CAZyme Information: MGYG000003767_00927

Basic Information

• Species: Bifidobacterium sp002884815
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium sp002884815
• CAZyme ID: MGYG000003767_00927
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
652		72376.19	8.2219

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003767	1161383	MAG	Canada	North America

• Gene Location: Start: 17616; End: 19574 Strand: -

Full Sequence      

MGQFIVRVIASLVSIATALVVNSAPAFKVENRLDFKNVASKVADVADGENSAELSDNGTN
TVEEDQLNAFSNGDSRNDSKLPKKVASSFTNKDEVVSSKYAIADNGELKSIKTGQTVTDS
KLVGTKDKQPDPLAKSNGERFTPITVGDLRKEIKRENSSSTNADSSTTNNTPISSKKRVE
NKRSLRKNKVVLISSNQKNPEETDSNEKSQESQALESRTSTYTTYGSVRKISLPTNGFGT
RWGDYNGTQAFYDGNGSLFAYNASGVIDVSEHQKEINWAAAKAAGVEGAIIRISYGWENG
YDKYALRNIRECKRLGIPFGIYMYSYAEKPEDGANEGADVASLLRRAGVSPGDLSYPVYY
DLEKWVWAGHTAPTSPYVYQNIVSSWWNQLYNAGYTNLGIYSYANYLKGPLNSQYIHDRA
SWVASYGATPLFNIRTALRGWQYTSKARISGIDGNVDVSAFGTGPNSPVTQTSVDFTWII
RNNDIAVGAAVTGNLNRHLEYRWLSYDLYNKQWNTISDWSVGNWASWVTSNGDYWLHCEV
RDAYTYKSLGTKTIAFHYQVNNPVEPEFVEKTIVSGTYAAWQGSSVLLGAVTNNPSGYTI
IKIYDYNAKQWVSQFKGPWALWSPHPGIYWTHFEAYSKDGKLQDTKTYAFGV

Enzyme Prediction     

No EC number prediction in MGYG000003767_00927.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	267	452	1.5e-34	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.02e-57	266	461	3	190	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	9.41e-29	266	461	2	186	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.
cd06523	GH25_PlyB-like	6.12e-21	266	460	2	176	PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) 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	9.36e-18	266	459	3	189	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.
pfam01183	Glyco_hydro_25	1.43e-16	267	452	1	180	Glycosyl hydrolases family 25.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AYZ21008.1	1.95e-314	1	652	1	639
AEF31386.1	1.59e-313	1	652	1	639
VEH17511.1	4.08e-313	1	652	1	636
SDR77012.1	4.08e-313	1	652	1	636
ADP39306.1	4.08e-313	1	652	1	636

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	1.47e-30	262	461	267	467	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	3.61e-30	262	461	267	467	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.007646	0.991427	0.000262	0.000215	0.000212	0.000217

TMHMM  Annotations     

start	end
5	27