You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000003115_01319
You are here: Home > Sequence: MGYG000003115_01319
Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Franconibacter helveticus | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Franconibacter; Franconibacter helveticus | |||||||||||
| CAZyme ID | MGYG000003115_01319 | |||||||||||
| CAZy Family | GH38 | |||||||||||
| CAZyme Description | Mannosylglycerate hydrolase | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 726; End: 3365 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH38 | 7 | 265 | 2.6e-75 | 0.9479553903345725 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK09819 | PRK09819 | 0.0 | 3 | 874 | 2 | 875 | mannosylglycerate hydrolase. |
| COG0383 | AMS1 | 0.0 | 6 | 875 | 5 | 943 | Alpha-mannosidase [Carbohydrate transport and metabolism]. |
| cd10815 | GH38N_AMII_EcMngB_like | 6.93e-160 | 6 | 276 | 1 | 270 | 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. |
| cd10790 | GH38N_AMII_1 | 2.40e-136 | 6 | 276 | 1 | 273 | N-terminal catalytic domain of putative prokaryotic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38). This mainly bacterial subfamily corresponds to a group of putative class II alpha-mannosidases, including various proteins assigned as alpha-mannosidases, Streptococcus pyogenes (SpGH38) encoded by ORF spy1604. Escherichia coli MngB encoded by the mngB/ybgG gene, and Thermotoga maritime TMM, and similar proteins. SpGH38 targets alpha-1,3 mannosidic linkages. 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. MngB exhibits alpha-mannosidase activity that catalyzes the conversion of 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. TMM is a homodimeric enzyme that hydrolyzes p-nitrophenyl-alpha-D-mannopyranoside, alpha -1,2-mannobiose, alpha -1,3-mannobiose, alpha -1,4-mannobiose, and alpha -1,6-mannobiose. The GH38 family contains retaining glycosyl hydrolases that 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. Divalent metal ions, such as zinc or cobalt ions, are suggested to be required for the catalytic activities of typical class II alpha-mannosidases. However, TMM requires the cobalt or cadmium for its activity. The cadmium ion dependency is unique to TMM. Moreover, TMM is inhibited by swainsonine but not 1-deoxymannojirimycin, which is in agreement with the features of cytosolic alpha-mannosidase. |
| cd10814 | GH38N_AMII_SpGH38_like | 3.68e-92 | 6 | 276 | 1 | 271 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QFH72249.1 | 0.0 | 1 | 877 | 1 | 877 |
| QLA61109.1 | 0.0 | 1 | 875 | 1 | 875 |
| ADF62536.1 | 0.0 | 1 | 875 | 1 | 875 |
| QCZ38079.1 | 0.0 | 1 | 875 | 1 | 875 |
| QUG53484.1 | 0.0 | 1 | 875 | 1 | 875 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2WYH_A | 5.26e-108 | 3 | 838 | 24 | 892 | 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] |
| 5KBP_A | 4.36e-94 | 5 | 828 | 7 | 858 | 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 | 5.44e-90 | 5 | 828 | 7 | 858 | TheCrystal Structure of a Protein in the Glycosyl Hydrolase Family 38 from Enterococcus faecalis to 2.55A [Enterococcus faecalis V583] |
| 5JM0_A | 1.68e-11 | 2 | 351 | 299 | 652 | Structureof the S. cerevisiae alpha-mannosidase 1 [Saccharomyces cerevisiae S288C] |
| 6LZ1_A | 2.59e-10 | 5 | 419 | 281 | 698 | Structureof S.pombe alpha-mannosidase Ams1 [Schizosaccharomyces pombe 972h-],6LZ1_B Structure of S.pombe alpha-mannosidase Ams1 [Schizosaccharomyces pombe 972h-],6LZ1_C Structure of S.pombe alpha-mannosidase Ams1 [Schizosaccharomyces pombe 972h-],6LZ1_D Structure of S.pombe alpha-mannosidase Ams1 [Schizosaccharomyces pombe 972h-] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P54746 | 0.0 | 1 | 875 | 1 | 876 | Mannosylglycerate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=mngB PE=1 SV=2 |
| Q9KER1 | 3.56e-76 | 8 | 849 | 6 | 873 | 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 |
| Q9NTJ4 | 7.73e-19 | 2 | 401 | 248 | 638 | Alpha-mannosidase 2C1 OS=Homo sapiens OX=9606 GN=MAN2C1 PE=1 SV=1 |
| Q54K67 | 3.80e-15 | 2 | 819 | 252 | 1027 | Alpha-mannosidase G OS=Dictyostelium discoideum OX=44689 GN=manG PE=1 SV=1 |
| Q91W89 | 6.43e-15 | 2 | 401 | 247 | 637 | Alpha-mannosidase 2C1 OS=Mus musculus OX=10090 GN=Man2c1 PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000063 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |