CAZyme Information: MGYG000001604_00686

Basic Information

• Species: Barnesiella sp002159975
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae; Barnesiella; Barnesiella sp002159975
• CAZyme ID: MGYG000001604_00686
• CAZy Family: GH85
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1262	MGYG000001604_5|CGC1	139986.8	4.5688

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001604	2665014	MAG	China	Asia

• Gene Location: Start: 34928; End: 38716 Strand: +

Full Sequence      

MKAPKLLLSVLACAAAVGSYAQNVPTHDSYVMPFDDGKSKPFSEYFRNWEPGTPLSEDEN
FYISRVPLKQRFENSATQVDPTMTTARKFCLWTPMGISDTYWQSLPRYVFDGDNFSMWSY
VDSQGGWSLPWVRVPGAYSDVTHRNGVANSGGLVFFDSWGGDNTESNNSINMLVEKEGGQ
FKWVEKFVKFLRYYGVDGIGINPEGPVPQASALQDFFIQCREYAESIGWQFHVYWYGTNT
NTGSMDLGHVFNSGKANWLWKNNKQVTDMYMLNYEWSNYASSSVSYAESIGANPYTLYAG
YDIQGNWLGRGSWTTLKNTKMSIAFWGNHTTNMIYQNSSEFGSGDEAVQACYLEKQEQVF
SGGNRNPAKRPAVANGITSSSEVAMMKFHGIAEFLPARSVLQELPFVTRFCLGNGKSFRD
HGVVTFDHKWFNVGVQDYLPTWRWWITDDNKNVPNDPITCGFTFDDAWFAGSSMQFSGAT
AVSNVRLFKTNFNVSESDDVSMVVKLKSGTDTHMKLFWSFVGSEDQLHYCDITGAQEGAW
TKISAKASEIGMNGNVALVGLKFENTPANYEILIGEMSIIPAKTFAPVQPTITTAENNIL
KKRTYNSLDFKFSWDCASTKNDADPSIPVYNEDVDTWYFEVYVQAQGEDPILCGTTSSWA
HYVVSAPVSANTEVTDYRVGVCAVAPDGVTKSAITWTNYMTTDLTLVDGIVCDKAVIKAG
EEFTLSLIDPNQEAPFVWEIINATTGGNAVASQSGGKSFTTTLQDEGYYDVKITNFDLST
LMYRGYIQISPESTGSIPSIEDFTASKTNVTSADEEVTLSYTGNKGEGTVSRGLRIDDPY
IFRIPAEFLPMNQNQYTIALWIKPEKFTYAQHAMGLMGQRDLDIHWPHNNWGTFWLDVWP
EKYGADGKKVRDANVLSYTMYGGNTYVDQVGGGGNRHENPNPNCMTDGYSLSENQWTHVL
ISYDGSKQRIYFNGKKTGEAEYPKLTYSDLNGGTGAVAEAPIFIGGSRVYYAGFTGTIDD
VQIWHKALSDTEVVDAMKGYYGREIPSDLKGYWTFESDDYNDADKTFENKGTLSTTSKAA
YVEIRGSGGENTSLNEENLLPANINVEGNPAMSGTMPITTTSAFTIPDAEVVNNGDNATA
TFSKDGKYSVTLTLTNGWGSDSKTKDEYIVVVLEGSGVEDNLVNNLTVYPNPFIDNVNLQ
FAADGNYVIDVYDAQGRLVTTRKHEAMAGEICTLTINGGKGVYYVAVSKDNKRIRTLKVV
AE

Enzyme Prediction     

No EC number prediction in MGYG000001604_00686.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH85	109	418	5.1e-54	0.946031746031746

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4724	COG4724	3.72e-55	31	579	19	549	Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism].
cd06547	GH85_ENGase	1.17e-33	109	450	21	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.
pfam13385	Laminin_G_3	2.55e-18	854	1033	17	150	Concanavalin A-like lectin/glucanases superfamily. This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.
pfam18962	Por_Secre_tail	6.32e-07	1188	1254	1	66	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.
TIGR04183	Por_Secre_tail	7.06e-07	1188	1260	1	70	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
AHF12130.1	0.0	1	1262	1	1287
ADK97378.1	1.03e-291	7	1260	6	1255
ASE18174.1	1.03e-291	7	1260	6	1255
QUB76736.1	1.93e-289	7	1260	6	1257
QUB72359.1	5.43e-289	7	1260	6	1257

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VTF_A	6.36e-38	42	596	17	544	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]
3FHQ_A	8.05e-38	42	525	12	469	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]
3FHA_A	2.57e-37	42	525	12	469	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]
5HON_A	2.54e-08	814	1035	35	203	Structureof Domain 4 of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus, in complex with arabinotriose [Geobacillus stearothermophilus],5HON_B Structure of Domain 4 of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus, in complex with arabinotriose [Geobacillus stearothermophilus]
5HO0_A	1.97e-07	814	1035	674	842	Crystalstructure of AbnA (closed conformation), a GH43 extracellular arabinanase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5HO2_A Crystal structure of AbnA (open conformation), a GH43 extracellular arabinanase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5HOF_A Crystal structure of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus, in complex with arabinopentaose [Geobacillus stearothermophilus],5HP6_A Structure of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus (a new conformational state) [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A1L251	1.73e-06	115	516	130	489	Cytosolic endo-beta-N-acetylglucosaminidase OS=Danio rerio OX=7955 GN=engase PE=2 SV=1

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
0.000428	0.998170	0.000852	0.000192	0.000178	0.000162

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001604_00686.