Species | Enterococcus_B durans | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus_B; Enterococcus_B durans | |||||||||||
CAZyme ID | MGYG000000162_03017 | |||||||||||
CAZy Family | GH0 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 477; End: 2579 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd10791 | GH38N_AMII_like_1 | 2.12e-33 | 1 | 170 | 96 | 254 | N-terminal catalytic domain of mainly uncharacterized eukaryotic proteins similar to alpha-mannosidases; glycoside hydrolase family 38 (GH38). The subfamily of mainly uncharacterized eukaryotic proteins shows sequence homology with class II alpha-mannosidases (AlphaAMIIs). AlphaAMIIs possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyze the degradation of N-linked oligosaccharides. The N-terminal catalytic domain of alphaMII adopts a structure consisting of parallel 7-stranded beta/alpha barrel. This subfamily belongs to the GH38 family of retaining glycosyl hydrolases, which employ a two-step mechanism involving the formation of a covalent glycosyl enzyme complex; two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst. |
cd10814 | GH38N_AMII_SpGH38_like | 4.54e-10 | 60 | 206 | 146 | 269 | N-terminal catalytic domain of SPGH38, a putative alpha-mannosidase of Streptococcus pyogenes, and its prokaryotic homologs; glycoside hydrolase family 38 (GH38). The subfamily is represented by SpGH38 of Streptococcus pyogenes, which has been assigned as a putative alpha-mannosidase, and is encoded by ORF spy1604. SpGH38 appears to exist as an elongated dimer and display alpha-1,3 mannosidase activity. It is active on disaccharides and some aryl glycosides. SpGH38 can also effectively deglycosylate human N-glycans in vitro. A divalent metal ion, such as a zinc ion, is required for its activity. SpGH38 is inhibited by swainsonine. The absence of any secretion signal peptide suggests that SpGH38 may be intracellular. |
cd10815 | GH38N_AMII_EcMngB_like | 8.56e-06 | 60 | 206 | 146 | 268 | N-terminal catalytic domain of Escherichia coli alpha-mannosidase MngB and its bacterial homologs; glycoside hydrolase family 38 (GH38). The bacterial subfamily is represented by Escherichia coli alpha-mannosidase MngB, which is encoded by the mngB gene (previously called ybgG). MngB exhibits alpha-mannosidase activity that converts 2-O-(6-phospho-alpha-mannosyl)-D-glycerate to mannose-6-phosphate and glycerate in the pathway which enables use of mannosyl-D-glycerate as a sole carbon source. A divalent metal ion is required for its activity. |
pfam07748 | Glyco_hydro_38C | 3.27e-05 | 428 | 550 | 1 | 111 | Glycosyl hydrolases family 38 C-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. |
PRK09819 | PRK09819 | 0.008 | 153 | 206 | 221 | 273 | mannosylglycerate hydrolase. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ALE07311.1 | 6.13e-273 | 1 | 700 | 94 | 791 |
ASN05648.1 | 6.47e-168 | 10 | 696 | 111 | 809 |
AUS96542.1 | 2.79e-166 | 14 | 697 | 128 | 829 |
SQI58910.1 | 2.25e-165 | 10 | 696 | 111 | 809 |
AYY08756.1 | 4.92e-163 | 3 | 694 | 104 | 799 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000049 | 0.000002 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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