CAZyme Information: MGYG000002489_00578

Basic Information

• Species: Neisseria gonorrhoeae
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Burkholderiales; Neisseriaceae; Neisseria; Neisseria gonorrhoeae
• CAZyme ID: MGYG000002489_00578
• CAZy Family: GH104
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
181	MGYG000002489_3|CGC1	20463.96	10.6529

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002489	2153911	Isolate	Canada	North America

• Gene Location: Start: 115507; End: 116052 Strand: -

Full Sequence      

MWRGISSGRHVRGNYVLKASTAHNQAELERYVHNPQVRAFLDFIAASEGVKHGYQTAIGN
YRITDFSRHPGNSVRRSFTRTDGSRSTSDASGRYQFMGYTWKGLAKQYGFTDFSPATQDK
AAVALILAKKGAMEAILNGDYEQAVMKLGGIWASFPTAPNEYRQHKRSWGFVHNFFRQRG
F

Enzyme Prediction     

No EC number prediction in MGYG000002489_00578.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH104	33	179	4.6e-43	0.9793103448275862

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00736	lambda_lys-like	1.18e-60	35	180	1	140	Bacteriophage lambda lysozyme and similar proteins. Lysozyme from bacteriophage lambda hydrolyzes the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), as do other lysozymes. However, unlike other lysozymes, bacteriophage lambda does not produce a reducing end upon cleavage of the peptidoglycan, but rather uses the 6-OH of the same MurNAc residue to produce a 1,6-anhydromuramic acid terminal residue and is therefore a lytic transglycosylase. An identical 1,6-anhydro bond is formed in bacterial peptidoglycans by the action of the lytic transglycosylases of E. coli, though they differ structurally.
COG4678	COG4678	8.27e-28	35	180	35	175	Muramidase (phage lambda lysozyme) [Cell wall/membrane/envelope biogenesis, Mobilome: prophages, transposons].
cd00442	Lyz-like	0.002	86	123	20	57	lysozyme-like domains. This family contains several members, including soluble lytic transglycosylases (SLT), goose egg-white lysozymes (GEWL), hen egg-white lysozymes (HEWL), chitinases, bacteriophage lambda lysozymes, endolysins, autolysins, chitosanases, and pesticin. Typical members are involved in the hydrolysis of beta-1,4- linked polysaccharides.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ARC03691.1	1.14e-133	1	181	1	181
AKP10250.1	1.14e-133	1	181	1	181
QBK54041.1	1.14e-133	1	181	1	181
BBH59109.1	1.14e-133	1	181	1	181
BBH61385.1	1.14e-133	1	181	1	181

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1D9U_A	1.79e-21	34	166	5	138	ChainA, Bacteriophage Lambda Lysozyme [Lambdavirus lambda],1D9U_B Chain B, Bacteriophage Lambda Lysozyme [Lambdavirus lambda],3D3D_A Chain A, Lysozyme [Lambdavirus lambda],3D3D_B Chain B, Lysozyme [Lambdavirus lambda]
1AM7_A	2.54e-18	34	166	5	138	ChainA, LYSOZYME [Lambdavirus lambda],1AM7_B Chain B, LYSOZYME [Lambdavirus lambda],1AM7_C Chain C, LYSOZYME [Lambdavirus lambda]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P03706	1.08e-20	34	166	5	138	Endolysin OS=Escherichia phage lambda OX=10710 GN=R PE=1 SV=1
P51771	4.82e-16	37	165	10	148	Endolysin OS=Escherichia phage P2 OX=10679 GN=K PE=3 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
1.000067	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002489_00578.