CAZyme Information: MGYG000003063_01238

Basic Information

• Species: Eisenbergiella sp900544445
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella sp900544445
• CAZyme ID: MGYG000003063_01238
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1204	MGYG000003063_20|CGC2	128580.4	4.5607

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003063	3890464	MAG	United States	North America

• Gene Location: Start: 28462; End: 32076 Strand: -

Full Sequence      

MTEKERGQEEMSKKTDDLQRAFEDGWEISEDDFEETQDLAETAAQLSDLKDSFEDDEEPD
DYEEEAAEELWEEGTPRKESAVRREKRDSDRRDAGGHDASHQNDVARRNGTVRRDNAARR
NDAVRRNDVEHRNRGRETDVHKGRPSGKRQADYGRHVRPDESPRRTCAAGRQGKRNRRQE
NGFLTFLKGLSAMDRVIGLTGAAVCLFAVFTFSFVLAARAQEKQVASFAAVGEELARISV
ADESTFLAVADGLLARQQAAENVETEYEETDDVSDIQVGLNMTSVEKDLKIKFVNRKTGK
LIPYVAFEAKITGPDQTYQKTDDDEDGIIYLTGITGGSYTVEVTGPEDLEGYVLPDGAQS
VTVKNQIDYEKIDVSDEIKSESEVNAAAEDTEIKTEVESVLQDTVEWVESTRTPIGDEGS
LYIEVKKADIPDPSQSANLEFALFAGVRKDGSLLKTAARTSSEIQTLTEPQTTEPADPPA
ETDTQPPEETPPQTVAVTGVSASPSSLSGKVGESGDISVTVSPDNASNKSVSFSSDNGGV
AEVDGNGHVSFKGAGNATITVKTSDGGYTASVSVSVSEAEKKVESVSISGDSTVTVGSSI
SLSASVSPSDAAYNGISWSSSDTGIATVDNGKVTGVAAGRATITAEAGGVKATKEIEVKA
AEVTLTGIQITGSTSAKKGDTVQLSITAEPSGADASVTWSSSNANIASVDGNGKVTCSAV
GSTTITAVSQKNSNIKSSITFTVTSNESNSVTLNEMKITAGQTKAADVKTTGSVSSRSFS
IANTKYATVDGNGNIKAIRAGSTELTVKVTFSDGSTQTKTAKLTVEAAEVKGITLDKTKV
TLKVGESLKLNPTIDTTGYTGCLWYTSDSSIVTVTEHGNGTITAVKAGKVTITACSSEDT
SKKATCEVTVTGGKAEEDTKTLLKDKDGRQLYIKKDGKYVEAVVADYFKYDVFYRLNDNV
EYKYTGWQTIDGKRYYFDKNGNKVTGKQVIQGVQYDFGADGALSSGSGVLGIDVSKHNGS
IDWEKVKNSGVSFVIIRCGYRGSATGVMVEDPKFRSNIQGATAAGLKVGVYYFSQAVNQR
EAVEEASAALELISGYKISYPVFIDVEAAGGRADGISSADRTAVVQAFCNTIRDSGYTAG
VYANKNWLGSKMNTGSFGSYNIWLAQYAAAPTYNGRYEMWQYSSTGKIDGISGNVDLNIS
YLGY

Enzyme Prediction     

No EC number prediction in MGYG000003063_01238.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	1012	1191	3.4e-49	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.14e-90	1011	1201	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	3.37e-45	1011	1199	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	1.14e-37	1012	1191	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	6.14e-32	1011	1198	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.
cd06522	GH25_AtlA-like	1.91e-31	1012	1201	4	192	AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family includes the AtlA and Aml autolysins from Streptococcus mutans which have a C-terminal glycosyl hydrolase family 25 (GH25) catalytic domain as well as six tandem N-terminal repeats of the GBS (group B Streptococcus) Bsp-like peptidoglycan-binding domain. Other members of this family have one or more C-terminal peptidoglycan-binding domain(s) (SH3 or LysM) in addition to the GH25 domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADL33290.1	3.04e-160	183	1201	248	1225
QNM02116.1	1.31e-148	168	1204	189	1102
AOZ95561.1	1.19e-143	147	1201	226	1213
QNM02113.1	1.72e-72	1004	1201	232	431
CBK74089.1	6.53e-71	842	1200	153	516

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	4.60e-20	965	1201	244	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	4.60e-20	965	1201	244	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
4KRU_A	2.37e-14	1011	1198	22	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
1JFX_A	2.55e-14	1007	1198	3	200	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRT_A	1.31e-13	1011	1198	22	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
P34020	2.53e-16	1011	1198	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
P25310	4.97e-13	1007	1198	80	277	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836	2.06e-12	1011	1198	11	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
Q8X7H0	7.64e-11	1011	1199	69	253	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P76421	1.38e-10	1011	1199	69	253	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2

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
1.000077	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
196	218