CAZyme Information: MGYG000001479_00324

Basic Information

• Species: Clostridium_AA polynesiense
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium_AA; Clostridium_AA polynesiense
• CAZyme ID: MGYG000001479_00324
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
309		34969.05	4.8692

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001479	3560738	Isolate	not provided	not provided

• Gene Location: Start: 52720; End: 53649 Strand: +

Full Sequence      

MQNRNPGSLFGIDINEYSQNANFQELARTVDFLYLRSSGSGSGRFRVDRKFLEFAKASRD
FGIPVGAYHFALPTTSLPAADAQADDFADVLQQGFGQGDYGDLFPVLDVETPVDKSLTTE
QLVNWIDRFRRRFENRTRRRLMLYTGAFFIDIYDNFFIPGRGYPLSNMPLWIAMYTSIPG
NPPYPVDQGGWTRWRIWQFSEDGKVNGVDPPTDLNWGPNSIDLLRAPRDVSGLRVYEDAN
NVYANWNPNPDLDLAGYNIFLNGNYVTTLNKGRNSYVISKRRYGITPTSPVTVGVEAFDI
DGEFSKTGL

Enzyme Prediction     

No EC number prediction in MGYG000001479_00324.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	12	208	2e-38	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00599	GH25_muramidase	2.13e-29	11	216	2	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.
cd06524	GH25_YegX-like	7.27e-22	10	215	1	190	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.
pfam01183	Glyco_hydro_25	8.68e-20	12	208	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	6.28e-18	11	215	2	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.
cd06412	GH25_CH-type	1.96e-12	11	215	3	190	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
AOR24425.1	4.87e-151	1	306	1	306
ATD55806.1	8.02e-150	1	306	1	306
SLK21690.1	8.02e-150	1	306	1	306
QBJ76106.1	8.02e-150	1	306	1	306
ATD56520.1	8.02e-150	1	306	1	306

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5JIP_A	1.53e-141	2	306	7	311	Crystalstructure of the Clostridium perfringens spore cortex lytic enzyme SleM [Clostridium perfringens],5JIP_B Crystal structure of the Clostridium perfringens spore cortex lytic enzyme SleM [Clostridium perfringens]
4KRU_A	5.79e-12	8	215	19	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	1.62e-11	8	215	19	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]
6ZM8_A	2.06e-09	11	226	4	203	ChainA, muramidase [Sodiomyces alcalophilus]
5A6S_A	2.08e-07	13	238	26	223	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
Q8FFY2	1.71e-14	8	225	66	262	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P76421	3.19e-14	8	226	66	263	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8X7H0	2.43e-12	8	215	66	252	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX 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
1.000069	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001479_00324.