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Conserved domains on  [gi|665404755|ref|NP_001285709|]
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uncharacterized protein Dmel_CG5171, isoform F [Drosophila melanogaster]

Protein Classification

trehalose-phosphatase( domain architecture ID 11546968)

trehalose-phosphatase catalyzes the dephosphorylation of trehalose 6-phosphate to produce trehalose and phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
31-259 4.91e-72

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.


:

Pssm-ID: 319767 [Multi-domain]  Cd Length: 228  Bit Score: 220.62  E-value: 4.91e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755  31 AVLLDYDGTLAPIADNPAKTKMPVELEAILHKIAKHPKVFLAVISGRGLKDVQKQVNIDGITYAGNHGLEIEYPDGSRHD 110
Cdd:cd01627    1 LLFLDYDGTLAPIVPDPDAAVPSPELLEALKKLAADPKNAVAIVSGRDLDDLDKWLGLPGIGLAGEHGAEIRLPGGGEWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755 111 YELPTEIQKNYTQMVRELKEKVEK-NGAWVEDKKVSLTYHYRDTP----AALKDQQKQLASEICTKfgFRANQAHEAIEA 185
Cdd:cd01627   81 TLAPKADLEWKEEVEAIFKYFTERtPGSLVEDKGASLAWHYRNADpegaRAALELALHLASDLLKA--LEVVPGKKVVEV 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665404755 186 KpPVNWNKGEAAVYILKQKFGDNwsqkVSVVFAGDDTTDEDAMRVLRGL-GRSFRISADAQIQTYADFRLPKQAV 259
Cdd:cd01627  159 R-PVGVNKGEAVERILGELPFAG----DFVLCAGDDVTDEDAFRALNGEgGFSVKVGEGPTAAKFRLDDPPDVVA 228
 
Name Accession Description Interval E-value
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
31-259 4.91e-72

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.


Pssm-ID: 319767 [Multi-domain]  Cd Length: 228  Bit Score: 220.62  E-value: 4.91e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755  31 AVLLDYDGTLAPIADNPAKTKMPVELEAILHKIAKHPKVFLAVISGRGLKDVQKQVNIDGITYAGNHGLEIEYPDGSRHD 110
Cdd:cd01627    1 LLFLDYDGTLAPIVPDPDAAVPSPELLEALKKLAADPKNAVAIVSGRDLDDLDKWLGLPGIGLAGEHGAEIRLPGGGEWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755 111 YELPTEIQKNYTQMVRELKEKVEK-NGAWVEDKKVSLTYHYRDTP----AALKDQQKQLASEICTKfgFRANQAHEAIEA 185
Cdd:cd01627   81 TLAPKADLEWKEEVEAIFKYFTERtPGSLVEDKGASLAWHYRNADpegaRAALELALHLASDLLKA--LEVVPGKKVVEV 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665404755 186 KpPVNWNKGEAAVYILKQKFGDNwsqkVSVVFAGDDTTDEDAMRVLRGL-GRSFRISADAQIQTYADFRLPKQAV 259
Cdd:cd01627  159 R-PVGVNKGEAVERILGELPFAG----DFVLCAGDDVTDEDAFRALNGEgGFSVKVGEGPTAAKFRLDDPPDVVA 228
OtsB COG1877
Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];
28-268 2.39e-64

Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];


Pssm-ID: 441481 [Multi-domain]  Cd Length: 242  Bit Score: 201.57  E-value: 2.39e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755  28 SPVAVLLDYDGTLAPIADNPAKTKMPVELEAILHKIAKHPKVFLAVISGRGLKDVQKQVNIDGITYAGNHGLEIEYPDGS 107
Cdd:COG1877    2 PRLLLFLDFDGTLAPIVPDPDAARPPPELRELLRRLAARPGGAVAIVSGRDLADLDRLLGPLGLPLAGSHGAERRLPGGE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755 108 RHDYELPTEIQKNYTQMVRELKEKVEKN-GAWVEDKKVSLTYHYRDTPAALKDQQKQLASEICTKFG--FRANQAHEAIE 184
Cdd:COG1877   82 WEVLPLAAEAPEWLDALRAALEALAARTpGVLVEDKGASLALHYRQAPPEEAEELRAALRELAARLGpgLEVLPGKKVVE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755 185 AKPPvNWNKGEAAVYILKQ-KFGdnwsqkVSVVFAGDDTTDEDAMRVLRGLGRSFRISADAqiqTYADFRLPKQAVMTDL 263
Cdd:COG1877  162 LRPA-GVDKGRAVRALLAElPFG------RAPVFIGDDVTDEDAFAALPAGGLGIKVGSGP---TAARYRLADPAEVRAL 231

                 ....*
gi 665404755 264 LKWIA 268
Cdd:COG1877  232 LARLA 236
T6PP TIGR00685
trehalose-phosphatase; Trehalose, a neutral disaccharide of two glucose residues, is an ...
31-268 6.75e-42

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]


Pssm-ID: 273219 [Multi-domain]  Cd Length: 244  Bit Score: 143.82  E-value: 6.75e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755   31 AVLLDYDGTLAPIADNPAKTKMPVELEAILHKIAKHPKVFLAVISGRGLKDVQKQVNIDGITYAGNHGLEIEyPDGSRHD 110
Cdd:TIGR00685   5 AFFFDYDGTLSEIVPDPDAAVVSDRLLTILQKLAARPHNAIWIISGRKFLEKWLGVKLPGLGLAGEHGCEMK-DNGSCQD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755  111 YELPTEIQKNYTQMVRELKEKV-EKNGAWVEDKKVSLTYHYRDT--PAALKDQQKQLASEICTKFGFRANQAHEAIEAKP 187
Cdd:TIGR00685  84 WVNLTEKIPSWKVRANELREEItTRPGVFIERKGVALAWHYRQApvPELARFRAKELKEKILSFTDLEVMDGKAVVELKP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755  188 PvNWNKGEAAVYILKQKFGdnwsQKVSVVFAGDDTTDEDAMRVLRGL-----GRSFRIsADAQIQTYADFRLPKQAVMTD 262
Cdd:TIGR00685 164 R-FVNKGEIVKRLLWHQPG----SGISPVYLGDDITDEDAFRVVNNQwgnygFYPVPI-GSGSKKTVAKFHLTGPQQVLE 237

                  ....*.
gi 665404755  263 LLKWIA 268
Cdd:TIGR00685 238 FLGLLV 243
Trehalose_PPase pfam02358
Trehalose-phosphatase; This family consist of trehalose-phosphatases EC:3.1.3.12 these enzyme ...
33-255 1.05e-40

Trehalose-phosphatase; This family consist of trehalose-phosphatases EC:3.1.3.12 these enzyme catalyze the de-phosphorylation of trehalose-6-phosphate to trehalose and orthophosphate. The aligned region is present in trehalose-phosphatases and comprises the entire length of the protein it is also found in the C-terminus of trehalose-6-phosphate synthase EC:2.4.1.15 adjacent to the trehalose-6-phosphate synthase domain - pfam00982. It would appear that the two equivalent genes in the E. coli otsBA operon otsA the trehalose-6-phosphate synthase and otsB trehalose-phosphatase (this family) have undergone gene fusion in most eukaryotes and Swiss:P93653. Trehalose is a common disaccharide of bacteria, fungi and invertebrates that appears to play a major role in desiccation tolerance.


Pssm-ID: 426737 [Multi-domain]  Cd Length: 234  Bit Score: 140.55  E-value: 1.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755   33 LLDYDGTLAPIADNPAKTKMPVELEAILHKIAKHPKVFLAVISGRGLKDVQKQVNIDGITYAGNHGLEIEYPDGSRHdYE 112
Cdd:pfam02358   1 FLDYDGTLSPIVSDPIAAVPSDRMLSALQDLASDPPNTVAIISGRSRQEEDLFVGVPNLGLAAEHGAFVRLPGGGDW-YN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755  113 LPTEIQKNYTQMVRE-LKEKVEK-NGAWVEDKKVSLTYHYRDTP-----AALKDQQKQLASEICTKFGFRANQAHEAIEA 185
Cdd:pfam02358  80 QAEVEDLPWKKEVAPiLEYYTERtPGSYVENKKSALSWHYRNADddfgsFQAKELAEHLESVLQDNPPLRVTQGKKVVEV 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665404755  186 KPPVNWnKGEAAVYILKQKFGDNwSQKVSVVFAGDDTTDEDAMRVLR-----GLGRSFRISADAQIQTYADFRLP 255
Cdd:pfam02358 160 RPVGVS-KGKAVEFILEELGSAG-SLPDFPLCIGDDRTDEDMFSVLRptkpsGVGIEVFAVSVGSKPSSASYFLD 232
PRK14501 PRK14501
putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional
32-265 2.16e-31

putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional


Pssm-ID: 184712 [Multi-domain]  Cd Length: 726  Bit Score: 122.34  E-value: 2.16e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755  32 VLLDYDGTLAPIADNPAKTKMPVELEAILHKIAKHPKVFLAVISGRGLKDVQKQVNIDGITYAGNHGLEIEYPDGsrhDY 111
Cdd:PRK14501 495 LLLDYDGTLVPFAPDPELAVPDKELRDLLRRLAADPNTDVAIISGRDRDTLERWFGDLPIHLVAEHGAWSRAPGG---EW 571
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755 112 ELPTEIQKNYTQMVR-ELKEKVEKN-GAWVEDKKVSLTYHYRDTPAALKDQQ-KQLA---SEICTKFGFRANQAHEAIEA 185
Cdd:PRK14501 572 QLLEPVATEWKDAVRpILEEFVDRTpGSFIEEKEASLAWHYRNADPELGEARaNELIlalSSLLSNAPLEVLRGNKVVEV 651
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755 186 KPPvNWNKGEAAVYILKQKFGDnwsqkvSVVFAGDDTTDEDAMRVLRGLGRSFRISADaqiQTYADFRLPKQAVMTDLLK 265
Cdd:PRK14501 652 RPA-GVNKGRAVRRLLEAGPYD------FVLAIGDDTTDEDMFRALPETAITVKVGPG---ESRARYRLPSQREVRELLR 721
 
Name Accession Description Interval E-value
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
31-259 4.91e-72

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.


Pssm-ID: 319767 [Multi-domain]  Cd Length: 228  Bit Score: 220.62  E-value: 4.91e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755  31 AVLLDYDGTLAPIADNPAKTKMPVELEAILHKIAKHPKVFLAVISGRGLKDVQKQVNIDGITYAGNHGLEIEYPDGSRHD 110
Cdd:cd01627    1 LLFLDYDGTLAPIVPDPDAAVPSPELLEALKKLAADPKNAVAIVSGRDLDDLDKWLGLPGIGLAGEHGAEIRLPGGGEWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755 111 YELPTEIQKNYTQMVRELKEKVEK-NGAWVEDKKVSLTYHYRDTP----AALKDQQKQLASEICTKfgFRANQAHEAIEA 185
Cdd:cd01627   81 TLAPKADLEWKEEVEAIFKYFTERtPGSLVEDKGASLAWHYRNADpegaRAALELALHLASDLLKA--LEVVPGKKVVEV 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665404755 186 KpPVNWNKGEAAVYILKQKFGDNwsqkVSVVFAGDDTTDEDAMRVLRGL-GRSFRISADAQIQTYADFRLPKQAV 259
Cdd:cd01627  159 R-PVGVNKGEAVERILGELPFAG----DFVLCAGDDVTDEDAFRALNGEgGFSVKVGEGPTAAKFRLDDPPDVVA 228
OtsB COG1877
Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];
28-268 2.39e-64

Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];


Pssm-ID: 441481 [Multi-domain]  Cd Length: 242  Bit Score: 201.57  E-value: 2.39e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755  28 SPVAVLLDYDGTLAPIADNPAKTKMPVELEAILHKIAKHPKVFLAVISGRGLKDVQKQVNIDGITYAGNHGLEIEYPDGS 107
Cdd:COG1877    2 PRLLLFLDFDGTLAPIVPDPDAARPPPELRELLRRLAARPGGAVAIVSGRDLADLDRLLGPLGLPLAGSHGAERRLPGGE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755 108 RHDYELPTEIQKNYTQMVRELKEKVEKN-GAWVEDKKVSLTYHYRDTPAALKDQQKQLASEICTKFG--FRANQAHEAIE 184
Cdd:COG1877   82 WEVLPLAAEAPEWLDALRAALEALAARTpGVLVEDKGASLALHYRQAPPEEAEELRAALRELAARLGpgLEVLPGKKVVE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755 185 AKPPvNWNKGEAAVYILKQ-KFGdnwsqkVSVVFAGDDTTDEDAMRVLRGLGRSFRISADAqiqTYADFRLPKQAVMTDL 263
Cdd:COG1877  162 LRPA-GVDKGRAVRALLAElPFG------RAPVFIGDDVTDEDAFAALPAGGLGIKVGSGP---TAARYRLADPAEVRAL 231

                 ....*
gi 665404755 264 LKWIA 268
Cdd:COG1877  232 LARLA 236
T6PP TIGR00685
trehalose-phosphatase; Trehalose, a neutral disaccharide of two glucose residues, is an ...
31-268 6.75e-42

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]


Pssm-ID: 273219 [Multi-domain]  Cd Length: 244  Bit Score: 143.82  E-value: 6.75e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755   31 AVLLDYDGTLAPIADNPAKTKMPVELEAILHKIAKHPKVFLAVISGRGLKDVQKQVNIDGITYAGNHGLEIEyPDGSRHD 110
Cdd:TIGR00685   5 AFFFDYDGTLSEIVPDPDAAVVSDRLLTILQKLAARPHNAIWIISGRKFLEKWLGVKLPGLGLAGEHGCEMK-DNGSCQD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755  111 YELPTEIQKNYTQMVRELKEKV-EKNGAWVEDKKVSLTYHYRDT--PAALKDQQKQLASEICTKFGFRANQAHEAIEAKP 187
Cdd:TIGR00685  84 WVNLTEKIPSWKVRANELREEItTRPGVFIERKGVALAWHYRQApvPELARFRAKELKEKILSFTDLEVMDGKAVVELKP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755  188 PvNWNKGEAAVYILKQKFGdnwsQKVSVVFAGDDTTDEDAMRVLRGL-----GRSFRIsADAQIQTYADFRLPKQAVMTD 262
Cdd:TIGR00685 164 R-FVNKGEIVKRLLWHQPG----SGISPVYLGDDITDEDAFRVVNNQwgnygFYPVPI-GSGSKKTVAKFHLTGPQQVLE 237

                  ....*.
gi 665404755  263 LLKWIA 268
Cdd:TIGR00685 238 FLGLLV 243
Trehalose_PPase pfam02358
Trehalose-phosphatase; This family consist of trehalose-phosphatases EC:3.1.3.12 these enzyme ...
33-255 1.05e-40

Trehalose-phosphatase; This family consist of trehalose-phosphatases EC:3.1.3.12 these enzyme catalyze the de-phosphorylation of trehalose-6-phosphate to trehalose and orthophosphate. The aligned region is present in trehalose-phosphatases and comprises the entire length of the protein it is also found in the C-terminus of trehalose-6-phosphate synthase EC:2.4.1.15 adjacent to the trehalose-6-phosphate synthase domain - pfam00982. It would appear that the two equivalent genes in the E. coli otsBA operon otsA the trehalose-6-phosphate synthase and otsB trehalose-phosphatase (this family) have undergone gene fusion in most eukaryotes and Swiss:P93653. Trehalose is a common disaccharide of bacteria, fungi and invertebrates that appears to play a major role in desiccation tolerance.


Pssm-ID: 426737 [Multi-domain]  Cd Length: 234  Bit Score: 140.55  E-value: 1.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755   33 LLDYDGTLAPIADNPAKTKMPVELEAILHKIAKHPKVFLAVISGRGLKDVQKQVNIDGITYAGNHGLEIEYPDGSRHdYE 112
Cdd:pfam02358   1 FLDYDGTLSPIVSDPIAAVPSDRMLSALQDLASDPPNTVAIISGRSRQEEDLFVGVPNLGLAAEHGAFVRLPGGGDW-YN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755  113 LPTEIQKNYTQMVRE-LKEKVEK-NGAWVEDKKVSLTYHYRDTP-----AALKDQQKQLASEICTKFGFRANQAHEAIEA 185
Cdd:pfam02358  80 QAEVEDLPWKKEVAPiLEYYTERtPGSYVENKKSALSWHYRNADddfgsFQAKELAEHLESVLQDNPPLRVTQGKKVVEV 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665404755  186 KPPVNWnKGEAAVYILKQKFGDNwSQKVSVVFAGDDTTDEDAMRVLR-----GLGRSFRISADAQIQTYADFRLP 255
Cdd:pfam02358 160 RPVGVS-KGKAVEFILEELGSAG-SLPDFPLCIGDDRTDEDMFSVLRptkpsGVGIEVFAVSVGSKPSSASYFLD 232
PRK14501 PRK14501
putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional
32-265 2.16e-31

putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional


Pssm-ID: 184712 [Multi-domain]  Cd Length: 726  Bit Score: 122.34  E-value: 2.16e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755  32 VLLDYDGTLAPIADNPAKTKMPVELEAILHKIAKHPKVFLAVISGRGLKDVQKQVNIDGITYAGNHGLEIEYPDGsrhDY 111
Cdd:PRK14501 495 LLLDYDGTLVPFAPDPELAVPDKELRDLLRRLAADPNTDVAIISGRDRDTLERWFGDLPIHLVAEHGAWSRAPGG---EW 571
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755 112 ELPTEIQKNYTQMVR-ELKEKVEKN-GAWVEDKKVSLTYHYRDTPAALKDQQ-KQLA---SEICTKFGFRANQAHEAIEA 185
Cdd:PRK14501 572 QLLEPVATEWKDAVRpILEEFVDRTpGSFIEEKEASLAWHYRNADPELGEARaNELIlalSSLLSNAPLEVLRGNKVVEV 651
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755 186 KPPvNWNKGEAAVYILKQKFGDnwsqkvSVVFAGDDTTDEDAMRVLRGLGRSFRISADaqiQTYADFRLPKQAVMTDLLK 265
Cdd:PRK14501 652 RPA-GVNKGRAVRRLLEAGPYD------FVLAIGDDTTDEDMFRALPETAITVKVGPG---ESRARYRLPSQREVRELLR 721
PLN03017 PLN03017
trehalose-phosphatase
30-240 2.24e-30

trehalose-phosphatase


Pssm-ID: 178591 [Multi-domain]  Cd Length: 366  Bit Score: 116.66  E-value: 2.24e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755  30 VAVLLDYDGTLAPIADNPAKTKMPVELEAILHKIAK-HPKvflAVISGRGLKDVQKQVNIDGITYAGNHGLEIEYPDG-- 106
Cdd:PLN03017 112 IVMFLDYDGTLSPIVDDPDKAFMSSKMRRTVKKLAKcFPT---AIVTGRCIDKVYNFVKLAELYYAGSHGMDIKGPAKgf 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755 107 SRHDYELPTEIQK---NYTQMVREL-KEKVEKN----GAWVEDKKVSLTYHYRDTpaalkDQQK--QLASE---ICTKF- 172
Cdd:PLN03017 189 SRHKRVKQSLLYQpanDYLPMIDEVyRQLLEKTkstpGAKVENHKFCASVHFRCV-----DEKKwsELVLQvrsVLKNFp 263
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665404755 173 GFRANQAHEAIEAKPPVNWNKGEAAVYILkQKFGDNWSQKVSVVFAGDDTTDEDAMRVLRGLGRSFRI 240
Cdd:PLN03017 264 TLKLTQGRKVFEIRPMIEWDKGKALEFLL-ESLGFGNTNNVFPVYIGDDRTDEDAFKMLRDRGEGFGI 330
PLN02151 PLN02151
trehalose-phosphatase
30-235 1.59e-29

trehalose-phosphatase


Pssm-ID: 177812  Cd Length: 354  Bit Score: 114.00  E-value: 1.59e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755  30 VAVLLDYDGTLAPIADNPAKTKMPVELEAILHKIAK-HPKvflAVISGRGLKDVQKQVNIDGITYAGNHGLEIEYPD-GS 107
Cdd:PLN02151  99 IVMFLDYDGTLSPIVDDPDRAFMSKKMRNTVRKLAKcFPT---AIVSGRCREKVSSFVKLTELYYAGSHGMDIKGPEqGS 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755 108 RHDYE---LPTEIQKNYTQMVRELKEK-VEKN----GAWVEDKKVSLTYHYRDTPA-ALKDQQKQLASEICTKFGFRANQ 178
Cdd:PLN02151 176 KYKKEnqsLLCQPATEFLPVINEVYKKlVEKTksipGAKVENNKFCASVHFRCVEEnKWSDLANQVRSVLKNYPKLMLTQ 255
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665404755 179 AHEAIEAKPPVNWNKGEAAVYILkQKFGDNWSQKVSVVFAGDDTTDEDAMRVLR----GLG 235
Cdd:PLN02151 256 GRKVLEIRPIIKWDKGKALEFLL-ESLGYANCTDVFPIYIGDDRTDEDAFKILRdkkqGLG 315
PLN02580 PLN02580
trehalose-phosphatase
30-240 1.74e-28

trehalose-phosphatase


Pssm-ID: 215317 [Multi-domain]  Cd Length: 384  Bit Score: 111.83  E-value: 1.74e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755  30 VAVLLDYDGTLAPIADNPAKTKMPVELEAILHKIAKH-PKvflAVISGRGLKDVQKQVNIDGITYAGNHGLEIEYPDGSR 108
Cdd:PLN02580 120 IALFLDYDGTLSPIVDDPDRALMSDAMRSAVKNVAKYfPT---AIISGRSRDKVYELVGLTELYYAGSHGMDIMGPVRES 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755 109 HDYELPTEIQKNYTQ-------------------MVRELKEKVEK-NGAWVEDKKVSLTYHYRDTpaalkDQQK-----Q 163
Cdd:PLN02580 197 VSNDHPNCIKSTDQQgkevnlfqpaseflpmideVFRSLVESTKDiKGAKVENHKFCVSVHYRNV-----DEKNwplvaQ 271
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665404755 164 LASEICTKFG-FRANQAHEAIEAKPPVNWNKGEAAVYILkQKFGDNWSQKVSVVFAGDDTTDEDAMRVLRGLGRSFRI 240
Cdd:PLN02580 272 CVHDVLKKYPrLRLTHGRKVLEVRPVIDWNKGKAVEFLL-ESLGLSNCDDVLPIYIGDDRTDEDAFKVLREGNRGYGI 348
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
31-232 4.79e-18

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 80.12  E-value: 4.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755   31 AVLLDYDGTLAPiadnPAKTKMPVELEAILHKIAKHPkVFLAVISGRGL---KDVQKQVNIDgITYAGNHGLEIEYPDGS 107
Cdd:TIGR01484   1 LLFFDLDGTLLD----PNAHELSPETIEALERLREAG-VKVVIVTGRSLaeiKELLKQLNLP-LPLIAENGALIFYPGEI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755  108 --RHDYELPTEI-QKNYTQMVRELKEKVE-KNGAWVEDKKVSLTYHYRDTPAALKDQQKQLAS-EI--CTKFGFRANQAH 180
Cdd:TIGR01484  75 lyIEPSDVFEEIlGIKFEEIGAELKSLSEhYVGTFIEDKAIAVAIHYVGAELGQELDSKMRERlEKigRNDLELEAIYSG 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665404755  181 EAIEAKPPVNWNKGEAAVYILKQKFGDnwsqKVSVVFAGDDTTDEDAMRVLR 232
Cdd:TIGR01484 155 KTDLEVLPAGVNKGSALQALLQELNGK----KDEILAFGDSGNDEEMFEVAG 202
PRK10187 PRK10187
trehalose-6-phosphate phosphatase; Provisional
25-270 1.44e-13

trehalose-6-phosphate phosphatase; Provisional


Pssm-ID: 182291 [Multi-domain]  Cd Length: 266  Bit Score: 68.61  E-value: 1.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755  25 ISESPV-----AVLLDYDGTLAPIADNPAKTKMPVELEAILHKIAKHPKVFLAVISGRGLkdvqkqVNIDGITY------ 93
Cdd:PRK10187   5 LTVPPElsanyAWFFDLDGTLAEIKPHPDQVVVPDNILQGLQLLATANDGALALISGRSM------VELDALAKpyrfpl 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755  94 AGNHGLEIEYPDGSRHDYELPTEIqknytqmVRELKEKVEK-----NGAWVEDKKVSLTYHYRDTPAAlKDQQKQLASEI 168
Cdd:PRK10187  79 AGVHGAERRDINGKTHIVHLPDAI-------ARDISVQLHTalaqlPGAELEAKGMAFALHYRQAPQH-EDALLALAQRI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755 169 CTKFGFRANQAHEAIEAKPPVNWNKGEA-AVYILKQKFGDNwsqkvSVVFAGDDTTDEDAMRVLRGL-GRSFRISADAqi 246
Cdd:PRK10187 151 TQIWPQLALQPGKCVVEIKPRGTNKGEAiAAFMQEAPFAGR-----TPVFVGDDLTDEAGFAVVNRLgGISVKVGTGA-- 223
                        250       260
                 ....*....|....*....|....
gi 665404755 247 qTYADFRLpkqAVMTDLLKWIANV 270
Cdd:PRK10187 224 -TQASWRL---AGVPDVWSWLEMI 243
PLN02205 PLN02205
alpha,alpha-trehalose-phosphate synthase [UDP-forming]
31-258 3.85e-05

alpha,alpha-trehalose-phosphate synthase [UDP-forming]


Pssm-ID: 177855 [Multi-domain]  Cd Length: 854  Bit Score: 44.63  E-value: 3.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755  31 AVLLDYDGTLAPIAdNPAKTKMPVELEaILHKIAKHPKVFLAVISGRGLKDVQKQVN-IDGITYAGNHGLEIEYpdgsRH 109
Cdd:PLN02205 598 AILLDYDGTLMPQA-SIDKSPSSKSID-ILNTLCRDKNNMVFIVSARSRKTLADWFSpCEKLGIAAEHGYFLRL----KR 671
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755 110 DYELPTEIQ------KNYTQMVRELKEKVeKNGAWVEDKKVSLTYHYRDT-PAALKDQQKQLASEIctkfgfranqahEA 182
Cdd:PLN02205 672 DVEWETCVPvadcswKQIAEPVMQLYTET-TDGSTIEDKETALVWCYEDAdPDFGSCQAKELLDHL------------ES 738
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404755 183 IEAKPPVNWNKGEAAVYILKQKFG-------------DNWSQKVSVVFAGDDTTDEDAMRVLRGLGRSFRISADAQIQTY 249
Cdd:PLN02205 739 VLANEPVTVKSGQNIVEVKPQGVSkglvakrllsimqERGMLPDFVLCIGDDRSDEDMFEVITSSMAGPSIAPRAEVFAC 818

                 ....*....
gi 665404755 250 ADFRLPKQA 258
Cdd:PLN02205 819 TVGQKPSKA 827
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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