CAZyme Information: MGYG000001338_00576

Basic Information

• Species: Blautia_A wexlerae_A
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A wexlerae_A
• CAZyme ID: MGYG000001338_00576
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
485		54969.69	9.3121

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001338	3930699	Isolate	not provided	not provided

• Gene Location: Start: 637948; End: 639405 Strand: -

Full Sequence      

MKRDFLKIRKRLIVGCLAAAIAVAQPVSSVFANPHYDRRDTVAEEEFIYSARTSGTESSR
KKVNSKAWKKINGVCYNGSGEIIPGAITRGMDVSEWQGNIDWKQVKRSDIDFAFVRISYG
LTHEDYTYDENMTNAELAGVPTGTYVYSTALSTTTALKEAQLAISKMQGYKVSYPVVYDL
EYAKASKLSAKTVSEMALTFCNEVRRAGYYPMVYCNTNWYDNYIDWSLLSGVDVWIARYG
DTIQAPDKERYNYTIWQSTDGNRESGLNSTSGLVAGIPAGNDVDMDFGYVDYTKKITPRW
KSLHSYVPAMKPDTGSNDGSQEQTGLHQENGKYYYVNENGERVSDQWVTVNGKTYYISSD
GYALMGMKKVDGKCYWFHTKSGYMFKNRRVTRSTGDIYYFGSDGVRCENGMYKVREKSGE
HTYYFRKNGKAYKGWLTLNGKKYYFYKGSSALSGTRAENITLTSSNRIVSVFDGNGVCTR
QYKKR

Enzyme Prediction     

No EC number prediction in MGYG000001338_00576.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	91	266	1.2e-46	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	9.36e-64	89	289	2	191	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	9.92e-34	92	267	2	180	Glycosyl hydrolases family 25.
cd00599	GH25_muramidase	9.40e-33	89	286	1	184	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.
cd06525	GH25_Lyc-like	3.37e-26	89	287	1	183	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	4.45e-23	88	285	3	186	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
QCU01355.1	8.72e-166	9	479	5	506
CBL21600.1	2.56e-72	9	206	5	200
ASM68843.1	1.37e-51	56	347	65	330
SET59461.1	1.66e-45	56	361	23	312
ADL03867.1	2.49e-42	64	361	31	312

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAG_A	4.16e-11	89	268	17	195	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
4KRU_A	4.75e-11	89	284	21	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	1.52e-10	89	284	21	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]
1JFX_A	2.42e-10	89	267	6	193	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P34020	1.63e-10	89	288	2	195	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
P49331	2.14e-09	330	477	1181	1329	Glucosyltransferase-S OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfD PE=3 SV=3
P11001	2.87e-09	331	447	1076	1187	Glucosyltransferase-I OS=Streptococcus downei OX=1317 GN=gtfI PE=3 SV=1
P25310	3.18e-09	89	267	83	270	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836	7.83e-09	89	284	10	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc 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
0.000366	0.998922	0.000164	0.000199	0.000167	0.000147

TMHMM  Annotations     

start	end
12	31