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CAZyme Information: MGYG000002267_02508

You are here: Home > Sequence: MGYG000002267_02508

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 Eisenbergiella sp003478085
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella sp003478085
CAZyme ID MGYG000002267_02508
CAZy Family GH38
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
810 MGYG000002267_9|CGC3 92801.49 5.171
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002267 7234430 Isolate China Asia
Gene Location Start: 80437;  End: 82869  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002267_02508.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH38 6 258 6.1e-60 0.9591078066914498

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd10789 GH38N_AMII_ER_cytosolic 4.55e-98 5 246 1 247
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 1.86e-59 5 247 1 254
Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
COG0383 AMS1 2.61e-59 6 796 200 941
Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10813 GH38N_AMII_Man2C1 3.96e-44 5 245 1 246
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 2.66e-42 6 228 2 229
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
QGH33633.1 1.95e-163 2 806 5 807
QIZ10335.1 2.49e-162 2 806 17 815
QGH33655.1 1.90e-160 1 809 1 804
QIZ10350.1 3.89e-160 1 809 1 805
QJU15804.1 6.40e-159 4 793 2 789

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6LZ1_A 1.92e-53 3 768 280 1020
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 2.85e-53 3 768 280 1020
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]
1HWW_A 1.50e-09 3 149 50 198
GOLGIALPHA-MANNOSIDASE II IN COMPLEX WITH SWAINSONINE [Drosophila melanogaster],1HXK_A Golgi Alpha-Mannosidase Ii In Complex With Deoxymannojirimicin [Drosophila melanogaster]
1PS3_A 1.51e-09 3 149 80 228
Golgialpha-mannosidase II in complex with kifunensine [Drosophila melanogaster]
1QWN_A 1.51e-09 3 149 80 228
GOLGIALPHA-MANNOSIDASE II Covalent Intermediate Complex with 5-fluoro-gulosyl-fluoride [Drosophila melanogaster],1R33_A Golgi alpha-mannosidase II complex with 5-thio-D-mannopyranosylamine [Drosophila melanogaster],1R34_A Golgi alpha-mannosidase II complex with 5-thio-D-mannopyranosylamidinium salt [Drosophila melanogaster],1TQS_A Golgi alpha-Mannosidase II In Complex With Salacinol [Drosophila melanogaster],1TQT_A Golgi alpha-Mannosidase II In Complex With A Diastereomer of Salacinol [Drosophila melanogaster],1TQU_A Golgi alpha-Mannosidase II In Complex With The Salacinol Analog Ghavamiol [Drosophila melanogaster],1TQV_A Golgi alpha-Mannosidase II In Complex With Seleno-Salacinol (Blintol) [Drosophila melanogaster],1TQW_A Golgi alpha-Mannosidase II In Complex With A Diastereomer of Seleno-Salacinol [Drosophila melanogaster],2ALW_A Golgi alpha-mannosidase II complex with Noeuromycin [Drosophila melanogaster],2F18_A GOLGI ALPHA-MANNOSIDASE II complex with (2R,3R,4S)-2-({[(1R)-2-hydroxy-1-phenylethyl]amino}methyl)pyrrolidine-3,4-diol [Drosophila melanogaster],2F1A_A GOLGI ALPHA-MANNOSIDASE II COMPLEX WITH (2R,3R,4S)-2-({[(1S)-2-hydroxy-1-phenylethyl]amino}methyl)pyrrolidine-3,4-diol [Drosophila melanogaster],2F1B_A GOLGI ALPHA-MANNOSIDASE II COMPLEX WITH (2R,3R,4S,5R)-2-({[(1R)-2-hydroxy-1-phenylethyl]amino}methyl)-5-methylpyrrolidine-3,4-diol [Drosophila melanogaster],2F7O_A Golgi alpha-mannosidase II complex with mannostatin A [Drosophila melanogaster],2F7P_A Golgi alpha-mannosidase II complex with benzyl-mannostatin A [Drosophila melanogaster],2F7Q_A Golgi alpha-mannosidase II complex with aminocyclopentitetrol [Drosophila melanogaster],2F7R_A Golgi alpha-mannosidase II complex with benzyl-aminocyclopentitetrol [Drosophila melanogaster],2FYV_A Golgi alpha-mannosidase II complex with an amino-salacinol carboxylate analog [Drosophila melanogaster],2OW6_A Golgi alpha-mannosidase II complex with (1r,5s,6s,7r,8s)-1-thioniabicyclo[4.3.0]nonan-5,7,8-triol chloride [Drosophila melanogaster],2OW7_A Golgi alpha-mannosidase II complex with (1R,6S,7R,8S)-1-thioniabicyclo[4.3.0]nonan-7,8-diol chloride [Drosophila melanogaster],3BLB_A Crystal structure of Golgi Mannosidase II in complex with swainsonine at 1.3 Angstrom resolution [Drosophila melanogaster],3BUB_A Golgi alpha-mannosidase II with an empty active site [Drosophila melanogaster],3D4Y_A GOLGI MANNOSIDASE II complex with mannoimidazole [Drosophila melanogaster],3D4Z_A GOLGI MANNOSIDASE II complex with gluco-imidazole [unidentified],3D50_A GOLGI MANNOSIDASE II complex with N-octyl-6-epi-valienamine [Drosophila melanogaster],3D51_A GOLGI MANNOSIDASE II complex with gluco-hydroxyiminolactam [Drosophila melanogaster],3D52_A GOLGI MANNOSIDASE II complex with an N-aryl carbamate derivative of gluco-hydroxyiminolactam [Drosophila melanogaster],3DDF_A GOLGI MANNOSIDASE II complex with (3R,4R,5R)-3,4-Dihydroxy-5-({[(1R)-2-hydroxy-1 phenylethyl]amino}methyl) pyrrolidin-2-one [Drosophila melanogaster],3DDG_A GOLGI MANNOSIDASE II complex with (3R,4R,5R)-3,4-Dihydroxy-5-({[(1R)-2-hydroxy-1 phenylethyl]amino}methyl) methylpyrrolidin-2-one [Drosophila melanogaster],3DX0_A Golgi alpha-Mannosidase II in complex with Mannostatin A at pH 5.75 [Drosophila melanogaster],3DX1_A Golgi alpha-Mannosidase II in complex with Mannostatin analog (1S,2S,3R,4R)-4-aminocyclopentane-1,2,3-triol [Drosophila melanogaster],3DX2_A Golgi mannosidase II complex with MANNOSTATIN B [Drosophila melanogaster],3DX4_A Golgi alpha-Mannosidase II in complex with Mannostatin analog (1R,2R,3R,4S,5R)-4-amino-5-methoxycyclopentane-1,2,3-triol [Drosophila melanogaster],3EJP_A Golgi alpha-Mannosidase II in complex with 5-substituted swainsonine analog: (5R)-5-[2'-oxo-2'-(phenyl)ethyl]-swainsonine [Drosophila melanogaster],3EJQ_A Golgi alpha-Mannosidase II in complex with 5-substitued swainsonine analog: (5R)-5-[2'-oxo-2'-(4-methylphenyl)ethyl]-swainsonine [Drosophila melanogaster],3EJR_A Golgi alpha-Mannosidase II in complex with 5-substitued swainsonine analog: (5R)-5-[2'-oxo-2'-(4-tert-butylphenyl)ethyl]-swainsonine [Drosophila melanogaster],3EJS_A Golgi alpha-Mannosidase II in complex with 5-substituted swainsonine analog: (5S)-5-[2'-(4-tert-butylphenyl)ethyl]-swainsonine [Drosophila melanogaster],3EJT_A Golgi alpha-Mannosidase II in complex with 5-substituted swainsonine analog:(5R)-5-[2'-(4-tert-butylphenyl)ethyl]-swainsonine [Drosophila melanogaster],3EJU_A Golgi alpha-Mannosidase II in complex with 5-substituted swainsonine analog:(5S)-5-[2'-oxo-2'-(4-tert-butylphenyl)ethyl]-swainsonine [Drosophila melanogaster]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q54K67 1.05e-56 6 770 257 1033
Alpha-mannosidase G OS=Dictyostelium discoideum OX=44689 GN=manG PE=1 SV=1
Q9UT61 9.25e-53 3 768 280 1020
Alpha-mannosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ams1 PE=1 SV=1
Q9NTJ4 3.58e-52 5 771 252 984
Alpha-mannosidase 2C1 OS=Homo sapiens OX=9606 GN=MAN2C1 PE=1 SV=1
Q91W89 2.06e-51 5 771 251 983
Alpha-mannosidase 2C1 OS=Mus musculus OX=10090 GN=Man2c1 PE=1 SV=1
P21139 8.90e-51 5 771 251 984
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
1.000038 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002267_02508.