Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma05g27431.1 |
Family | GT57 |
Protein Properties | Length: 384 Molecular Weight: 43028.9 Isoelectric Point: 8.6903 |
Chromosome | Chromosome/Scaffold: 05 Start: 33362847 End: 33368939 |
Description | ALG6, ALG8 glycosyltransferase family |
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 |
GT57 | 2 | 375 | 0 |
LFIVDHVHFQYNGFLIGILLISLSYLEEGRDLLGGFVFAVLLCFKHLFAVAAPVYFVYLLRHYCWGGTVRGIGRLLIMGGVVTAVFASAFGPFFHLGQTQ QIIQRLFPFGRGLCHAYWAPNFWVFYIMSDKGLAFIFRKLGFNVQTPTGSFTAGLVGDSSPFSVLPQITPFVTFIMVLLALSPCLFKAWKNPQPQMISRW IAYAYTCGFLFGWHVHEKASLHFVIPLAIVAPQTLEDARHYFLLSIVSCYSIFPLLFEAQENSIKVLLLLLHSILMWSGFSAQFCDGAEATRAPTANSKK NADQFVSEGNSGATVNKGFAIGWIERIYLIGLVVVEIWGQILYPLLLGDKFAFAPLMLISIYCAFGIMYSWIWQ |
Full Sequence |
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Protein Sequence Length: 384 Download |
MLFIVDHVHF QYNGFLIGIL LISLSYLEEG RDLLGGFVFA VLLCFKHLFA VAAPVYFVYL 60 LRHYCWGGTV RGIGRLLIMG GVVTAVFASA FGPFFHLGQT QQIIQRLFPF GRGLCHAYWA 120 PNFWVFYIMS DKGLAFIFRK LGFNVQTPTG SFTAGLVGDS SPFSVLPQIT PFVTFIMVLL 180 ALSPCLFKAW KNPQPQMISR WIAYAYTCGF LFGWHVHEKA SLHFVIPLAI VAPQTLEDAR 240 HYFLLSIVSC YSIFPLLFEA QENSIKVLLL LLHSILMWSG FSAQFCDGAE ATRAPTANSK 300 KNADQFVSEG NSGATVNKGF AIGWIERIYL IGLVVVEIWG QILYPLLLGD KFAFAPLMLI 360 SIYCAFGIMY SWIWQLISIV KSR* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03155 | Alg6_Alg8 | 5.0e-55 | 2 | 374 | 375 | + ALG6, ALG8 glycosyltransferase family. N-linked (asparagine-linked) glycosylation of proteins is mediated by a highly conserved pathway in eukaryotes, in which a lipid (dolichol phosphate)-linked oligosaccharide is assembled at the endoplasmic reticulum membrane prior to the transfer of the oligosaccharide moiety to the target asparagine residues. This oligosaccharide is composed of Glc(3)Man(9)GlcNAc(2). The addition of the three glucose residues is the final series of steps in the synthesis of the oligosaccharide precursor. Alg6 transfers the first glucose residue, and Alg8 transfers the second one. In the human alg6 gene, a C->T transition, which causes Ala333 to be replaced with Val, has been identified as the cause of a congenital disorder of glycosylation, designated as type Ic OMIM:603147. |
Gene Ontology | |
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GO Term | Description |
GO:0005789 | endoplasmic reticulum membrane |
GO:0016758 | transferase activity, transferring hexosyl groups |
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 | CBI16712.1 | 0 | 2 | 382 | 108 | 471 | unnamed protein product [Vitis vinifera] |
GenBank | EAY87118.1 | 0 | 2 | 381 | 150 | 517 | hypothetical protein OsI_08520 [Oryza sativa Indica Group] |
RefSeq | NP_001047779.1 | 0 | 2 | 381 | 147 | 514 | Os02g0688500 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_181994.5 | 0 | 2 | 380 | 145 | 505 | transferase, transferring glycosyl groups / transferase, transferring hexosyl groups [Arabidopsis thaliana] |
RefSeq | XP_002269114.1 | 0 | 2 | 382 | 152 | 531 | PREDICTED: hypothetical protein [Vitis vinifera] |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
dolichyl-diphosphooligosaccharide biosynthesis | RXN-5471 | EC-2.4.1.265 | Dol-P-Glc:Glc1Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase |