CAZyme Information: MGYG000001069_01153

Basic Information

• Species: UBA4871 sp900554535
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UBA4871; UBA4871 sp900554535
• CAZyme ID: MGYG000001069_01153
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
314	MGYG000001069_185|CGC1	34827.57	5.4356

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001069	2409721	MAG	Sweden	Europe

• Gene Location: Start: 2860; End: 3804 Strand: +

Full Sequence      

MKGIDVSRYNGNVDWATAKAAGLEFAILRCGYGSDETSQDDGQFARNVQECDRLGIPWGA
YLYSYALNLSDAKSELQHILRLLRGKKPLFPIYLDMEDADGYKQRNGMPSRQMLTDIVKT
VCSGLEDAGYFAGYYVNRDWYYNRIYPDQLKQYAFWYARPGVDQPDLSCGLWQNEFPSTG
GKWPGANIPGSGGCDTDKSFVDYPALVREKGLNGWTATQKARVAGEDTIIQTTCVVDTTL
DVKKPLGECYTLLLTCPVQPKVTVDAPVVCACPLSSLRPGAWLCNLVGYQKGDAGICTQV
PGEPVCIRFRYHVV

Enzyme Prediction     

No EC number prediction in MGYG000001069_01153.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	4	173	5.4e-35	0.9378531073446328

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	3.21e-69	1	200	1	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	1.13e-30	2	198	1	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	5.08e-17	4	166	1	158	Glycosyl hydrolases family 25.
cd06413	GH25_muramidase_1	3.94e-15	2	173	4	170	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.
cd06525	GH25_Lyc-like	9.87e-15	2	198	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNO19532.1	5.15e-151	1	313	1	318
QKN23667.1	4.73e-115	3	224	4	224
QKO29660.1	4.73e-115	3	224	4	224
ARP50591.1	4.73e-115	3	224	4	224
QNK41811.1	5.52e-105	2	304	5	302

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	6.55e-14	4	151	272	422	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	1.59e-13	4	151	272	422	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
1JFX_A	1.35e-06	1	171	5	176	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	1.78e-06	1	212	1	217	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

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
0.999893	0.000122	0.000005	0.000001	0.000000	0.000002

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001069_01153.