CAZyme Information: MGYG000001615_00817

Basic Information

• Species: Eisenbergiella sp900548905
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella sp900548905
• CAZyme ID: MGYG000001615_00817
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1355		145135.06	6.3683

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001615	6842156	MAG	China	Asia

• Gene Location: Start: 235274; End: 239341 Strand: +

Full Sequence      

MSNHSNDEKRNDMQDKTGKRLSNPNDELTGKRTARVSPEELLPEKIEKVTESLLSQWEIS
EDDFEDTQDLTETAARLSGYEAPPLRREEGRRTDKAPAARTGSMEERRTAAERKESRTAD
TGRTVSASRTAGAAGTAGAGGNGSGREERQKASGSQSGDMRRSSPDKGGTHGASSNRTPS
ERRNMERVSAERRADSGSHKSDAVRSRQENSGKEKAQRSEKGDPRQDERAPRHVSSERSR
NTSRAQVADREDHRRKEAARIREEESGRKAADTGRKKADPGRKAAERRQQPSGGRSDSRL
GYDDERFGNSGHGSGSGKSSSRRKQANPVVEFWNSLHTMDKVVGFTGIFVCIFAVVTFSV
LANAKSTDKQVEAFAAVGQNLSQINVADDSIFLAVADAHRAKQEAADITDTDESEEYNEK
DDNSDVQVGLNMTSVEKDLKIKFVNRKTGKLVPRVDFQVEIKGPDKTYTKNDDDQDGIIY
LTGITPGKYTVKITGPENAEGYSIPSDAQEVTVKDHIEYKKIDVSDEVKKESEINAAKED
TQVKTQTESVLQDTVEWVESTKTPVGGSGNDGAYVEVKKADVPDPSASASLIFDKFLGVK
SQKPWIMLTAETVLPRTETDGKEDSNTDTNTGSGEGENQTNTPEQVEVEKITISPESASG
TVGGGQNFTAQISPDNAADKSVVWSSSDKNVATVNNGSVTFVGAGTTEIKVASANGKTAT
ASVTVSAKETQVGSVAINGDTAVTVGGTIKLTASVSPDDASYNGVTWSSTDTSIATVVGG
TVTGIKAGTVTIKAEAGGVTGSSEITVKEAEVVLKSIKISGDSAGKKGAAVQLAITPDPA
GADASVTWKSSNDSVASVDANGKVTCNSAGEVTITAVSKKNAGITATFTFKVTEDVQKKF
DMKDVSVTAGQFKNLEDYCTIQGSSSRSFSIENTKYATVDGNGRIKAIRSGETKITVTVK
FQDGGSQTQTKKLIVNAAEVKGITLDKTKLTLNVGDSLKLNPTIDTTGYTGCLWYSTDKT
IVTVEEHGGGTIKALKPGKVTITAKSSENTSKTATCEVTVTGEDPRNDTKTPLKDKSGKP
LFVKTADGKYVAAVVADYYKYDVFYRENENVEYKYTGWQTIDGKRYYFDKNGNKVTGDQI
IQGVKYSFGSDGALSSGSGVLGIDVSKHNGNINWTEVKNSGVSYVIIRCGYRGSSTGALI
EDPKFKANVQGATAAGLKVGIYFFTQAVNQIEAVEEASMTVSLIKNYKISYPVFLDVEAS
GGRADGLDAGTRTQIVNAYCQTIQNSGYTAGVYANKSWLNSKLNVGSLGSYKIWLAQYAA
APTYNGRYDMWQYSSTGKIGGISGNTDLNISYLGY

Enzyme Prediction     

No EC number prediction in MGYG000001615_00817.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	1163	1342	2.3e-46	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	2.65e-88	1162	1352	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	8.19e-41	1162	1350	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.
cd06525	GH25_Lyc-like	1.08e-37	1162	1349	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.
pfam01183	Glyco_hydro_25	5.41e-35	1163	1342	1	180	Glycosyl hydrolases family 25.
cd06522	GH25_AtlA-like	2.56e-27	1163	1352	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	7.32e-180	329	1352	248	1225
QNM02116.1	6.39e-163	315	1355	193	1102
AOZ95561.1	2.77e-153	339	1352	272	1213
QNM02113.1	7.86e-70	1155	1352	232	431
CBK74089.1	9.72e-70	1073	1351	244	516

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	2.97e-24	1116	1352	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	7.09e-24	1116	1352	244	468	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
4KRU_A	9.68e-16	1162	1349	22	205	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
1JFX_A	1.89e-15	1158	1349	3	200	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRT_A	6.21e-15	1162	1349	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
P25310	3.97e-14	1158	1349	80	277	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836	4.04e-14	1162	1349	11	194	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	3.55e-12	1162	1349	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
P85991	4.88e-08	644	792	86	240	Ig-like virion protein OS=Serratia phage KSP90 OX=552528 PE=1 SV=2
P33747	1.40e-07	651	777	40	167	Uncharacterized protein CA_P0160 OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=CA_P0160 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
1.000044	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
342	364