CAZyme Information: MGYG000001512_03091

Basic Information

• Species: Coprobacter secundus
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Coprobacteraceae; Coprobacter; Coprobacter secundus
• CAZyme ID: MGYG000001512_03091
• CAZy Family: GH85
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1283	MGYG000001512_19|CGC29	143987.35	4.6644

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001512	4253015	Isolate	not provided	not provided

• Gene Location: Start: 1364265; End: 1368116 Strand: -

Full Sequence      

MRIKNLFLATGLLVSAGALAQSVPTHPNYINYGTDNNQRFTTEFVKMLETWEPGKPYLSP
DDPEYSNYTDDNFFISRVRVKDRITNTATQANPNLVPGEEAVNEKKLCWFSPIGEMTKQW
GAMSRYTFDADNFSMWQYLDVHSNVSSQLFRSPGVFNDVAHKNGVITGAYYFIDWASTVS
PTSPAGEPLYELSKKENGKFKYAKKLIQLMKYYGIDGMAFNPEGYFSSDLNTQFQEFLAE
CHRIAKEEEDWHFHVDWYGYVTNSGGLNDGGSTLTANHSNWFHNDALNYPVTDVYFLNYN
WSEGSLQTSVNVAKSKKRSPFDVYAGFDQQGRGYGGWGNGGWGVLSKYPVSIVVWGAHDR
SQIYTGSNEFGTSELTIQNTYQDKLEMLFTGGTQNVLSAQKIPLNESNEKVTTSHNDLKK
WHGYSRFINAKSTLQELPFITRFNLGNGMSFKKEGKVTFNQKWYNISMQDYLPTWRWWVD
AGNREVPADAINCDFDFNEAWYGGSSLKFHGATQKSEVNLYKTKFTVESENDKFGLTFML
KNGTDPKLKFKVSLVGSENTYKYYTIPAESVKAGEWNTISFTAADLGLKANDVIATMGLA
FENTDANYQINIGELSLIPASYNKTPRAPRIVSVTPCKRTYKAVDFKMTWSMLDEGKEDI
SPNYPGCPTYNEDVDTWYYEVYIKTEDSEPTLLTATTSWASYVIDAPLPVENTEKYMVGV
RAIGLNGSASEITWSDKQTSEIEIINTISINKPIIKPNEEFTIGFDDPNHAPSTIIITDA
ITGDEVAKATEVRTLTTKLSELGTYDVEVITGEESTMTRGCLLISPEETGRMPEIEGYTA
NPAEPKTNEEITLTPAFNDGTTYQDSPATVSQGAYILNPSMFYVDKQILDNHTNNTFCFW
FKSDKFEHGAKGTLLTQKVNKNYSGTWTEKVWGEMWCVIRPADFKNGNLENEISISFDAP
PAGTANYEHNNDVDGISQNYPLSSGVWNHIAIVKENKNIRLYINGHEVISTTSKGSGPKE
WNANFYIGGALDNTSGFNGYIDEVQLWNKSLTAEEVKEAMSGYFLAPEGLQGYFKFEDME
DDGKGNQAFRNEGQNSTLVPYGYIGQFTTENERSVEKPETPTVGLGVPFITGVSNIRLES
VEWILEGATHTTDDENVATATYATQGKYPVTLKVTNSWGTTTKTFDDYLEIKAEETGVEK
EIVENMYVYPNPFVKDVNLRFAADGNYDIKVYDAQGRLVTGQLYKADKGEICTLSIDNGS
GMYYVVVSQNGKCLKSFKVVSQK

Enzyme Prediction     

No EC number prediction in MGYG000001512_03091.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH85	125	451	3.7e-55	0.9523809523809523

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4724	COG4724	1.90e-49	52	617	28	549	Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
cd06547	GH85_ENGase	1.55e-42	127	483	21	339	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	2.01e-33	127	448	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	8.33e-22	970	1057	64	151	Concanavalin A-like lectin/glucanases superfamily. This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.
smart00560	LamGL	7.71e-08	985	1053	61	132	LamG-like jellyroll fold domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCI64756.1	0.0	1	1283	1	1284
QUT77741.1	0.0	1	1283	1	1279
AHF12130.1	1.30e-271	1	1282	1	1287
QUB42054.1	5.33e-254	1	1282	1	1255
QUB76736.1	3.32e-253	5	1282	9	1259

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VTF_A	1.12e-39	44	631	17	540	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]
2W91_A	3.60e-39	99	731	51	626	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]
3FHQ_A	1.45e-38	44	563	12	472	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	1.94e-38	44	563	12	472	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]
3GDB_A	2.01e-38	99	731	202	777	Crystalstructure of Spr0440 glycoside hydrolase domain, Endo-D from Streptococcus pneumoniae R6 [Streptococcus pneumoniae R6]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A1L251	1.41e-16	133	626	130	587	Cytosolic endo-beta-N-acetylglucosaminidase OS=Danio rerio OX=7955 GN=engase PE=2 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
0.000231	0.999148	0.000151	0.000159	0.000140	0.000128

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001512_03091.