| Species | UMGS2055 sp900557635 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; UMGS2055; UMGS2055 sp900557635 | |||||||||||
| CAZyme ID | MGYG000003996_01597 | |||||||||||
| CAZy Family | GH38 | |||||||||||
| CAZyme Description | Mannosylglycerate hydrolase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 41; End: 1765 Strand: - | |||||||||||
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK09819 | PRK09819 | 1.12e-69 | 10 | 573 | 290 | 874 | mannosylglycerate hydrolase. |
| COG0383 | AMS1 | 4.44e-67 | 3 | 573 | 307 | 941 | Alpha-mannosidase [Carbohydrate transport and metabolism]. |
| pfam18438 | Glyco_hydro_38 | 4.38e-13 | 136 | 194 | 50 | 109 | Glycosyl hydrolases family 38 C-terminal domain 1. The enzymatic hydrolysis of alpha-mannosides is catalyzed by glycoside hydrolases (GH), termed alpha-mannosidases. Streptococcal (Sp) GH38 alpha-mannosidase active on N-glycans and possibly O-glycans. SpGH38 structure can be considered as five domains: an N-terminal alpha/beta-domain, a three-helix bundle and three predominantly beta-sheet domains. This is the first of the three beta-sheet domains found in GH38, termed Beta-1. Structural analysis indicate that the beta-1 domain bows outward from the protein core, is involved in dimer interactions whilst also forming a lid 'above' and somewhat into the active centre of its dimer. |
| smart00872 | Alpha-mann_mid | 8.04e-13 | 3 | 76 | 5 | 79 | Alpha mannosidase, middle domain. Members of this entry belong to the glycosyl hydrolase family 38, This domain, which is found in the central region adopts a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. The domain is predominantly found in the enzyme alpha-mannosidase. |
| pfam09261 | Alpha-mann_mid | 3.84e-09 | 2 | 94 | 5 | 98 | Alpha mannosidase middle domain. Members of this family adopt a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. They are predominantly found in the enzyme alpha-mannosidase. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ANS76723.1 | 1.94e-118 | 1 | 573 | 294 | 909 |
| BBI31684.1 | 6.88e-118 | 1 | 571 | 297 | 903 |
| QDM44645.1 | 3.82e-116 | 1 | 563 | 296 | 891 |
| ALS26621.1 | 4.52e-114 | 1 | 520 | 295 | 852 |
| APO47530.1 | 3.75e-113 | 1 | 561 | 295 | 895 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5KBP_A | 2.69e-92 | 2 | 524 | 298 | 853 | Thecrystal structure of an alpha-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583],5KBP_B The crystal structure of an alpha-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583] |
| 3LVT_A | 5.40e-90 | 2 | 524 | 298 | 853 | TheCrystal Structure of a Protein in the Glycosyl Hydrolase Family 38 from Enterococcus faecalis to 2.55A [Enterococcus faecalis V583] |
| 2WYH_A | 2.18e-84 | 2 | 567 | 318 | 922 | Structureof the Streptococcus pyogenes family GH38 alpha-mannosidase [Streptococcus pyogenes M1 GAS],2WYH_B Structure of the Streptococcus pyogenes family GH38 alpha-mannosidase [Streptococcus pyogenes M1 GAS],2WYI_A Structure of the Streptococcus pyogenes family GH38 alpha-mannosidase complexed with swainsonine [Streptococcus pyogenes M1 GAS],2WYI_B Structure of the Streptococcus pyogenes family GH38 alpha-mannosidase complexed with swainsonine [Streptococcus pyogenes M1 GAS] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q9KER1 | 2.45e-73 | 1 | 574 | 294 | 896 | Putative mannosylglycerate hydrolase OS=Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) OX=272558 GN=mngB PE=3 SV=2 |
| P54746 | 4.32e-39 | 5 | 520 | 286 | 821 | Mannosylglycerate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=mngB PE=1 SV=2 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000036 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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