CAZyme Information: MGYG000003856_01265

Basic Information

• Species: Paramuribaculum sp900551515
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Paramuribaculum; Paramuribaculum sp900551515
• CAZyme ID: MGYG000003856_01265
• CAZy Family: GH85
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1279	MGYG000003856_49|CGC1	139980.43	4.785

Genome Property

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

• Gene Location: Start: 7558; End: 11397 Strand: +

Full Sequence      

MRKITLLFLCATAAIGANAQYLYQGDISSGTSADFYTYVKNWSSSQKITDDDNFYIARQK
PRARFTNTATQVKTNYTNGERRIMMWVPVNAKDSNGWPRSAMPSGRFESECFTMWSYIDN
YSDWSCSISQLYGGFADVAHKNGVGVAGMLWVDFGSPSAAQQVTLKGYSEMDPAMAAKVL
RYFGNDGLTYNSEFSTYSRNTFTPAMLKTLMGTVHENIMSNLTTLYNNTPNVSNYTLREN
IWYDGTQYATAAYNFDGGLTQRNVDGWYSSDGKYRSSLFFNYNWNSTNLKPSSTYASRGD
VTRLYAGINMQGGSAGLAHWQNFDASPVGLGLWGAHDYNYFWNARGDKGGRPEVIQECYQ
LTLENYFTGSSFNPLSAPTALASYSQAKFNNVGFHGLARYRSAASAMSWDLGYEPFITNF
NVGNGKFFNYEGKRMNDIEWYNIGVQDYMPTWRWWWATSFIGKTAATGMTAAFSWDDAYL
GGSCLSITGSTSSKQYLHLLKTKYDLKSGDEIVVRYKLIKGSANAYLSLSAEGSETTEIA
KSLITNETCPNSEEWQTLKLIVGTDVELDNKTLAMVALRFDNASNAQIYLGEFSIVRGSY
PAPTAPTVTKAEVKRNHYKGVDVKMIFNVPNTIEDKANGRPCYNDEVNNVFYKIYTQEEG
GEPMLYGITTTWAAMLYSVPCSSSKVRVGVSAVNFDHSQESEIAWSENWLDVPSTRVYSD
DITISKEIITPDESFVLATVDPMRSFTWQIIDKSGNVVAESDGESKEWTCNGLSSTGYYD
VKVIGPNNNSSDANASIVYSNRISVTPAATGRLPEILSITANNQTSDVDIMEGNDVTFAY
TGREADGFSSRGLHLGGVEFGVYADDLGLNGTQSFSVAGWIKMLALPEGSSKFFDIRASE
AGWTGGESGWQWSDINENGSFAFINNGFGVNSAGTGGPQTTKSAENLPTDAYFAVGKWTH
FAFVYTLSTSSFKREIYIDGNLVHTDTYTTNSVFNAAEGRTAQWWTDYTVRNRLSLGGGR
SAQVSNEIGGKRFEGVLDDFSVWNKAMTAEEVKASLEGLDKNNLPGSVLAFWDFETVADT
EGVIPCVGGSKNINAYYYDITGADTGAQGYPVNTKHDYTSGCPFLASTAFPVVTVANFQV
NGAKVGNATGNATEGSAVANYANSGVYSGKLTLTNELGSHTMALPVVNVKDLAGIDGIDA
DGDNIKTYVVNDILFVMADADGEYGISVYNISGMQMASRSMHIAAGETAAINFGVPSGVY
IVHITKDGVNAGAFKVLKK

Enzyme Prediction     

No EC number prediction in MGYG000003856_01265.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH85	104	428	8.9e-32	0.9523809523809523

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4724	COG4724	3.39e-32	106	595	98	549	Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
cd06547	GH85_ENGase	2.22e-20	84	455	6	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	1.53e-14	869	1053	13	151	Concanavalin A-like lectin/glucanases superfamily. This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.
smart00560	LamGL	7.75e-05	908	1049	12	132	LamG-like jellyroll fold domain.
TIGR04183	Por_Secre_tail	0.004	1209	1279	6	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
QFQ13703.1	2.92e-277	7	1279	6	1247
QUT74450.1	5.20e-263	2	1279	3	1253
AHF11930.1	1.77e-260	14	1279	15	1253
QUB42055.1	4.99e-247	1	1277	1	1244
QUB57152.1	1.05e-241	1	1279	1	1244

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3FHA_A	6.32e-20	92	517	63	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	6.32e-20	92	517	63	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]
2VTF_A	1.12e-19	92	522	68	461	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
0.000226	0.999159	0.000150	0.000157	0.000147	0.000135

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003856_01265.