CAZyme Information: MGYG000003768_00203

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Clostridium_A
• CAZyme ID: MGYG000003768_00203
• CAZy Family: GH85
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1638		182014.17	4.0714

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003768	1681255	MAG	Canada	North America

• Gene Location: Start: 39915; End: 44831 Strand: -

Full Sequence      

MKKRRKWRRSVISFMLASAMVLPGVGTAFAGGDTLPPREGEQGYKGEHQPSTHGYNRANI
LNWSPETDGYAEFMRSKVPLQERNEAFTATQANPLLDQEVESLSLMGDYGIGFFDSFQYN
DQFSQYLFNFWQYLDYHASWHGMATDPQPHDLFTPGNPEGQGKFEFGVVNLPNPAYTNAA
HKNGVKSLGCIFFPRTEHTEDFVYQDENGRFPIADKLVEIAKYYGFDGYFINAEEDLKPE
QMPIYEEFCRAMTSQGIYIQAYASCLYGPDNEDKWGTMDYGEKNAGKFSNWLKGADDETI
AANSLYMNPDPTKQQIDDSVTSMEALGLDPKKVVFQTLEAGQTGFSGKRGTLFNTLDENL
VPRTGLAFLGADTSKNHLDEQVFGHVGKNSYKYNKRDNPEYQKYVFARERTWWSGALDQP
YYEPFKTQQPDDYFPEELCQEILDATPDPYQTANNPKRGQANEGEDYQSWPGLAAFISER
SVIDGSNFYTNFNTGHGMQYFVDGQVSNDNEWSNINIQDILPTWQWWIETEGTRLDVDFD
YGEKYSPAFELNQVGGYNGGSSLVVKGKLDAENTLRLYKTNLEVKENTKISVTYNKTSAT
DNSKMELAVIFKNDPNTVVTFNVPQANQETDGWVTKDISLGDYAGEEIVSLGFNFDPGKE
TMEDYQMNIGELKVSDGSVAAPSVPTGLSIDESFETSETYISWDLDDYDAVQRYNVYMKD
GDGNRTYLGGTYDDIYYIKDLYDVQGDITIQVTAVGKDGTESAPAEVVLQQDKAVRDIQV
TQEAGKFDISWTNPETDYDHAEVTVTFESHPDDVYTAEAAKGETGINLEIPIMDGTNYTV
RVSLMDAEGQVIGFMDQTGQLEDYYCHPYDQDVRFANNLLSFAPPSVNDWSTMYAFYKGE
PIKFRSGNIGAIRGYDDMRGILINDDCGVVEVELEDYAGNRSEQIRVPFHKDGMTCAAID
ETAFPDPALLEAVKKVAETPADLLNVTTLDLSNSEVKDLTGLRYLRNLESLNLSNCTSLE
LIQEQDLSLNVHLKEINLTGCTQLKAASLADTTLETIVCEDVSALSQLYFLDVSGSRFDL
SEGTPEREFVDAVTAQAEGKGDFTVNLPNPVNLAYNMKATDTNLIMASYLFDGDTSNPMR
CVWIPNIPSHVTLQFDSPKEVLSYHMDVPNDDPSVGLKDFRLQGSMDGQQWTDLSVVTGH
TGESCTITVENPQAYTYYRFQIDGKVPASGPAKLTELEMTGYGDVTFTAGVQYDNQRPVA
YEKEMPETVRLEKQLGGTYDLTANLENNVTIHGNDLASLKGADFIDQDYDLDKVAQNKVQ
YIRVTGEDGSQLTNEISLDQDGAYTVEYLTYKDAGYQARTVATQTVYVRGVTTVLEKIIA
EAEELLNNGALDNTMEVVVEEFKAALAHAKEILAKDDATQQEINDATKRLLDVMAKVDWK
QGDKTALQVAVDIANTIKPDLDLYVEEGKQEFLDALAKGEELLASGNAWADEIQTATEEL
IKAMSNLRMAPNKDILNDMIDKASGLDLSDYTQDSAAVLTSALAEAQEVAADENATQEEV
DEAADTLEAAMNGLVFVNSDENNNTQDDTISNPDDTENAPVGDGTAPIKTGDAGAAGLAG
LAVMSALGIVWMLRKREK

Enzyme Prediction     

No EC number prediction in MGYG000003768_00203.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH85	106	501	7.2e-61	0.9936507936507937

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4724	COG4724	1.13e-78	44	676	23	551	Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
cd06547	GH85_ENGase	5.29e-55	102	532	3	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	6.97e-52	121	497	3	291	Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.
cd21340	PPP1R42	4.44e-06	960	1045	105	185	protein phosphatase 1 regulatory subunit 42. Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.
pfam07554	FIVAR	8.77e-06	1516	1575	3	69	FIVAR domain. This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Bacillus sp. Gellan lyase, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUH30609.1	0.0	8	949	3	958
SMF77083.1	9.03e-224	1	943	1	916
AWB44945.1	5.33e-214	12	1210	21	1198
QNO18499.1	5.01e-210	10	948	20	919
ALA43266.1	5.20e-208	6	942	12	910

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2W91_A	5.58e-57	121	777	78	640	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	2.02e-55	121	777	229	791	Crystalstructure of Spr0440 glycoside hydrolase domain, Endo-D from Streptococcus pneumoniae R6 [Streptococcus pneumoniae R6]
3FHA_A	1.33e-43	60	757	16	604	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	1.79e-43	60	757	16	604	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	1.91e-43	60	757	21	609	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9SRL4	3.26e-11	164	760	109	679	Cytosolic endo-beta-N-acetylglucosaminidase 2 OS=Arabidopsis thaliana OX=3702 GN=ENGASE2 PE=1 SV=1
A1L251	2.66e-07	164	255	142	235	Cytosolic endo-beta-N-acetylglucosaminidase OS=Danio rerio OX=7955 GN=engase PE=2 SV=1
Q8BX80	2.70e-07	164	255	156	250	Cytosolic endo-beta-N-acetylglucosaminidase OS=Mus musculus OX=10090 GN=Engase PE=1 SV=1
Q8NFI3	1.39e-06	164	255	164	258	Cytosolic endo-beta-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=ENGASE PE=1 SV=1
P0C7A1	2.37e-06	60	255	91	256	Cytosolic endo-beta-N-acetylglucosaminidase OS=Gallus gallus OX=9031 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
0.000496	0.998488	0.000302	0.000319	0.000196	0.000165

TMHMM  Annotations     

start	end
12	31
1614	1633