CAZyme Information: MGYG000000132_01394

Basic Information

• Species: Beduini sp902363625
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Beduini; Beduini sp902363625
• CAZyme ID: MGYG000000132_01394
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
410		45643.27	3.9044

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000132	2897757	Isolate	Canada	North America

• Gene Location: Start: 255343; End: 256575 Strand: +

Full Sequence      

MSQLGIDISEFQGAMDFEAIAGNIDYVIIRAGYADVVDPQFERSYAECKRLNIPCGTYFY
SYALNTEEAQAEADFYLSLLAGKVFEYPIYLDMEDGDHYKEEHGLTDPQEYVAITQTFLS
RVEAQNNYVGIYSSQSWFDKCLGAPSLKRYDRWIANWGTNDGTIQVDVSDQAGMLQYTSV
GSIEGYDGNVDRDIAYLDYPSIIVGGNFNGNGQNEEPPAQTEYKIGDHVKFESCYRSSTA
KIGWPPEGEALVPDTNHGVITAIYDGTNNPYLINDGMCFVNNGDIQGYYEVKQTTYEVGD
HVMFNSCYRSSTATVGWPPFGEALVPDVDHGIITAIYDGTNNPYLINDGMCFVNNGDITG
YYDKNTYVVQAGDTLSEIAEQYGISYQALAQMNQISDPNLIYPGQTLRVP

Enzyme Prediction     

No EC number prediction in MGYG000000132_01394.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	6	185	1.6e-38	0.9887005649717514
CBM50	367	410	2.9e-17	0.975

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.68e-60	5	196	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	3.96e-34	5	195	2	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.
cd06524	GH25_YegX-like	3.10e-24	4	194	1	191	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	1.12e-21	6	185	1	179	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	1.98e-19	5	193	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMW75290.1	7.89e-56	1	287	1	273
QQY26763.1	7.89e-56	1	287	1	273
QPS14372.1	7.89e-56	1	287	1	273
BCT44624.1	2.51e-55	1	350	1	344
QQV06256.1	3.07e-55	1	287	1	273

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	1.65e-14	6	196	272	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae at 1.6 A resolution [Streptococcus pneumoniae R6],2WWD_A 3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment [Streptococcus pneumoniae R6]
2WWC_A	3.93e-14	6	196	272	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
2L9Y_A	7.89e-07	329	410	29	108	Solutionstructure of the MoCVNH-LysM module from the rice blast fungus Magnaporthe oryzae protein (MGG_03307) [Pyricularia oryzae 70-15]
5C8O_A	2.93e-06	329	409	32	103	Crystalstructure of MoCVNH3 variant (Mo0v) [Pyricularia oryzae],5C8P_A Crystal structure of MoCVNH3 variant (Mo0v) in complex with (N-GlcNAc)3 [Pyricularia oryzae],5C8Q_B Crystal structure of MoCVNH3 variant (Mo0v) in complex with (N-GlcNAc)4 [Pyricularia oryzae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9CH26	5.61e-06	363	410	401	448	Teichoic acids export ATP-binding protein TagH OS=Lactococcus lactis subsp. lactis (strain IL1403) OX=272623 GN=tagH 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
1.000058	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000132_01394.