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Basic Information | |
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Species | Manihot esculenta |
Cazyme ID | cassava4.1_001602m |
Family | GH38 |
Protein Properties | Length: 853 Molecular Weight: 96369.7 Isoelectric Point: 6.4798 |
Chromosome | Chromosome/Scaffold: 05432 Start: 289111 End: 302425 |
Description | Glycosyl hydrolase family 38 protein |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH38 | 1 | 221 | 0 |
MCMHDEATPHYIDLIDQTTLGHQFIKDEFGQLPRVGWQIDPFGHSSVQAYLLGAELGFDSLFFARIDYQDRAKRLREKSLEVIWQGSKSLGSTSQIFTGI FPRHYDPPDGFTFEINDVSPPIQDDILLFDYNVQERVNDFVAAALAQVNVTRTNHIMWLMGTDFRYQYANSWFRQMDKFIHYVNKDGRVNAFYSTPSIYT DAKYAADERWPLKTEDFFPYA |
Full Sequence |
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Protein Sequence Length: 853 Download |
MCMHDEATPH YIDLIDQTTL GHQFIKDEFG QLPRVGWQID PFGHSSVQAY LLGAELGFDS 60 LFFARIDYQD RAKRLREKSL EVIWQGSKSL GSTSQIFTGI FPRHYDPPDG FTFEINDVSP 120 PIQDDILLFD YNVQERVNDF VAAALAQVNV TRTNHIMWLM GTDFRYQYAN SWFRQMDKFI 180 HYVNKDGRVN AFYSTPSIYT DAKYAADERW PLKTEDFFPY ADHPNAYWTG YFTSRPAFKG 240 YVRMISGYYL AARQLEFFKG RSASGPNTNK LADALAIAQH HDAVSGTERQ HVAADYSLRL 300 SIGYMEAEKL VASSLAFLAE SGSSTRQEKT VTSFQQCPLL NISYCPPSEA ILSDKKSLVI 360 VVYNPLGWKR EEVIRIPVST EKVVVQDSSG REIESQLLPI SSTTFNLRNK YVKAYLGRFP 420 SETPRYWLAF SASIPPLGFS TYLVSSARQT GPSSTTSLVQ TLEESTSNTI EVGQGSLKLL 480 YSADVGKLTH YVNTRSLVTA TIEQSYGYYS GNDGTDKDPQ ASGAYVFRPN GTFPIKSENQ 540 VPLTFVRGPL LDEVHQQLNP WISQITRVYK GKEHAEVEFT IGPIPVDDGI GKEITTQITT 600 TMRTNKTFYT DSNGRDFIKR IRDFRTDWDL QVNQPVAGNY YPVCFFNTVH DLFIYSSDYL 660 EKKENTTNSA LKLIQGKYFV RIDHLGEGAK WRRTTGQEIY SPVLLAFTEQ DGSNWMNSHT 720 TTFSGIDPSY SLPNNVAIIT LQELENGKVL LRLAHLYETE EGKDNSVVAS VELKKLFPNK 780 KISKVTELSL SANQERADME KKRLVWKVAG AAEERKVARG GPVDPAKLVV ELAPMEIRTF 840 LIDLIHLQTF DS* 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam01074 | Glyco_hydro_38 | 2.0e-58 | 1 | 221 | 225 | + Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. | ||
cd00451 | GH38N_AMII_euk | 1.0e-61 | 1 | 185 | 185 | + 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. | ||
PLN02701 | PLN02701 | 1.0e-63 | 3 | 642 | 723 | + alpha-mannosidase | ||
cd10810 | GH38N_AMII_LAM_like | 2.0e-110 | 2 | 185 | 186 | + 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. |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0004559 | alpha-mannosidase activity |
GO:0005975 | carbohydrate metabolic process |
GO:0006013 | mannose metabolic process |
GO:0008270 | zinc ion binding |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI21275.1 | 0 | 1 | 852 | 127 | 1013 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_189306.1 | 0 | 1 | 842 | 130 | 1001 | glycosyl hydrolase family 38 protein [Arabidopsis thaliana] |
RefSeq | XP_002276199.1 | 0 | 1 | 852 | 127 | 1012 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002301760.1 | 0 | 1 | 852 | 133 | 1020 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002512839.1 | 0 | 1 | 850 | 130 | 1015 | lysosomal alpha-mannosidase, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1ps3_A | 0 | 3 | 643 | 167 | 831 | A Chain A, Golgi Alpha-mannosidase Ii In Complex With Kifunensine |
PDB | 1hxk_A | 0 | 3 | 643 | 137 | 801 | A Chain A, Golgi Alpha-Mannosidase Ii In Complex With Deoxymannojirimicin |
PDB | 1hww_A | 0 | 3 | 643 | 137 | 801 | A Chain A, Golgi Alpha-Mannosidase Ii In Complex With Deoxymannojirimicin |
PDB | 1hty_A | 0 | 3 | 643 | 137 | 801 | A Chain A, Golgi Alpha-Mannosidase Ii |
PDB | 3eju_A | 0 | 3 | 643 | 167 | 831 | A Chain A, Golgi Alpha-Mannosidase Ii |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO780062 | 603 | 202 | 767 | 0 |
FG227394 | 493 | 58 | 549 | 0 |
DT472107 | 302 | 37 | 338 | 0 |
HO780062 | 87 | 117 | 203 | 9e-38 |
HO780062 | 24 | 281 | 304 | 0.11 |
Sequence Alignments (This image is cropped. Click for full image.) |
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