CAZyme Information: MGYG000000839_00834

Basic Information

• Species: Clostridium sp900540255
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium sp900540255
• CAZyme ID: MGYG000000839_00834
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
313		35471.06	9.0049

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000839	2735655	MAG	China	Asia

• Gene Location: Start: 33027; End: 33968 Strand: -

Full Sequence      

MQNKSDKSLFGIDINEYSQGVDFTVLATTIDFLYLRSSGSATGRFRVDRKFLEFARNARS
MKIPVGAYHFGVPSYDLTTADSQCDDFINILQDAFGEKDYGDLFPVLDVETPTDKSISTQ
ALINWIERFKIRFEKKTRRRLMLYTGVFFVEIYNNFFIPNKGYPLKNMILWIAYYTAISG
NAPVPPDVGGWTRWRVWQYSESATVAGVTSKVDANWGPNSIDLLTQPRNVSGLTVSRKGN
TLNISWKKNTDTDLVGYNIFANNYWIGTVDAKDTSFSINTNQLPFKVSGPIKISIEAFDN
DGETSKRRSSFTI

Enzyme Prediction     

No EC number prediction in MGYG000000839_00834.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	12	208	2e-33	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00599	GH25_muramidase	1.74e-40	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	3.05e-30	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	1.60e-27	12	208	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	8.17e-26	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.
cd06413	GH25_muramidase_1	3.59e-20	11	215	5	187	Uncharacterized bacterial muramidase containing 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QAS61852.1	3.82e-163	1	313	1	313
AYE33697.1	3.82e-163	1	313	1	313
ATD55806.1	5.43e-163	1	313	1	313
SLK21690.1	5.43e-163	1	313	1	313
QBJ76106.1	5.43e-163	1	313	1	313

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5JIP_A	3.44e-122	2	313	7	318	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]
4KRT_A	3.84e-12	8	256	19	246	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	2.39e-11	11	215	7	200	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRU_A	2.01e-09	8	215	19	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	2.45e-12	1	271	1	250	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	2.93e-10	11	215	84	277	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm 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
1.000081	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000839_00834.