CAZyme Information: MGYG000000452_01072

Basic Information

• Species: Barnesiella sp002159975
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae; Barnesiella; Barnesiella sp002159975
• CAZyme ID: MGYG000000452_01072
• CAZy Family: GH85
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1253	MGYG000000452_26|CGC1	138363.47	4.3478

Genome Property

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

• Gene Location: Start: 3503; End: 7264 Strand: -

Full Sequence      

MKRNLFLFSGILALSLTANAQELKEEYMTWPNSQGLGEYASQWTPGEYLFEDENFYISRV
KPKARFRNANTQINETLTEETDKNLVFWVPIGTASGGNPNARPNGKFDSEVFSMWSYVTH
YGNWTAPQGWVPGGFADAAHKNGVGVSGVASIPWGSLSSDWATALDNMSKNATIREKVAK
FLHYHGVDGLGYNSEFNTSNTTMLSNVRALNEEVHKYLTEQGNPVAENFWYDGTNDNGQI
NFDQGLGSHNNETFGDGEHIRTSLFLNYNWWGTPLSTFNTGTINSQAPGRSLLDLYAGFN
MQGGDPSTWTLLEDYNVSIGLWGAHDFNMLWADRANYGSTDMSKQLGYQNVIEQFFSNGR
RNPIDKIAVFDRGSHHPNEGWFGMSAFMTARSSLSWDLATEPFITYFNLGNGQFFNWMGE
RQNDNEWYNIGVQDYLPTWRFWFASEFLGKTADKVVANGLDAKFTFDDAYVGGSCLRIFG
SAADEYLHLFKTAFTLASGDKITVRYKLIRGQADINLALSAVGDETTILRESGFKVLTVA
DSEADDEMWVEKTFTISGTLASLANRNIAMVALHFENAENLELYLGEFSITRNEMTTPAA
PVIKIAKVLASHYKGVDAKVIFEMNNTKPLGEPVYNLDVNASMFKLYAQQENEEPIFMGI
TTSWAGMYYSIPTNLQGSDRIRLGVAAVSVDMKSDSEISWSEYMDMGEYTTTDDIQIDKT
TIKPNESFEISYVDPRHDPADWKLLNSDGETVKQATNTTVFSVEDGISEIGGYDLQVTCN
GQTSTFGYYVQITSESVGALPEIYTLTVDGEETSAAEVKVDLDQTLTLGYTGRKADGASS
RGIEINDSWIGGNLNEAGIVGGKSFSVSAWVRFTTLPESSAFFSIENRAGGWPVNNWGWM
WSNITSEGRVTAYTVRGDGNASPVAVNYTFPNTIVSPNAWNHVVLTFEYNDQGQFRSLFY
LNGVLQESTWTYGSSASGKTEDWVPKASYDVSASDWFCFAGGRGEQPVTNNGIVDDLLIW
DGGMTQEEVNQVKAGLDASDLPDKVIAYWDFETDANDQNYFLSKGSKEGAKACSFKLVAS
TAQGSGVQTPQRPLYISGCPFIAGTAFQVETLPTWTAKRGELSESTGTDTEGSTKLTYSK
SGDYTVTLTLENTLGSDTKSYPVFLVDQKDAVEDGVADEMRTYTVEDLLFVEFAEAGAYQ
VGVYNVSGMLVAQEEATVAAGQHMSITLGAKGVYVVKVMKEGKVVRTVKVLNR

Enzyme Prediction     

No EC number prediction in MGYG000000452_01072.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH85	102	415	1.3e-42	0.9587301587301588

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4724	COG4724	1.01e-45	40	593	31	552	Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
cd06547	GH85_ENGase	5.11e-29	94	442	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.
pfam03644	Glyco_hydro_85	1.48e-17	106	412	4	291	Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.
pfam13385	Laminin_G_3	7.45e-12	860	1029	14	150	Concanavalin A-like lectin/glucanases superfamily. This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.
pfam00801	PKD	3.96e-04	1097	1158	4	69	PKD domain. This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AHF11930.1	0.0	1	1253	1	1253
QUT74450.1	0.0	1	1253	1	1253
QFQ13703.1	0.0	7	1253	7	1247
EFC71164.1	0.0	2	1253	4	1247
BBA29896.1	0.0	1	1249	1	1240

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VTF_A	7.87e-29	37	605	10	542	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	1.30e-27	32	605	8	537	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	3.03e-27	37	605	5	537	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
0.000343	0.998908	0.000235	0.000173	0.000155	0.000142

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000452_01072.