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CAZyme Information: MGYG000000701_01793

You are here: Home > Sequence: MGYG000000701_01793

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 Prevotella sp900552675
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900552675
CAZyme ID MGYG000000701_01793
CAZy Family GH38
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
789 89258.67 7.9105
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000701 3061545 MAG Kazakhstan Asia
Gene Location Start: 14221;  End: 16590  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000701_01793.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH38 33 182 3.5e-23 0.5539033457249071

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0383 AMS1 1.25e-16 92 771 286 927
Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10789 GH38N_AMII_ER_cytosolic 1.93e-08 92 200 90 196
N-terminal catalytic domain of endoplasmic reticulum(ER)/cytosolic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38). The subfamily is represented by Saccharomyces cerevisiae vacuolar alpha-mannosidase Ams1, rat ER/cytosolic alpha-mannosidase Man2C1, and similar proteins. Members in this family share high sequence similarity. None of them have any classical signal sequence or membrane spanning domains, which are typical of sorting or targeting signals. Ams1 functions as a second resident vacuolar hydrolase in S. cerevisiae. It aids in recycling macromolecular components of the cell through hydrolysis of terminal, non-reducing alpha-d-mannose residues. Ams1 utilizes both the cytoplasm to vacuole targeting (Cvt, nutrient-rich conditions) and autophagic (starvation conditions) pathways for biosynthetic delivery to the vacuole. Man2C1is involved in oligosaccharide catabolism in both the ER and cytosol. It can catalyze the cobalt-dependent cleavage of alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose residues. Members in this family are retaining glycosyl hydrolases of family GH38 that employs 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.
smart00872 Alpha-mann_mid 3.43e-07 281 328 14 62
Alpha mannosidase, middle domain. Members of this entry belong to the glycosyl hydrolase family 38, This domain, which is found in the central region adopts a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. The domain is predominantly found in the enzyme alpha-mannosidase.
pfam09261 Alpha-mann_mid 5.10e-06 281 332 15 65
Alpha mannosidase middle domain. Members of this family adopt a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. They are predominantly found in the enzyme alpha-mannosidase.
pfam01074 Glyco_hydro_38 7.13e-06 76 143 74 141
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
BBL06663.1 4.52e-260 6 788 54 880
BBL11622.1 1.69e-255 11 788 60 883
BBL08830.1 1.69e-255 11 788 60 883
BBL00893.1 9.28e-255 11 788 61 882
QQA07855.1 9.64e-249 11 781 24 841

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      help

has no Swissprot hit.

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 0.000011 0.000001 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000701_01793.