y
Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.L01540.1 |
Family | GT8 |
Protein Properties | Length: 482 Molecular Weight: 55737.1 Isoelectric Point: 9.8925 |
Chromosome | Chromosome/Scaffold: 258 Start: 9513 End: 11450 |
Description | plant glycogenin-like starch initiation protein 4 |
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 |
GT8 | 190 | 411 | 3.40516e-43 |
YLSRSSQRKANGTKYRPREAYATVLHSSEAYVCGAISLAQSIRRTGSTKDLVLLADDSITSKSLAGLRAAGWKIRHIHRIRSPNAKKGAYNEWNFSKLRV WQLTQYDKVIFIDADLIVLRNLDEFFVYPQLSAVPNNGVLFNSGIMVIEPSNCVFEDLMSKSFKLDSYNGGDQGFLNEFFTWWHRWPSRLNYLKIFARRK DKEHTVPDNLYTMHFLGLKPWM |
Full Sequence |
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Protein Sequence Length: 482 Download |
MKGKKVRVGF VNIDDITDPE FAMKGLAKAV KVTFDRVPGN LTWVNFFPSW INEDPKGRKP 60 SCPDIPMPKF EDYRDLDVIV AKVPCEDGGD RRRGLRDVFR LQVNLVVANL AVGTGRINLD 120 MNRKIYAVFL GSCGPMVEIF RCDDLVRHVG DYWVYKPEQG RLKQKVLMPV GSCQIAPAYA 180 ENGKERWRGY LSRSSQRKAN GTKYRPREAY ATVLHSSEAY VCGAISLAQS IRRTGSTKDL 240 VLLADDSITS KSLAGLRAAG WKIRHIHRIR SPNAKKGAYN EWNFSKLRVW QLTQYDKVIF 300 IDADLIVLRN LDEFFVYPQL SAVPNNGVLF NSGIMVIEPS NCVFEDLMSK SFKLDSYNGG 360 DQGFLNEFFT WWHRWPSRLN YLKIFARRKD KEHTVPDNLY TMHFLGLKPW MCYRDYDCNW 420 DKESYHAFAS DSVNRLWWEV YDSMPRKLQS FCGLTEKMDF RIRKWRGIAK KANLANGHWK 480 IN 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00505 | Glyco_transf_8 | 2.0e-12 | 282 | 410 | 164 | + 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 | 3.0e-15 | 198 | 442 | 289 | + galactinol synthase | ||
cd06914 | GT8_GNT1 | 3.0e-16 | 210 | 370 | 173 | + 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 | 8.0e-35 | 211 | 410 | 246 | + 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 | 4.0e-71 | 208 | 444 | 247 | + 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 | ABR67414.1 | 0 | 4 | 481 | 106 | 598 | glycosyl transferase [Cucumis melo] |
EMBL | CAN81983.1 | 0 | 1 | 481 | 56 | 533 | hypothetical protein [Vitis vinifera] |
RefSeq | NP_172373.3 | 0 | 4 | 481 | 75 | 553 | PGSIP5 (PLANT GLYCOGENIN-LIKE STARCH INITIATION PROTEIN 5); transferase, transferring glycosyl groups [Arabidopsis thaliana] |
RefSeq | NP_175891.1 | 0 | 1 | 481 | 67 | 544 | PGSIP4 (PLANT GLYCOGENIN-LIKE STARCH INITIATION PROTEIN 4); transferase, transferring glycosyl groups [Arabidopsis thaliana] |
RefSeq | XP_002280832.1 | 0 | 1 | 481 | 56 | 533 | PREDICTED: hypothetical protein [Vitis vinifera] |
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 | 3u2w_B | 2e-22 | 208 | 443 | 5 | 256 | A Chain A, Golgi Alpha-Mannosidase Ii |
PDB | 3u2w_A | 2e-22 | 208 | 443 | 5 | 256 | A Chain A, Golgi Alpha-Mannosidase Ii |
PDB | 3qvb_A | 2e-22 | 208 | 443 | 5 | 256 | A Chain A, Golgi Alpha-Mannosidase Ii |
PDB | 3q4s_A | 2e-22 | 208 | 443 | 5 | 256 | A Chain A, Crystal Structure Of Human Glycogenin-1 (Gyg1), Apo Form |
PDB | 3u2x_B | 6e-22 | 208 | 443 | 5 | 256 | A Chain A, Crystal Structure Of Human Glycogenin-1 (Gyg1), Apo Form |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
EL450640 | 321 | 124 | 444 | 0 |
EL376918 | 266 | 217 | 481 | 0 |
DN503302 | 243 | 194 | 435 | 0 |
CO253323 | 313 | 153 | 457 | 0 |
EE614675 | 262 | 124 | 385 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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