y
Basic Information | |
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Species | Setaria italica |
Cazyme ID | Si006441m |
Family | GT13 |
Protein Properties | Length: 443 Molecular Weight: 51293.8 Isoelectric Point: 7.2808 |
Chromosome | Chromosome/Scaffold: 4 Start: 38699645 End: 38706175 |
Description | alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase, putative |
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 |
GT13 | 22 | 437 | 0 |
IQVRLFATQSHYADRLAEAERSENQCTSQLKSLIDQVSMQQEKIVALEEMKIRQDEERAQLKILIQDLEKRSVQKLLNKNVVPVAAVVIMACNRPDYLER TVESILKYQTSVASKFPLFISQDGTNGAVKKKALDYKQITYMQHMDLEPVRAERPGELTAYYKIAKHYKWALDQLFIKHNFARVIILEDDMEIAPDFFDY FEAAAKLLDNDKTIMAVSSWNDNGQKQFVNDPKALYRSDFFPGLGWMLTKSTWIELSPKWPKAYWDDWVRLKEVHGNRQFIHPEICRTYNFGKHGSSLGQ FFEQYLEPIKLNDVHIDWNSEDLSYLREDKFLTKFGKEVASAMPLHGSDAVLKAQNMAADVRIQYNDQEDFEQIARQFGIFEEWKDGIPRTAYKGVVVFR YKSSPRRIFLVSPDSL |
Full Sequence |
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Protein Sequence Length: 443 Download |
MARSPCDLRL LLLAAAAAFI YIQVRLFATQ SHYADRLAEA ERSENQCTSQ LKSLIDQVSM 60 QQEKIVALEE MKIRQDEERA QLKILIQDLE KRSVQKLLNK NVVPVAAVVI MACNRPDYLE 120 RTVESILKYQ TSVASKFPLF ISQDGTNGAV KKKALDYKQI TYMQHMDLEP VRAERPGELT 180 AYYKIAKHYK WALDQLFIKH NFARVIILED DMEIAPDFFD YFEAAAKLLD NDKTIMAVSS 240 WNDNGQKQFV NDPKALYRSD FFPGLGWMLT KSTWIELSPK WPKAYWDDWV RLKEVHGNRQ 300 FIHPEICRTY NFGKHGSSLG QFFEQYLEPI KLNDVHIDWN SEDLSYLRED KFLTKFGKEV 360 ASAMPLHGSD AVLKAQNMAA DVRIQYNDQE DFEQIARQFG IFEEWKDGIP RTAYKGVVVF 420 RYKSSPRRIF LVSPDSLRQL GV* 480 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00761 | Glyco_tranf_GTA_type | 0.009 | 108 | 241 | 138 | + 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. | ||
pfam13641 | Glyco_tranf_2_3 | 0.004 | 107 | 327 | 244 | + Glycosyltransferase like family 2. Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis. | ||
cd06532 | Glyco_transf_25 | 0.002 | 149 | 237 | 96 | + Glycosyltransferase family 25 [lipooligosaccharide (LOS) biosynthesis protein] is a family of glycosyltransferases involved in LOS biosynthesis. The members include the beta(1,4) galactosyltransferases: Lgt2 of Moraxella catarrhalis, LgtB and LgtE of Neisseria gonorrhoeae and Lic2A of Haemophilus influenzae. M. catarrhalis Lgt2 catalyzes the addition of galactose (Gal) to the growing chain of LOS on the cell surface. N. gonorrhoeae LgtB and LgtE link Gal-beta(1,4) to GlcNAc (N-acetylglucosamine) and Glc (glucose), respectively. The genes encoding LgtB and LgtE are two genes of a five gene locus involved in the synthesis of gonococcal LOS. LgtE is believed to perform the first step in LOS biosynthesis. | ||
cd02514 | GT13_GLCNAC-TI | 2.0e-167 | 105 | 436 | 337 | + 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 | 19 | 441 | 429 | + 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 |
GenBank | ACF83572.1 | 0 | 1 | 442 | 1 | 425 | unknown [Zea mays] |
GenBank | ACG37957.1 | 0 | 1 | 442 | 1 | 442 | N-acetylglucosaminyltransferase I [Zea mays] |
RefSeq | NP_001048631.1 | 0 | 1 | 442 | 1 | 442 | Os02g0832800 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001142278.1 | 0 | 1 | 442 | 1 | 442 | hypothetical protein LOC100274447 [Zea mays] |
RefSeq | XP_002441861.1 | 0 | 1 | 442 | 1 | 442 | hypothetical protein SORBIDRAFT_08g003660 [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 | 1foa_A | 0 | 105 | 436 | 8 | 339 | A Chain A, Crystal Structure Of N-acetylglucosaminyltransferase I |
PDB | 1fo9_A | 0 | 105 | 436 | 8 | 339 | A Chain A, Crystal Structure Of N-acetylglucosaminyltransferase I |
PDB | 2apc_A | 0 | 105 | 436 | 2 | 333 | A Chain A, Crystal Structure Of N-acetylglucosaminyltransferase I |
PDB | 2am5_A | 0 | 105 | 436 | 2 | 333 | A Chain A, Crystal Structure Of N-acetylglucosaminyltransferase I |
PDB | 2am4_A | 0 | 105 | 436 | 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 |
GO802527 | 323 | 29 | 350 | 0 |
GO802714 | 312 | 29 | 339 | 0 |
GO865783 | 318 | 19 | 336 | 0 |
GT047470 | 295 | 121 | 415 | 0 |
JG822016 | 257 | 145 | 401 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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