CAZyme Information: MGYG000000678_01676

Basic Information

• Species: CAG-485 sp002491165
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; CAG-485 sp002491165
• CAZyme ID: MGYG000000678_01676
• CAZy Family: GH85
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
363		40930.32	7.9207

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000678	2629642	MAG	Kazakhstan	Asia

• Gene Location: Start: 112; End: 1203 Strand: +

Full Sequence      

MKQKLLFSLSVLAALSTGGAAAQQLRPEYVDWGTRGTGFPAALCDWQKGQKWSPDDNFFI
SRVRPKVRFRNVATQVNPSFTEENDKKLIFWVPINSPEYNALPDGAFDREVFPMWSYITH
YGNWSTTLVRMPGNFMDVAHKNGVPVSVVASVPWGNISAEWEAALKKMLEAGPEKMADFL
EYYGVDGLGYNSEFQGDSIMVQNLGRYHASLVKLLKESGRMPLHENIWYDGTNEKGKISF
DRGLGTHNDDLWGYGDSIKTSLFFNYNWNNTVLLDRTVEHAQKLGRSPLDLYAGMNMQGG
EPKSGERWPMLARYPLYIGLWGAHSENMFFESRAEKGGVRRTCVRLPTSKGWSSGSPEVP
ATR

Enzyme Prediction     

No EC number prediction in MGYG000000678_01676.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH85	106	326	5.4e-40	0.726984126984127

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4724	COG4724	1.58e-21	1	311	1	310	Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
pfam03644	Glyco_hydro_85	9.17e-17	115	322	13	225	Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.
cd06547	GH85_ENGase	2.15e-14	115	361	30	286	Endo-beta-N-acetylglucosaminidase (ENGase) hydrolyzes the N-N'-diacetylchitobiosyl core of N-glycosylproteins. The beta-1,4-glycosyl bond located between two N-acetylglucosamine residues is hydrolyzed such that N-acetylglucosamine 1 remains with the protein and N-acetylglucosamine 2 forms the reducing end of the released glycan. ENGase is a key enzyme in the processing of free oligosaccharides in the cytosol of eukaryotes. Oligosaccharides formed in the lumen of the endoplasmic reticulum are transported into the cytosol where they are catabolized by cytosolic ENGases and other enzymes, possibly to maximize the reutilization of the component sugars. ENGases have an eight-stranded alpha/beta barrel topology and are classified as a family 85 glycosyl hydrolase (GH85) domain. The GH85 ENGases are sequence-similar to the family 18 glycosyl hydrolases, also known as GH18 chitinases. An ENGase-like protein is also found in bacteria and is included in this alignment model.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QFQ13703.1	9.18e-123	14	361	12	359
QUB57152.1	1.81e-120	22	356	20	359
QUB59112.1	1.81e-120	22	356	20	359
ADK97201.1	2.70e-118	22	356	20	359
ASE18175.1	2.70e-118	22	356	20	359

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2W91_A	4.93e-20	46	308	17	287	Structureof a Streptococcus pneumoniae family 85 glycoside hydrolase, Endo-D. [Streptococcus pneumoniae TIGR4],2W92_A Structure of a Streptococcus pneumoniae family 85 glycoside hydrolase, Endo-D, in complex with NAG-thiazoline. [Streptococcus pneumoniae TIGR4]
3GDB_A	5.92e-20	46	308	168	438	Crystalstructure of Spr0440 glycoside hydrolase domain, Endo-D from Streptococcus pneumoniae R6 [Streptococcus pneumoniae R6]
3FHA_A	7.61e-16	39	308	12	282	ChainA, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHA_B Chain B, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHA_C Chain C, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHA_D Chain D, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae]
3FHQ_A	1.02e-15	39	308	12	282	ChainA, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHQ_B Chain B, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHQ_D Chain D, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae],3FHQ_F Chain F, Endo-beta-N-acetylglucosaminidase [Glutamicibacter protophormiae]
2VTF_A	2.45e-15	39	308	17	287	X-raycrystal structure of the Endo-beta-N-acetylglucosaminidase from Arthrobacter protophormiae E173Q mutant reveals a TIM barrel catalytic domain and two ancillary domains [Glutamicibacter protophormiae],2VTF_B X-ray crystal structure of the Endo-beta-N-acetylglucosaminidase from Arthrobacter protophormiae E173Q mutant reveals a TIM barrel catalytic domain and two ancillary domains [Glutamicibacter protophormiae]

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
0.000663	0.998260	0.000335	0.000274	0.000208	0.000189

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000678_01676.