y
Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma05g32370.1 |
Family | GT8 |
Protein Properties | Length: 641 Molecular Weight: 73950.5 Isoelectric Point: 7.0955 |
Chromosome | Chromosome/Scaffold: 05 Start: 37302528 End: 37308088 |
Description | plant glycogenin-like starch initiation protein 1 |
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 |
GT8 | 310 | 520 | 1.79997e-41 |
YATILHSAHVYVCGAIAAAQSIRMSGSTRDLVILVDETISEYHRSGLEAAGWKIRTIQRIRNPKAEKDAYNEWNYSKFRLWQLTEYDKIIFIDADLLILR NIDFLFGMPEITATGNNGTLFNSGVMVVEPSNCTFKLLMDHINEFESYNGGDQGYLNEIFTWWHRIPRHMNFLKHFWVGDEEEKKQMKTLLFGADPPILY VLHYLGMKPWL |
Full Sequence |
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Protein Sequence Length: 641 Download |
MDTSPRAGEG RHRFPASIVD LYRRRLPKRN AKDVEKPIQL SIQDRSSRCN FSFLKPFVLL 60 MTICGTYVTL LYSPKVYNNN HLSSSGSGPN FVNRWIWDGL DPRYVSNVDI NWGDILQITA 120 KLTGKKEFQG VGLVNFNNTE LDHWEQLIPN ATHVVLELEY AAKNVTWESL YPEWIDEEEE 180 TEVPVCHSLP SLRSPGIRLN LIAVKLPHVN GGNWSRDVAR LHLQLAVARL ATSFKGNYPV 240 YVLFVTNFFP IPNLFTCKEL VGHEGDVWLY KPNLKVLGEK LHLPVGSCEL ALPLRGKELS 300 YVGNVRREAY ATILHSAHVY VCGAIAAAQS IRMSGSTRDL VILVDETISE YHRSGLEAAG 360 WKIRTIQRIR NPKAEKDAYN EWNYSKFRLW QLTEYDKIIF IDADLLILRN IDFLFGMPEI 420 TATGNNGTLF NSGVMVVEPS NCTFKLLMDH INEFESYNGG DQGYLNEIFT WWHRIPRHMN 480 FLKHFWVGDE EEKKQMKTLL FGADPPILYV LHYLGMKPWL CFRDYDCNWN SDIFHEFASD 540 VAHGRWWKVH DAMPELLQQF CMLKSKQKAQ LEWDRRQAEI ANYTNGHWQI KVKDKRLKKC 600 IDNLCSWENM LKHWGETNWT DDESYTPTPP AISTSSLSDL * 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00505 | Glyco_transf_8 | 5.0e-9 | 313 | 519 | 245 | + Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis and glycogen synthesis. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. GT-8 comprises enzymes with a number of known activities: lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase, and N-acetylglucosaminyltransferase. GT-8 enzymes contains a conserved DXD motif which is essential in the coordination of a catalytic divalent cation, most commonly Mn2+. | ||
PLN00176 | PLN00176 | 6.0e-16 | 307 | 519 | 257 | + galactinol synthase | ||
cd06914 | GT8_GNT1 | 2.0e-16 | 320 | 519 | 235 | + GNT1 is a fungal enzyme that belongs to the GT 8 family. N-acetylglucosaminyltransferase is a fungal enzyme that catalyzes the addition of N-acetyl-D-glucosamine to mannotetraose side chains by an alpha 1-2 linkage during the synthesis of mannan. The N-acetyl-D-glucosamine moiety in mannan plays a role in the attachment of mannan to asparagine residues in proteins. The mannotetraose and its N-acetyl-D-glucosamine derivative side chains of mannan are the principle immunochemical determinants on the cell surface. N-acetylglucosaminyltransferase is a member of glycosyltransferase family 8, which are, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed, retaining glycosyltransferases. | ||
pfam01501 | Glyco_transf_8 | 5.0e-40 | 311 | 521 | 257 | + Glycosyl transferase family 8. This family includes enzymes that transfer sugar residues to donor molecules. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. This family includes Lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, and glycogenin glucosyltransferase. | ||
cd02537 | GT8_Glycogenin | 5.0e-72 | 308 | 553 | 256 | + Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen. Glycogenin initiates the biosynthesis of glycogen by incorporating glucose residues through a self-glucosylation reaction at a Tyr residue, and then acts as substrate for chain elongation by glycogen synthase and branching enzyme. It contains a conserved DxD motif and an N-terminal beta-alpha-beta Rossmann-like fold that are common to the nucleotide-binding domains of most glycosyltransferases. The DxD motif is essential for coordination of the catalytic divalent cation, most commonly Mn2+. Glycogenin can be classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. It is placed in glycosyltransferase family 8 which includes lipopolysaccharide glucose and galactose transferases and galactinol synthases. |
Gene Ontology | |
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GO Term | Description |
GO:0016757 | transferase activity, transferring glycosyl 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 |
GenBank | AAX33316.1 | 0 | 4 | 640 | 10 | 649 | secondary cell wall-related glycosyltransferase family 8 [Populus tremula x Populus tremuloides] |
GenBank | AAX33317.1 | 0 | 1 | 640 | 1 | 636 | secondary cell wall-related glycosyltransferase family 8 [Populus tremula x Populus tremuloides] |
RefSeq | XP_002275240.1 | 0 | 1 | 638 | 1 | 635 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002310513.1 | 0 | 1 | 640 | 1 | 630 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002517237.1 | 0 | 20 | 636 | 24 | 625 | glycogenin, 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 | 3u2t_A | 3e-22 | 296 | 519 | 14 | 242 | A Chain A, Crystal Structure Of Human Glycogenin-1 (Gyg1) Complexed With Manganese |
PDB | 3u2x_B | 2e-21 | 308 | 519 | 5 | 221 | A Chain A, Crystal Structure Of Human Glycogenin-1 (Gyg1) Complexed With Manganese |
PDB | 3u2x_A | 2e-21 | 308 | 519 | 5 | 221 | A Chain A, Crystal Structure Of Human Glycogenin-1 (Gyg1) Complexed With Manganese |
PDB | 3u2v_B | 2e-21 | 308 | 519 | 5 | 221 | A Chain A, Crystal Structure Of Human Glycogenin-1 (Gyg1) Complexed With Manganese |
PDB | 3u2v_A | 2e-21 | 308 | 519 | 5 | 221 | A Chain A, Crystal Structure Of Human Glycogenin-1 (Gyg1) Complexed With Manganese |