CAZyme Information: MGYG000000215_02176

Basic Information

• Species: Prevotella stercorea
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella stercorea
• CAZyme ID: MGYG000000215_02176
• CAZy Family: GH85
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1019		112120.08	6.0483

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000215	3117648	Isolate	China	Asia

• Gene Location: Start: 322; End: 3381 Strand: +

Full Sequence      

MKKKVLLSTLAMAAFMSAMPSVNAVAADDSKASAVYDFSGFNDVNLINLFYKAYKDGRKY
PTEAEFAAAGIQQSDIAFIRSHVRNKGIIDRSGRLIKDTYEKRNLWMNIPMGFGKDGSVG
QPSKNFDSDVYSMWNYTNIFGSWNHGFFSAPAAWTDAAHKNGSDIYSGIKFFDTTGGRPD
GAGSWIQYCTEKDANGNFKYVDAIINCLMYFGFDGINYNWEDAGYNKTDIVNFHRALWKK
AAENGFDNYHSGIYTSQSSIASAMQAKWLLGDKEGRTHDLMLNYSSGDFSYQLSSSAKVA
IDATGSTDGIYAGMWFVTMNRGWNRLNADDYSKQMNICLWGEHASSRIWSYTSGLDPQDR
QANYQYMMERLMSGGNRNPLERPAVSNSGNDWEVERGSSNKPLQGFAGLATWIPERSSIF
GNLPFGTNFSLGNGDRYAYKGKKTAGKWYNMATQDVVPTYRWLVVKPGTQTVSTDVDATF
THADQYIGGSSLLLTGKATAAGTDVVLYKTDLNVSAGNPFAKIAVKSGKEGTNASSLYVI
VQKADGSWVEAPVGNVTGANWQEVKVALNGVSKSDVIKHIGLRVKGSDNAYKMYVGKLEI
NDDVKATPAAIKNLTVEVKEETKTSLTAKVFWGVDAKAQKRAAWDLVYNDEANIDHFEIL
YKNGENGKVSEVGRTTTWATLVNDIQLETTDEPYIGVRSVSTDLKTYSSVEWVKVTRGDI
ASLPEANPESYPISQMNPDCDGAGIARQQRYVTDVTTTGADQNLDYHTDHPVADGSQYDD
QTARVLKVKQGQKVKLHVKCFDSSNSTWEGSKKVDGLRYCFAGGWIDFNGDYNFYPKTMQ
EDPANGEMLFFAGTIRQASPQFETTGIDCEFTIPSDAKPGSSRLRIVFSDAWFAGDFLPS
GLHNKGFSMDFSVEITGNNPGRKPAADIHDQGVADEPENLTGGVVDAINSASQGVSKVEA
ADGKFNFQNVEKAWVYDASGVLVKYLVNPTSFDAQQLASGVYLVKMQNGNIIRSQKLVK

Enzyme Prediction     

No EC number prediction in MGYG000000215_02176.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH85	121	437	1.7e-41	0.9587301587301588

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4724	COG4724	7.03e-29	120	603	90	552	Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
cd06547	GH85_ENGase	3.04e-25	121	464	17	335	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	2.14e-11	122	434	1	291	Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.
TIGR04183	Por_Secre_tail	1.14e-06	964	1019	14	71	Por secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.
pfam18962	Por_Secre_tail	6.01e-05	961	1018	6	71	Secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber have on average twenty or more copies of this C-terminal domain, associated with sorting to the outer membrane and covalent modification. This domain targets proteins to type IX secretion systems and is secreted then cleaved off by a C-terminal signal peptidease. Based on similarity to other families it is likely that this domain adopts an immunoglobulin like fold.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AGB28382.1	0.0	35	1018	206	1188
BCI64641.1	0.0	30	1019	32	1006
QUB82357.1	0.0	1	1017	1	1007
QUB64521.1	0.0	1	1017	1	1006
QKH88107.1	0.0	1	1017	1	1006

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VTF_A	4.49e-24	117	668	72	575	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	1.02e-23	117	668	67	570	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	1.02e-23	117	668	67	570	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     

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
0.000224	0.999057	0.000170	0.000207	0.000173	0.000149

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000215_02176.