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Basic Information | |
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Species | Sorghum bicolor |
Cazyme ID | Sb01g026405.1 |
Family | GH38 |
Protein Properties | Length: 875 Molecular Weight: 98217.9 Isoelectric Point: 7.2346 |
Chromosome | Chromosome/Scaffold: 1 Start: 44440213 End: 44464605 |
Description | Glycosyl hydrolase family 38 protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH38 | 1 | 220 | 0 |
MHDEAVVHYIDMIDQTTLGHRMIKKQFKKIPRAGWQIDPFGHSAVQAYLLGAELGFDSVHFARIDYQDRATRKANKGLEVIWRGSRTFGSSSQIFTNVFP DHYNAPDGFSFEVLAENVIPVQDDMSLFDYNVQERVNDFVATAIAQANVTRTNHIMWTMGDDFNYQYAESWFRNMDKLIQYVNKDGRVHALYSTPSIYTD AKHASNESWPVKYDDYFPYA |
Full Sequence |
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Protein Sequence Length: 875 Download |
MHDEAVVHYI DMIDQTTLGH RMIKKQFKKI PRAGWQIDPF GHSAVQAYLL GAELGFDSVH 60 FARIDYQDRA TRKANKGLEV IWRGSRTFGS SSQIFTNVFP DHYNAPDGFS FEVLAENVIP 120 VQDDMSLFDY NVQERVNDFV ATAIAQANVT RTNHIMWTMG DDFNYQYAES WFRNMDKLIQ 180 YVNKDGRVHA LYSTPSIYTD AKHASNESWP VKYDDYFPYA DSTNAYWTGY FTSRPTFKRY 240 IRVYSGYYLA ARQIEFLIGR SSLGLFTSSL EDAMGIAQHH DAISGTAKQH TTDDYSKRIA 300 IGASKVEKGV NIALTCLTNS NKTCASSTVK FSQCPLLNIS YCPSTEEAIS ATKHLVVVAY 360 NPLGWERSDF IRLPVNDENL VVKSFDGNIV VSQIVEVDNV TGNLRKLYVK AFLGVATDKA 420 PKYWLTFQAS VPPMGWNSYF ILKSTGAGYN NTEYVPAVVS PSNRTIEVGP GHLKMSFSSA 480 SGQLERIINS ASGVDLPVQQ SFLWYRSSKG DSLDPQASGA YIFRPDGNTP TIVSSSVTLK 540 VIRGPLFDEV HQQFSSWIYQ ITRLYKNKEH AEVEYTIGPI PVDDDVGKEV ITQLTANMST 600 NSTFYTDSNG RDFLKRVRNY RKDWNLQVTQ PVAGNYYPVN LGVYIADNKY ELSVLVDRAI 660 GASSIQDGQL EIMLHRRLLN DDGRGVAEPL DEVVCVDQHC EGLTARGTYY INVEKLGHGA 720 HWRRTYGQQV YSPFLLAFTH EDATSAKSYN VAKATMMDVN YSLPDNVAII TLQNLDDGTT 780 LLRLAHLFQA GEDPKYSVVA KVDLKKVFGR RTIKELTETN LSANQKKSEM KKLKWRVIGD 840 MENGTTSVKG GPVDCRALVV ALGPMEIRTF LLRF* 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07748 | Glyco_hydro_38C | 3.0e-41 | 452 | 870 | 453 | + Glycosyl hydrolases family 38 C-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. | ||
pfam01074 | Glyco_hydro_38 | 1.0e-55 | 1 | 220 | 224 | + Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. | ||
cd00451 | GH38N_AMII_euk | 1.0e-62 | 1 | 184 | 184 | + 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. | ||
PLN02701 | PLN02701 | 4.0e-76 | 1 | 688 | 774 | + alpha-mannosidase | ||
cd10810 | GH38N_AMII_LAM_like | 6.0e-102 | 1 | 184 | 186 | + 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 |
GenBank | ABG65906.1 | 0 | 1 | 874 | 1 | 873 | glycosyl hydrolase family 38 protein, putative, expressed [Oryza sativa (japonica cultivar-group)] |
GenBank | EEC66555.1 | 0 | 1 | 874 | 132 | 1004 | hypothetical protein OsI_32713 [Oryza sativa Indica Group] |
RefSeq | NP_001064140.1 | 0 | 1 | 874 | 132 | 1004 | Os10g0140200 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_002464752.1 | 0 | 1 | 874 | 134 | 1007 | hypothetical protein SORBIDRAFT_01g026390 [Sorghum bicolor] |
RefSeq | XP_002464754.1 | 0 | 1 | 874 | 1 | 874 | hypothetical protein SORBIDRAFT_01g026405 [Sorghum bicolor] |
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_D | 0 | 472 | 715 | 9 | 246 | C Chain C, The Structure Of The Bovine Lysosomal A-Mannosidase Suggests A Novel Mechanism For Low Ph Activation |
PDB | 1hxk_A | 0 | 1 | 688 | 137 | 850 | A Chain A, Golgi Alpha-Mannosidase Ii In Complex With Deoxymannojirimicin |
PDB | 1hww_A | 0 | 1 | 688 | 137 | 850 | A Chain A, Golgi Alpha-Mannosidase Ii In Complex With Deoxymannojirimicin |
PDB | 1hty_A | 0 | 1 | 688 | 137 | 850 | A Chain A, Golgi Alpha-Mannosidase Ii |
PDB | 1ps3_A | 0 | 1 | 688 | 167 | 880 | A Chain A, Golgi Alpha-mannosidase Ii In Complex With Kifunensine |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO780062 | 602 | 201 | 798 | 0 |
HO780062 | 81 | 121 | 201 | 0 |
GO883487 | 330 | 460 | 789 | 0 |
GO857052 | 328 | 458 | 785 | 0 |
HO780062 | 55 | 280 | 329 | 0.95 |
Sequence Alignments (This image is cropped. Click for full image.) |
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