logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000002370_03330

You are here: Home > Sequence: MGYG000002370_03330

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 Clostridioides difficile_A
Lineage Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Peptostreptococcaceae; Clostridioides; Clostridioides difficile_A
CAZyme ID MGYG000002370_03330
CAZy Family GH38
CAZyme Description Mannosylglycerate hydrolase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
866 MGYG000002370_47|CGC2 99622.98 5.4656
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002370 4277521 Isolate France Europe
Gene Location Start: 148509;  End: 151109  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002370_03330.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH38 3 256 2.7e-60 0.9330855018587361

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK09819 PRK09819 1.75e-166 3 865 5 865
mannosylglycerate hydrolase.
cd10815 GH38N_AMII_EcMngB_like 3.65e-126 3 271 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.
COG0383 AMS1 4.34e-105 1 866 3 943
Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10814 GH38N_AMII_SpGH38_like 9.27e-55 3 270 1 270
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.
cd10790 GH38N_AMII_1 7.93e-49 3 220 1 217
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
CDS88812.1 0.0 1 866 1 866
AXU80531.1 0.0 1 866 1 866
CDS89424.1 0.0 1 866 1 866
AXU54829.1 0.0 1 866 1 866
CDS94470.1 0.0 1 866 1 866

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5KBP_A 1.95e-61 3 740 8 786
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 1.71e-57 3 740 8 786
TheCrystal Structure of a Protein in the Glycosyl Hydrolase Family 38 from Enterococcus faecalis to 2.55A [Enterococcus faecalis V583]
2WYH_A 2.19e-52 3 694 27 784
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]
6LZ1_A 1.09e-12 3 503 280 778
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-]
7DD9_A 1.20e-12 3 503 280 778
ChainA, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct],7DD9_C Chain C, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct],7DD9_E Chain E, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct],7DD9_G Chain G, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P54746 2.35e-102 3 707 6 724
Mannosylglycerate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=mngB PE=1 SV=2
Q9KER1 1.23e-43 4 702 5 762
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
Q9UT61 5.86e-12 3 503 280 778
Alpha-mannosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ams1 PE=1 SV=1
Q91W89 9.10e-09 5 350 253 593
Alpha-mannosidase 2C1 OS=Mus musculus OX=10090 GN=Man2c1 PE=1 SV=1
Q54K67 9.22e-09 7 751 260 995
Alpha-mannosidase G OS=Dictyostelium discoideum OX=44689 GN=manG 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
1.000043 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002370_03330.