CAZyme Information: MGYG000001045_00231

Basic Information

• Species: Enterocloster sp005845215
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Enterocloster; Enterocloster sp005845215
• CAZyme ID: MGYG000001045_00231
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
338	MGYG000001045_9|CGC1	37066.66	4.2744

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001045	5511723	MAG	Denmark	Europe

• Gene Location: Start: 76693; End: 77709 Strand: +

Full Sequence      

MKYLRGAAGIILSLIFAVCFMCSPAFAASRLYHGMDVSSWQGDIDFQAVRAAGIEVVYIR
TGVGPDYVDSRFQSNYENALDAGMKIGYYHYVTASNTIQARQQAEFFYSLIQDKQIDCYP
AMDFESFPGLSRQEINAIGLAFMETLASRLGYGPALYTDSYNAAALWNSGFSSYPLWVAD
YDVNQPESTGPWDTWDGFQYSDTGQVPGVSGNADMDFFKDSMFIVSQPPQPEPSPGAIGA
LLTYKVQGGDTLWGISRRFRTTVGQLAELNRIANPNVIYTGQILEIPDAPGTIIYRVKSG
DTLSAIANRFDTSVSDLAYTNGIANPNLIYAGQVLVIP

Enzyme Prediction     

No EC number prediction in MGYG000001045_00231.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	35	209	1.6e-49	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06525	GH25_Lyc-like	4.13e-86	34	218	2	184	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	1.95e-51	33	218	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.
cd06414	GH25_LytC-like	1.10e-49	34	218	3	190	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.
pfam01183	Glyco_hydro_25	1.36e-48	36	209	2	180	Glycosyl hydrolases family 25.
COG3757	Acm	2.12e-41	32	221	63	256	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QJU21453.1	1.86e-208	1	338	1	338
ASN94242.1	5.31e-208	1	338	1	338
QRP41080.1	5.31e-208	1	338	1	338
QJS18123.1	7.23e-104	32	337	33	342
QIB56830.1	6.52e-96	22	337	20	347

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	1.58e-38	34	226	22	215	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	3.00e-37	34	226	22	215	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	5.44e-23	34	221	7	205	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
2WAG_A	1.88e-10	34	211	18	196	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
4B8V_A	9.46e-10	242	338	42	161	ChainA, Extracellular Protein 6 [Fulvia fulva],4B9H_A Chain A, Extracellular Protein 6 [Fulvia fulva]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	4.82e-37	34	225	11	203	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	5.17e-33	34	224	3	186	Autolytic lysozyme OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=lyc PE=1 SV=1
P25310	1.31e-21	34	221	84	282	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
Q8FFY2	3.10e-20	28	222	63	258	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
Q8X7H0	1.53e-19	28	218	63	254	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 SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000944	0.545113	0.453156	0.000330	0.000227	0.000211

TMHMM  Annotations     

start	end
7	29