| Basic Information | |
|---|---|
| Species | Sorghum bicolor |
| Cazyme ID | Sb10g008770.1 |
| Family | GH38 |
| Protein Properties | Length: 1185 Molecular Weight: 134639 Isoelectric Point: 7.0613 |
| Chromosome | Chromosome/Scaffold: 10 Start: 9184942 End: 9191455 |
| Description | golgi alpha-mannosidase II |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH38 | 168 | 507 | 0 |
| KVFVAPHSHNDPGWIRTVEEYYERQSRHILDTIVESLSKDSRRKFIWEEMSYLERWWRDATPKKQEAFAKLVRDGQLEIVSGGWVMNDEANSHYFAIIEQ IMEGNMWLNDTIGVIPKNSWSIDPFGYSSTMAYLLRRMGFHNMLIQRTHYEVKKELAMKKNLEYLWRQNWDIEETTDIFVHMMPFYSYDIPHTCGPEPAI CCQFDFARMRGFSYESCPWRFDPVETNPDNVKERATKLLDQYRKKSTLYRTNTLLVPLGDDFRYVSVEEAEVQFRNYEKLFDYINSNPHLNAEVKFGTLE DYFSTLRDEAEKINYTRPGELGSAELQGFPTLSGDFFTYA | |||
| Full Sequence |
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| Protein Sequence Length: 1185 Download |
| MPFFSGSGGG RSGALLPTTS KPKAHHHLRS KSSLSAPASS RRRGGGLHSA SSPYSRRALC 60 LAATAFAALF ILAFLRLGFP SSRSAALSSP ARPRARLTRR PAFRLRDSAA AEAAAAAVAA 120 RIGREAPVDI TTRDLYERIE FSDEDGGAWK QGWEVKYRGD EWDAEKLKVF VAPHSHNDPG 180 WIRTVEEYYE RQSRHILDTI VESLSKDSRR KFIWEEMSYL ERWWRDATPK KQEAFAKLVR 240 DGQLEIVSGG WVMNDEANSH YFAIIEQIME GNMWLNDTIG VIPKNSWSID PFGYSSTMAY 300 LLRRMGFHNM LIQRTHYEVK KELAMKKNLE YLWRQNWDIE ETTDIFVHMM PFYSYDIPHT 360 CGPEPAICCQ FDFARMRGFS YESCPWRFDP VETNPDNVKE RATKLLDQYR KKSTLYRTNT 420 LLVPLGDDFR YVSVEEAEVQ FRNYEKLFDY INSNPHLNAE VKFGTLEDYF STLRDEAEKI 480 NYTRPGELGS AELQGFPTLS GDFFTYADRN QDYWSGYYVS RPFFKAVDRV LEQTLRASEI 540 LGSFVLGYCQ KFQCAKLPIS FSHKLTAARR NLALFQHHDG VTGTAKDHVV VDYGTRMHTS 600 LQDLQLFMSR AVEVLLGDFH DRSDPTLLSH FEPVQERSKY DVQPVHRVLH PDEGKAQSVV 660 FFNPLEQTRD EVVMVVVSTP DVSVLNSNGS CLPSQVSPEW QFVSNEKIST GRHRLYWRAS 720 VPPLGLETYY VVTGQDCEKA IPAVVKRYTA AQEFPCPEPY HCSKLEGKTV EMKNSNYTLS 780 FDTSHGLLQT VTRHKDGEQT VIGEEIGMYR SHGSGAYLFK PVGEARSIVE GGGHFILTEG 840 PLVQEAHSLP KTEWHESPLS HSTRMYNCGD SVQDMLIEKE YHVELVGHAF NDKELIVRYK 900 TDIDNQRIFY SDLNGFQMSR RQTYDKIPLQ GNYYPMPSLA FLQDSHGKRF SVHSKQSLGA 960 ASLKNGWLEI MLDRRLVQDD GRGLGQGVMD NRPMNVIFHL LMESNVSALP KTHSLLTLQP 1020 SLLSHRVGAH LNYPMHAFMS KKPHGKSFKL AQQSFAPLAA SLPCDVHIVN LKVPQPLRFP 1080 HTEAAEPRFA VLLQRRGWDA SYCKRGGLQC TTVGEEPVNL FYMFKDLSAV NVKATSLNLL 1140 HDDPEMLGYL EQIGDVAQEG NVLISPMEIQ AYKLDLQPPS TQEE* 1200 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00451 | GH38N_AMII_euk | 8.0e-109 | 167 | 453 | 288 | + 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. | ||
| cd11667 | GH38N_Man2A2 | 4.0e-152 | 167 | 518 | 352 | + N-terminal catalytic domain of Golgi alpha-mannosidase IIx, and similar proteins; glycoside hydrolase family 38 (GH38). This subfamily is represented by 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 (found in another subfamily), and as an isoenzyme of GMII. It is thought to also function in the N-glycosylation pathway. MX specifically hydrolyzes the same oligosaccharide substrate as does MII. It specifically removes two mannosyl residues from GlcNAc(Man)5(GlcNAc)2 to yield GlcNAc(Man)3(GlcNAc)2(GlcNAc, N-acetylglucosmine). | ||
| cd11666 | GH38N_Man2A1 | 2.0e-161 | 167 | 518 | 352 | + N-terminal catalytic domain of Golgi alpha-mannosidase II 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 of 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. | ||
| PLN02701 | PLN02701 | 0 | 128 | 1177 | 1052 | + alpha-mannosidase | ||
| cd10809 | GH38N_AMII_GMII_SfManIII_like | 0 | 166 | 518 | 353 | + 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. | ||
| Gene Ontology | |
|---|---|
| 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| DDBJ | BAF19191.2 | 0 | 154 | 1184 | 1 | 1032 | Os06g0245700 [Oryza sativa Japonica Group] |
| GenBank | EEC80313.1 | 0 | 78 | 1184 | 56 | 1150 | hypothetical protein OsI_22355 [Oryza sativa Indica Group] |
| GenBank | EEE65435.1 | 0 | 138 | 1184 | 47 | 1083 | hypothetical protein OsJ_20797 [Oryza sativa Japonica Group] |
| RefSeq | NP_001057277.1 | 0 | 1 | 1184 | 1 | 1173 | Os06g0245700 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | XP_002438145.1 | 0 | 1 | 1184 | 1 | 1184 | hypothetical protein SORBIDRAFT_10g008770 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3eju_A | 0 | 128 | 1172 | 41 | 1039 | A Chain A, Crystal Structure Of The Nasturtium Seedling Mutant Xyloglucanase Isoform Nxg1-Delta-Yniig |
| PDB | 3ejt_A | 0 | 128 | 1172 | 41 | 1039 | A Chain A, Crystal Structure Of The Nasturtium Seedling Mutant Xyloglucanase Isoform Nxg1-Delta-Yniig |
| PDB | 3ejs_A | 0 | 128 | 1172 | 41 | 1039 | A Chain A, Crystal Structure Of The Nasturtium Seedling Mutant Xyloglucanase Isoform Nxg1-Delta-Yniig |
| PDB | 3ejr_A | 0 | 128 | 1172 | 41 | 1039 | A Chain A, Crystal Structure Of The Nasturtium Seedling Mutant Xyloglucanase Isoform Nxg1-Delta-Yniig |
| PDB | 3ejq_A | 0 | 128 | 1172 | 41 | 1039 | A Chain A, Crystal Structure Of The Nasturtium Seedling Mutant Xyloglucanase Isoform Nxg1-Delta-Yniig |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| FL714386 | 273 | 254 | 526 | 0 |
| CB662086 | 281 | 298 | 578 | 0 |
| JG904639 | 284 | 902 | 1185 | 0 |
| JG907572 | 285 | 879 | 1163 | 0 |
| GR318037 | 268 | 127 | 394 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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