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CAZyme Information: H257_15244-t26_1-p1

You are here: Home > Sequence: H257_15244-t26_1-p1

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 Aphanomyces astaci
Lineage Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces astaci
CAZyme ID H257_15244-t26_1-p1
CAZy Family GT41
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
988 110870.86 6.5263
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AastaciAPO3 19584 N/A 465 19119
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.24:47 3.2.1.113:25 3.2.1.114:7

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH38 51 351 1.7e-73 0.9962825278810409

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
212121 GH38N_AMII_LAM_like 2.04e-152 50 314 1 278
N-terminal catalytic domain of lysosomal alpha-mannosidase and similar proteins; glycoside hydrolase family 38 (GH38). The subfamily is represented by lysosomal alpha-mannosidase (LAM, Man2B1, EC 3.2.1.114), which is a broad specificity exoglycosidase hydrolyzing all known alpha 1,2-, alpha 1,3-, and alpha 1,6-mannosidic linkages from numerous high mannose type oligosaccharides. LAM is expressed in all tissues and in many species. In mammals, the absence of LAM can cause the autosomal recessive disease alpha-mannosidosis. LAM has an acidic pH optimum at 4.0-4.5. It is stimulated by zinc ion and is inhibited by cobalt ion and plant alkaloids, such as swainsonine (SW). LAM catalyzes hydrolysis by a double displacement mechanism in which a glycosyl-enzyme intermediate is formed and hydrolyzed via oxacarbenium ion-like transition states. A carboxylic acid in the active site acts as the catalytic nucleophile in the formation of the covalent intermediate while a second carboxylic acid acts as a general acid catalyst. The same residue is thought to assist in the hydrolysis (deglycosylation) step, this time acting as a general base.
212095 GH38N_AMII_euk 2.85e-105 50 313 1 257
N-terminal catalytic domain of eukaryotic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38). The family corresponds to a group of eukaryotic class II alpha-mannosidases (AlphaMII), which contain Golgi alpha-mannosidases II (GMII), the major broad specificity lysosomal alpha-mannosidases (LAM, MAN2B1), the noval core-specific lysosomal alpha 1,6-mannosidases (Epman, MAN2B2), and similar proteins. GMII catalyzes the hydrolysis of the terminal both alpha-1,3-linked and alpha-1,6-linked mannoses from the high-mannose oligosaccharide GlcNAc(Man)5(GlcNAc)2 to yield GlcNAc(Man)3(GlcNAc)2 (GlcNAc, N-acetylglucosmine), which is the committed step of complex N-glycan synthesis. LAM is a broad specificity exoglycosidase hydrolyzing all known alpha 1,2-, alpha 1,3-, and alpha 1,6-mannosidic linkages from numerous high mannose type oligosaccharides. Different from LAM, Epman can efficiently cleave only the alpha 1,6-linked mannose residue from (Man)3GlcNAc, but not (Man)3(GlcNAc)2 or other larger high mannose oligosaccharides, in the core of N-linked glycans. 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.
178304 PLN02701 3.71e-91 48 791 38 858
alpha-mannosidase
395852 Glyco_hydro_38 1.98e-87 51 351 1 271
Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
212120 GH38N_AMII_GMII_SfManIII_like 1.10e-83 49 362 1 340
N-terminal catalytic domain of Golgi alpha-mannosidase II, Spodoptera frugiperda Sf9 alpha-mannosidase III, and similar proteins; glycoside hydrolase family 38 (GH38). This subfamily is represented by Golgi alpha-mannosidase II (GMII, also known as mannosyl-oligosaccharide 1,3- 1,6-alpha mannosidase, EC 3.2.1.114, Man2A1), a monomeric, membrane-anchored class II alpha-mannosidase existing in the Golgi apparatus of eukaryotes. GMII plays a key role in the N-glycosylation pathway. It catalyzes the hydrolysis of the terminal both alpha-1,3-linked and alpha-1,6-linked mannoses from the high-mannose oligosaccharide GlcNAc(Man)5(GlcNAc)2 to yield GlcNAc(Man)3(GlcNAc)2(GlcNAc, N-acetylglucosmine), which is the committed step of complex N-glycan synthesis. GMII is activated by zinc or cobalt ions and is strongly inhibited by swainsonine. Inhibition of GMII provides a route to block cancer-induced changes in cell surface oligosaccharide structures. GMII has a pH optimum of 5.5-6.0, which is intermediate between those of acidic (lysosomal alpha-mannosidase) and neutral (ER/cytosolic alpha-mannosidase) enzymes. GMII is a retaining glycosyl hydrolase 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. This subfamily also includes human alpha-mannosidase 2x (MX, also known as mannosyl-oligosaccharide 1,3- 1,6-alpha mannosidase, EC 3.2.1.114, Man2A2). MX is enzymatically and functionally very similar to GMII, and is thought to also function in the N-glycosylation pathway. Also found in this subfamily is class II alpha-mannosidase encoded by Spodoptera frugiperda Sf9 cell. This alpha-mannosidase is an integral membrane glycoprotein localized in the Golgi apparatus. It shows high sequence homology with mammalian Golgi alpha-mannosidase II(GMII). It can hydrolyze p-nitrophenyl alpha-D-mannopyranoside (pNP-alpha-Man), and it is inhibited by swainsonine. However, the Sf9 enzyme is stimulated by cobalt and can hydrolyze (Man)5(GlcNAc)2 to (Man)3(GlcNAc)2, but it cannot hydrolyze GlcNAc(Man)5(GlcNAc)2, which is distinct from that of GMII. Thus, this enzyme has been designated as Sf9 alpha-mannosidase III (SfManIII). It probably functions in an alternate N-glycan processing pathway in Sf9 cells.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 26 954 19 932
0.0 10 973 4 974
1.15e-287 15 967 12 1020
9.28e-267 74 954 2 947
2.11e-214 39 951 5 978

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.70e-209 39 930 3 932
Structure of GH 38 Jack Bean alpha-mannosidase [Canavalia ensiformis],6B9O_B Structure of GH 38 Jack Bean alpha-mannosidase [Canavalia ensiformis]
3.70e-209 39 930 3 932
Structure of GH 38 Jack Bean alpha-mannosidase in complex with a 36-valent iminosugar cluster inhibitor [Canavalia ensiformis],6B9P_B Structure of GH 38 Jack Bean alpha-mannosidase in complex with a 36-valent iminosugar cluster inhibitor [Canavalia ensiformis]
3.13e-78 39 319 3 297
The structure of the bovine lysosomal a-mannosidase suggests a novel mechanism for low pH activation [Bos taurus]
6.39e-74 49 799 50 858
GOLGI ALPHA-MANNOSIDASE II IN COMPLEX WITH SWAINSONINE [Drosophila melanogaster],1HXK_A Golgi Alpha-Mannosidase Ii In Complex With Deoxymannojirimicin [Drosophila melanogaster]
7.72e-74 49 799 68 876
Chain A, Alpha-mannosidase 2 [Drosophila melanogaster],6RQZ_A Chain A, Alpha-mannosidase 2 [Drosophila melanogaster],6RRH_A Chain A, Alpha-mannosidase 2 [Drosophila melanogaster],6RRJ_A Chain A, Alpha-mannosidase 2 [Drosophila melanogaster],6RRN_A Chain A, Alpha-mannosidase 2 [Drosophila melanogaster],6RRU_A Chain A, Alpha-mannosidase 2 [Drosophila melanogaster],6RRW_A Chain A, Alpha-mannosidase 2 [Drosophila melanogaster],6RRX_A Chain A, Alpha-mannosidase 2 [Drosophila melanogaster],6RRY_A Chain A, Alpha-mannosidase 2 [Drosophila melanogaster],6RS0_A Chain A, Alpha-mannosidase 2 [Drosophila melanogaster]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.55e-211 39 930 26 957
Probable alpha-mannosidase At5g13980 OS=Arabidopsis thaliana OX=3702 GN=At5g13980 PE=2 SV=1
1.94e-201 39 930 3 932
Alpha-mannosidase OS=Canavalia ensiformis OX=3823 PE=1 SV=1
1.28e-199 39 930 27 954
Alpha-mannosidase At3g26720 OS=Arabidopsis thaliana OX=3702 GN=At3g26720 PE=1 SV=1
3.21e-194 39 930 36 985
Probable alpha-mannosidase At5g66150 OS=Arabidopsis thaliana OX=3702 GN=At5g66150 PE=3 SV=1
1.30e-180 39 951 53 997
Lysosomal alpha-mannosidase OS=Felis catus OX=9685 GN=MAN2B1 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.003428 0.996543 CS pos: 18-19. Pr: 0.6722

TMHMM  Annotations      help

There is no transmembrane helices in H257_15244-t26_1-p1.