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Conserved domains on  [gi|20129309|ref|NP_609114|]
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uncharacterized protein Dmel_CG5177, isoform A [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 ...
32-258 8.88e-60

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: 189.42  E-value: 8.88e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309  32 ALLLDYDGTLAPL--TEELSVMPKDTEINIKKLAANEKIFMVVFSGRELSEIKNHLKFPNVTYAGNHGLEVEYPSGKKFK 109
Cdd:cd01627   1 LLFLDYDGTLAPIvpDPDAAVPSPELLEALKKLAADPKNAVAIVSGRDLDDLDKWLGLPGIGLAGEHGAEIRLPGGGEWV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309 110 IEMPEELLEKHNKLVSELKEKVV-CSGAWVEDKKISVTYHYKGVT-DKLKAKLIAEAKGLIQAHGFqlietPYALEGK-- 185
Cdd:cd01627  81 TLAPKADLEWKEEVEAIFKYFTErTPGSLVEDKGASLAWHYRNADpEGARAALELALHLASDLLKA-----LEVVPGKkv 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20129309 186 ---PRVNWDKGEGAKMILEKQFDADwaknLKIVYVGDDTTDEDAIKVLHG-IGKTFRVSELPTLKTYANYQIKTVEE 258
Cdd:cd01627 156 vevRPVGVNKGEAVERILGELPFAG----DFVLCAGDDVTDEDAFRALNGeGGFSVKVGEGPTAAKFRLDDPPDVVA 228
 
Name Accession Description Interval E-value
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
32-258 8.88e-60

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: 189.42  E-value: 8.88e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309  32 ALLLDYDGTLAPL--TEELSVMPKDTEINIKKLAANEKIFMVVFSGRELSEIKNHLKFPNVTYAGNHGLEVEYPSGKKFK 109
Cdd:cd01627   1 LLFLDYDGTLAPIvpDPDAAVPSPELLEALKKLAADPKNAVAIVSGRDLDDLDKWLGLPGIGLAGEHGAEIRLPGGGEWV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309 110 IEMPEELLEKHNKLVSELKEKVV-CSGAWVEDKKISVTYHYKGVT-DKLKAKLIAEAKGLIQAHGFqlietPYALEGK-- 185
Cdd:cd01627  81 TLAPKADLEWKEEVEAIFKYFTErTPGSLVEDKGASLAWHYRNADpEGARAALELALHLASDLLKA-----LEVVPGKkv 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20129309 186 ---PRVNWDKGEGAKMILEKQFDADwaknLKIVYVGDDTTDEDAIKVLHG-IGKTFRVSELPTLKTYANYQIKTVEE 258
Cdd:cd01627 156 vevRPVGVNKGEAVERILGELPFAG----DFVLCAGDDVTDEDAFRALNGeGGFSVKVGEGPTAAKFRLDDPPDVVA 228
OtsB COG1877
Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];
28-265 4.79e-50

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


Pssm-ID: 441481 [Multi-domain]  Cd Length: 242  Bit Score: 164.98  E-value: 4.79e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309  28 TDQVALLLDYDGTLAPLTE--ELSVMPKDTEINIKKLAANEKIFMVVFSGRELSEIKNHLKFPNVTYAGNHGLEVEYPSG 105
Cdd:COG1877   1 APRLLLFLDFDGTLAPIVPdpDAARPPPELRELLRRLAARPGGAVAIVSGRDLADLDRLLGPLGLPLAGSHGAERRLPGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309 106 KKFKIEMPEELLEKHNKLVSELKEKVV-CSGAWVEDKKISVTYHYKGVTDKLKAKLIAEAKGLIQAHGFQLIETP--YAL 182
Cdd:COG1877  81 EWEVLPLAAEAPEWLDALRAALEALAArTPGVLVEDKGASLALHYRQAPPEEAEELRAALRELAARLGPGLEVLPgkKVV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309 183 EGKPRvNWDKGEGAKMILEkQFDADWAknlkIVYVGDDTTDEDAIKVLHGIGKTFRVSELPTLktyANYQIKTVEEVGYL 262
Cdd:COG1877 161 ELRPA-GVDKGRAVRALLA-ELPFGRA----PVFIGDDVTDEDAFAALPAGGLGIKVGSGPTA---ARYRLADPAEVRAL 231

                ...
gi 20129309 263 LKA 265
Cdd:COG1877 232 LAR 234
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
32-234 3.55e-33

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: 120.18  E-value: 3.55e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309    32 ALLLDYDGTLAPLTEelsvMPKDTEIN--IKKLAANEkIFMVVFSGRELSEIKNHLKFPNV--TYAGNHGLEVEYPSGKK 107
Cdd:TIGR01484   1 LLFFDLDGTLLDPNA----HELSPETIeaLERLREAG-VKVVIVTGRSLAEIKELLKQLNLplPLIAENGALIFYPGEIL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309   108 FK--IEMPEELL-EKHNKLVSELKEKVVCS-GAWVEDKKISVTYHYKG--VTDKLKAKLIAEAKGL-IQAHGFQLI-ETP 179
Cdd:TIGR01484  76 YIepSDVFEEILgIKFEEIGAELKSLSEHYvGTFIEDKAIAVAIHYVGaeLGQELDSKMRERLEKIgRNDLELEAIySGK 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 20129309   180 YALEGKPrVNWDKGEGAKMILEKQFdadwAKNLKIVYVGDDTTDEDAIKVLHGIG 234
Cdd:TIGR01484 156 TDLEVLP-AGVNKGSALQALLQELN----GKKDEILAFGDSGNDEEMFEVAGLAV 205
PLN02151 PLN02151
trehalose-phosphatase
5-259 2.96e-29

trehalose-phosphatase


Pssm-ID: 177812  Cd Length: 354  Bit Score: 113.61  E-value: 2.96e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309    5 KKAPLLKKEEDYVKALEGFIN-PETDQVALLLDYDGTLAPLTEE--LSVMPKDTEINIKKLAaneKIF-MVVFSGRELSE 80
Cdd:PLN02151  72 KQSCWIKEHPSALNMFEEILHkSEGKQIVMFLDYDGTLSPIVDDpdRAFMSKKMRNTVRKLA---KCFpTAIVSGRCREK 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309   81 IKNHLKFPNVTYAGNHGLEVEYP-SGKKFKIEMPE-------ELLEKHNKLVSELKEKVVCS-GAWVEDKKISVTYHYKG 151
Cdd:PLN02151 149 VSSFVKLTELYYAGSHGMDIKGPeQGSKYKKENQSllcqpatEFLPVINEVYKKLVEKTKSIpGAKVENNKFCASVHFRC 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309  152 VTDKLKAKLIAEAKGLIQAH-GFQLIETPYALEGKPRVNWDKGEGAKMILEKQFDADwAKNLKIVYVGDDTTDEDAIKVL 230
Cdd:PLN02151 229 VEENKWSDLANQVRSVLKNYpKLMLTQGRKVLEIRPIIKWDKGKALEFLLESLGYAN-CTDVFPIYIGDDRTDEDAFKIL 307
                        250       260       270
                 ....*....|....*....|....*....|...
gi 20129309  231 ----HGIGktFRVSELPTlKTYANYQIKTVEEV 259
Cdd:PLN02151 308 rdkkQGLG--ILVSKYAK-ETNASYSLQEPDEV 337
Trehalose_PPase pfam02358
Trehalose-phosphatase; This family consist of trehalose-phosphatases EC:3.1.3.12 these enzyme ...
34-251 9.68e-25

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: 98.94  E-value: 9.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309    34 LLDYDGTLAPLTEELSVMPKDTEI--NIKKLAANEKIFMVVFSGRELSEIKNHLKFPNVTYAGNHGLEVEYPSGKKfKIE 111
Cdd:pfam02358   1 FLDYDGTLSPIVSDPIAAVPSDRMlsALQDLASDPPNTVAIISGRSRQEEDLFVGVPNLGLAAEHGAFVRLPGGGD-WYN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309   112 MPEEL-LEKHNKLVSELKEKVV-CSGAWVEDKKISVTYHYKGVTDKLKAkliAEAKGLIQAH------GFQLIETPY--A 181
Cdd:pfam02358  80 QAEVEdLPWKKEVAPILEYYTErTPGSYVENKKSALSWHYRNADDDFGS---FQAKELAEHLesvlqdNPPLRVTQGkkV 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20129309   182 LEGKPRVNWdKGEGAKMILEKQfDADWAKNLKIVYVGDDTTDEDAIKVLH-----GIGKTFRVSELPTLKTYANY 251
Cdd:pfam02358 157 VEVRPVGVS-KGKAVEFILEEL-GSAGSLPDFPLCIGDDRTDEDMFSVLRptkpsGVGIEVFAVSVGSKPSSASY 229
 
Name Accession Description Interval E-value
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
32-258 8.88e-60

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: 189.42  E-value: 8.88e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309  32 ALLLDYDGTLAPL--TEELSVMPKDTEINIKKLAANEKIFMVVFSGRELSEIKNHLKFPNVTYAGNHGLEVEYPSGKKFK 109
Cdd:cd01627   1 LLFLDYDGTLAPIvpDPDAAVPSPELLEALKKLAADPKNAVAIVSGRDLDDLDKWLGLPGIGLAGEHGAEIRLPGGGEWV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309 110 IEMPEELLEKHNKLVSELKEKVV-CSGAWVEDKKISVTYHYKGVT-DKLKAKLIAEAKGLIQAHGFqlietPYALEGK-- 185
Cdd:cd01627  81 TLAPKADLEWKEEVEAIFKYFTErTPGSLVEDKGASLAWHYRNADpEGARAALELALHLASDLLKA-----LEVVPGKkv 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20129309 186 ---PRVNWDKGEGAKMILEKQFDADwaknLKIVYVGDDTTDEDAIKVLHG-IGKTFRVSELPTLKTYANYQIKTVEE 258
Cdd:cd01627 156 vevRPVGVNKGEAVERILGELPFAG----DFVLCAGDDVTDEDAFRALNGeGGFSVKVGEGPTAAKFRLDDPPDVVA 228
OtsB COG1877
Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];
28-265 4.79e-50

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


Pssm-ID: 441481 [Multi-domain]  Cd Length: 242  Bit Score: 164.98  E-value: 4.79e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309  28 TDQVALLLDYDGTLAPLTE--ELSVMPKDTEINIKKLAANEKIFMVVFSGRELSEIKNHLKFPNVTYAGNHGLEVEYPSG 105
Cdd:COG1877   1 APRLLLFLDFDGTLAPIVPdpDAARPPPELRELLRRLAARPGGAVAIVSGRDLADLDRLLGPLGLPLAGSHGAERRLPGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309 106 KKFKIEMPEELLEKHNKLVSELKEKVV-CSGAWVEDKKISVTYHYKGVTDKLKAKLIAEAKGLIQAHGFQLIETP--YAL 182
Cdd:COG1877  81 EWEVLPLAAEAPEWLDALRAALEALAArTPGVLVEDKGASLALHYRQAPPEEAEELRAALRELAARLGPGLEVLPgkKVV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309 183 EGKPRvNWDKGEGAKMILEkQFDADWAknlkIVYVGDDTTDEDAIKVLHGIGKTFRVSELPTLktyANYQIKTVEEVGYL 262
Cdd:COG1877 161 ELRPA-GVDKGRAVRALLA-ELPFGRA----PVFIGDDVTDEDAFAALPAGGLGIKVGSGPTA---ARYRLADPAEVRAL 231

                ...
gi 20129309 263 LKA 265
Cdd:COG1877 232 LAR 234
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
32-234 3.55e-33

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: 120.18  E-value: 3.55e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309    32 ALLLDYDGTLAPLTEelsvMPKDTEIN--IKKLAANEkIFMVVFSGRELSEIKNHLKFPNV--TYAGNHGLEVEYPSGKK 107
Cdd:TIGR01484   1 LLFFDLDGTLLDPNA----HELSPETIeaLERLREAG-VKVVIVTGRSLAEIKELLKQLNLplPLIAENGALIFYPGEIL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309   108 FK--IEMPEELL-EKHNKLVSELKEKVVCS-GAWVEDKKISVTYHYKG--VTDKLKAKLIAEAKGL-IQAHGFQLI-ETP 179
Cdd:TIGR01484  76 YIepSDVFEEILgIKFEEIGAELKSLSEHYvGTFIEDKAIAVAIHYVGaeLGQELDSKMRERLEKIgRNDLELEAIySGK 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 20129309   180 YALEGKPrVNWDKGEGAKMILEKQFdadwAKNLKIVYVGDDTTDEDAIKVLHGIG 234
Cdd:TIGR01484 156 TDLEVLP-AGVNKGSALQALLQELN----GKKDEILAFGDSGNDEEMFEVAGLAV 205
PLN02151 PLN02151
trehalose-phosphatase
5-259 2.96e-29

trehalose-phosphatase


Pssm-ID: 177812  Cd Length: 354  Bit Score: 113.61  E-value: 2.96e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309    5 KKAPLLKKEEDYVKALEGFIN-PETDQVALLLDYDGTLAPLTEE--LSVMPKDTEINIKKLAaneKIF-MVVFSGRELSE 80
Cdd:PLN02151  72 KQSCWIKEHPSALNMFEEILHkSEGKQIVMFLDYDGTLSPIVDDpdRAFMSKKMRNTVRKLA---KCFpTAIVSGRCREK 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309   81 IKNHLKFPNVTYAGNHGLEVEYP-SGKKFKIEMPE-------ELLEKHNKLVSELKEKVVCS-GAWVEDKKISVTYHYKG 151
Cdd:PLN02151 149 VSSFVKLTELYYAGSHGMDIKGPeQGSKYKKENQSllcqpatEFLPVINEVYKKLVEKTKSIpGAKVENNKFCASVHFRC 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309  152 VTDKLKAKLIAEAKGLIQAH-GFQLIETPYALEGKPRVNWDKGEGAKMILEKQFDADwAKNLKIVYVGDDTTDEDAIKVL 230
Cdd:PLN02151 229 VEENKWSDLANQVRSVLKNYpKLMLTQGRKVLEIRPIIKWDKGKALEFLLESLGYAN-CTDVFPIYIGDDRTDEDAFKIL 307
                        250       260       270
                 ....*....|....*....|....*....|...
gi 20129309  231 ----HGIGktFRVSELPTlKTYANYQIKTVEEV 259
Cdd:PLN02151 308 rdkkQGLG--ILVSKYAK-ETNASYSLQEPDEV 337
PLN03017 PLN03017
trehalose-phosphatase
30-259 9.04e-28

trehalose-phosphatase


Pssm-ID: 178591 [Multi-domain]  Cd Length: 366  Bit Score: 109.73  E-value: 9.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309   30 QVALLLDYDGTLAPLTEE--LSVMPKDTEINIKKLAaneKIF-MVVFSGRELSEIKNHLKFPNVTYAGNHGLEVEYPSG- 105
Cdd:PLN03017 111 QIVMFLDYDGTLSPIVDDpdKAFMSSKMRRTVKKLA---KCFpTAIVTGRCIDKVYNFVKLAELYYAGSHGMDIKGPAKg 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309  106 -KKFKIEMPEELLEKHN-------KLVSELKEKVVCS-GAWVEDKKISVTYHYKGVTDKLKAKLIAEAKGLIQAH-GFQL 175
Cdd:PLN03017 188 fSRHKRVKQSLLYQPANdylpmidEVYRQLLEKTKSTpGAKVENHKFCASVHFRCVDEKKWSELVLQVRSVLKNFpTLKL 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309  176 IETPYALEGKPRVNWDKGEGAKMILEkQFDADWAKNLKIVYVGDDTTDEDAIKVLHGIGKTF--RVSELPTlKTYANYQI 253
Cdd:PLN03017 268 TQGRKVFEIRPMIEWDKGKALEFLLE-SLGFGNTNNVFPVYIGDDRTDEDAFKMLRDRGEGFgiLVSKFPK-DTDASYSL 345

                 ....*.
gi 20129309  254 KTVEEV 259
Cdd:PLN03017 346 QDPSEV 351
T6PP TIGR00685
trehalose-phosphatase; Trehalose, a neutral disaccharide of two glucose residues, is an ...
30-259 2.34e-25

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: 100.68  E-value: 2.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309    30 QVALLLDYDGTLAPLTE--ELSVMPKDTEINIKKLAANEKIFMVVFSGRELSEIKNHLKFPNVTYAGNHGLEVEyPSGKK 107
Cdd:TIGR00685   3 KRAFFFDYDGTLSEIVPdpDAAVVSDRLLTILQKLAARPHNAIWIISGRKFLEKWLGVKLPGLGLAGEHGCEMK-DNGSC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309   108 FKIEMPEELLEKHNKLVSELKEKVV-CSGAWVEDKKISVTYHYKGVTD---------KLKAKlIAEAKGLIQAHGFQLIE 177
Cdd:TIGR00685  82 QDWVNLTEKIPSWKVRANELREEITtRPGVFIERKGVALAWHYRQAPVpelarfrakELKEK-ILSFTDLEVMDGKAVVE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309   178 TpyalegKPRvNWDKGEGAKMILEKQFdadwAKNLKIVYVGDDTTDEDAIKVLHGI-----GKTFRVSElPTLKTYANYQ 252
Cdd:TIGR00685 161 L------KPR-FVNKGEIVKRLLWHQP----GSGISPVYLGDDITDEDAFRVVNNQwgnygFYPVPIGS-GSKKTVAKFH 228

                  ....*..
gi 20129309   253 IKTVEEV 259
Cdd:TIGR00685 229 LTGPQQV 235
Trehalose_PPase pfam02358
Trehalose-phosphatase; This family consist of trehalose-phosphatases EC:3.1.3.12 these enzyme ...
34-251 9.68e-25

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: 98.94  E-value: 9.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309    34 LLDYDGTLAPLTEELSVMPKDTEI--NIKKLAANEKIFMVVFSGRELSEIKNHLKFPNVTYAGNHGLEVEYPSGKKfKIE 111
Cdd:pfam02358   1 FLDYDGTLSPIVSDPIAAVPSDRMlsALQDLASDPPNTVAIISGRSRQEEDLFVGVPNLGLAAEHGAFVRLPGGGD-WYN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309   112 MPEEL-LEKHNKLVSELKEKVV-CSGAWVEDKKISVTYHYKGVTDKLKAkliAEAKGLIQAH------GFQLIETPY--A 181
Cdd:pfam02358  80 QAEVEdLPWKKEVAPILEYYTErTPGSYVENKKSALSWHYRNADDDFGS---FQAKELAEHLesvlqdNPPLRVTQGkkV 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20129309   182 LEGKPRVNWdKGEGAKMILEKQfDADWAKNLKIVYVGDDTTDEDAIKVLH-----GIGKTFRVSELPTLKTYANY 251
Cdd:pfam02358 157 VEVRPVGVS-KGKAVEFILEEL-GSAGSLPDFPLCIGDDRTDEDMFSVLRptkpsGVGIEVFAVSVGSKPSSASY 229
PRK14501 PRK14501
putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional
33-265 9.90e-24

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


Pssm-ID: 184712 [Multi-domain]  Cd Length: 726  Bit Score: 100.38  E-value: 9.90e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309   33 LLLDYDGTLAPLTE--ELSVMPKDTEINIKKLAANEKIFMVVFSGRELSEIKNHLKFPNVTYAGNHGLEVEYPSGKKFKI 110
Cdd:PRK14501 495 LLLDYDGTLVPFAPdpELAVPDKELRDLLRRLAADPNTDVAIISGRDRDTLERWFGDLPIHLVAEHGAWSRAPGGEWQLL 574
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309  111 EMPEEllEKHNKLVSELKEKVVCS-GAWVEDKKISVTYHYKGVTDKLKAK----LIAEAKGLIQAHGFQLIETPYALEGK 185
Cdd:PRK14501 575 EPVAT--EWKDAVRPILEEFVDRTpGSFIEEKEASLAWHYRNADPELGEAraneLILALSSLLSNAPLEVLRGNKVVEVR 652
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309  186 PRvNWDKGEGAKMILEKqfdADWAknlKIVYVGDDTTDEDAIKVLHGIGKTFRVSelpTLKTYANYQIKTVEEVGYLLKA 265
Cdd:PRK14501 653 PA-GVNKGRAVRRLLEA---GPYD---FVLAIGDDTTDEDMFRALPETAITVKVG---PGESRARYRLPSQREVRELLRR 722
PLN02580 PLN02580
trehalose-phosphatase
30-266 1.35e-21

trehalose-phosphatase


Pssm-ID: 215317 [Multi-domain]  Cd Length: 384  Bit Score: 92.95  E-value: 1.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309   30 QVALLLDYDGTLAPLTEE--LSVMPKDTEINIKKLAaneKIF-MVVFSGRELSEIKNHLKFPNVTYAGNHGLEVEYPSGK 106
Cdd:PLN02580 119 KIALFLDYDGTLSPIVDDpdRALMSDAMRSAVKNVA---KYFpTAIISGRSRDKVYELVGLTELYYAGSHGMDIMGPVRE 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309  107 KFKIEMPE--ELLEKHNKLV------SE---LKEKVVCS---------GAWVEDKKISVTYHYKGVTDKlKAKLIAEA-- 164
Cdd:PLN02580 196 SVSNDHPNciKSTDQQGKEVnlfqpaSEflpMIDEVFRSlvestkdikGAKVENHKFCVSVHYRNVDEK-NWPLVAQCvh 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309  165 ------KGLIQAHGFQLietpyaLEGKPRVNWDKGEGAKMILEkQFDADWAKNLKIVYVGDDTTDEDAIKVL----HGIG 234
Cdd:PLN02580 275 dvlkkyPRLRLTHGRKV------LEVRPVIDWNKGKAVEFLLE-SLGLSNCDDVLPIYIGDDRTDEDAFKVLregnRGYG 347
                        250       260       270
                 ....*....|....*....|....*....|..
gi 20129309  235 ktFRVSELPTlKTYANYQIKTVEEVGYLLKAV 266
Cdd:PLN02580 348 --ILVSSVPK-ESNAFYSLRDPSEVMEFLKSL 376
PRK10187 PRK10187
trehalose-6-phosphate phosphatase; Provisional
24-274 1.69e-09

trehalose-6-phosphate phosphatase; Provisional


Pssm-ID: 182291 [Multi-domain]  Cd Length: 266  Bit Score: 57.06  E-value: 1.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309   24 INPE-TDQVALLLDYDGTLA---PLTEELsVMPKDTEINIKKLAANEKIFMVVFSGR---ELSEIKNHLKFPnvtYAGNH 96
Cdd:PRK10187   7 VPPElSANYAWFFDLDGTLAeikPHPDQV-VVPDNILQGLQLLATANDGALALISGRsmvELDALAKPYRFP---LAGVH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309   97 GLEVEYPSGKKFKIEMPEELLEK-HNKLVSELKEkvvCSGAWVEDKKISVTYHYKGVTDKlKAKLIAEAKGLIQAHGfQL 175
Cdd:PRK10187  83 GAERRDINGKTHIVHLPDAIARDiSVQLHTALAQ---LPGAELEAKGMAFALHYRQAPQH-EDALLALAQRITQIWP-QL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129309  176 IETP--YALEGKPRvNWDKGEG-AKMILEKQFdadwaKNLKIVYVGDDTTDEDAIKVLHGI-GKTFRVSElptLKTYANY 251
Cdd:PRK10187 158 ALQPgkCVVEIKPR-GTNKGEAiAAFMQEAPF-----AGRTPVFVGDDLTDEAGFAVVNRLgGISVKVGT---GATQASW 228
                        250       260
                 ....*....|....*....|....
gi 20129309  252 QIKTVEEV-GYLLKAVQAYYEKKK 274
Cdd:PRK10187 229 RLAGVPDVwSWLEMITTAQQQKRE 252
 
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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