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CAZyme Information: MGYG000000450_01358

You are here: Home > Sequence: MGYG000000450_01358

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 MGYG000000450_01358
CAZy Family GH38
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1033 MGYG000000450_27|CGC1 118618.69 5.0679
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000450 2671977 MAG Sweden Europe
Gene Location Start: 418;  End: 3519  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.24

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH38 241 517 1.3e-90 0.9739776951672863

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0383 AMS1 0.0 242 1033 203 942
Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10789 GH38N_AMII_ER_cytosolic 7.22e-133 239 501 2 252
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.
pfam01074 Glyco_hydro_38 2.23e-102 241 511 4 270
Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10813 GH38N_AMII_Man2C1 3.98e-83 242 501 5 252
N-terminal catalytic domain of mammalian cytosolic alpha-mannosidase Man2C1 and similar proteins; glycoside hydrolase family 38 (GH38). The subfamily corresponds to cytosolic alpha-mannosidase Man2C1 (also known as ER-mannosidase II or neutral/cytosolic mannosidase), mainly found in various vertebrates, and similar proteins. Man2C1 plays an essential role in the catabolism of cytosolic free oligomannosides derived from dolichol intermediates and the degradation of newly synthesized glycoproteins in ER or cytosol. It can catalyze the cleavage of alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose residues. Man2C1 is a cobalt-dependent enzyme belonging to alpha-mannosidase class II. It has a neutral pH optimum and is strongly inhitibed by furanose analogs swainsonine (SW) and 1,4-dideoxy-1,4-imino-D-mannitol (DIM), moderately by deoxymannojirimycin (DMM), but not by kifunensine (KIF). DMM and KIF, both pyranose analogs, are normally known to inhibit class I alpha-mannosidase.
cd10812 GH38N_AMII_ScAms1_like 4.52e-78 242 501 5 258
N-terminal catalytic domain of yeast vacuolar alpha-mannosidases and similar proteins; glycoside hydrolase family 38 (GH38). The family is represented by Saccharomyces cerevisiae alpha-mannosidase (Ams1) and its eukaryotic homologs. 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 forms an oligomer in the cytoplasm and retains its oligomeric form during the import process. It utilizes both the Cvt (nutrient-rich conditions) and autophagic (starvation conditions) pathways for biosynthetic delivery to the vacuole. Mutants in either pathway are defective in Ams1 import. Members in this family show high sequence similarity with rat ER/cytosolic alpha-mannosidase Man2C1.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBL14320.1 0.0 5 1032 2 1028
VCV20389.1 0.0 5 1032 2 1028
QOV19737.1 0.0 5 1033 2 1028
BCJ98684.1 0.0 6 1033 3 1029
BCJ95065.1 0.0 5 1032 23 1048

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6LZ1_A 1.60e-151 63 1032 97 1075
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-]
7DD9_A 7.99e-148 63 1032 97 1075
ChainA, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct],7DD9_C Chain C, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct],7DD9_E Chain E, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct],7DD9_G Chain G, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct]
5JM0_A 9.69e-127 41 1032 106 1094
Structureof the S. cerevisiae alpha-mannosidase 1 [Saccharomyces cerevisiae S288C]
5KBP_A 4.49e-18 242 1031 12 896
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 1.06e-15 242 1031 12 896
TheCrystal Structure of a Protein in the Glycosyl Hydrolase Family 38 from Enterococcus faecalis to 2.55A [Enterococcus faecalis V583]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q54K67 1.76e-155 47 1031 59 1083
Alpha-mannosidase G OS=Dictyostelium discoideum OX=44689 GN=manG PE=1 SV=1
Q9NTJ4 3.34e-153 38 1030 47 1031
Alpha-mannosidase 2C1 OS=Homo sapiens OX=9606 GN=MAN2C1 PE=1 SV=1
Q9UT61 2.37e-151 63 1032 97 1075
Alpha-mannosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ams1 PE=1 SV=1
Q91W89 2.86e-149 38 1030 46 1030
Alpha-mannosidase 2C1 OS=Mus musculus OX=10090 GN=Man2c1 PE=1 SV=1
P21139 4.31e-140 38 1030 46 1031
Alpha-mannosidase 2C1 OS=Rattus norvegicus OX=10116 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
1.000051 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000450_01358.