CAZyme Information: MGYG000000072_00108

Basic Information

• Species: UBA1394 sp900066845
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; UBA1394; UBA1394 sp900066845
• CAZyme ID: MGYG000000072_00108
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
313		35593.95	4.0388

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000072	2648835	Isolate	United Kingdom	Europe

• Gene Location: Start: 116354; End: 117295 Strand: +

Full Sequence      

MKAVIKNILIIVELILIIFLSVVVYFLYQKNNEAVTTMGAGSISTDQYEDIDRKVNENYY
ELSGKKILLEDGTYGEIWIPVLENVPAFSKEIDQIKTRNGRKYYLDGSDITSLLGVDVSV
HQENIDWQKVKESGIDFAMIRLGYRGYGSGEAGLDENYAENIQGAREAGIDAGVYFFSQA
ITVEEAVEEANLVIESLKGLDINYPVVYDWEIIYDDTARTDNVSVDVLTDCCVAFCETIR
NAGYTPMIYQNKRTTIFKLDLNRLTDYDFWLAEYGSEPTYYYDFDMWQYTSTGSVPGIEG
DVDLNISFKDYSK

Enzyme Prediction     

No EC number prediction in MGYG000000072_00108.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	116	298	1.5e-46	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.12e-85	115	308	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	1.38e-43	115	306	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	2.46e-30	116	298	1	180	Glycosyl hydrolases family 25.
cd06413	GH25_muramidase_1	1.57e-27	115	305	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.
COG3757	Acm	6.79e-26	115	305	65	251	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
CBL16942.1	2.01e-116	6	308	6	316
QEK18217.1	4.36e-73	82	310	70	300
QHI72152.1	2.04e-69	83	313	63	293
ABX43465.1	1.28e-68	79	312	389	622
QRO38911.1	1.44e-68	38	311	18	288

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	1.26e-16	58	306	207	466	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	1.26e-16	58	306	207	466	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
4KRU_A	9.34e-16	112	305	19	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	3.81e-15	112	305	19	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	5.45e-07	109	305	1	200	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	4.80e-13	115	305	3	178	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
P76421	1.22e-08	115	306	69	253	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2
Q8X7H0	1.22e-08	115	306	69	253	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
Q8FFY2	1.64e-08	115	306	69	253	Uncharacterized protein YegX OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=yegX PE=3 SV=2
P25310	3.77e-06	108	305	77	277	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 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
0.899905	0.090390	0.001475	0.000674	0.000340	0.007243

TMHMM  Annotations     

start	end
7	29