CAZyme Information: MGYG000001837_00435

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UBA737
• CAZyme ID: MGYG000001837_00435
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
547	MGYG000001837_10|CGC1	60129.67	4.5016

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001837	1602907	MAG	Denmark	Europe

• Gene Location: Start: 30722; End: 32365 Strand: -

Full Sequence      

MKNYFKNITVILLALCLLSFCGCKNGGTLSSEMTASETDYIQTELNNIAEDETVDPENTE
TAAEPGVQMSFKNIQAAKGQANGIDVSKWQGKINWQSVKNAGIDFAVIRMGYRGENGVIY
RDSNADYNIQQAQKAGILVGVYFFSTAVNTSEATEEAAWVCEAVKGYDISYPVVYDCEGY
TDSSSRMYGVSAASRTDNALAFADYVHGKGYTGMVYGAKSEFENPDYWQMERIEQKCRIW
VAHYSSPTYPDKPNPDYNRKYDMWQYTNRGTVDGVIGNCDMVVSYFTAERSSAKDNSATP
PAADAPKTQEEMVYTEINDRVTAKEEVNLRTGAGTKYDIAGSLKSGEFLTRTGIGTNGWS
RLLYNGQTVYAITSYLSNEIVNVEKPDVVNGQIFTAAGDRVTAKSEVNLRALPTTDSNIV
GSLKSGTFLTRTAIGDKGWSRLDFNGTAVYAVTNYLTDKAPEISSDDTPSEQGSVTEYGM
EFKLTAVNVTAKEEVNLRDKPETGGSNVVYTLKNGEYITKTGESNSGWARLDFNGQTVYA
INSFLMQ

Enzyme Prediction     

No EC number prediction in MGYG000001837_00435.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	84	275	3.5e-46	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	5.77e-65	83	285	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	4.43e-38	83	283	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	8.56e-33	84	275	1	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	1.79e-26	82	281	1	181	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.
COG3757	Acm	4.64e-25	83	280	65	249	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
CBK89713.1	2.47e-107	69	457	82	482
ACR77025.1	4.91e-107	69	457	82	482
CBK93417.1	2.74e-106	69	457	82	482
ACR73526.1	4.29e-105	83	457	123	505
CUH92515.1	1.13e-100	39	456	60	485

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JFX_A	6.43e-18	83	280	7	198	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]
4KRT_A	2.81e-17	83	376	22	283	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]
4KRU_A	1.95e-15	83	289	22	210	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4JZ5_A	2.31e-10	84	281	26	209	High-resolutionstructure of catalytic domain of endolysin ply40 from bacteriophage P40 of Listeria monocytogenes [Listeria phage P40]
2WAG_A	9.93e-10	80	289	15	211	TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25310	1.35e-16	83	280	84	275	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P26836	1.84e-16	83	442	11	324	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	1.44e-11	83	281	3	177	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
O32041	6.98e-09	318	542	102	314	Putative N-acetylmuramoyl-L-alanine amidase YrvJ OS=Bacillus subtilis (strain 168) OX=224308 GN=yrvJ PE=3 SV=1
P76421	7.54e-09	82	293	68	263	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 LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000007	0.000925	0.999102	0.000001	0.000002	0.000001

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001837_00435.