Species | Streptococcus mitis | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus; Streptococcus mitis | |||||||||||
CAZyme ID | MGYG000003392_00267 | |||||||||||
CAZy Family | GH38 | |||||||||||
CAZyme Description | Mannosylglycerate hydrolase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 21; End: 1820 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG0383 | AMS1 | 2.84e-173 | 2 | 598 | 291 | 943 | Alpha-mannosidase [Carbohydrate transport and metabolism]. |
PRK09819 | PRK09819 | 1.16e-57 | 16 | 566 | 284 | 834 | mannosylglycerate hydrolase. |
pfam18438 | Glyco_hydro_38 | 2.40e-44 | 114 | 222 | 2 | 111 | 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 | 5.13e-19 | 17 | 85 | 7 | 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 | 1.03e-10 | 17 | 88 | 8 | 83 | 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 |
---|---|---|---|---|---|
QBZ12529.1 | 0.0 | 1 | 599 | 283 | 881 |
QGS43035.1 | 0.0 | 1 | 599 | 283 | 881 |
ALD67339.1 | 0.0 | 1 | 599 | 283 | 881 |
AYF96638.1 | 0.0 | 1 | 599 | 283 | 881 |
QKL33946.1 | 0.0 | 1 | 599 | 283 | 881 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5KBP_A | 3.78e-143 | 1 | 591 | 285 | 894 | 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 | 4.94e-140 | 1 | 591 | 285 | 894 | TheCrystal Structure of a Protein in the Glycosyl Hydrolase Family 38 from Enterococcus faecalis to 2.55A [Enterococcus faecalis V583] |
2WYH_A | 6.19e-132 | 1 | 575 | 305 | 900 | 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 | 1.02e-92 | 3 | 554 | 284 | 845 | 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 | 3.73e-19 | 7 | 554 | 274 | 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 |
---|---|---|---|---|---|
1.000070 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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