CAZyme Information: MGYG000001467_00327

Basic Information

• Species: Clostridium_E jeddahense
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Clostridium_E; Clostridium_E jeddahense
• CAZyme ID: MGYG000001467_00327
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
291		32267.59	6.1149

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001467	3613503	Isolate	not provided	Asia

• Gene Location: Start: 14823; End: 15698 Strand: -

Full Sequence      

MLNGIDVSNANGRVDWDKLKGNIDFAILRCGYGSDMVSQDDKQWAHNVVECSRLNIPWGA
YLYSYAINMAEAESEAAHTLRLLEGLKPVYPVYIDMEDADGYKAKRGGISKQMATAICLL
FCERLTAAGYTAGVYANKDWATNRLDMAQLSKYTFWLAQYNDRVTYPGQYDMWQYTSDGS
MPGVSGRVDLNYCCKDFSLAAVPNISGLSLDTSSKDMNSGEKYTVLARCQEKPAVITVGR
DVIAVSEPRPDPKGRGWLIDVRGLPPEPVVRHGHIMVTSGGQTVQCNFNVR

Enzyme Prediction     

No EC number prediction in MGYG000001467_00327.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	5	184	9.1e-43	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	2.99e-92	4	193	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.
cd00599	GH25_muramidase	3.91e-36	4	192	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	5.88e-24	4	192	2	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.
cd06525	GH25_Lyc-like	1.44e-21	3	192	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.
pfam01183	Glyco_hydro_25	2.70e-21	5	184	1	180	Glycosyl hydrolases family 25.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAB1243797.1	1.43e-156	2	291	3	290
CAB1250843.1	1.24e-143	3	290	4	288
QNK41811.1	2.30e-60	4	197	6	207
QCP36075.1	1.13e-58	4	238	99	324
AWY97591.1	6.78e-58	4	192	97	283

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	4.15e-27	5	191	272	465	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	1.07e-26	5	191	272	465	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
5A6S_A	9.47e-12	6	197	26	205	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
2NW0_A	3.98e-10	5	199	4	180	ChainA, PlyB [Bacteriophage sp.],2NW0_B Chain B, PlyB [Bacteriophage sp.]

Swiss-Prot Hits     

has no Swissprot hit.

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
1.000006	0.000020	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001467_00327.