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CAZyme Information: MGYG000003543.1_02180
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | HGM04593 sp900769465 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; HGM04593; HGM04593 sp900769465 | |||||||||||
| CAZyme ID | MGYG000003543.1_02180 | |||||||||||
| CAZy Family | GT2 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 6795; End: 7802 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT2 | 5 | 126 | 9.8e-25 | 0.7470588235294118 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG1216 | GT2 | 7.78e-48 | 1 | 253 | 3 | 255 | Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism]. |
| cd04186 | GT_2_like_c | 1.85e-44 | 5 | 219 | 1 | 166 | Subfamily of Glycosyltransferase Family GT2 of unknown function. GT-2 includes diverse families of glycosyltransferases 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families. |
| pfam00535 | Glycos_transf_2 | 3.11e-22 | 5 | 149 | 2 | 149 | Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids. |
| cd00761 | Glyco_tranf_GTA_type | 7.78e-19 | 5 | 208 | 1 | 155 | 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. |
| cd02522 | GT_2_like_a | 6.86e-12 | 3 | 205 | 1 | 174 | GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function. Glycosyltransferase family 2 (GT-2) subfamily of unknown function. GT-2 includes diverse families of glycosyltransferases 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QNL39066.1 | 4.95e-148 | 1 | 334 | 1 | 337 |
| QFQ12252.1 | 1.19e-147 | 2 | 335 | 12 | 347 |
| QQT78972.1 | 1.90e-145 | 1 | 334 | 1 | 337 |
| ASM67710.1 | 1.90e-145 | 1 | 334 | 1 | 337 |
| QRP59721.1 | 1.90e-145 | 1 | 334 | 1 | 337 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6E7I_A | 1.75e-07 | 14 | 218 | 115 | 317 | HumanppGalNAcT2 I253A/L310A Mutant with EA2 and UDP [Homo sapiens] |
| 6NQT_A | 1.81e-07 | 14 | 218 | 158 | 360 | GalNac-T2soaked with UDP-sugar [Homo sapiens],6NQT_B GalNac-T2 soaked with UDP-sugar [Homo sapiens],6NQT_C GalNac-T2 soaked with UDP-sugar [Homo sapiens],6NQT_D GalNac-T2 soaked with UDP-sugar [Homo sapiens],6NQT_E GalNac-T2 soaked with UDP-sugar [Homo sapiens],6NQT_F GalNac-T2 soaked with UDP-sugar [Homo sapiens] |
| 2FFU_A | 3.00e-07 | 14 | 218 | 88 | 290 | CrystalStructure of Human ppGalNAcT-2 complexed with UDP and EA2 [Homo sapiens],2FFV_A Human ppGalNAcT-2 complexed with manganese and UDP [Homo sapiens],2FFV_B Human ppGalNAcT-2 complexed with manganese and UDP [Homo sapiens] |
| 6EGS_A | 3.00e-07 | 14 | 218 | 90 | 292 | Crystalstructure of the GalNAc-T2 F104S mutant in complex with UDP-GalNAc [Homo sapiens],6EGS_B Crystal structure of the GalNAc-T2 F104S mutant in complex with UDP-GalNAc [Homo sapiens] |
| 4D0T_A | 3.20e-07 | 14 | 218 | 158 | 360 | GalNAc-T2crystal soaked with UDP-GalNAc, EA2 peptide and manganese [Homo sapiens],4D0T_B GalNAc-T2 crystal soaked with UDP-GalNAc, EA2 peptide and manganese [Homo sapiens],4D0T_C GalNAc-T2 crystal soaked with UDP-GalNAc, EA2 peptide and manganese [Homo sapiens],4D0T_D GalNAc-T2 crystal soaked with UDP-GalNAc, EA2 peptide and manganese [Homo sapiens],4D0T_E GalNAc-T2 crystal soaked with UDP-GalNAc, EA2 peptide and manganese [Homo sapiens],4D0T_F GalNAc-T2 crystal soaked with UDP-GalNAc, EA2 peptide and manganese [Homo sapiens],4D0Z_A GalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 and manganese (Higher resolution dataset) [Homo sapiens],4D0Z_B GalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 and manganese (Higher resolution dataset) [Homo sapiens],4D0Z_C GalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 and manganese (Higher resolution dataset) [Homo sapiens],4D0Z_D GalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 and manganese (Higher resolution dataset) [Homo sapiens],4D0Z_E GalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 and manganese (Higher resolution dataset) [Homo sapiens],4D0Z_F GalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 and manganese (Higher resolution dataset) [Homo sapiens],4D11_A GalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 peptide and manganese (Lower resolution dataset) [Homo sapiens],4D11_B GalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 peptide and manganese (Lower resolution dataset) [Homo sapiens],4D11_D GalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 peptide and manganese (Lower resolution dataset) [Homo sapiens],4D11_E GalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 peptide and manganese (Lower resolution dataset) [Homo sapiens],4D11_F GalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 peptide and manganese (Lower resolution dataset) [Homo sapiens],5AJN_A Crystal structure of the inactive form of GalNAc-T2 in complex with the glycopeptide MUC5AC-Cys13 [Homo sapiens],5AJO_A Crystal structure of the inactive form of GalNAc-T2 in complex with the glycopeptide MUC5AC-3,13 [Homo sapiens],5AJP_A Crystal structure of the active form of GalNAc-T2 in complex with UDP and the glycopeptide MUC5AC-13 [Homo sapiens],5FV9_A Crystal structure of GalNAc-T2 in complex with compound 16d [Homo sapiens],5FV9_B Crystal structure of GalNAc-T2 in complex with compound 16d [Homo sapiens],5FV9_C Crystal structure of GalNAc-T2 in complex with compound 16d [Homo sapiens],5FV9_D Crystal structure of GalNAc-T2 in complex with compound 16d [Homo sapiens],5FV9_E Crystal structure of GalNAc-T2 in complex with compound 16d [Homo sapiens],5FV9_F Crystal structure of GalNAc-T2 in complex with compound 16d [Homo sapiens],5NDF_A Small-molecule inhibition of ppGalNAc-Ts selectively reduces mucin-type O-glycosylation [Homo sapiens],5NDF_B Small-molecule inhibition of ppGalNAc-Ts selectively reduces mucin-type O-glycosylation [Homo sapiens],5NDF_C Small-molecule inhibition of ppGalNAc-Ts selectively reduces mucin-type O-glycosylation [Homo sapiens],5NDF_D Small-molecule inhibition of ppGalNAc-Ts selectively reduces mucin-type O-glycosylation [Homo sapiens],5NDF_E Small-molecule inhibition of ppGalNAc-Ts selectively reduces mucin-type O-glycosylation [Homo sapiens],5NDF_F Small-molecule inhibition of ppGalNAc-Ts selectively reduces mucin-type O-glycosylation [Homo sapiens] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P9WMY3 | 5.42e-15 | 5 | 217 | 7 | 235 | N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=wbbL PE=1 SV=2 |
| P9WMY2 | 5.42e-15 | 5 | 217 | 7 | 235 | N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=wbbL PE=3 SV=2 |
| O88422 | 2.92e-09 | 14 | 218 | 508 | 714 | Polypeptide N-acetylgalactosaminyltransferase 5 OS=Rattus norvegicus OX=10116 GN=Galnt5 PE=2 SV=1 |
| Q8C102 | 5.19e-09 | 14 | 249 | 508 | 745 | Polypeptide N-acetylgalactosaminyltransferase 5 OS=Mus musculus OX=10090 GN=Galnt5 PE=2 SV=2 |
| A0QSC1 | 9.05e-09 | 1 | 217 | 82 | 281 | Pre-mycofactocin glycosyltransferase OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=mftF PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000062 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |