CAZyme Information: MGYG000003194_00978

Basic Information

• Species: Paramuribaculum sp900546365
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Paramuribaculum; Paramuribaculum sp900546365
• CAZyme ID: MGYG000003194_00978
• CAZy Family: GH85
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1305	MGYG000003194_6|CGC1	143157.45	4.6071

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003194	2001061	MAG	United States	North America

• Gene Location: Start: 111418; End: 115335 Strand: -

Full Sequence      

MKKQVLFISAAALLVGGLNAQQLRPGYITAPNSSSFHKYVQAWEPGKELSVTYTDNGEEA
WEDEEFFVSRVALKPYFVNLKTQVDKTKSDADNKRLLFWVPINEASGAEKEWLNALPNAK
YDSEVFSTWSYVTHYGNWTSPFGWVPAAMADAAHKNGVLVSGVASIPNASIPSSWASCLA
GVGAMNSTEGVEKLGKFLRYHGVDGLGYNSEYYNGGSYGANLRGVHGKLVKYMKQYQPDF
ENVWYGGTNDNGSVNFNDQLSSDFYETFGYKDEPRTILFLNYNWNTTTKLSQDAAGINAT
GRDPRDIYMGMNMQGGLKTPTEWDQHLNIPYSIGLWGAHQVNYIWINRNQEGGTDAAKQA
TYQKHLEYWFTNGKRNPAYKMDPVNSLTATKDFMGMSRYMEARSTLKWDLTKEPFVTFFN
IGGGAQYNWKGTEAHVGPWYNLGVQDYMPTWRFWFATDYLGTTPAENIDANITWNDAYMG
GTSLRITANNTEASYLHLFKTEFEAKNGAKLTIRYKVIKGSGDMELVWSKLGSESEQAQK
TYGMVFDKDGKTYSTNKADGDLDYDADWQVKTLTLSSRNGLTGTIAALGLKFANANDLEV
LIGEISLTGGSYETPAAPIITRAKVLANNYKGVDGKIFFKMANTKELGEPVYNLDVKTSL
FRLWSRTDKDSEPQFLGTTSSWAGMIFSAPAEGATKIQFGVSAVSLDFSSASDIAWSEEL
PVGDYVAVEDLKVSKSPVTTGEEFYVEFVDPAHPAVDWKLTDEGGNVLASASNATRLDVA
GIDVTGAYDVYAGDVKHEGLVSVSDPGSGRQPIIESLTINGDEASAENAVQIQPNETLEL
GYTGREANGIGSRGVHLNELAFGTKVSDLGIGTYKSFSVAFWLKLDTYPTAAPGSLLLIE
NRLGSWPKNNWGYFWSRTVEGSFRNYLIDGGFGKSLDSGADGNRLYLDLNGNLGVSKWNH
LVYVFEYNEQNRVRIRFYLNGVLQKSNWLWCNKMTRENAIGDSNSGWDDIELTPGYASFA
SGSGKDAENTDWCIDNYPLAQTDWIKVGGAGPNGMAAVDGVIDDFQIWGKAMTQEDVNLS
KTGLGTLETLPEDVIAFWDLESDADANYGFISKGQKQIPAYLFEYAQTANEGQAGALPVE
AEFSAGSPFVPGSAYEVTTAPSWTARKGILSEGTGTDREGSVKLSYGDNRMGGDYTVTLS
LANALGADTKNYPVFSVTSAIDGVAADTEDGVEAYTVADGLFVQFAEAGNYTVEVYNTSG
MLMAQKAQAMEAGQNMSVRLGVQGVYIVRVLRDGQLARTIKVVRK

Enzyme Prediction     

No EC number prediction in MGYG000003194_00978.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH85	119	427	4.2e-44	0.9492063492063492

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4724	COG4724	3.86e-35	120	608	98	550	Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
cd06547	GH85_ENGase	6.29e-26	118	454	19	334	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.
pfam03644	Glyco_hydro_85	6.74e-17	120	424	4	291	Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.
pfam13385	Laminin_G_3	4.55e-06	875	1077	17	150	Concanavalin A-like lectin/glucanases superfamily. This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.
TIGR04183	Por_Secre_tail	1.43e-04	1241	1305	11	72	Por secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT74450.1	0.0	1	1305	1	1253
AHF11930.1	0.0	1	1305	1	1253
QFQ13703.1	1.78e-311	1	1305	1	1247
EFC71164.1	1.94e-272	18	1305	20	1247
QUB76735.1	2.64e-263	1	1305	1	1250

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VTF_A	2.69e-29	32	618	13	538	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]
3FHQ_A	1.43e-28	32	618	8	533	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]
3FHA_A	1.90e-28	126	618	81	533	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8NFI3	2.41e-06	117	486	149	467	Cytosolic endo-beta-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=ENGASE PE=1 SV=1

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
0.000500	0.997497	0.001365	0.000231	0.000202	0.000178

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003194_00978.