Basic Information | |
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Species | Phaseolus vulgaris |
Cazyme ID | Phvul.001G084700.1 |
Family | GH38 |
Protein Properties | Length: 1030 Molecular Weight: 117106 Isoelectric Point: 6.306 |
Chromosome | Chromosome/Scaffold: 01 Start: 15147569 End: 15163821 |
Description | Glycosyl hydrolase family 38 protein |
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 | 49 | 360 | 0 |
NVHLVAHTHDDVGWLKTVDQYYVGSNNSIQGACVENVLDSMVHALLADKNRKFIYVEMAFFKRWWRDQSEAVQDVVKKLVSSGQLEFINGAMSMHDEAVT HYIDMIDQTALGHQFLKEEFGVTPRIGWQIDPFGHSAVQAYLLGAEVGFDSLFFGRIDYQDRAKRKKEKSLEVIWQGSKSLGSSSQIFAGAFPENYEPPS GFYFEVNDNSPIVQDNMELFDYNVQERVNDFVAAALSQANITRTNHIMWTMGTDFKYQYAHTWFRQLDKLIHYVNKDGRVNALYSTPSIYTDAKYATNEY WPIKTDDFFPYA |
Full Sequence |
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Protein Sequence Length: 1030 Download |
MGEATIPHFQ QLMAKKLLFL LTLLEILLCG QSKFMVYNTS QGIVPGKLNV HLVAHTHDDV 60 GWLKTVDQYY VGSNNSIQGA CVENVLDSMV HALLADKNRK FIYVEMAFFK RWWRDQSEAV 120 QDVVKKLVSS GQLEFINGAM SMHDEAVTHY IDMIDQTALG HQFLKEEFGV TPRIGWQIDP 180 FGHSAVQAYL LGAEVGFDSL FFGRIDYQDR AKRKKEKSLE VIWQGSKSLG SSSQIFAGAF 240 PENYEPPSGF YFEVNDNSPI VQDNMELFDY NVQERVNDFV AAALSQANIT RTNHIMWTMG 300 TDFKYQYAHT WFRQLDKLIH YVNKDGRVNA LYSTPSIYTD AKYATNEYWP IKTDDFFPYA 360 DRANGYWTGY FTSRPAIKRY VRLMSGYYLA ARQLEFFRGR MNSGPNTDSL ADALAIAQHH 420 DAVTGTEKQH VANDYSKRLA IGYREAEELV SSSLACLVES PLLSRCQNPV PKFQQCPLLN 480 ISYCPASEVD LVQGKNLVIL VYNSLGWWRN EVIRFPVTEA NVIVQNSDGK EIESQLLPQA 540 EKYLDLRNYY VKAYVGRAPP KSPKYWLAFT VSVPPLGFST YTVSTAKKTG STRSSVATYK 600 SSEKSKFEVG KGNLKLKFST DQEKCTNYVN TRDKVAEQVE LSYLYYSGYN GTNQKDPQNS 660 GAYIFRPNGT YQINHEKKVP LTVLNGPVLD EVHQQINPWI YQITRLYKGK EHVEVEFIVG 720 PIPIEDGTGK EIATQISTTM ETNKTFYTDS NGRDFIKRIR DYRTDWDLEV NQPAAGNYYP 780 INLGIYMEDN KTEFSVLVDR AIGGSSLQDG QIELMLHRRL LLDDSRGVAE ALNETDCVGG 840 DCRGLTVQGK YYYRINPSGE GAKWRRTFGQ EIYSPLLLAF AEKDEKDDWM NSHVLTFSGI 900 DSSYALPDNI AIITLQELED GKILLRLAHL YEIEEDKDLS VMATVELKKL FPGRKIKEVK 960 EMSLSANQER TEMEKKRLNW KVEGSSGNRH VSRGGPVDPK ELKVELSPME IRTFIISFDG 1020 VSDQLFYSM* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd10809 | GH38N_AMII_GMII_SfManIII_like | 9.0e-73 | 47 | 371 | 357 | + 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. | ||
pfam01074 | Glyco_hydro_38 | 1.0e-94 | 49 | 360 | 316 | + Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. | ||
PLN02701 | PLN02701 | 4.0e-103 | 47 | 1014 | 1088 | + alpha-mannosidase | ||
cd00451 | GH38N_AMII_euk | 3.0e-105 | 48 | 324 | 277 | + 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. | ||
cd10810 | GH38N_AMII_LAM_like | 5.0e-177 | 48 | 324 | 279 | + 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 | CBI21276.1 | 0 | 18 | 1016 | 5 | 1005 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002276092.1 | 0 | 18 | 1016 | 5 | 1005 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002318770.1 | 0 | 19 | 1019 | 8 | 1012 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002321075.1 | 0 | 33 | 1019 | 24 | 1000 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002512840.1 | 0 | 15 | 1026 | 4 | 975 | 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 | 1o7d_A | 0 | 37 | 330 | 3 | 298 | C Chain C, The Structure Of The Bovine Lysosomal A-Mannosidase Suggests A Novel Mechanism For Low Ph Activation |
PDB | 3eju_A | 0 | 47 | 832 | 80 | 882 | C Chain C, The Structure Of The Bovine Lysosomal A-Mannosidase Suggests A Novel Mechanism For Low Ph Activation |
PDB | 3ejt_A | 0 | 47 | 832 | 80 | 882 | C Chain C, The Structure Of The Bovine Lysosomal A-Mannosidase Suggests A Novel Mechanism For Low Ph Activation |
PDB | 3ejs_A | 0 | 47 | 832 | 80 | 882 | C Chain C, The Structure Of The Bovine Lysosomal A-Mannosidase Suggests A Novel Mechanism For Low Ph Activation |
PDB | 3ejr_A | 0 | 47 | 832 | 80 | 882 | C Chain C, The Structure Of The Bovine Lysosomal A-Mannosidase Suggests A Novel Mechanism For Low Ph Activation |