CAZyme Information: MGYG000003658_01466

Basic Information

• Species: CAG-110 sp900546915
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; CAG-110; CAG-110 sp900546915
• CAZyme ID: MGYG000003658_01466
• CAZy Family: GH85
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1645	MGYG000003658_40|CGC1	182396.78	3.9424

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003658	2415548	MAG	United States	North America

• Gene Location: Start: 6107; End: 11044 Strand: +

Full Sequence      

MKDNMKRLLAFVLAAVMLVSLCPTLGLTAAAAEPGEEEAQGETSNSYEPWKHGYRFVDVL
NWSPETDNYSEELRAQVPLQERNEPFAATQANPNLKSDALVYNVAMGNYRSTDTAEAPWN
GNQYYDEFNYNLFKFWQYTDFIGSGGRPTTGFDSETASEQGRYEYGVVAIPIAAFVNAAH
KNGVRALGEYFIPRDPQYTEEWLYKDEDGNFPYGQKLIDLMNYYGFDGYFINQEGAFDSS
LFPVFKEMMAWMREQGCYIQWYDSINDDGGVSYLNEFNSQNSHWVQDEIYGRVTDSIWLN
YWWNLERIDNSVAHAEELGLDPYETVFLGIECGMGRFEGGELYSSGYCRSEATVEYLDDW
YLDETGNPKMSLALWGGDFVHEAYGKTDNVRYTDGYQWISEERERMWYTSPKESVLDHSM
DNVNRADVEVGEEVVWPGLSNFIAERSAINGTVFITNFNNGHGMQYFLDGEVSRDMGWSN
MNLQDFMPTWQWWVESEGTALNLDWDYGPEQEKVLLDGTTGSFDYEQIGAYNGGSSLAIY
GDLEAGKAQKINLYKTDLEVTADSTLSLVYNKPSADDGSTLALALIFQDAPENAVVLTVA
DSGKQTSGWQPVEFDLSAYAGRNIAAIGVQVLSETDVTGYQLNLGQLKLSDGRSYAPEAP
EGFVVDKVFDTTGEIELAWTLNEDYDTVKLYHVYAVYADGSERFVSGAYADNLYIQNLED
RDQVVGLNLRAVGADGSESEPAFAALQTEGNVTNVRTVSRDGKLVVTWDEPEVDFDQVQV
ALSYWYSDRTAPASVTVDKGVKTATLDIGLEDSSRYLLTLTTTGENASTVYYFGELADNY
SEPYDGEVRVHADGGRFSLTTPLAEDWTSLYLTMDGVTTTYSRHSGNKLYDIAMPEGLTL
ASVVVEDMNGNRSTPVTFRFQDGQLVDLDETVADEIIPDEVLRKALFEKAGGNTYGDLIA
LSGELDLSGLEIQDLTGMYLLVNVAELNLSGTQISDLSPLTTLTNLKKLVARDVELTALA
AGVLPANLEELDLSENSKLTQVEEGVIASLAGLKTLNLSDNTALTTLYLDNTPAMTVNVS
GCTALQQLILTGTQMSDFDITGLSQLTHFYGNNSNLAMLTAGEAAEYPALDTFDLSGSKF
DLSEKTPERALIDGLAEIANLKYDGQRPEIIYAELPATLEVWKNSGDIRTMDYFENIYLH
STTVRGTLYSSIVEEDWIAEDYDAAGLCAVPSNVYVEIRDEEGNYINEPEQPDDLVDVET
NRALNATVLGYTAQNTGEEASMLFDGSYSSKWCTSGASGWVAFHLAEAVQVGRWVTAHAQ
ANNEPMEFNTVDFELQVLNTEAVGMSEEEFLASDGKNDAAILGNDANWTTIAHVTDNHEA
IVDQELETAAPTAQIYRLKVNMGYGDTQWGAIRFQELELYAASNVVRDYEGILSTEIPGT
YQVAFKKGLQTTLNTMEVIVESAETKFQDVKTDAWYYDAVDYVASRGIMIGTSDNTFSPV
AKMTRGQMITILYRLAGSPAVEGTVPFTDVKENRFFYQAVVWAYQNGIGKGTTLTTFAPD
SDMTREQMVTFLYRYSEMAGVDVSEKADLSSYTDASAISAYAVQAMAWAVAEGHIIGVTE
TRLAPRGDAIRAQVAEMIMRYLEEA

Enzyme Prediction     

EC	3.2.1.96

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH85	121	467	7e-68	0.9682539682539683

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4724	COG4724	1.59e-93	60	651	40	551	Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
cd06547	GH85_ENGase	1.59e-69	105	498	6	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	2.53e-67	125	463	2	291	Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.
sd00033	LRR_RI	6.35e-19	964	1137	27	224	leucine-rich repeats, ribonuclease inhibitor (RI)-like subfamily. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions.
sd00033	LRR_RI	2.23e-17	986	1137	3	152	leucine-rich repeats, ribonuclease inhibitor (RI)-like subfamily. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SMF77083.1	5.85e-201	6	913	3	915
QNO18499.1	3.87e-187	37	917	48	917
AUS27834.1	1.72e-186	48	914	49	911
AHM67228.1	1.72e-186	48	914	49	911
AIY08018.1	1.72e-186	48	914	49	911

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2W91_A	4.08e-61	58	742	19	628	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	9.11e-60	29	742	136	779	Crystalstructure of Spr0440 glycoside hydrolase domain, Endo-D from Streptococcus pneumoniae R6 [Streptococcus pneumoniae R6]
2VTF_A	1.19e-59	58	732	20	607	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]
3FHA_A	2.65e-59	58	732	15	602	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	3.57e-59	58	732	15	602	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
C6CRV0	9.44e-20	1434	1640	1249	1457	Endo-1,4-beta-xylanase A OS=Paenibacillus sp. (strain JDR-2) OX=324057 GN=xynA1 PE=1 SV=1
P0C7A1	1.53e-16	58	661	90	614	Cytosolic endo-beta-N-acetylglucosaminidase OS=Gallus gallus OX=9031 GN=ENGASE PE=1 SV=1
A1L251	3.41e-16	163	591	142	495	Cytosolic endo-beta-N-acetylglucosaminidase OS=Danio rerio OX=7955 GN=engase PE=2 SV=1
P19424	8.64e-15	1467	1642	41	214	Endoglucanase OS=Bacillus sp. (strain KSM-635) OX=1415 PE=1 SV=1
P38535	2.42e-13	1467	1645	908	1084	Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 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
0.000841	0.998048	0.000548	0.000219	0.000173	0.000165

TMHMM  Annotations     

start	end
9	31