CAZyme Information: MGYG000003771_03185

Basic Information

• Species: Blautia sp002161285
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia; Blautia sp002161285
• CAZyme ID: MGYG000003771_03185
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
362	MGYG000003771_207|CGC1	39343.28	6.8961

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003771	3602220	MAG	Canada	North America

• Gene Location: Start: 220; End: 1308 Strand: +

Full Sequence      

MALNGIDVSQYQGNVDWNQVKGAGIAFAMLRGGYGKNNVDPYFHQNASACQKLGIPFGIY
WFSYAYNAQMAAQEAEYCAALAKQYKVTWPLAYDLEYDTVRYAAQQGITIGKALATTMTA
AFCDKVKASGYIPMYYSNLDYYRTMFDTERLPYDLWFAQYASAASVSDMAMWQYTSTGSV
PGISGNCDRNYSYKDYGKGTVSPEPAPSVPDIYTVQSGDTLSGIALRFGTTVSSLAKING
ISDPDVIYPGQVLRLSGSPVSGQTIYTVKAGDTLSKIAADFGTSYQTLAQLNGILNPDLI
YPGQKLSIPSGSSTSISYYTIRPGDTLSGIALRFGTTVSRLQSLNNISDPDKIYAGTKIR
IN

Enzyme Prediction     

No EC number prediction in MGYG000003771_03185.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	6	183	8e-45	0.9943502824858758
CBM50	266	309	2.3e-16	0.975

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.30e-76	5	193	3	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.
cd00599	GH25_muramidase	1.78e-36	5	191	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.
pfam01183	Glyco_hydro_25	7.85e-29	6	183	1	180	Glycosyl hydrolases family 25.
cd06413	GH25_muramidase_1	5.11e-27	5	190	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.
cd06525	GH25_Lyc-like	1.28e-24	4	191	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QEK16471.1	2.08e-113	1	361	1	325
QYX27151.1	8.32e-108	1	361	1	325
QHB23957.1	1.70e-74	1	258	1	268
QEI31463.1	1.70e-74	1	258	1	268
QRT30197.1	1.70e-74	1	258	1	268

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4B8V_A	3.18e-16	213	359	44	214	ChainA, Extracellular Protein 6 [Fulvia fulva],4B9H_A Chain A, Extracellular Protein 6 [Fulvia fulva]
1JFX_A	6.13e-11	2	190	4	200	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
2WAG_A	6.39e-11	3	185	16	196	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]
4KRU_A	1.32e-10	3	190	20	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	3.54e-10	3	190	20	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8CMN2	2.35e-30	213	361	29	190	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=sle1 PE=3 SV=1
Q5HRU2	2.35e-30	213	361	29	190	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=sle1 PE=3 SV=1
Q49UX4	2.41e-28	213	361	29	193	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
Q2G0U9	2.55e-26	213	361	29	201	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=sle1 PE=1 SV=1
Q2FJH7	2.55e-26	213	361	29	201	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain USA300) OX=367830 GN=sle1 PE=3 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
0.999768	0.000225	0.000012	0.000003	0.000001	0.000004

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003771_03185.