logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000000174_03268

You are here: Home > Sequence: MGYG000000174_03268

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 Parabacteroides faecis
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides faecis
CAZyme ID MGYG000000174_03268
CAZy Family GH38
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
832 MGYG000000174_9|CGC3 95855.76 7.948
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000174 6515019 Isolate China Asia
Gene Location Start: 208131;  End: 210629  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000174_03268.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH38 45 209 7.8e-25 0.5985130111524164

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0383 AMS1 3.10e-19 107 830 286 941
Alpha-mannosidase [Carbohydrate transport and metabolism].
PRK09819 PRK09819 1.59e-18 360 829 363 865
mannosylglycerate hydrolase.
pfam01074 Glyco_hydro_38 2.73e-11 45 196 32 179
Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
pfam07748 Glyco_hydro_38C 1.65e-10 474 672 1 180
Glycosyl hydrolases family 38 C-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10786 GH38N_AMII_like 1.77e-07 74 191 61 172
N-terminal catalytic domain of class II alpha-mannosidases and similar proteins; glycoside hydrolase family 38 (GH38). Alpha-mannosidases (EC 3.2.1.24) are extensively found in eukaryotes and play important roles in the processing of newly formed N-glycans and in degradation of mature glycoproteins. A deficiency of this enzyme causes the lysosomal storage disease alpha-mannosidosis. Many bacterial and archaeal species also possess putative alpha-mannosidases, but their activity and specificity is largely unknown. Based on different functional characteristics and sequence homology, alpha-mannosidases have been organized into two classes (class I, belonging to glycoside hydrolase family 47, and class II, belonging to glycoside hydrolase family 38). Members of this family corresponds to class II alpha-mannosidases (alphaMII), which contain intermediate Golgi alpha-mannosidases II, acidic lysosomal alpha-mannosidases, animal sperm and epididymal alpha -mannosidases, neutral ER/cytosolic alpha-mannosidases, and some putative prokaryotic alpha-mannosidases. AlphaMII possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyzes the degradation of N-linked oligosaccharides. The N-terminal catalytic domain of alphaMII adopts a structure consisting of parallel 7-stranded beta/alpha barrel. 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCA48608.1 6.69e-279 19 830 19 846
AAO79177.1 9.48e-279 19 830 19 846
QMW86426.1 9.48e-279 19 830 19 846
ALJ43681.1 9.48e-279 19 830 19 846
QUT69752.1 1.90e-278 19 830 19 846

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 SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.004723 0.991878 0.002342 0.000353 0.000332 0.000342

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000174_03268.