain family also includes LysL of Lactococcus lactis.
cd00599	GH25_muramidase	1.81e-27	37	218	2	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.
pfam01183	Glyco_hydro_25	8.70e-21	39	209	2	179	Glycosyl hydrolases family 25.
cd06412	GH25_CH-type	1.38e-15	37	224	3	198	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.
cd06415	GH25_Cpl1-like	6.50e-09	36	205	2	184	Cpl-1 lysin (also known as Cpl-9 lysozyme / muramidase) is a bacterial cell wall endolysin encoded by the pneumococcal bacteriophage Cp-1, which cleaves the glycosidic N-acetylmuramoyl-(beta1,4)-N-acetylglucosamine bonds of the pneumococcal glycan chain, thus acting as an enzymatic antimicrobial agent (an enzybiotic) against streptococcal infections. Cpl-1 belongs to the CP family of lysozymes (CPL lysozymes) which includes the Cpl-7 lysin. Cpl-1 has a glycosyl hydrolase family 25 (GH25) catalytic domain with an irregular (beta/alpha)5-beta3 barrel and a C-terminal cell wall-anchoring module formed by six similar choline-binding repeats (ChBr's). The ChBr's facilitate the anchoring of Cpl-1 to the choline-containing teichoic acid of the pneumococcal cell wall. Other members of this domain family have an N-terminal CHAP (cysteine, histidine-dependent amidohydrolases/peptidases) domain similar to that of the firmicute CHAP lysins and associated with endopeptidase activity. The Cpl-7 lysin is also included here as is LysB of Lactococcus phage, and the Mur lysin of Lactobacillus phage.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAQ27398.1	8.12e-192	7	413	3	413
VEG24063.1	8.12e-192	7	413	3	413
ADB10077.1	8.12e-192	7	413	3	413
AJE06518.1	1.24e-157	1	414	1	415
AXR42563.1	2.97e-124	10	414	5	409

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

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
0.000310	0.998902	0.000199	0.000220	0.000189	0.000162

TMHMM  Annotations     

start	end
12	31