You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000001262_00651
You are here: Home > Sequence: MGYG000001262_00651
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 | Sphingomonas ginsenosidimutans | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; Sphingomonadaceae; Sphingomonas; Sphingomonas ginsenosidimutans | |||||||||||
| CAZyme ID | MGYG000001262_00651 | |||||||||||
| CAZy Family | GT20 | |||||||||||
| CAZyme Description | Trehalose-6-phosphate synthase | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 4276; End: 5658 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT20 | 2 | 455 | 1.6e-163 | 0.9726315789473684 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd03788 | GT20_TPS | 0.0 | 3 | 454 | 1 | 463 | trehalose-6-phosphate synthase. Trehalose-6-Phosphate Synthase (TPS, EC 2.4.1.15) is a glycosyltransferase that catalyses the synthesis of alpha,alpha-1,1-trehalose-6-phosphate from glucose-6-phosphate using a UDP-glucose donor. It is a key enzyme in the trehalose synthesis pathway. Trehalose is a nonreducing disaccharide present in a wide variety of organisms and may serve as a source of energy and carbon. It is characterized most notably in insect, plant, and microbial cells. Its production is often associated with a variety of stress conditions, including desiccation, dehydration, heat, cold, and oxidation. This family represents the catalytic domain of the TPS. Some members of this domain family coexist with a C-terminal trehalose phosphatase domain. |
| TIGR02400 | trehalose_OtsA | 0.0 | 3 | 455 | 1 | 456 | alpha,alpha-trehalose-phosphate synthase [UDP-forming]. This enzyme catalyzes the key, penultimate step in biosynthesis of trehalose, a compatible solute made as an osmoprotectant in some species in all three domains of life. The gene symbol OtsA stands for osmotically regulated trehalose synthesis A. Trehalose helps protect against both osmotic and thermal stresses, and is made from two glucose subunits. This model excludes glucosylglycerol-phosphate synthase, an enzyme of an analogous osmoprotectant system in many cyanobacterial strains. This model does not identify archaeal examples, as they are more divergent than glucosylglycerol-phosphate synthase. Sequences that score in the gray zone between the trusted and noise cutoffs include a number of yeast multidomain proteins in which the N-terminal domain may be functionally equivalent to this family. The gray zone also includes the OtsA of Cornyebacterium glutamicum (and related species), shown to be responsible for synthesis of only trace amounts of trehalose while the majority is synthesized by the TreYZ pathway; the significance of OtsA in this species is unclear (see Wolf, et al., ). [Cellular processes, Adaptations to atypical conditions] |
| COG0380 | OtsA | 1.20e-178 | 1 | 456 | 14 | 480 | Trehalose-6-phosphate synthase [Carbohydrate transport and metabolism]. |
| PRK14501 | PRK14501 | 4.10e-162 | 2 | 457 | 1 | 464 | putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional |
| pfam00982 | Glyco_transf_20 | 5.15e-160 | 2 | 455 | 1 | 470 | Glycosyltransferase family 20. Members of this family belong to glycosyl transferase family 20. OtsA (Trehalose-6-phosphate synthase) is homologous to regions in the subunits of yeast trehalose-6-phosphate synthase/phosphate complex,. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QJU59113.1 | 5.66e-262 | 1 | 456 | 1 | 456 |
| QBM76717.1 | 1.15e-259 | 1 | 453 | 1 | 454 |
| QIG79290.1 | 6.75e-259 | 1 | 453 | 1 | 454 |
| ANC88275.1 | 4.95e-258 | 1 | 459 | 1 | 460 |
| ATI57382.1 | 8.16e-257 | 1 | 459 | 1 | 460 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5HXA_A | 4.47e-150 | 1 | 454 | 9 | 461 | Crystalstructure of an UDP-forming alpha, alpha-terhalose-phosphate synthase from Burkholderia xenovorans [Paraburkholderia xenovorans LB400] |
| 5UOF_A | 1.87e-143 | 1 | 454 | 9 | 462 | Crystalstructure of alpha,alpha-trehalose 6-phosphate sythase from Burkholderia multivorans [Burkholderia multivorans ATCC 17616],5UOF_B Crystal structure of alpha,alpha-trehalose 6-phosphate sythase from Burkholderia multivorans [Burkholderia multivorans ATCC 17616] |
| 5TVG_A | 3.03e-142 | 3 | 454 | 11 | 462 | Crystalstructure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia vietnamiensis [Burkholderia vietnamiensis G4],5TVG_B Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia vietnamiensis [Burkholderia vietnamiensis G4],5TVG_C Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia vietnamiensis [Burkholderia vietnamiensis G4],5TVG_D Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia vietnamiensis [Burkholderia vietnamiensis G4],5TVG_E Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia vietnamiensis [Burkholderia vietnamiensis G4],5TVG_F Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia vietnamiensis [Burkholderia vietnamiensis G4],5TVG_G Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia vietnamiensis [Burkholderia vietnamiensis G4],5TVG_H Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia vietnamiensis [Burkholderia vietnamiensis G4] |
| 5V0T_A | 8.50e-140 | 1 | 454 | 9 | 466 | Crystalstructure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia xenovorans in complex with glucose-6-phosphate [Paraburkholderia xenovorans LB400],5V0T_B Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia xenovorans in complex with glucose-6-phosphate [Paraburkholderia xenovorans LB400],5V0T_C Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia xenovorans in complex with glucose-6-phosphate [Paraburkholderia xenovorans LB400],5V0T_D Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia xenovorans in complex with glucose-6-phosphate [Paraburkholderia xenovorans LB400],5V0T_E Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia xenovorans in complex with glucose-6-phosphate [Paraburkholderia xenovorans LB400],5V0T_F Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia xenovorans in complex with glucose-6-phosphate [Paraburkholderia xenovorans LB400],5V0T_G Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia xenovorans in complex with glucose-6-phosphate [Paraburkholderia xenovorans LB400],5V0T_H Crystal structure of an alpha,alpha-trehalose-phosphate synthase (UDP-forming) from Burkholderia xenovorans in complex with glucose-6-phosphate [Paraburkholderia xenovorans LB400] |
| 2WTX_A | 4.20e-127 | 1 | 455 | 1 | 453 | Insightinto the mechanism of enzymatic glycosyltransfer with retention through the synthesis and analysis of bisubstrate glycomimetics of trehalose-6-phosphate synthase [Escherichia coli K-12],2WTX_B Insight into the mechanism of enzymatic glycosyltransfer with retention through the synthesis and analysis of bisubstrate glycomimetics of trehalose-6-phosphate synthase [Escherichia coli K-12],2WTX_C Insight into the mechanism of enzymatic glycosyltransfer with retention through the synthesis and analysis of bisubstrate glycomimetics of trehalose-6-phosphate synthase [Escherichia coli K-12],2WTX_D Insight into the mechanism of enzymatic glycosyltransfer with retention through the synthesis and analysis of bisubstrate glycomimetics of trehalose-6-phosphate synthase [Escherichia coli K-12] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P55612 | 1.80e-144 | 1 | 450 | 1 | 453 | Trehalose-6-phosphate synthase OS=Sinorhizobium fredii (strain NBRC 101917 / NGR234) OX=394 GN=otsA PE=3 SV=1 |
| A4WBR1 | 4.11e-135 | 1 | 455 | 1 | 453 | Trehalose-6-phosphate synthase OS=Enterobacter sp. (strain 638) OX=399742 GN=otsA PE=3 SV=1 |
| A6TB47 | 1.95e-130 | 1 | 454 | 1 | 452 | Trehalose-6-phosphate synthase OS=Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) OX=272620 GN=otsA PE=3 SV=1 |
| A7MEE9 | 1.11e-129 | 1 | 455 | 1 | 453 | Trehalose-6-phosphate synthase OS=Cronobacter sakazakii (strain ATCC BAA-894) OX=290339 GN=otsA PE=3 SV=1 |
| Q2NTK9 | 6.09e-128 | 1 | 455 | 1 | 452 | Trehalose-6-phosphate synthase OS=Sodalis glossinidius (strain morsitans) OX=343509 GN=otsA 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 |
|---|---|---|---|---|---|
| 0.999771 | 0.000270 | 0.000002 | 0.000000 | 0.000000 | 0.000000 |