CAZyme Information: MGYG000002042_01365

Basic Information

• Species: CAG-110 sp900762935
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; CAG-110; CAG-110 sp900762935
• CAZyme ID: MGYG000002042_01365
• CAZy Family: GH85
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2025		217248.19	4.352

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002042	2052895	MAG	China	Asia

• Gene Location: Start: 6953; End: 13030 Strand: +

Full Sequence      

MKLSFLKRATSLLCAIALLAGCFAGVTVSVSAAGARLGYWPEPLDIPNQFYYENETLQPY
GSCFLIDELKNWSPDNDPDARYNRGSIALRDRWMGPNVNPLASRDAKVMPLAMANARASE
APSQGGDGDFVYAFNNFQYVDIYNFWGGSSAEGPIAIPSPEVIDSAHRNGVPATGTIFIP
WGDSAYGNQFVKEMVEKDENGHFIAADKLIEIAQYYGFDGYIFNAESGTGVAGFKEFLAY
LQENKPDNFTISWYNGSGSLSAGSIKSWMQDGDTRITDEWWLDMSGSGNVDGTIAAAQQT
GVNPWNIHSTWEYWPMAGNAKGGRYQTRLDADGLLKCSLGILAPTTSLTSSKDSDDFINV
QDQKLWVGPSLDPSSTYRPEYEFCGFANLVADRTPIIGTDFATTFTTGNGYRFYENGAVV
GKENGWYNRSLTDVLPTWRWIIDSEGQKLSAKIDFDDAWYAGTSLKLSGAMDAGKANHVK
LYSCQLDLTAASKFSITYKTGTAGVDLSLGLCFGDTYDDGNFKFYPVTTTANGEWTTATV
DLSADAGKRAIAISLKLSAPEGVSDYALNVGRMAITTDETAPAATTQVTLDEVIYPTDKT
MEARVYWEKASNAFMYRIFRVHADGSREFVGATPSDAFYLGSFEKDGSEKSCKFEITSYS
ENGIKGGTQTFEIDWPAEVEDGFVPYFDEGENIALKMPAVSSVRTADDGSARLINDGVIP
QSKWCADTTRGYAVIDLGENKTIQRWVVYHANCKGAGESVDMNTVCFDLQYAPDDGKPLL
TGDDNESRTRVAALTYTKADEVTGNKQDVTDRNLDAPITARYVKLNVTQSDSSAWHAIRI
YEFELYEKACPYGNTASPYERNVSVRNNAGAADTVVVDNVPMIYSSGTYSDKNGTFHEDT
GKVRLFKDLTSTEPIAVVQATQPNESYKQRSVGIAKFENLELDANGGRLFYDVLDGSSGV
VKNSRRASVAYAPESGTAIKTPSGATLTRTTGGEQLRKQYATLTVTGVEEGAVLKVYASE
TADSPILHSLPAKADGIIRQSRVPLDRNGGKVYYEIHKEGKPDSQRYALDYADPMALTAD
PEGLNQLIARCAAVRQADCTTATWPAFSEALASARTVAAGTPTGTQAEAARTALAEAYAA
LRFRNSAQRLGELCELFEQTYQESHYTADSFKTFRDTLTEAKAMVSGYDSSAYQVEQMRI
RLEAAVRGLVEGSGGVTGVIVTPATVALDKGSSGFKFSATVEGEGEISQEVTWTVTGNTD
DFTQMVRNTLYVGPNETAATLTVTATSVTDPTVSGTAIVTVNGNGGEQPEPPTPGDSKLL
SSGADILGVGSTKGTTASDGANYAFDGDYSTKWCSERTPNWVVFDIKTAANPDRLKITHA
GGATPPEDERFNTNDFALQILNTEKISEEEFLAKSETERAAIMGDDSYWTEIKGYKANEA
NVTDDPLTVEGNIRLFRFVVTDGDDNWWQGPDTLRIYEIEVYGKKAGAPAEEIAVSITPE
TMKVERTPGQKGQFTATVTGTDNVEVTWSISGNVSEGTMITNGQLFIGEGEKAGTLTVTA
TSVADPTKSATATVTVVDPTYTVTVDASVTNGTVTPSAGEATEGTEITLTVTPAEGYRLR
TGTLKVNGTVMEDLKFTMPGENAYITAEFVKIADLQTAIAQAADLTESAYTSSSWAEVAR
KLAAAQTVLNRTDASQTEIDAAANALTAAVNALVYRGDKSELNALIAEVEALNEEDYTPA
TWAGLAEKLAAAKTVAGNADAVQSEIDAAKEALAAARDALLARADKTALNELIAEAEALD
ENGYTEESWAKLAEALAAAKTVAEDANAAQDAVDAAAAALADAKAGLEARVTVNKDALNA
LIAQAEALDENGYTEESWAKLAEALEAAKTVSANPDATQEEVNAAGEALEKALKALEASG
NADALTKLIEEAKKKDLSKLTDKSAAEIRDAIAKAEEVIAKRGTQEKLDGAYAALKSALD
HAAKKEAPKTPSTGDEMQLLLPLVGMMSAAALAVVTVLNKKKHAR

Enzyme Prediction     

No EC number prediction in MGYG000002042_01365.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH85	113	414	1.5e-55	0.9968253968253968

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4724	COG4724	9.38e-129	58	576	28	550	Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
pfam03644	Glyco_hydro_85	2.96e-74	125	410	1	291	Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.
cd06547	GH85_ENGase	2.52e-65	108	446	1	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.
pfam18998	Flg_new_2	2.04e-09	1581	1653	1	74	Divergent InlB B-repeat domain. This family of domains are found in bacterial cell surface proteins. They are often found in tandem array. This domain is closely related to pfam09479.
pfam00754	F5_F8_type_C	2.80e-05	698	839	1	124	F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ASM70437.1	0.0	26	1211	25	1212
ABG82927.1	6.55e-189	22	1061	16	1019
ASY50962.1	1.75e-188	47	1061	36	1019
BAB80524.1	1.75e-188	47	1061	36	1019
AWS25459.1	1.75e-188	47	1061	36	1019

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3GDB_A	3.83e-107	45	840	149	937	Crystalstructure of Spr0440 glycoside hydrolase domain, Endo-D from Streptococcus pneumoniae R6 [Streptococcus pneumoniae R6]
2W91_A	3.14e-91	55	685	5	644	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]
2VTF_A	3.41e-85	59	673	11	621	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	3.41e-84	59	673	6	616	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	4.62e-84	59	673	6	616	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
A1L251	3.98e-23	42	511	44	489	Cytosolic endo-beta-N-acetylglucosaminidase OS=Danio rerio OX=7955 GN=engase PE=2 SV=1
Q8NFI3	3.36e-18	37	515	63	517	Cytosolic endo-beta-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=ENGASE PE=1 SV=1
Q8BX80	1.16e-16	37	515	55	509	Cytosolic endo-beta-N-acetylglucosaminidase OS=Mus musculus OX=10090 GN=Engase PE=1 SV=1
P0C7A1	1.51e-16	25	497	55	488	Cytosolic endo-beta-N-acetylglucosaminidase OS=Gallus gallus OX=9031 GN=ENGASE PE=1 SV=1
E8MGH9	4.10e-10	1785	1994	1667	1887	Beta-L-arabinobiosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=hypBA2 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.004783	0.049491	0.944662	0.000535	0.000378	0.000150

TMHMM  Annotations     

start	end
12	34
1999	2018