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CAZyme Information: MGYG000004849_00177

You are here: Home > Sequence: MGYG000004849_00177

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; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; UMGS1826;
CAZyme ID MGYG000004849_00177
CAZy Family GH92
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
671 MGYG000004849_4|CGC1 75857.01 6.1674
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004849 3246607 MAG China Asia
Gene Location Start: 93;  End: 2108  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.113

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH92 210 650 6.4e-135 0.8615071283095723

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam07971 Glyco_hydro_92 3.91e-170 227 668 1 453
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.
COG3537 COG3537 1.35e-169 2 668 40 729
Putative alpha-1,2-mannosidase [Carbohydrate transport and metabolism].
TIGR01180 aman2_put 8.29e-96 23 649 47 692
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 The identification of members of this family as putative alpha-1,2-mannosidases is based on an unpublished characterization of the aman2 gene in Bacillus sp.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 3.33e-43 20 657 19 663
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 7.96e-28 20 221 10 231
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
BBI31946.1 1.71e-196 1 643 1 656
AWV33843.1 3.78e-194 4 654 24 690
SYX83483.1 3.65e-193 1 650 1 664
QTH40714.1 5.86e-193 1 649 1 663
QDM46979.1 4.54e-190 1 650 17 680

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6DWO_A 1.08e-166 4 649 3 641
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]
7FE1_A 1.08e-166 4 649 3 641
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]
7FE2_A 3.04e-166 4 649 3 641
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]
5SWI_A 6.44e-152 4 640 28 651
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 1.21e-144 4 650 8 665
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 1.06e-58 23 649 62 695
Uncharacterized glycosidase Rv0584 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv0584 PE=3 SV=1
D4ATR3 6.19e-31 212 637 274 673
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
1.000004 0.000019 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004849_00177.