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CAZyme Information: MGYG000002388_02740

You are here: Home > Sequence: MGYG000002388_02740

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 Lacticaseibacillus paracasei
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lacticaseibacillus; Lacticaseibacillus paracasei
CAZyme ID MGYG000002388_02740
CAZy Family GH38
CAZyme Description Mannosylglycerate hydrolase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
879 MGYG000002388_1|CGC28 98697.47 5.8083
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002388 3076437 Isolate China Asia
Gene Location Start: 2777589;  End: 2780228  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002388_02740.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH38 3 252 5.3e-59 0.9442379182156134

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK09819 PRK09819 0.0 3 863 5 872
mannosylglycerate hydrolase.
cd10815 GH38N_AMII_EcMngB_like 5.83e-139 3 264 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.
cd10814 GH38N_AMII_SpGH38_like 1.01e-71 3 264 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.
COG0383 AMS1 9.05e-61 1 866 3 942
Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10790 GH38N_AMII_1 7.68e-56 3 262 1 271
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
QJI68016.1 0.0 1 879 1 879
QPC24579.1 0.0 1 879 1 879
QPC27475.1 0.0 1 879 1 879
AKU60802.1 0.0 1 879 1 879
QKK91741.1 0.0 1 879 1 879

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5KBP_A 9.54e-56 2 730 7 782
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 1.17e-52 2 730 7 782
TheCrystal Structure of a Protein in the Glycosyl Hydrolase Family 38 from Enterococcus faecalis to 2.55A [Enterococcus faecalis V583]
2WYH_A 1.10e-50 2 776 26 834
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P54746 7.44e-120 1 863 4 872
Mannosylglycerate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=mngB PE=1 SV=2
Q9KER1 2.53e-37 5 811 6 846
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
1.000057 0.000002 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002388_02740.