CAZyme Information: MGYG000001097_01025

Basic Information

• Species: Prevotella pectinovora
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella pectinovora
• CAZyme ID: MGYG000001097_01025
• CAZy Family: GH85
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1086		122670.27	6.2978

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001097	3372203	MAG	China	Asia

• Gene Location: Start: 130; End: 3390 Strand: -

Full Sequence      

MKNTITTIAVALITCMTATAQRTPKHDFDFEKVTVGGEKKEINWKNLYRFFDSWQPGTPP
CGLSRIDDEFFISRQRPLKRITDGDYQVRNDVEAERRMFLWTPLDDPTTKWKALPRYCFE
GDNFSMWQYIDTHGNWSAPWLRVSAGISDAAAKNGVTVGCVLSVPWDAEVGDTVKADYSQ
TLMKLAERNTDGSFRNSLKLARLMKYYGINALGVNSEFNTDKATMMRLQDFFIDVHRKAK
DIGWTFELQWYDVTDDNGELSLDCGLGEQNKRMFGTKDSIATDRLFANYNWTDDILKASA
KYARSLGRSPYDYYAGFDIQGRAWNNKHWQDLVNNDISVGVWGAHSQNLLHQSATDDGTA
DVIIQKAYLLKQELSFSGGYRNPALLPEVLTDCSLSNADLRTFHGLARLLTAKSTIQQVP
FVTRFNLGNGLHYYKDGKVAFDSKWYNLNTQDYLPTWRFWITDENDRTTAENIGSFVNAE
LSWDDSYTGGSCLQLHGATKFSRIKLFKTKLLTEPSYELSLTYKMPKGRDTHARLFVALK
GNTSEYKEIALPAAKRENTWTTFKTPLKKLGLKAGDEVAMMGIVVEGTGDDYVMNIGEMA
VRNPRQRFNTVKPWIKEIEVMRGWNNTVDFKMRYASKEEKGDEKTYNDEVGTWYYEIYFQ
QKGRPQQLLTATESWAAYVIGAPLAEGCKRECRFGVRAVSPDGQQGSDIAWSDYRVIEYN
ALNSTPAIDRERIKPGEAFTIYYKDNMMPPAKEWRIIDALTDKVVAKAENSTSITTSIDK
DGIYDLMTINGDGSQTMTRGLVKVSPLSSTSKALKLNDPYMLTIPAEALPGLEYSVALWV
KADDWTHDKQGTNIVSKNSIADKWPFNNWGDLWVQVCPPWTDEKSGKEHPANEIMYRTMG
CGGDIEGHGDMTTDGYSIPAGVWTHIMVTQDKEKVQRVYINGRLVAGPLQMPESTRRELM
PADNKRIDHNAVADIRIGGSGVYKAGLNGAIDDVQIWNRALTAEEVLRCMRGFTDKEVPE
GLSAYFTFEETDADGVFPNHGKTPGCQARIMRMADSGGEYTGKAKYVDRNGETHIKSQAS
TSDRPL

Enzyme Prediction     

No EC number prediction in MGYG000001097_01025.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH85	119	434	2.2e-57	0.946031746031746

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4724	COG4724	1.68e-58	119	603	99	551	Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
cd06547	GH85_ENGase	2.12e-41	123	465	26	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	7.10e-35	119	430	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	5.63e-17	822	1006	7	150	Concanavalin A-like lectin/glucanases superfamily. This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.
smart00560	LamGL	1.35e-04	919	1003	59	132	LamG-like jellyroll fold domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUB42054.1	0.0	9	1075	9	1097
QUB72359.1	0.0	1	1075	1	1101
QUB76736.1	0.0	1	1075	1	1101
QUB82359.1	0.0	1	1075	1	1101
QKH88109.1	0.0	1	1075	1	1101

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VTF_A	3.01e-44	54	601	24	528	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	2.95e-43	54	587	19	508	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	1.05e-42	38	703	11	622	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]
3FHA_A	1.28e-42	54	587	19	508	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]
3GDB_A	1.38e-42	31	802	155	876	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
0.000247	0.999119	0.000155	0.000163	0.000148	0.000136

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001097_01025.