y
Basic Information | |
---|---|
Species | Vitis vinifera |
Cazyme ID | GSVIVT01032586001 |
Family | GH38 |
Protein Properties | Length: 1057 Molecular Weight: 121011 Isoelectric Point: 7.9336 |
Chromosome | Chromosome/Scaffold: 14 Start: 28585492 End: 28592518 |
Description | golgi alpha-mannosidase II |
View CDS |
External Links |
---|
NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GH38 | 139 | 478 | 0 |
KIFVVPHSHNDPGWKLTVEEYYDRQSRHILDTIVETLSKDARRKFIWEEMSYLERWWRDASDTRKEAFTNLVKNGQLEIVGGGWVMNDEANSHYFAIIEQ ITEGNMWLNDTIGVVPKNSWAIDPFGYSPTMAYLLRRMGFENMLIQRTHYELKKELSWHKNLEYIWRQSWDAEESTDIFVHMMPFYSYDVPHTCGPEPAI CCQFDFARMRGFMYELCPWGQHPVETNQENVQERALKLLDQYKKKSTLYRTNTLLVPLGDDFRYISIDEAEAQFRNYQLLFDYINSNPSLNAEAKFGTLE DYFHTLREEADRINYSRPGEIGSGQVGGFPSLSGDFFTYA |
Full Sequence |
---|
Protein Sequence Length: 1057 Download |
MAFSSRRGGW AHSLLPSSNS KSKLPRKARK RTFLKDFFLA NFFTIGLSLS LIFLLFITFR 60 YGVPKPLAFK SSNSRLPKLR KQGPRKPISP EVAGSGAAVD ITTKDLYDKI EFLDKDGGPW 120 KQGWVVNYKG NEWDSEKLKI FVVPHSHNDP GWKLTVEEYY DRQSRHILDT IVETLSKDAR 180 RKFIWEEMSY LERWWRDASD TRKEAFTNLV KNGQLEIVGG GWVMNDEANS HYFAIIEQIT 240 EGNMWLNDTI GVVPKNSWAI DPFGYSPTMA YLLRRMGFEN MLIQRTHYEL KKELSWHKNL 300 EYIWRQSWDA EESTDIFVHM MPFYSYDVPH TCGPEPAICC QFDFARMRGF MYELCPWGQH 360 PVETNQENVQ ERALKLLDQY KKKSTLYRTN TLLVPLGDDF RYISIDEAEA QFRNYQLLFD 420 YINSNPSLNA EAKFGTLEDY FHTLREEADR INYSRPGEIG SGQVGGFPSL SGDFFTYADR 480 QHDYWSGYYV SRPFFKAVDR VLEQTLRATE MLIALLLGHC HRAQCERLPT GFAYKLTAAR 540 RNLALFQHHD GVTGTAKDHV VEDYGTRMHT SLQDLQIFMS KAIEVLLGIR HEKSDQTTAQ 600 FEPAQLRSKY DIQPTHRAIS PPEGSAQSVV FFNPLEQTRN EVVMVVVNRP DVTVLASNWT 660 CVKSQVSPEW QHDKSKIFTG RHRVHWKASV PAMGLETYYI AVGYVGCEKA KQAKLKFATK 720 SNHLPCPAPY ACSKLEGDTA EIQNRHQTLT FDVKLGLLQK ISHKDGSQSV VGEDISMYSS 780 WGSGAYLFKP TGDAQPIIKS GGQMVISEGP LMQEEYHVEL IGQDFNDKEL IVRYKTDIDN 840 KRIFYSDLNG FQMSRRETYD KIPLQGNYYP MPSLAFMQGS NGQRFSVHTR QSLGAASLKN 900 GWLEIMLDRR LLRDDERGLG QGVMDNRPMN VVFHILVESN ISSTSNPVSN PLPLDPSLLS 960 HSVDPRFVLM LQRRKWDSSY CRKGRSQCTR IADEPVNLFS MFKGLTVLNA RATSLNLLHE 1020 DTEMLGYSEK VGEAAQEGPV LISPMEIQAY KLELRP* 1080 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02701 | PLN02701 | 2.0e-42 | 966 | 1055 | 90 | + alpha-mannosidase | ||
cd11667 | GH38N_Man2A2 | 2.0e-152 | 138 | 489 | 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 | 8.0e-159 | 138 | 489 | 355 | + 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 | 99 | 943 | 880 | + alpha-mannosidase | ||
cd10809 | GH38N_AMII_GMII_SfManIII_like | 0 | 137 | 489 | 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 |
EMBL | CBI35021.1 | 0 | 1 | 1056 | 1 | 1056 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_196999.1 | 0 | 10 | 1056 | 22 | 1171 | GMII (GOLGI ALPHA-MANNOSIDASE II); alpha-mannosidase [Arabidopsis thaliana] |
RefSeq | XP_002276468.1 | 0 | 1 | 1056 | 1 | 1149 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002438145.1 | 0 | 94 | 1056 | 123 | 1178 | hypothetical protein SORBIDRAFT_10g008770 [Sorghum bicolor] |
RefSeq | XP_002517418.1 | 0 | 1 | 1056 | 1 | 1178 | 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 | 1ps3_A | 0 | 75 | 938 | 17 | 897 | A Chain A, Golgi Alpha-mannosidase Ii In Complex With Kifunensine |
PDB | 3eju_A | 0 | 75 | 938 | 17 | 897 | A Chain A, Golgi Alpha-mannosidase Ii In Complex With Kifunensine |
PDB | 3ejt_A | 0 | 75 | 938 | 17 | 897 | A Chain A, Golgi Alpha-mannosidase Ii In Complex With Kifunensine |
PDB | 3ejs_A | 0 | 75 | 938 | 17 | 897 | A Chain A, Golgi Alpha-mannosidase Ii In Complex With Kifunensine |
PDB | 3ejr_A | 0 | 75 | 938 | 17 | 897 | A Chain A, Golgi Alpha-mannosidase Ii In Complex With Kifunensine |