CAZyme Information: MGYG000000452_00827

Basic Information

• Species: Barnesiella sp002159975
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae; Barnesiella; Barnesiella sp002159975
• CAZyme ID: MGYG000000452_00827
• CAZy Family: GH85
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1013	MGYG000000452_18|CGC1	112165.83	4.4788

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000452	2678398	MAG	Sweden	Europe

• Gene Location: Start: 9196; End: 12237 Strand: +

Full Sequence      

MKKFTVFGAALLLGTAVNVQAQDVTYPASASTEIFDFTPWDDDQLLVLFAKAADEGRKYP
TKEEFEAAGFNLDLEFSRSHVRPAAIMEDATKNIVPDVYPTRRLWMNIPTGQGDLIGGYP
SAEFHNDVYSMWNYTNLYGAWNHSILQAPGSWADAAHKNGTHMFSGIKFFESWGTTSSAY
IDFITAKNDDGSFRYVDALLNALIYLGLDGINYNFEDEGYKQTDVVNFHKALYKRADEIG
FDSFHIGIYTSMSSLTSYNLDAVFGTKETGKTADLMLNYAANDFSWNMDSSVTTAEQAMG
SADGLYAGVWMVTLNRRWTALNQDEQSKKCGVCLWGEHKVSRIFQYTVGNSLMELQSNYQ
TLLEKVFSGANRTPLNRPVVSNSAGNFQVSPSVGIDQQLTSFCGLASFIPERTAIQGDLP
FNTNFTLGNGDFYAYKGKKTLGSWYNMGQQDYVPTYRWVIYNTGTETLSNDIKAEFTHED
AYIGGSSLRLKGTPTSTGADVWLYRAKLNVSAGNPKAKIAVKTGVKGSNPSNLYLILRKF
DDSNWMEFPVGDLAGATWEEKEIALTGLNAGDVIEYIGFRVKGSAANDDYKIMIGQLMLS
DDRASSAPASIDGESIIAEVKEETTSSLSVKLTWKVDPTGFSPARQDYGMIYNDEVNVDH
FELFYKNGEDGRVSEVGRTSTWSAYVGNIQFENENDDPYIGIRSVSKDMKTYSPIEWVHI
ARSTETLPEASSSQYPPTYINSAADGYETALRTRYIAEVKTTGATQNIDYSRSDSVGGEN
YLFAEDYVLKVEQGQKVTLTLKGANLDDNLKYCFGVAYMDWDINYEFDATTDEKLFEVGQ
LNAGTDSIVSGSTFIINVPEDAAVGTTRLRMVFSDAWFPHPGPTGGTQKGFSIDFPVEVS
GTNPGREPAASYTEFRDQGVADEPEMNEVSGIENVVNGENGLASVSSMYPTVTSDMIYFN
NVEKAWIYTADGQFVKFLKNNPESANVSDLSAGVYVVKMQNGRVIRNQKMIKK

Enzyme Prediction     

No EC number prediction in MGYG000000452_00827.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH85	122	433	1.8e-41	0.9492063492063492

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4724	COG4724	6.49e-31	118	602	90	552	Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
cd06547	GH85_ENGase	6.57e-24	114	464	5	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	2.11e-08	118	430	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	8.18e-07	950	1013	5	72	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	0.001	948	1011	1	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
QUT74553.1	0.0	1	1012	1	1019
BCI64641.1	0.0	13	1012	18	1006
QFQ13761.1	0.0	9	1010	12	989
QQR07923.1	0.0	30	1012	26	1008
ASB37183.1	0.0	30	1012	26	1008

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3FHQ_A	6.32e-21	73	707	26	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	6.43e-21	73	707	31	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]
3FHA_A	1.10e-20	73	707	26	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]

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
0.000292	0.998981	0.000168	0.000190	0.000172	0.000153

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000452_00827.