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CAZyme Information: MGYG000000162_01048

You are here: Home > Sequence: MGYG000000162_01048

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 Enterococcus_B durans
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus_B; Enterococcus_B durans
CAZyme ID MGYG000000162_01048
CAZy Family GH92
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
719 MGYG000000162_16|CGC2 82011.42 5.2672
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000162 3083618 Isolate China Asia
Gene Location Start: 23885;  End: 26044  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.113

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH92 210 697 4.6e-159 0.9633401221995926

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3537 COG3537 0.0 3 716 39 760
Putative alpha-1,2-mannosidase [Carbohydrate transport and metabolism].
pfam07971 Glyco_hydro_92 0.0 225 697 1 464
Glycosyl hydrolase family 92. Members of this family are alpha-1,2-mannosidases, enzymes which remove alpha-1,2-linked mannose residues from Man(9)(GlcNAc)(2) by hydrolysis. They are critical for the maturation of N-linked oligosaccharides and ER-associated degradation.
TIGR01180 aman2_put 1.08e-95 25 701 50 749
alpha-1,2-mannosidase, putative. The identification of members of this family as putative alpha-1,2-mannosidases is based on an unpublished characterization of the aman2 gene in Bacillus sp. M-90 by Maruyama,Y., Nakajima,M. and Nakajima,T. (Genbank accession BAA76709, pid g4587313). Most members of this family appear to have signal sequences. Members from the dental pathogen Porphyromonas gingivalis have been described as immunoreactive with periodontitis patient serum. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
NF035929 lectin_1 5.35e-49 11 713 16 698
lectin. Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor.
pfam17678 Glyco_hydro_92N 2.93e-15 6 185 2 186
Glycosyl hydrolase family 92 N-terminal domain. This domain is found at the N-terminus of family 92 glycosyl hydrolase proteins.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ASV96653.1 0.0 1 719 16 734
QCJ65381.1 0.0 1 719 16 734
AKZ47567.1 0.0 1 719 1 719
AKX86195.1 0.0 1 719 1 719
QPQ28493.1 0.0 1 719 16 734

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6DWO_A 0.0 1 717 1 712
Crystalstructure of alpha-1-2-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583],6DWO_B Crystal structure of alpha-1-2-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583],6DWO_C Crystal structure of alpha-1-2-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583],6DWO_D Crystal structure of alpha-1-2-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583]
7FE2_A 0.0 1 717 1 712
ChainA, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE2_B Chain B, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE2_C Chain C, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE2_D Chain D, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100]
7FE1_A 0.0 1 717 1 712
ChainA, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE1_B Chain B, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE1_C Chain C, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100],7FE1_D Chain D, Alpha-1,2-mannosidase [Enterococcus faecalis ATCC 10100]
5SWI_A 1.09e-201 3 701 28 716
Crystalstructure of SpGH92 in complex with mannose [Streptococcus pneumoniae],5SWI_B Crystal structure of SpGH92 in complex with mannose [Streptococcus pneumoniae],5SWI_C Crystal structure of SpGH92 in complex with mannose [Streptococcus pneumoniae],5SWI_D Crystal structure of SpGH92 in complex with mannose [Streptococcus pneumoniae]
2WVY_A 5.80e-150 3 716 8 737
StructureOf The Family Gh92 Inverting Mannosidase Bt2199 From Bacteroides Thetaiotaomicron Vpi-5482 [Bacteroides thetaiotaomicron VPI-5482],2WVY_B Structure Of The Family Gh92 Inverting Mannosidase Bt2199 From Bacteroides Thetaiotaomicron Vpi-5482 [Bacteroides thetaiotaomicron VPI-5482],2WVY_C Structure Of The Family Gh92 Inverting Mannosidase Bt2199 From Bacteroides Thetaiotaomicron Vpi-5482 [Bacteroides thetaiotaomicron VPI-5482],2WW2_A Structure of the Family GH92 Inverting Mannosidase BT2199 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],2WW2_B Structure of the Family GH92 Inverting Mannosidase BT2199 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],2WW2_C Structure of the Family GH92 Inverting Mannosidase BT2199 from Bacteroides thetaiotaomicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O86365 5.83e-60 25 704 65 757
Uncharacterized glycosidase Rv0584 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv0584 PE=3 SV=1
D4ATR3 3.61e-38 214 718 278 762
Uncharacterized secreted glycosidase ARB_07629 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_07629 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
1.000058 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000162_01048.