y
Basic Information | |
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Species | Aquilegia coerulea |
Cazyme ID | Aquca_002_00345.1 |
Family | GH38 |
Protein Properties | Length: 1103 Molecular Weight: 126830 Isoelectric Point: 6.8139 |
Chromosome | Chromosome/Scaffold: 2 Start: 3059674 End: 3064854 |
Description | golgi alpha-mannosidase II |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH38 | 265 | 483 | 3.6e-32 |
NPFGYSPTMAYLLRRMGFENMLIQRTHYELKKDLAKHKNLEYIWRQTWDIDESTDIFVHMMPFYSYDIPHTCGPEPAICCQFDFARIQGNSMYELCPWRQ HPVEIDQDNVQDQALKLLDQYRKKSTLYRTNTLLVPLGDDFRYISVDEAEAQFRNYQLLFDYINSDSNLNAEAKFGTLDDYFEALREETDRINYSRPGEI GSAQVMGFPSLSGDFFTYA | |||
GH38 | 162 | 261 | 8.7e-33 |
KIFVVPHSHNDPGWKLTVDEYYEKQSRRILDTIVETLSKDVRRKFIWEEMSYLERWWRDSSETSRESFSNLVRNGQLEIVGGGWVMNDEANSHYFGILEQ |
Full Sequence |
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Protein Sequence Length: 1103 Download |
MAFFSSYTGN TRRGGWTQSL LPTTTSSSTS SSSSPRPKHS RKPRHRRISS SIQNFLITNF 60 FTIGLSISLL FFITVVIRYG IPNPLSSHTK HRHSSFYRSR KPINRKPILS DSGIQVGSIS 120 VVDITTKDLY DKIEFLDIDG GPWKQGWRVN YKGDEWDFEK LKIFVVPHSH NDPGWKLTVD 180 EYYEKQSRRI LDTIVETLSK DVRRKFIWEE MSYLERWWRD SSETSRESFS NLVRNGQLEI 240 VGGGWVMNDE ANSHYFGILE QGCFNPFGYS PTMAYLLRRM GFENMLIQRT HYELKKDLAK 300 HKNLEYIWRQ TWDIDESTDI FVHMMPFYSY DIPHTCGPEP AICCQFDFAR IQGNSMYELC 360 PWRQHPVEID QDNVQDQALK LLDQYRKKST LYRTNTLLVP LGDDFRYISV DEAEAQFRNY 420 QLLFDYINSD SNLNAEAKFG TLDDYFEALR EETDRINYSR PGEIGSAQVM GFPSLSGDFF 480 TYADRQQDYW SGYYVSRPFF KAVDRVLEQT LRGSEIMIAL LLGYCHKPVC EKFPTSFTYK 540 LTAARRNLAL FQHHDGVTGT AKDHVVEDYG IRMHTSLQDL QIFMSKAVEL LLGYPHEKSD 600 KDPSMFEPEQ VRSKYDVQPV HRSINTPEGS AHAVVFFNPL EQTRDEIVMV TVNRPDMTVL 660 DSNWSCVKSQ VSPEFQHDKG KILTGKHRLY WQASVPALGL QTYYIAHGFN GCEKAKPAIL 720 RLFSDSDQLH CPSPYACSRL EEDMAEIKNQ HQTLSFDLRL GLLKKINDND GTMTVVGEEI 780 GMYSSPESGA YLFKPSGEAK PIVQGGGHMV ISEGPLVQEF YSYPKTAWDE SPISHSTRIY 840 SGKGTTQEFI IEKEYHVELL GHDFNDKELI VRYKTDLDSR RVFHSDLNGF QTSRRETYDK 900 IPLQGNYYPM PSLAFLQSLN GHRLSVHSRQ SLGVASLENG WLEIMLDRRL VRDDGRGLGQ 960 GVMDNRPMNI IFNILKESNI SSALNPVSTS LPLNPSLLSH RQPPEDSRFV LVLQRRQWDS 1020 SYCRKGGTNC SKIADEAVNL FHMFKDLRVL NARATSLNLL HDDTEKLGYI EQSGDVAQEG 1080 HVKISPMEIQ AYKMELRPQE RT* 1140 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02701 | PLN02701 | 2.0e-40 | 1000 | 1097 | 98 | + alpha-mannosidase | ||
cd11667 | GH38N_Man2A2 | 8.0e-136 | 161 | 494 | 353 | + 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 | 8.0e-139 | 161 | 494 | 353 | + 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 | 122 | 983 | 882 | + alpha-mannosidase | ||
cd10809 | GH38N_AMII_GMII_SfManIII_like | 0 | 160 | 494 | 354 | + 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 | |
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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 | CBI35021.1 | 0 | 10 | 1098 | 4 | 1056 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_196999.1 | 0 | 4 | 1100 | 3 | 1173 | GMII (GOLGI ALPHA-MANNOSIDASE II); alpha-mannosidase [Arabidopsis thaliana] |
RefSeq | XP_002276468.1 | 0 | 10 | 1098 | 4 | 1149 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002438145.1 | 0 | 73 | 1098 | 71 | 1178 | hypothetical protein SORBIDRAFT_10g008770 [Sorghum bicolor] |
RefSeq | XP_002517418.1 | 0 | 4 | 1100 | 3 | 1180 | mannosidase alpha class 2a, 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 | 103 | 1080 | 22 | 988 | A Chain A, Golgi Alpha-mannosidase Ii In Complex With Kifunensine |
PDB | 1hxk_A | 0 | 116 | 1080 | 5 | 958 | A Chain A, Golgi Alpha-Mannosidase Ii In Complex With Deoxymannojirimicin |
PDB | 1hww_A | 0 | 116 | 1080 | 5 | 958 | A Chain A, Golgi Alpha-Mannosidase Ii In Complex With Deoxymannojirimicin |
PDB | 1hty_A | 0 | 116 | 1080 | 5 | 958 | A Chain A, Golgi Alpha-Mannosidase Ii |
PDB | 3eju_A | 0 | 103 | 1080 | 22 | 988 | A Chain A, Golgi Alpha-Mannosidase Ii |