| Species | Brevibacterium senegalense | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Brevibacteriaceae; Brevibacterium; Brevibacterium senegalense | |||||||||||
| CAZyme ID | MGYG000001408_02441 | |||||||||||
| CAZy Family | GH15 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 134058; End: 136799 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH15 | 545 | 901 | 8.7e-71 | 0.9778393351800554 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG3387 | SGA1 | 1.91e-84 | 313 | 911 | 15 | 611 | Glucoamylase (glucan-1,4-alpha-glucosidase), GH15 family [Carbohydrate transport and metabolism]. |
| pfam00723 | Glyco_hydro_15 | 3.14e-51 | 540 | 903 | 3 | 417 | Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits. |
| cd01627 | HAD_TPP | 1.43e-34 | 73 | 292 | 1 | 227 | trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase OtsB and Saccharomyces cerevisiae trehalose-phosphatase TPS2. Trehalose biosynthesis in bacteria is known through three pathways - OtsAB, TreYZ and TreS. The OtsAB pathway, also known as the trehalose 6-phosphate synthase (TSP)/ Trehalose-6-phosphate phosphatase (TPP) pathway, is the most common route known to be involved in the stress response of Escherichia coli. It involves converting glucose-6-phosphate and UDP-glucose to form trehalose-6-phosphate (T6P), catalyzed by TPS, the product of the otsA gene, this step is followed by the dephosphorylation of T6P to yield trehalose and inorganic phosphate, catalyzed by a specific TPP, the product of otsB gene. This OtsAB (or TSP/TPP) pathway, is also the most common route known to be involved in the stress response of yeast In Saccharomyces cerevisiae, the corresponding enzymes, TPS1p and TPS2p, form a multimeric synthase complex together with additional regulatory subunits encoded by Tsl1 and Tps3. Trehalose is a common disaccharide accumulated by organisms as a reservation of carbohydrate and in response to unfavorable growth conditions. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. |
| COG1877 | OtsB | 1.59e-26 | 71 | 303 | 18 | 256 | Trehalose-6-phosphatase [Carbohydrate transport and metabolism]. |
| TIGR00685 | T6PP | 5.86e-22 | 71 | 291 | 3 | 235 | trehalose-phosphatase. Trehalose, a neutral disaccharide of two glucose residues, is an important osmolyte for dessication and/or salt tolerance in a number of prokaryotic and eukaryotic species, including E. coli, Saccharomyces cerevisiae, and Arabidopsis thaliana. Many bacteria also utilize trehalose in the synthesis of trehalolipids, specialized cell wall constituents believed to be involved in the uptake of hydrophobic substances. Trehalose dimycolate (TDM, cord factor) and related substances are important constituents of the mycobacterial waxy coat and responsible for various clinically important immunological interactions with host organism. This enzyme, trehalose-phosphatase, removes a phosphate group in the final step of trehalose biosynthesis. The trehalose-phosphatase from Saccharomyces cerevisiae is fused to the synthase. At least 18 distinct sequences from Arabidopsis have been identified, roughly half of these are of the fungal type, with a fused synthase and half are like the bacterial members having only the phosphatase domain. It has been suggested that trehalose is being used in Arabidopsis as a regulatory molecule in development and possibly other processes. [Cellular processes, Adaptations to atypical conditions] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QIN29585.1 | 0.0 | 42 | 908 | 18 | 892 |
| QCP04601.1 | 0.0 | 42 | 908 | 18 | 906 |
| SDS51321.1 | 0.0 | 21 | 906 | 7 | 876 |
| AZU02090.1 | 0.0 | 47 | 906 | 29 | 876 |
| QUL79052.1 | 0.0 | 35 | 907 | 17 | 877 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5GVX_A | 1.69e-16 | 9 | 286 | 116 | 404 | Structuralinsight into dephosphorylation by Trehalose 6-phosphate Phosphatase (OtsB2) from Mycobacterium Tuberculosis [Mycobacterium tuberculosis H37Rv] |
| 6QJ6_A | 9.62e-12 | 77 | 310 | 37 | 267 | Thestructure of Trehalose-6-phosphatase from Burkholderia pseudomallei [Burkholderia pseudomallei K96243],6QJ6_E The structure of Trehalose-6-phosphatase from Burkholderia pseudomallei [Burkholderia pseudomallei K96243],6RCZ_A The structure of Burkholderia pseudomallei trehalose-6-phosphatase [Burkholderia pseudomallei K96243],6RCZ_E The structure of Burkholderia pseudomallei trehalose-6-phosphatase [Burkholderia pseudomallei K96243] |
| 6UPB_A | 2.68e-08 | 77 | 285 | 20 | 230 | Structureof apo trehalose-6-phosphate phosphatase from Salmonella typhimurium [Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344],6UPB_B Structure of apo trehalose-6-phosphate phosphatase from Salmonella typhimurium [Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344],6UPC_A Structure of trehalose-6-phosphate phosphatase from Salmonella typhimurium in complex with trehalose 6-sulfate [Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344],6UPC_B Structure of trehalose-6-phosphate phosphatase from Salmonella typhimurium in complex with trehalose 6-sulfate [Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344],6UPD_A Structure of trehalose-6-phosphate phosphatase from Salmonella typhimurium in complex with trehalose [Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344],6UPD_B Structure of trehalose-6-phosphate phosphatase from Salmonella typhimurium in complex with trehalose [Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344],6UPE_A Structure of trehalose-6-phosphate phosphatase from Salmonella typhimurium inhibited by 4-n-octylphenyl alpha-D-glucopyranoside-6-sulfate [Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344],6UPE_B Structure of trehalose-6-phosphate phosphatase from Salmonella typhimurium inhibited by 4-n-octylphenyl alpha-D-glucopyranoside-6-sulfate [Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P71741 | 5.82e-86 | 276 | 902 | 26 | 657 | Trehalase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv2402 PE=1 SV=2 |
| A0R0W9 | 5.96e-84 | 313 | 902 | 41 | 645 | Trehalase OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=MSMEG_4535 PE=1 SV=1 |
| Q978S7 | 5.38e-82 | 314 | 907 | 30 | 612 | Trehalase OS=Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1) OX=273116 GN=TVG1381191 PE=1 SV=1 |
| Q9HLE2 | 4.73e-77 | 526 | 907 | 191 | 570 | Trehalase OS=Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) OX=273075 GN=Ta0286 PE=1 SV=1 |
| Q10211 | 5.92e-70 | 314 | 907 | 19 | 641 | Uncharacterized protein C4H3.03c OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPAC4H3.03c PE=4 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000024 | 0.000016 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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