CAZyme Information: MGYG000004638_00516

Basic Information

• Species: F0040 sp000318095
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; F0040; F0040 sp000318095
• CAZyme ID: MGYG000004638_00516
• CAZy Family: GH85
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1008	MGYG000004638_9|CGC2	111146.7	6.5699

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004638	1864341	MAG	Germany	Europe

• Gene Location: Start: 45616; End: 48642 Strand: +

Full Sequence      

MRKFTLLATMACALLGLPSFAQTISAEKAASASVYDFSGFSETKILELFAKVKAEGRDYP
TLKEFESIGILPSDLAFVRSHMRPRNLLSQANRVVQSTREGRDLWMNIPMDAGKGGDVGY
PSGKFAADVYSMWNYTNLFGSWNHGLFTAPGCWVDAAHKHGTDIFSGIKFFDTTGGRNGS
SNAWEAFILAKTPEGKFTYAEPLINVLMYFGSDGINYNWEDSGFDRADIVAFHQELWKIA
AKKGFKNYHSGIYTSHSSLNEGDAVALFGDQTKGGKTHDLMLNYNAGNFTSNSAMKRSIE
TAQKSMGTTEGLYSGVWIVTMDRAWNNIKNNPDMNVCLWGEHSESRFMSYNKGKDAFDAQ
RNYQRLLERAFSGGNRNPLQRPAVSSSGNNWEQDGNKLPLQTFCGLAEFIPERSTVQGNL
PFRTHFNLGNGERFNYKGKKTAGSWYNMAAQDMMPTYRWLVYNAGTKNISTAIQPEFSHD
DAYIGGSCLELKGDASQATDIVLYQTDLKVGAANPVVKLAVKQLSGAGKSNLSAILKVGD
NWVEVPYGDVSGNTWEEKKLPVNLSQGSTITAIGLRVKDGSDKYLLNVGKLEINDDSFLK
PAELKDLLVEVKAETNKSMTAKLSWGVDAEAKTRKANDLLYNDEANIDHFEVLYKNGQDG
KVQVVGLTSQWAAVVPNFSLEDRAEPYFGVRAVSADLKQYSTVKWQKVTRDPKAPQIEEV
DPYGVSAMDPNCEGADIARQQRYVTDVTTTGATQDLNYHANGPVADGTQYADARNQVLKV
KQGQKVTLTIKCFDTSNLTKKDGLRWCFAGGWMDLDGSKSFNPDPIATNPKEGEQIFKVG
KVRAGTPEFETQGISTTFEVPADARPGRSRLRIVFSDAWFAGAFLPTGLHNKGFSIDFGV
EIEGTNAGRMPNDSHDQGAADEPDRIKDEKPNYPTAVNKVFDEVSRANYADDVLQFTNVQ
QAWVYGADGKFVVGSNGEAINTQDLVPGVYLVKMQNKGVIRSTKFVVK

Enzyme Prediction     

No EC number prediction in MGYG000004638_00516.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH85	123	434	1.5e-41	0.9492063492063492

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4724	COG4724	1.65e-34	74	596	49	552	Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
cd06547	GH85_ENGase	4.08e-23	122	465	19	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	2.55e-10	121	431	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	3.58e-05	964	1008	25	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	0.010	964	1007	23	72	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
BCI64641.1	0.0	8	1006	11	1005
AGB28382.1	0.0	30	1008	202	1190
QUT74553.1	0.0	4	1004	6	1016
QUB47476.1	0.0	30	1008	33	1006
QUB60778.1	0.0	2	1008	3	1011

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3FHA_A	2.70e-26	74	602	26	531	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	1.11e-25	74	602	26	531	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	2.00e-25	125	602	81	536	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]

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
0.000458	0.995594	0.003334	0.000240	0.000190	0.000167

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004638_00516.