CAZyme Information: MGYG000000047_01262

Basic Information

• Species: Clostridium disporicum_A
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium disporicum_A
• CAZyme ID: MGYG000000047_01262
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
316	MGYG000000047_7|CGC3	34790.48	8.9261

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000047	3448648	Isolate	United Kingdom	Europe

• Gene Location: Start: 76835; End: 77785 Strand: +

Full Sequence      

MIKGIDISNYQAALNFTTAKNMGFEVCIIKATESINYTNPLLDSQVNSALSNNMKIGFYH
FFRNNGITEAQYFVSKIKPYLSKMTVKPAIDIETTYSYSQVLDFISYVENVLGIECMVYC
NYSYAKQLSLNNEIAKKTLWLAYYGINNGEYYEAPTNHGFAKFAGQQYSSANYIGAINTD
TNLFNENVYIKGKVNVTASTGSSSSSGGTSTNTTYTVVYGDTLSEIAKKYAVSVSELVSL
NKIVDQNLIYVGQILRIPTSSSDRVKTSQKIYYTVVSGDTLSGIAAKFGTTVAAIASLNK
ISNVNLIYVGQVLRIK

Enzyme Prediction     

No EC number prediction in MGYG000000047_01262.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	5	174	2.5e-33	0.9774011299435028
CBM50	273	315	6.8e-16	0.95

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06525	GH25_Lyc-like	9.56e-40	3	183	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.
cd00599	GH25_muramidase	6.16e-36	3	184	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.
pfam01183	Glyco_hydro_25	1.09e-34	5	177	1	180	Glycosyl hydrolases family 25.
cd06417	GH25_LysA-like	2.85e-25	2	185	1	189	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.
cd06412	GH25_CH-type	4.16e-25	2	185	1	193	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDM70433.1	1.59e-50	2	315	9	319
QBJ75914.1	6.92e-46	2	315	9	324
ATD56705.1	6.92e-46	2	315	9	324
SLK20760.1	6.92e-46	2	315	9	324
ATD55618.1	6.92e-46	2	315	9	324

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	9.33e-22	2	190	20	213	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	6.56e-21	2	190	20	213	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]
1JFX_A	2.05e-12	2	185	5	203	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4B8V_A	1.53e-11	208	315	37	160	ChainA, Extracellular Protein 6 [Fulvia fulva],4B9H_A Chain A, Extracellular Protein 6 [Fulvia fulva]
6ZMV_A	1.80e-08	2	150	2	167	ChainA, muramidase [Trichobolus zukalii],6ZMV_B Chain B, muramidase [Trichobolus zukalii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	4.34e-20	2	188	9	200	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
Q49UX4	1.31e-14	213	315	27	129	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 PE=3 SV=1
Q8CMN2	2.00e-13	213	315	27	127	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=sle1 PE=3 SV=1
Q5HRU2	2.00e-13	213	315	27	127	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=sle1 PE=3 SV=1
P54421	2.91e-13	174	316	47	193	Probable peptidoglycan endopeptidase LytE OS=Bacillus subtilis (strain 168) OX=224308 GN=lytE 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
1.000062	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000047_01262.