CAZyme Information: MGYG000004390_01512

Basic Information

• Species: Prevotella sp002265625
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp002265625
• CAZyme ID: MGYG000004390_01512
• CAZy Family: GH85
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1248	MGYG000004390_26|CGC2	137467.26	4.8394

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004390	3321071	MAG	Israel	Asia

• Gene Location: Start: 25752; End: 29498 Strand: -

Full Sequence      

MANFTHKTLTLAAGLMLSVMSSNAQQLREGYIDAGKDTGSEKFQFALQNWQNNHRLSKDD
NFYISRVKPHVRFRNAATQVRDLTAENDKKLIAWIPVSDPAFNALPNGVFDSEVFSMWSY
VTHYGDWTASLGRIPAAFLDAAHKNGVGVSGVASIPNASLGGDWLKMITAMGSADAELAA
KFFRYYGINGMGYNSEFYDRTGVVEDLRDFHADLVKAAEKNDPLFENFWYDGTNDGGGIS
FDQGLGSHNEETFGDGENRRTSLFFNYNWNKTYLMDKSVTKAEEMGRNPLDLYCGVNMQG
GEPRYTSWSLLPSRRLSIGLWGAHSNNMFWESRGEKGSNPDVKQNTYLQRIERYFTGGTR
NPANCPSIVDRHACNADNFAWHGMSTFMTARSALSWNLSEEPFITYFNLGNGKYFNLEGK
RQNNNSWYNVGMQDYLPTWRWWFASKLLGNKATDVPENGLDANFTWDDAYFGGSTIRLTG
STADEYLHLFKTEYALKAGDVITFKYKLAGGTSDIDLLLSAKGSETSAKTYNVLETSQKA
DDEEWIEKKFVVGTDFDGKDLALVALHFKNAKNLSLLLGEFSIVRGTSAAPAAPVITSSD
MLYNSYAGMDAKLIWNMENNKAVDEPCYNIDVKTSYFKLYAQEEGLEPVLCGTTTSWAGM
FFSIPVTNKAAKVRLGVSAVSLDQKSESQIAWTEYNTPTSYMLSDDIEIDKTTIKPGEKF
TMGYVDPVHKEGAWELIDEEGNSVYSGNGKTVTVENGIDKIGSYTLKLTGDVSGLEKVRE
YPGYVQITDNSVGALPEIYTLTANDSEEPISIKVGDQVKMKYTAREANGASSQGVDLQEY
RYGAKCSDLGITGTKSFSVAFWLKINELAEGETQLFSVANKLDAWPKTDWGWIWVNVNQD
GSVGSFTWRGADRTSNNEIRYKYANSKLPVGTWAHVALTFDYNAEGALRGELYINGKKQE
ITGWNRQANGDTYFNTDPGYQANPYNITDMQVLAVGGDAAFRSGIKGAVDNLQVWDHALT
ADEVQTTMGTIDSNNVPAGIIAFWDNEKTANDDFTFASVGQKKGVQAGLHAYTPTGDEGQ
GEFVWVAPKYTSGCPFIAGTAYQVETVPTWSAPKADIISQSGNDTEGEAVLSYEKEGVRN
VTLTLANSLGKDQRVFSAITIGSGTGIDQLGNGELKAYTVGEDVIVEFAEAGNYDVQIVN
VAGQAQARKAAAIAAGGNMQVRLANAGAYILTVKKDGKVVRTMKLIRK

Enzyme Prediction     

No EC number prediction in MGYG000004390_01512.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH85	108	415	1.3e-54	0.9492063492063492

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4724	COG4724	9.83e-46	110	583	99	549	Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
cd06547	GH85_ENGase	1.47e-34	109	442	21	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	4.57e-26	110	412	5	291	Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.
pfam13385	Laminin_G_3	2.55e-15	853	1025	15	151	Concanavalin A-like lectin/glucanases superfamily. This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QFQ13703.1	0.0	11	1248	7	1247
QUT74450.1	0.0	7	1248	3	1253
EFC71164.1	0.0	11	1248	9	1247
QUB60779.1	0.0	11	1248	7	1250
QUB72358.1	0.0	11	1248	7	1250

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VTF_A	1.14e-35	109	681	80	608	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	4.59e-35	109	507	75	451	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	4.59e-35	109	507	75	451	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]
2W91_A	3.21e-25	110	656	80	593	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	6.19e-25	110	656	231	744	Crystalstructure of Spr0440 glycoside hydrolase domain, Endo-D from Streptococcus pneumoniae R6 [Streptococcus pneumoniae R6]

Swiss-Prot Hits     

has no Swissprot hit.

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
0.004201	0.989281	0.002882	0.001370	0.000951	0.001276

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004390_01512.