CAZyme Information: MGYG000003856_00811

Basic Information

• Species: Paramuribaculum sp900551515
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Paramuribaculum; Paramuribaculum sp900551515
• CAZyme ID: MGYG000003856_00811
• CAZy Family: GH85
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1301	MGYG000003856_26|CGC1	142187.74	4.8635

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003856	2220083	MAG	United States	North America

• Gene Location: Start: 1324; End: 5229 Strand: -

Full Sequence      

MKKALLYAASLALATMPAAAQKLGEGYVTWPESSDFGSYVEQWTNNNGAITINGSTWEDA
NFFISRVKPKERFYNVSTQVYPGLTQYDASTGAGTDKRVEFWVPIGTEHRSGVKLNALPD
GIFDGETFSMWSYIDNYGNWNAPFGFTPGVFADVAHKNGVGTHGVAGIPFANYTTAWRNC
ISKMTTLGAEKVGKFLYYFGQDGLGYNSEWGSPGATSLGLVNFHNGLKTYMADRNPLWEV
MWYAGVCDGGGNAFDTGISRFTGIFQGASLFLNYNWNSVSTMTSSIQIAKNNKKSPFYIY
AGMNMQGGEPKSGSNYDLVKDYQYSIGLWGAHMVNMFWEGRYAKGSSESAKAAYYQEEIE
TWFGNGPRNPAIKLTPTLNRTHRPNSTWAGMSSMVSARSTLSWDLTKEPFYTFFNLGNGG
FLNWKGERMNDNEWYNIGVQDYMPTWRFWFAPTWMGGRSTSLQASDQKMNAVFTWEDAYV
GGSCLKVSGTADTEFLHLFKTNFTVDGSTKVRVTFKVLGGSSDVALCFNSTSAPGKDPGK
TLPLINKADCEDLEDQSFNDGWITKEVSIGSRFTTMGVIALKFTNAENLELLLGGLEVSR
NDNFATPAAPQITLSKVLAYNNSGVDAKLIWKMANSKASDEPCYNSDVNTSMFRMWAQQE
GGEAVNMGLTTSWAGIIFAAPVDNSGTKKMRFGVSALSVDTKSESDITWTDYLTLPAYKT
VDDITISKSIIKPGESFVLAFADPVHASATWTITDEAGATLWSGSGVSVECPGLDGIGAY
NLTVTSGSTSQEFPRYIAISSNAVGALPEIYSLAIDGTTTSSDASPVQIKVNDTKTLSYT
GRPADGSSSRGIDLNENWFGVQCGEIGLGSYKSFSVAAWIKYNELPTGRSNFITVEDRIN
GGWPYNNWGFFWSRINDEGRFIYDGIDTGYGWRVGPGTEGRRMFYRYNDAKVDVGAWTHV
AIVFEYNSSQQIRSHFYINGKKQMVSEWCSCLKSDFENKCGGVWSHLVTVAKKISGADYG
ENTYEPTFTSTTYPITDGMWISFGGSSQDISAVKGCVDDFQVWGKAMTDDDVKKSMEGLD
KSNLPAEVLGYWDLENEPASDYGFVGATGANATNKTPKAYWCEIPSQGENSNTRVVGQPT
YLVGCPFIAGTAYPVVTTPTWETRRAEINGSGTGESGSATLSWTKAGDYSVKLRLANGHG
EATMDYPVVKVSDSTQGIGEIGQDGEGFTTYTVEDALFVEFDADGAYTVEVYNMAGMLAA
QKAVNVVAGQNVSIALGQPGVYLVKVTRDGQLLRTVKVIRK

Enzyme Prediction     

No EC number prediction in MGYG000003856_00811.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH85	123	420	1.9e-37	0.9365079365079365

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4724	COG4724	9.47e-31	123	571	99	518	Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
pfam03644	Glyco_hydro_85	7.64e-21	123	419	5	291	Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.
cd06547	GH85_ENGase	1.14e-19	123	449	22	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.
pfam13385	Laminin_G_3	9.12e-11	872	1073	17	151	Concanavalin A-like lectin/glucanases superfamily. This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.
TIGR04183	Por_Secre_tail	6.41e-06	1237	1301	11	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AHF11930.1	0.0	1	1301	1	1253
QUT74450.1	0.0	1	1301	1	1253
QFQ13703.1	1.11e-314	12	1301	12	1247
EFC71164.1	1.00e-287	20	1301	22	1247
QUB76735.1	4.59e-270	20	1301	20	1250

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VTF_A	5.83e-27	69	698	30	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	9.51e-26	109	516	64	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	9.51e-26	109	516	64	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]

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
0.000297	0.998949	0.000206	0.000183	0.000175	0.000156

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003856_00811.