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CAZyme Information: MGYG000000408_00174
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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 | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Cyanobacteria; Vampirovibrionia; Gastranaerophilales; Gastranaerophilaceae; ; | |||||||||||
| CAZyme ID | MGYG000000408_00174 | |||||||||||
| CAZy Family | GH38 | |||||||||||
| CAZyme Description | Mannosylglycerate hydrolase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 195174; End: 197678 Strand: - | |||||||||||
Full Sequence Download help
| MKKKVLAYIH THWDREWYRE FEEFRLRLIE IFDLVLDLLL HNQIPSFYFD GQVSALLDYL | 60 |
| EIYPEKKSCI ENLINQKKLF IGPFFCSSDS FLVSLESFIR NLKLGLDYSY KLNCFDQLCY | 120 |
| IADSFGHSEM IPSVLKSFKL YDALFWRGIS SKTDLFFSWD GINVINLKSG YFQDYLSLNI | 180 |
| SYKEKATLIE NQLNKIDSNN SNLLLLPLGG DHLGLEHNIK DQIIHINSHL QNYYITIGSI | 240 |
| FDYLQEVKSN YSIHNLSSYK GEFRDNSSTF LLDGVLSSHF LLKYKNAKAQ WNLTRLAEVL | 300 |
| QCLFFKLNYS KSYQKEIDFA YNLLIKNQAH DSIYGCSIDP VFQDCITRFN KIEQISNGII | 360 |
| KRNIRDFSNF KNENEINSTN NISIINLSNF NYRGVVKFYS EQKLKGLQLV SKFKGFSDFK | 420 |
| LYNNNQVPIT EDFKNIYEYL IPAIDLKPFS ISSFNINDYL NNDTSKTFNI SENSIENDFI | 480 |
| KITIEDDKVN IFNKKNNIYL KDFILIEDIA DIGDSYNFGP LKDDLPIIAK LISTKIIQKG | 540 |
| KFQNILRLIY NIDIPQNSFL KGRTKKTYLH KINLDLILNK YSELLEFNLS FKNKSLNHKL | 600 |
| NIMFNLKNNI DTTFADNMSK IIKRNHDYNY SIYENIPAKK GIELKTNIFP LEKFVFTQNL | 660 |
| GFLTYGVNAF EIFKNQLKFS ILRSTGIISN KNNPARGTPA GPPLDVPKLQ NLGNIHASLA | 720 |
| FSFANQPKDL YKISEQFYKP VIAFIKESAP FHFINIENDN IILLALKLDD LNNIILRLFN | 780 |
| TNDSIETVRI ELFENKYNFK IIECTSLEKD LEIVKNQSLE FRPFEIKTLK FISI | 834 |
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH38 | 5 | 252 | 1.5e-40 | 0.9405204460966543 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK09819 | PRK09819 | 1.37e-72 | 1 | 829 | 2 | 872 | mannosylglycerate hydrolase. |
| cd10815 | GH38N_AMII_EcMngB_like | 6.60e-49 | 4 | 265 | 1 | 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. |
| cd10814 | GH38N_AMII_SpGH38_like | 1.02e-47 | 10 | 267 | 7 | 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. |
| COG0383 | AMS1 | 8.51e-38 | 1 | 831 | 2 | 941 | Alpha-mannosidase [Carbohydrate transport and metabolism]. |
| cd10790 | GH38N_AMII_1 | 8.16e-31 | 10 | 163 | 7 | 163 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AOR37692.1 | 7.38e-143 | 1 | 723 | 17 | 640 |
| QLK43823.1 | 3.44e-71 | 1 | 713 | 1 | 731 |
| CAE6908833.1 | 6.50e-71 | 1 | 713 | 1 | 731 |
| ARR44603.1 | 6.50e-71 | 1 | 713 | 1 | 731 |
| AQM67042.1 | 1.54e-69 | 1 | 713 | 1 | 731 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5KBP_A | 2.23e-49 | 2 | 831 | 6 | 897 | 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] |
| 2WYH_A | 8.43e-47 | 3 | 810 | 26 | 901 | 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] |
| 3LVT_A | 1.02e-46 | 2 | 831 | 6 | 897 | TheCrystal Structure of a Protein in the Glycosyl Hydrolase Family 38 from Enterococcus faecalis to 2.55A [Enterococcus faecalis V583] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P54746 | 6.90e-42 | 10 | 831 | 12 | 874 | Mannosylglycerate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=mngB PE=1 SV=2 |
| Q9KER1 | 8.82e-38 | 1 | 831 | 1 | 895 | 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 |
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 |
|---|---|---|---|---|---|
| 1.000064 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |