Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.009G168000.4 |
Family | GT13 |
Protein Properties | Length: 423 Molecular Weight: 49449.5 Isoelectric Point: 8.8819 |
Chromosome | Chromosome/Scaffold: 09 Start: 12774544 End: 12779205 |
Description | alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase, putative |
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 |
GT13 | 1 | 411 | 0 |
MRLFVTQSKYEDRLAAAIESENHCTSQSRLLIDQISIQQGTIVSLQEQNKRQSEECRQLKALLEDLERKGLKKLVDKVPVAAVVIMACNRADYLERTIES VLKYQSSVASKYPLFVSQDGTDPNVRSKAMSYDQLMYIQHLDSEPVHTERPGELIAYYKIARHYKWAMDQLFYKHNFSRVIILEDDMEIAPDFFDYFEAA AALLDKDKSIMAVSSWNDNGQKQFVHDPYELYRSDFFPGLGWMLTKSIWDELSPKWPKAYWDDWLRLKENHKGRQFIRPEVCRTYNFGEHGSSMGQFFQQ YLQPIKLNDVKVDWKSRDLSYLMKDKYTKHFADIVRKAKPIQGTDAVLKASNIEGDVRIQYKDQPDFERIARQLGIFQEWKDGIPRTSFKGVVVFRYRTT RRVFLVGPDSL |
Full Sequence |
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Protein Sequence Length: 423 Download |
MRLFVTQSKY EDRLAAAIES ENHCTSQSRL LIDQISIQQG TIVSLQEQNK RQSEECRQLK 60 ALLEDLERKG LKKLVDKVPV AAVVIMACNR ADYLERTIES VLKYQSSVAS KYPLFVSQDG 120 TDPNVRSKAM SYDQLMYIQH LDSEPVHTER PGELIAYYKI ARHYKWAMDQ LFYKHNFSRV 180 IILEDDMEIA PDFFDYFEAA AALLDKDKSI MAVSSWNDNG QKQFVHDPYE LYRSDFFPGL 240 GWMLTKSIWD ELSPKWPKAY WDDWLRLKEN HKGRQFIRPE VCRTYNFGEH GSSMGQFFQQ 300 YLQPIKLNDV KVDWKSRDLS YLMKDKYTKH FADIVRKAKP IQGTDAVLKA SNIEGDVRIQ 360 YKDQPDFERI ARQLGIFQEW KDGIPRTSFK GVVVFRYRTT RRVFLVGPDS LRQLGIKDAR 420 NI* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam13641 | Glyco_tranf_2_3 | 0.0009 | 82 | 208 | 130 | + Glycosyltransferase like family 2. Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis. | ||
cd00761 | Glyco_tranf_GTA_type | 0.0002 | 83 | 278 | 199 | + Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold. Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities. | ||
cd02514 | GT13_GLCNAC-TI | 3.0e-166 | 80 | 391 | 317 | + GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GLCNAC-T I , GNT-I) transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide, an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localized to the Golgi apparatus. The catalytic domain is located at the C-terminus. These proteins are members of the glycosy transferase family 13. | ||
pfam03071 | GNT-I | 0 | 1 | 418 | 426 | + GNT-I family. Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GNT-I, GLCNAC-T I) EC:2.4.1.101 transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide. This is an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localised to the Golgi apparatus, and is probably distributed in all tissues. The catalytic domain is located at the C-terminus. |
Gene Ontology | |
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GO Term | Description |
GO:0000139 | Golgi membrane |
GO:0003827 | alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity |
GO:0006487 | protein N-linked glycosylation |
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 | CAC80697.1 | 0 | 1 | 419 | 26 | 446 | N-acetylglucosaminyltransferase I [Solanum tuberosum] |
EMBL | CAC80702.1 | 0 | 1 | 419 | 26 | 446 | N-acetylglucosaminyltransferase I [Nicotiana tabacum] |
EMBL | CBI29533.1 | 0 | 1 | 416 | 24 | 438 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_195537.2 | 0 | 1 | 419 | 24 | 444 | CGL1 (COMPLEX GLYCAN LESS 1); alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase/ protein N-acetylglucosaminyltransferase/ transferase, transferring glycosyl groups [Arabidopsis thaliana] |
RefSeq | XP_002313578.1 | 0 | 1 | 422 | 24 | 444 | predicted protein [Populus trichocarpa] |
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 | 1foa_A | 0 | 75 | 410 | 3 | 339 | A Chain A, Crystal Structure Of N-acetylglucosaminyltransferase I |
PDB | 1fo9_A | 0 | 75 | 410 | 3 | 339 | A Chain A, Crystal Structure Of N-acetylglucosaminyltransferase I |
PDB | 1fo8_A | 0 | 80 | 410 | 3 | 334 | A Chain A, Crystal Structure Of N-Acetylglucosaminyltransferase I |
PDB | 2apc_A | 0 | 80 | 410 | 2 | 333 | A Chain A, Crystal Structure Of N-Acetylglucosaminyltransferase I |
PDB | 2am5_A | 0 | 80 | 410 | 2 | 333 | A Chain A, Crystal Structure Of N-Acetylglucosaminyltransferase I |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
ES841656 | 286 | 103 | 388 | 0 |
EH731153 | 291 | 127 | 417 | 0 |
GO802527 | 323 | 6 | 325 | 0 |
DT501093 | 241 | 1 | 241 | 0 |
GO802714 | 315 | 6 | 317 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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