y
Basic Information | |
---|---|
Species | Linum usitatissimum |
Cazyme ID | Lus10015337 |
Family | GH38 |
Protein Properties | Length: 1249 Molecular Weight: 142412 Isoelectric Point: 6.9036 |
Chromosome | Chromosome/Scaffold: 635 Start: 4803 End: 10326 |
Description | golgi alpha-mannosidase II |
View CDS |
External Links |
---|
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GH38 | 158 | 248 | 1.4e-30 |
KVIVMPHSHNDPGWKLTVDEYYEKQSRHILDTIVETLSKDVRRKFIWEEMSYLEKWWRDASEGKRASFTKLVKNGQLEIVGGGWVMNDELT | |||
GH38 | 248 | 571 | 0 |
TVDEYYEKQSRHILDTIVETLSKDVRRKFIWEEMSYLEKWWRDASEGKRASFTKLVKNGQLEIVGGGWVMNDEANSHFFSIIEQITEGNIWLNDTIGIIP KNSWAIDPFGYSSTMAYLLRRMGFENMLIQRTHYELKKELALHRNLEFVWRQSWDAGETTDIFVHMMPFYSYDIPHTCGPEPAICCQFDFARVPGFFYEL CPWHQNPEETTPENVHERAKLLLDQYKKKSVLYRTNTLLIPLGDDFRYVTVDEAEAQYRNYQMLFDHINSNPSLNAEAKFGTLDDYFQALHEESDRKNYS VPGEIGSSHIGGFPSLSGDFFTYA |
Full Sequence |
---|
Protein Sequence Length: 1249 Download |
MPLSSYIGSR RGGGSVGGSG SGWPQSILPT STTSKSKLIP SRKPRKRGAL INFLFTNFFT 60 ISLSISLLFL FFTVLHFGFP KPLFSSAFSS MPSPPVRQRK TTVRRNSIQN GMSNGTTVDL 120 TTKDLYDKIK FLDKDGGPWK QGWRVSYRGN EWDDEKLKVI VMPHSHNDPG WKLTVDEYYE 180 KQSRHILDTI VETLSKDVRR KFIWEEMSYL EKWWRDASEG KRASFTKLVK NGQLEIVGGG 240 WVMNDELTVD EYYEKQSRHI LDTIVETLSK DVRRKFIWEE MSYLEKWWRD ASEGKRASFT 300 KLVKNGQLEI VGGGWVMNDE ANSHFFSIIE QITEGNIWLN DTIGIIPKNS WAIDPFGYSS 360 TMAYLLRRMG FENMLIQRTH YELKKELALH RNLEFVWRQS WDAGETTDIF VHMMPFYSYD 420 IPHTCGPEPA ICCQFDFARV PGFFYELCPW HQNPEETTPE NVHERAKLLL DQYKKKSVLY 480 RTNTLLIPLG DDFRYVTVDE AEAQYRNYQM LFDHINSNPS LNAEAKFGTL DDYFQALHEE 540 SDRKNYSVPG EIGSSHIGGF PSLSGDFFTY ADREQDYWSG YYVSRPFFKA VDRVLEQTLR 600 ATEMMVALFV GHCQRLQCEK LVIGFSHKLT AARRNLALFQ HHDGVTGTAK DHVVRDYGMR 660 MHTSLEDLQI FMSKAIEVLL GMHLEKLDLN PAKFEAEQVR AKYNVQPVHK ALSPSEGTAQ 720 SVVLFNPTEQ VREEVVMVVV NRPDVTVLDS NWTCVQSQVS PELQHDGNNI FSGRHRVHWK 780 ASVPAMGLET YYVANGYVGC EKAKPAKLKY VSPNSFSCPT SYACSKAAGD WAEIQNGQQT 840 LTFNINHGLL QNVKHKNGSS YVMAEEIGMY SSDGSGAYLF KPIGDAKSII QNDGITVITE 900 GPLMQEVFSY PNTAFRRNPV SHSTRIYNGG NTVQEFVVET EYHVELLGDE FNDRELIVRY 960 KTDIDNKGVF YSDLNGFQMS RRETYDKIPL QGNYYPMPSL AFIQGSNGDR FSVNSRQSLG 1020 VASLKDGWLE IMVDRRLLRD DGRGLGQGVT DNRPMNVVFH LLFETNISST SNPVSNPVPL 1080 SPSLLSHRIG AHLNYPLFAF ISKDHEELSL QTYGRSFSPL AASLPCDLHI VNFKVARPAL 1140 FSRELVGDPR FVRDPRFILI FQRRQWDASY CRTGRSQCTR FADVPVNIFN MFQGFSVLNA 1200 EATSLNLLHD DMDVLGYNEK VGDVSEDGRV SISPMEIQAY KLELRPNQ* 1260 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10809 | GH38N_AMII_GMII_SfManIII_like | 4.0e-48 | 156 | 266 | 111 | + 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. | ||
PLN02701 | PLN02701 | 5.0e-80 | 118 | 246 | 129 | + alpha-mannosidase | ||
cd11666 | GH38N_Man2A1 | 3.0e-145 | 240 | 582 | 343 | + 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 | 240 | 1245 | 1009 | + alpha-mannosidase | ||
cd10809 | GH38N_AMII_GMII_SfManIII_like | 0 | 240 | 582 | 343 | + 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 |
RefSeq | NP_196999.1 | 0 | 240 | 1248 | 166 | 1173 | GMII (GOLGI ALPHA-MANNOSIDASE II); alpha-mannosidase [Arabidopsis thaliana] |
RefSeq | XP_002276468.1 | 0 | 9 | 246 | 5 | 227 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002276468.1 | 0 | 240 | 1246 | 151 | 1149 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002517418.1 | 0 | 1 | 246 | 1 | 257 | mannosidase alpha class 2a, putative [Ricinus communis] |
RefSeq | XP_002517418.1 | 0 | 189 | 1248 | 122 | 1180 | mannosidase alpha class 2a, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1hxk_A | 0 | 240 | 1111 | 64 | 913 | A Chain A, Golgi Alpha-Mannosidase Ii In Complex With Deoxymannojirimicin |
PDB | 1hxk_A | 6e-32 | 109 | 246 | 2 | 140 | A Chain A, Golgi Alpha-Mannosidase Ii In Complex With Deoxymannojirimicin |
PDB | 1hww_A | 0 | 240 | 1111 | 64 | 913 | A Chain A, Golgi Alpha-Mannosidase Ii In Complex With Deoxymannojirimicin |
PDB | 1hww_A | 6e-32 | 109 | 246 | 2 | 140 | A Chain A, Golgi Alpha-Mannosidase Ii In Complex With Deoxymannojirimicin |
PDB | 1hty_A | 0 | 240 | 1111 | 64 | 913 | A Chain A, Golgi Alpha-Mannosidase Ii |