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CAZyme Information: MGYG000002330_06373
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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 | Eisenbergiella tayi | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella tayi | |||||||||||
| CAZyme ID | MGYG000002330_06373 | |||||||||||
| CAZy Family | GT4 | |||||||||||
| CAZyme Description | Glycosyltransferase Gtf1 | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 56682; End: 57845 Strand: + | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd03801 | GT4_PimA-like | 1.62e-29 | 35 | 358 | 47 | 365 | phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea. |
| COG0438 | RfaB | 4.74e-29 | 3 | 365 | 21 | 381 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
| pfam00534 | Glycos_transf_1 | 2.38e-27 | 181 | 337 | 1 | 155 | Glycosyl transferases group 1. Mutations in this domain of PIGA lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family. |
| 340837 | cd03808 | 2.22e-23 | 179 | 337 | 186 | 340 | GT4_CapM-like capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides. |
| cd03820 | GT4_AmsD-like | 3.72e-20 | 207 | 347 | 208 | 351 | amylovoran biosynthesis glycosyltransferase AmsD and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AOZ97461.1 | 9.26e-141 | 1 | 382 | 1 | 382 |
| ADL35300.1 | 2.53e-131 | 1 | 382 | 5 | 385 |
| QNM02199.1 | 6.37e-113 | 1 | 385 | 1 | 414 |
| ARJ39639.1 | 1.18e-97 | 1 | 380 | 1 | 381 |
| AQQ09167.1 | 2.49e-91 | 10 | 377 | 1 | 368 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5I45_A | 1.74e-10 | 152 | 365 | 12 | 216 | 1.35Angstrom Crystal Structure of C-terminal Domain of Glycosyl Transferase Group 1 Family Protein (LpcC) from Francisella tularensis. [Francisella tularensis subsp. tularensis SCHU S4] |
| 3C4Q_A | 3.80e-08 | 185 | 359 | 226 | 404 | Structureof the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4Q_B Structure of the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4V_A Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum],3C4V_B Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum] |
| 3C48_A | 3.89e-08 | 185 | 359 | 246 | 424 | Structureof the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure. [Corynebacterium glutamicum],3C48_B Structure of the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure. [Corynebacterium glutamicum] |
| 4XSO_A | 2.56e-07 | 218 | 343 | 244 | 365 | ChainA, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSO_B Chain B, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSP_A Chain A, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSP_B Chain B, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSR_A Chain A, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSR_B Chain B, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSU_A Chain A, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSU_B Chain B, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q58469 | 6.13e-08 | 165 | 359 | 194 | 388 | Uncharacterized glycosyltransferase MJ1069 OS=Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) OX=243232 GN=MJ1069 PE=3 SV=1 |
| A4QB40 | 2.04e-07 | 185 | 359 | 226 | 404 | D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium glutamicum (strain R) OX=340322 GN=mshA PE=3 SV=1 |
| Q8NTA6 | 2.04e-07 | 185 | 359 | 226 | 404 | D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) OX=196627 GN=mshA PE=1 SV=1 |
| P13484 | 2.07e-07 | 181 | 337 | 346 | 499 | Poly(glycerol-phosphate) alpha-glucosyltransferase OS=Bacillus subtilis (strain 168) OX=224308 GN=tagE PE=1 SV=1 |
| O05083 | 2.27e-07 | 189 | 337 | 188 | 333 | Uncharacterized glycosyltransferase HI_1698 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_1698 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 |
|---|---|---|---|---|---|
| 1.000036 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
