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CAZyme Information: MGYG000002325_00416

You are here: Home > Sequence: MGYG000002325_00416

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 Listeria monocytogenes_B
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Listeriaceae; Listeria; Listeria monocytogenes_B
CAZyme ID MGYG000002325_00416
CAZy Family GH38
CAZyme Description Mannosylglycerate hydrolase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
877 MGYG000002325_1|CGC10 100320.99 4.619
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002325 3017944 Isolate Canada North America
Gene Location Start: 430905;  End: 433538  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002325_00416.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH38 7 263 1.3e-73 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 3 876 1 875
mannosylglycerate hydrolase.
COG0383 AMS1 0.0 3 877 1 941
Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10815 GH38N_AMII_EcMngB_like 1.49e-157 7 276 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.
cd10814 GH38N_AMII_SpGH38_like 7.91e-84 7 276 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.
pfam01074 Glyco_hydro_38 2.50e-73 7 263 1 260
Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AJA82129.1 0.0 1 877 1 877
AGR26657.1 0.0 1 877 1 877
AGR05035.1 0.0 1 877 1 877
EGF46734.2 0.0 1 877 1 877
AGR14885.1 0.0 1 877 1 877

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2WYH_A 1.00e-101 3 833 23 874
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 3.16e-97 3 754 4 782
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 2.18e-94 4 833 5 849
TheCrystal Structure of a Protein in the Glycosyl Hydrolase Family 38 from Enterococcus faecalis to 2.55A [Enterococcus faecalis V583]
5JM0_A 3.69e-13 6 343 302 644
Structureof the S. cerevisiae alpha-mannosidase 1 [Saccharomyces cerevisiae S288C]
6LZ1_A 3.74e-13 5 419 280 698
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 2.31e-176 4 834 3 822
Mannosylglycerate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=mngB PE=1 SV=2
Q9KER1 1.05e-77 3 842 1 854
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
Q91W89 2.70e-22 8 403 252 639
Alpha-mannosidase 2C1 OS=Mus musculus OX=10090 GN=Man2c1 PE=1 SV=1
P21139 5.54e-21 8 358 252 596
Alpha-mannosidase 2C1 OS=Rattus norvegicus OX=10116 GN=Man2c1 PE=1 SV=1
Q9NTJ4 1.13e-19 8 403 253 640
Alpha-mannosidase 2C1 OS=Homo sapiens OX=9606 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
1.000057 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002325_00416.