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Conserved domains on  [gi|1806365104|dbj|BBY54894|]
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trehalose-phosphate phosphatase [Mycolicibacillus koreensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OtsB COG1877
Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];
184-431 1.59e-68

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


:

Pssm-ID: 441481 [Multi-domain]  Cd Length: 242  Bit Score: 217.75  E-value: 1.59e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 184 GRTPAVFFDFDGTLSEIVDDPGAARLVDGADAALRALAAVC--PVAILSGRDLGDVVDRVGVPGLWYAGSHGFELRGPDG 261
Cdd:COG1877     1 APRLLLFLDFDGTLAPIVPDPDAARPPPELRELLRRLAARPggAVAIVSGRDLADLDRLLGPLGLPLAGSHGAERRLPGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 262 AHHQNETAAAAIPVLAEAADELRSRLASIDGVLVEHKRFAVAVHYRNAAREHVGAVTAAVREAGRRDR--LRVTTGREVI 339
Cdd:COG1877    81 EWEVLPLAAEAPEWLDALRAALEALAARTPGVLVEDKGASLALHYRQAPPEEAEELRAALRELAARLGpgLEVLPGKKVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 340 ELRPDiDWDKGKTLRWLTDRIGGAAserlLPVFVGDDITDEDAFAEISSDGIGIMVrhsddGDRATSARFAVADPAAVRD 419
Cdd:COG1877   161 ELRPA-GVDKGRAVRALLAELPFGR----APVFIGDDVTDEDAFAALPAGGLGIKV-----GSGPTAARYRLADPAEVRA 230

                         250
                  ....*....|..
gi 1806365104 420 FTEELARTLEAR 431
Cdd:COG1877   231 LLARLAEARRAA 242
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 12-158 4.84e-08

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member cd02598:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 174  Bit Score: 52.68  E-value: 4.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104  12 AVLFDLDAVV---------------------------PVHRRDDGAPA--LSTTVSLVQRLRRLGVGTAVVSANRDCAAA 62
Cdd:cd02598     1 GVIFDLDGVItdtaeyhyrawkkladkeelaarknriYVELIEELTPVdvLPGIASLLVDLKAKGIKIALASASKNAPKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104  63 LGAAGLGDLFAVHVDGAAAEPGpsgEADPAALLEAARRLGVRPDRCVVVENaEAGVAAARAGGFALVIGVDRDGPgtqls 142
Cdd:cd02598    81 LEKLGLAEYFDAIVDGAVLAKG---KPDPDIFLAAAEGLGLNPKDCIGVED-AQAGIRAIKAAGFLVVGVGREED----- 151

                         170
                  ....*....|....*..
gi 1806365104 143 RGGADSVVADL-GEVTV 158
Cdd:cd02598   152 LLGADIVVPDTtADLTI 168
 
Name Accession Description Interval E-value
OtsB COG1877
Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];
184-431 1.59e-68

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


Pssm-ID: 441481 [Multi-domain]  Cd Length: 242  Bit Score: 217.75  E-value: 1.59e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 184 GRTPAVFFDFDGTLSEIVDDPGAARLVDGADAALRALAAVC--PVAILSGRDLGDVVDRVGVPGLWYAGSHGFELRGPDG 261
Cdd:COG1877     1 APRLLLFLDFDGTLAPIVPDPDAARPPPELRELLRRLAARPggAVAIVSGRDLADLDRLLGPLGLPLAGSHGAERRLPGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 262 AHHQNETAAAAIPVLAEAADELRSRLASIDGVLVEHKRFAVAVHYRNAAREHVGAVTAAVREAGRRDR--LRVTTGREVI 339
Cdd:COG1877    81 EWEVLPLAAEAPEWLDALRAALEALAARTPGVLVEDKGASLALHYRQAPPEEAEELRAALRELAARLGpgLEVLPGKKVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 340 ELRPDiDWDKGKTLRWLTDRIGGAAserlLPVFVGDDITDEDAFAEISSDGIGIMVrhsddGDRATSARFAVADPAAVRD 419
Cdd:COG1877   161 ELRPA-GVDKGRAVRALLAELPFGR----APVFIGDDVTDEDAFAALPAGGLGIKV-----GSGPTAARYRLADPAEVRA 230

                         250
                  ....*....|..
gi 1806365104 420 FTEELARTLEAR 431
Cdd:COG1877   231 LLARLAEARRAA 242
T6PP TIGR00685
trehalose-phosphatase; Trehalose, a neutral disaccharide of two glucose residues, is an ...
 184-426 3.06e-67

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: 214.70  E-value: 3.06e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 184 GRTPAVFFDFDGTLSEIVDDPGAARLVDGADAALRALAAVCPVA--ILSGRDLGDVVDRVGVPGLWYAGSHGFELRGpDG 261
Cdd:TIGR00685   1 ARKRAFFFDYDGTLSEIVPDPDAAVVSDRLLTILQKLAARPHNAiwIISGRKFLEKWLGVKLPGLGLAGEHGCEMKD-NG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 262 AHHQNETAAAAIPVLAEAADELRSRLASIDGVLVEHKRFAVAVHYRNA-----AREHVGAVTAAVREAgrrDRLRVTTGR 336
Cdd:TIGR00685  80 SCQDWVNLTEKIPSWKVRANELREEITTRPGVFIERKGVALAWHYRQApvpelARFRAKELKEKILSF---TDLEVMDGK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 337 EVIELRPDiDWDKGKTLRWLTDRIGGAASErllPVFVGDDITDEDAFAEISS--DGIGIMVRHSDDGDRATSARFAVADP 414
Cdd:TIGR00685 157 AVVELKPR-FVNKGEIVKRLLWHQPGSGIS---PVYLGDDITDEDAFRVVNNqwGNYGFYPVPIGSGSKKTVAKFHLTGP 232

                         250
                  ....*....|..
gi 1806365104 415 AAVRDFTEELAR 426
Cdd:TIGR00685 233 QQVLEFLGLLVG 244
Trehalose_PPase pfam02358
Trehalose-phosphatase; This family consist of trehalose-phosphatases EC:3.1.3.12 these enzyme ...
 190-414 1.17e-65

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: 210.27  E-value: 1.17e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 190 FFDFDGTLSEIVDDPGAARLVDGADAALRALAAVCP--VAILSGRDLGDVVDRVGVPGLWYAGSHGFELRGPDGAHHQNE 267
Cdd:pfam02358   1 FLDYDGTLSPIVSDPIAAVPSDRMLSALQDLASDPPntVAIISGRSRQEEDLFVGVPNLGLAAEHGAFVRLPGGGDWYNQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 268 TAAAAIPVLAEAADELRSRLASIDGVLVEHKRFAVAVHYRNAARE----HVGAVTAAVREAGRRDR-LRVTTGREVIELR 342
Cdd:pfam02358  81 AEVEDLPWKKEVAPILEYYTERTPGSYVENKKSALSWHYRNADDDfgsfQAKELAEHLESVLQDNPpLRVTQGKKVVEVR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1806365104 343 PDIDWdKGKTLRWLTDRIGGAASERLLPVFVGDDITDEDAFAEIS---SDGIGIMVRHSDDGDRATSARFAVADP 414
Cdd:pfam02358 161 PVGVS-KGKAVEFILEELGSAGSLPDFPLCIGDDRTDEDMFSVLRptkPSGVGIEVFAVSVGSKPSSASYFLDDP 234
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
 188-418 1.35e-52

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: 175.94  E-value: 1.35e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 188 AVFFDFDGTLSEIVDDPGAARLVDGADAALRA--LAAVCPVAILSGRDLGDVVDRVGVPGLWYAGSHGFELRGPDGAHHQ 265
Cdd:cd01627     1 LLFLDYDGTLAPIVPDPDAAVPSPELLEALKKlaADPKNAVAIVSGRDLDDLDKWLGLPGIGLAGEHGAEIRLPGGGEWV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 266 NETAAAAIPVLAEAADELRSRLASIDGVLVEHKRFAVAVHYRNAAREHVGAVTAAVR--EAGRRDRLRVTTGREVIELRP 343
Cdd:cd01627    81 TLAPKADLEWKEEVEAIFKYFTERTPGSLVEDKGASLAWHYRNADPEGARAALELALhlASDLLKALEVVPGKKVVEVRP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1806365104 344 dIDWDKGKTLRWLTDRIGGAAserLLPVFVGDDITDEDAFAEISSDGiGIMVRHsddGDRATSARFAVADPAAVR 418
Cdd:cd01627   161 -VGVNKGEAVERILGELPFAG---DFVLCAGDDVTDEDAFRALNGEG-GFSVKV---GEGPTAAKFRLDDPPDVV 227
PLN02580 PLN02580
trehalose-phosphatase
 184-426 1.80e-47

trehalose-phosphatase


Pssm-ID: 215317 [Multi-domain]  Cd Length: 384  Bit Score: 167.29  E-value: 1.80e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 184 GRTPAVFFDFDGTLSEIVDDPGAARLVDGADAALRALAAVCPVAILSGRDLGDVVDRVGVPGLWYAGSHGFELRGPDGAH 263
Cdd:PLN02580  117 GKKIALFLDYDGTLSPIVDDPDRALMSDAMRSAVKNVAKYFPTAIISGRSRDKVYELVGLTELYYAGSHGMDIMGPVRES 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 264 HQNE-------------------TAAAAIPVLAEAADELRSRLASIDGVLVEHKRFAVAVHYRNAAREHVGAVTAAVREA 324
Cdd:PLN02580  197 VSNDhpncikstdqqgkevnlfqPASEFLPMIDEVFRSLVESTKDIKGAKVENHKFCVSVHYRNVDEKNWPLVAQCVHDV 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 325 GRR-DRLRVTTGREVIELRPDIDWDKGKTLRWLTDRIGGAASERLLPVFVGDDITDEDAFAEI--SSDGIGIMVRHSddg 401
Cdd:PLN02580  277 LKKyPRLRLTHGRKVLEVRPVIDWNKGKAVEFLLESLGLSNCDDVLPIYIGDDRTDEDAFKVLreGNRGYGILVSSV--- 353

                         250       260
                  ....*....|....*....|....*
gi 1806365104 402 DRATSARFAVADPAAVRDFTEELAR 426
Cdd:PLN02580  354 PKESNAFYSLRDPSEVMEFLKSLVT 378
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 12-158 4.84e-08

beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); Lactococcus lactis beta-PGM catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate as an intermediate. In the forward G6P-forming direction, this reaction links polysaccharide phosphorolysis to glycolysis, in the reverse direction, the reaction provides G1P for the biosynthesis of exo-polysaccharides. This subfamily belongs to the beta-phosphoglucomutase-like family whose other members include Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. 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: 319788 [Multi-domain]  Cd Length: 174  Bit Score: 52.68  E-value: 4.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104  12 AVLFDLDAVV---------------------------PVHRRDDGAPA--LSTTVSLVQRLRRLGVGTAVVSANRDCAAA 62
Cdd:cd02598     1 GVIFDLDGVItdtaeyhyrawkkladkeelaarknriYVELIEELTPVdvLPGIASLLVDLKAKGIKIALASASKNAPKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104  63 LGAAGLGDLFAVHVDGAAAEPGpsgEADPAALLEAARRLGVRPDRCVVVENaEAGVAAARAGGFALVIGVDRDGPgtqls 142
Cdd:cd02598    81 LEKLGLAEYFDAIVDGAVLAKG---KPDPDIFLAAAEGLGLNPKDCIGVED-AQAGIRAIKAAGFLVVGVGREED----- 151

                         170
                  ....*....|....*..
gi 1806365104 143 RGGADSVVADL-GEVTV 158
Cdd:cd02598   152 LLGADIVVPDTtADLTI 168
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
26-112 4.24e-05

Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 44.43  E-value: 4.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104  26 RDDGAPALSTTVSLVQRLRRLGVGTAVVSANRD--CAAALGAAGLGDLFAVHVDGAAAEPG-PsgeaDPAALLEAARRLG 102
Cdd:COG0637    81 AEEGLPLIPGVVELLEALKEAGIKIAVATSSPRenAEAVLEAAGLLDYFDVIVTGDDVARGkP----DPDIYLLAAERLG 156

                          90
                  ....*....|
gi 1806365104 103 VRPDRCVVVE 112
Cdd:COG0637   157 VDPEECVVFE 166
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 29-112 1.54e-03

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 39.33  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104  29 GAPALSTTVSLVQRLRRLGVGTAVVS-ANRDCAAALGAAGLGDLFAVHVDGAAAepgPSGEADPAALLEAARRLGVRPDR 107
Cdd:TIGR01509  78 KLKPLPGVRALLEALRARGKKLALLTnSPRAHKLVLALLGLRDLFDVVIDSSDV---GLGKPDPDIYLQALKALGLEPSE 154


                  ....*
gi 1806365104 108 CVVVE 112
Cdd:TIGR01509 155 CVFVD 159
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 11-112 2.03e-03

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 39.11  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104  11 DAVLFDLDAVVPVHrrdDGAPALSTTVSLVQRLRRLGVGTAVVSANRDCAAALGAAGLGDLFAVHVDgAAAEPGPSGEAD 90
Cdd:pfam00702  81 TVVLVELLGVIALA---DELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVV-ISGDDVGVGKPK 156

                          90       100
                  ....*....|....*....|..
gi 1806365104  91 PAALLEAARRLGVRPDRCVVVE 112
Cdd:pfam00702 157 PEIYLAALERLGVKPEEVLMVG 178
 
Name Accession Description Interval E-value
OtsB COG1877
Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];
184-431 1.59e-68

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


Pssm-ID: 441481 [Multi-domain]  Cd Length: 242  Bit Score: 217.75  E-value: 1.59e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 184 GRTPAVFFDFDGTLSEIVDDPGAARLVDGADAALRALAAVC--PVAILSGRDLGDVVDRVGVPGLWYAGSHGFELRGPDG 261
Cdd:COG1877     1 APRLLLFLDFDGTLAPIVPDPDAARPPPELRELLRRLAARPggAVAIVSGRDLADLDRLLGPLGLPLAGSHGAERRLPGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 262 AHHQNETAAAAIPVLAEAADELRSRLASIDGVLVEHKRFAVAVHYRNAAREHVGAVTAAVREAGRRDR--LRVTTGREVI 339
Cdd:COG1877    81 EWEVLPLAAEAPEWLDALRAALEALAARTPGVLVEDKGASLALHYRQAPPEEAEELRAALRELAARLGpgLEVLPGKKVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 340 ELRPDiDWDKGKTLRWLTDRIGGAAserlLPVFVGDDITDEDAFAEISSDGIGIMVrhsddGDRATSARFAVADPAAVRD 419
Cdd:COG1877   161 ELRPA-GVDKGRAVRALLAELPFGR----APVFIGDDVTDEDAFAALPAGGLGIKV-----GSGPTAARYRLADPAEVRA 230

                         250
                  ....*....|..
gi 1806365104 420 FTEELARTLEAR 431
Cdd:COG1877   231 LLARLAEARRAA 242
T6PP TIGR00685
trehalose-phosphatase; Trehalose, a neutral disaccharide of two glucose residues, is an ...
 184-426 3.06e-67

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: 214.70  E-value: 3.06e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 184 GRTPAVFFDFDGTLSEIVDDPGAARLVDGADAALRALAAVCPVA--ILSGRDLGDVVDRVGVPGLWYAGSHGFELRGpDG 261
Cdd:TIGR00685   1 ARKRAFFFDYDGTLSEIVPDPDAAVVSDRLLTILQKLAARPHNAiwIISGRKFLEKWLGVKLPGLGLAGEHGCEMKD-NG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 262 AHHQNETAAAAIPVLAEAADELRSRLASIDGVLVEHKRFAVAVHYRNA-----AREHVGAVTAAVREAgrrDRLRVTTGR 336
Cdd:TIGR00685  80 SCQDWVNLTEKIPSWKVRANELREEITTRPGVFIERKGVALAWHYRQApvpelARFRAKELKEKILSF---TDLEVMDGK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 337 EVIELRPDiDWDKGKTLRWLTDRIGGAASErllPVFVGDDITDEDAFAEISS--DGIGIMVRHSDDGDRATSARFAVADP 414
Cdd:TIGR00685 157 AVVELKPR-FVNKGEIVKRLLWHQPGSGIS---PVYLGDDITDEDAFRVVNNqwGNYGFYPVPIGSGSKKTVAKFHLTGP 232

                         250
                  ....*....|..
gi 1806365104 415 AAVRDFTEELAR 426
Cdd:TIGR00685 233 QQVLEFLGLLVG 244
Trehalose_PPase pfam02358
Trehalose-phosphatase; This family consist of trehalose-phosphatases EC:3.1.3.12 these enzyme ...
 190-414 1.17e-65

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: 210.27  E-value: 1.17e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 190 FFDFDGTLSEIVDDPGAARLVDGADAALRALAAVCP--VAILSGRDLGDVVDRVGVPGLWYAGSHGFELRGPDGAHHQNE 267
Cdd:pfam02358   1 FLDYDGTLSPIVSDPIAAVPSDRMLSALQDLASDPPntVAIISGRSRQEEDLFVGVPNLGLAAEHGAFVRLPGGGDWYNQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 268 TAAAAIPVLAEAADELRSRLASIDGVLVEHKRFAVAVHYRNAARE----HVGAVTAAVREAGRRDR-LRVTTGREVIELR 342
Cdd:pfam02358  81 AEVEDLPWKKEVAPILEYYTERTPGSYVENKKSALSWHYRNADDDfgsfQAKELAEHLESVLQDNPpLRVTQGKKVVEVR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1806365104 343 PDIDWdKGKTLRWLTDRIGGAASERLLPVFVGDDITDEDAFAEIS---SDGIGIMVRHSDDGDRATSARFAVADP 414
Cdd:pfam02358 161 PVGVS-KGKAVEFILEELGSAGSLPDFPLCIGDDRTDEDMFSVLRptkPSGVGIEVFAVSVGSKPSSASYFLDDP 234
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
 188-418 1.35e-52

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: 175.94  E-value: 1.35e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 188 AVFFDFDGTLSEIVDDPGAARLVDGADAALRA--LAAVCPVAILSGRDLGDVVDRVGVPGLWYAGSHGFELRGPDGAHHQ 265
Cdd:cd01627     1 LLFLDYDGTLAPIVPDPDAAVPSPELLEALKKlaADPKNAVAIVSGRDLDDLDKWLGLPGIGLAGEHGAEIRLPGGGEWV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 266 NETAAAAIPVLAEAADELRSRLASIDGVLVEHKRFAVAVHYRNAAREHVGAVTAAVR--EAGRRDRLRVTTGREVIELRP 343
Cdd:cd01627    81 TLAPKADLEWKEEVEAIFKYFTERTPGSLVEDKGASLAWHYRNADPEGARAALELALhlASDLLKALEVVPGKKVVEVRP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1806365104 344 dIDWDKGKTLRWLTDRIGGAAserLLPVFVGDDITDEDAFAEISSDGiGIMVRHsddGDRATSARFAVADPAAVR 418
Cdd:cd01627   161 -VGVNKGEAVERILGELPFAG---DFVLCAGDDVTDEDAFRALNGEG-GFSVKV---GEGPTAAKFRLDDPPDVV 227
PLN02580 PLN02580
trehalose-phosphatase
 184-426 1.80e-47

trehalose-phosphatase


Pssm-ID: 215317 [Multi-domain]  Cd Length: 384  Bit Score: 167.29  E-value: 1.80e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 184 GRTPAVFFDFDGTLSEIVDDPGAARLVDGADAALRALAAVCPVAILSGRDLGDVVDRVGVPGLWYAGSHGFELRGPDGAH 263
Cdd:PLN02580  117 GKKIALFLDYDGTLSPIVDDPDRALMSDAMRSAVKNVAKYFPTAIISGRSRDKVYELVGLTELYYAGSHGMDIMGPVRES 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 264 HQNE-------------------TAAAAIPVLAEAADELRSRLASIDGVLVEHKRFAVAVHYRNAAREHVGAVTAAVREA 324
Cdd:PLN02580  197 VSNDhpncikstdqqgkevnlfqPASEFLPMIDEVFRSLVESTKDIKGAKVENHKFCVSVHYRNVDEKNWPLVAQCVHDV 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 325 GRR-DRLRVTTGREVIELRPDIDWDKGKTLRWLTDRIGGAASERLLPVFVGDDITDEDAFAEI--SSDGIGIMVRHSddg 401
Cdd:PLN02580  277 LKKyPRLRLTHGRKVLEVRPVIDWNKGKAVEFLLESLGLSNCDDVLPIYIGDDRTDEDAFKVLreGNRGYGILVSSV--- 353

                         250       260
                  ....*....|....*....|....*
gi 1806365104 402 DRATSARFAVADPAAVRDFTEELAR 426
Cdd:PLN02580  354 PKESNAFYSLRDPSEVMEFLKSLVT 378
PLN02151 PLN02151
trehalose-phosphatase
 184-424 4.42e-47

trehalose-phosphatase


Pssm-ID: 177812  Cd Length: 354  Bit Score: 165.62  E-value: 4.42e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 184 GRTPAVFFDFDGTLSEIVDDPGAARLVDGADAALRALAAVCPVAILSGRDLGDVVDRVGVPGLWYAGSHGFELRGPD-GA 262
Cdd:PLN02151   96 GKQIVMFLDYDGTLSPIVDDPDRAFMSKKMRNTVRKLAKCFPTAIVSGRCREKVSSFVKLTELYYAGSHGMDIKGPEqGS 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 263 HHQNET-------AAAAIPVLAEAADELRSRLASIDGVLVEHKRFAVAVHYRNAAREHVGAVTAAVREAGRR-DRLRVTT 334
Cdd:PLN02151  176 KYKKENqsllcqpATEFLPVINEVYKKLVEKTKSIPGAKVENNKFCASVHFRCVEENKWSDLANQVRSVLKNyPKLMLTQ 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 335 GREVIELRPDIDWDKGKTLRWLTDRIGGAASERLLPVFVGDDITDEDAFAEI--SSDGIGIMVRHSddgDRATSARFAVA 412
Cdd:PLN02151  256 GRKVLEIRPIIKWDKGKALEFLLESLGYANCTDVFPIYIGDDRTDEDAFKILrdKKQGLGILVSKY---AKETNASYSLQ 332

                         250
                  ....*....|..
gi 1806365104 413 DPAAVRDFTEEL 424
Cdd:PLN02151  333 EPDEVMEFLERL 344
PLN03017 PLN03017
trehalose-phosphatase
 169-429 1.09e-42

trehalose-phosphatase


Pssm-ID: 178591 [Multi-domain]  Cd Length: 366  Bit Score: 154.03  E-value: 1.09e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 169 PDAVQAVSLTDDDTGGRTPAVFFDFDGTLSEIVDDPGAARLVDGADAALRALAAVCPVAILSGRDLGDVVDRVGVPGLWY 248
Cdd:PLN03017   94 PSALEMFEQIMEASRGKQIVMFLDYDGTLSPIVDDPDKAFMSSKMRRTVKKLAKCFPTAIVTGRCIDKVYNFVKLAELYY 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 249 AGSHGFELRGPDGAHHQN---------ETAAAAIPVLAEAADELRSRLASIDGVLVEHKRFAVAVHYRNAAREHVGAVTA 319
Cdd:PLN03017  174 AGSHGMDIKGPAKGFSRHkrvkqsllyQPANDYLPMIDEVYRQLLEKTKSTPGAKVENHKFCASVHFRCVDEKKWSELVL 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 320 AVREAGRR-DRLRVTTGREVIELRPDIDWDKGKTLRWLTDRIGGAASERLLPVFVGDDITDEDAFAEISS--DGIGIMVR 396
Cdd:PLN03017  254 QVRSVLKNfPTLKLTQGRKVFEIRPMIEWDKGKALEFLLESLGFGNTNNVFPVYIGDDRTDEDAFKMLRDrgEGFGILVS 333

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1806365104 397 HSddgDRATSARFAVADPAAVRDFteeLARTLE 429
Cdd:PLN03017  334 KF---PKDTDASYSLQDPSEVMDF---LARLVE 360
PRK14501 PRK14501
putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional
 189-426 2.41e-29

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


Pssm-ID: 184712 [Multi-domain]  Cd Length: 726  Bit Score: 121.18  E-value: 2.41e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 189 VFFDFDGTLSEIVDDPGAAR----LVDGADAALRALAAvcPVAILSGRDLGDVVDRVGVPGLWYAGSHGFELRGPDGAHH 264
Cdd:PRK14501  495 LLLDYDGTLVPFAPDPELAVpdkeLRDLLRRLAADPNT--DVAIISGRDRDTLERWFGDLPIHLVAEHGAWSRAPGGEWQ 572

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 265 QNETAA-----AAIPVLAEAADelrsRLAsidGVLVEHKRFAVAVHYRNAAREhVGAVTA-----AVREAGRRDRLRVTT 334
Cdd:PRK14501  573 LLEPVAtewkdAVRPILEEFVD----RTP---GSFIEEKEASLAWHYRNADPE-LGEARAnelilALSSLLSNAPLEVLR 644

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 335 GREVIELRPDiDWDKGKTLRWLTDRIGGAaserlLPVFVGDDITDEDAFAEISSDGIGIMVrhsddGDRATSARFAVADP 414
Cdd:PRK14501  645 GNKVVEVRPA-GVNKGRAVRRLLEAGPYD-----FVLAIGDDTTDEDMFRALPETAITVKV-----GPGESRARYRLPSQ 713

                         250
                  ....*....|..
gi 1806365104 415 AAVRDFTEELAR 426
Cdd:PRK14501  714 REVRELLRRLLD 725
PRK10187 PRK10187
trehalose-6-phosphate phosphatase; Provisional
 188-429 6.23e-17

trehalose-6-phosphate phosphatase; Provisional


Pssm-ID: 182291 [Multi-domain]  Cd Length: 266  Bit Score: 80.17  E-value: 6.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 188 AVFFDFDGTLSEIVDDP-----------GAARLVDGADAAlralaavcpVAILSGRDLGDVvDRVGVP-GLWYAGSHGFE 255
Cdd:PRK10187   16 AWFFDLDGTLAEIKPHPdqvvvpdnilqGLQLLATANDGA---------LALISGRSMVEL-DALAKPyRFPLAGVHGAE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 256 LRGpdgAHHQNETAAAAIPVLAEAADELRSRLASIDGVLVEHKRFAVAVHYRNAArEHVGAVTA-AVREAGRRDRLRVTT 334
Cdd:PRK10187   86 RRD---INGKTHIVHLPDAIARDISVQLHTALAQLPGAELEAKGMAFALHYRQAP-QHEDALLAlAQRITQIWPQLALQP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 335 GREVIELRPDiDWDKGKTLRWLTDRIGGAASErllPVFVGDDITDEDAFAEISSDGiGIMVRhsdDGDRATSARFAVADP 414
Cdd:PRK10187  162 GKCVVEIKPR-GTNKGEAIAAFMQEAPFAGRT---PVFVGDDLTDEAGFAVVNRLG-GISVK---VGTGATQASWRLAGV 233

                         250
                  ....*....|....*
gi 1806365104 415 AAVRDFTEELARTLE 429
Cdd:PRK10187  234 PDVWSWLEMITTAQQ 248
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 188-383 2.11e-09

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: 57.01  E-value: 2.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 188 AVFFDFDGTL----SEIVDDPGAA---RLVDGADaalralaavcPVAILSGRDLGDVV---DRVGVPgLWYAGSHGFELR 257
Cdd:TIGR01484   1 LLFFDLDGTLldpnAHELSPETIEaleRLREAGV----------KVVIVTGRSLAEIKellKQLNLP-LPLIAENGALIF 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 258 GPDGAHHqNETAAAAIPVLAEAADELRSRLASI----DGVLVEHKRFAVAVHYRNAAREHV--GAVTAAVREAGRRD-RL 330
Cdd:TIGR01484  70 YPGEILY-IEPSDVFEEILGIKFEEIGAELKSLsehyVGTFIEDKAIAVAIHYVGAELGQEldSKMRERLEKIGRNDlEL 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1806365104 331 RVT-TGREVIELRPdIDWDKGKTLRWLTDRIGGaasERLLPVFVGDDITDEDAF 383
Cdd:TIGR01484 149 EAIySGKTDLEVLP-AGVNKGSALQALLQELNG---KKDEILAFGDSGNDEEMF 198
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 12-158 4.84e-08

beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); Lactococcus lactis beta-PGM catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate as an intermediate. In the forward G6P-forming direction, this reaction links polysaccharide phosphorolysis to glycolysis, in the reverse direction, the reaction provides G1P for the biosynthesis of exo-polysaccharides. This subfamily belongs to the beta-phosphoglucomutase-like family whose other members include Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. 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: 319788 [Multi-domain]  Cd Length: 174  Bit Score: 52.68  E-value: 4.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104  12 AVLFDLDAVV---------------------------PVHRRDDGAPA--LSTTVSLVQRLRRLGVGTAVVSANRDCAAA 62
Cdd:cd02598     1 GVIFDLDGVItdtaeyhyrawkkladkeelaarknriYVELIEELTPVdvLPGIASLLVDLKAKGIKIALASASKNAPKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104  63 LGAAGLGDLFAVHVDGAAAEPGpsgEADPAALLEAARRLGVRPDRCVVVENaEAGVAAARAGGFALVIGVDRDGPgtqls 142
Cdd:cd02598    81 LEKLGLAEYFDAIVDGAVLAKG---KPDPDIFLAAAEGLGLNPKDCIGVED-AQAGIRAIKAAGFLVVGVGREED----- 151

                         170
                  ....*....|....*..
gi 1806365104 143 RGGADSVVADL-GEVTV 158
Cdd:cd02598   152 LLGADIVVPDTtADLTI 168
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 12-113 6.05e-07

beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; This family represents the beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. Family members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. It 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: 319808 [Multi-domain]  Cd Length: 143  Bit Score: 48.77  E-value: 6.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104  12 AVLFDLDAVV----PVHRR-----------------DDGAPALSTTVSLVQRLRRLGVGTAVVSANRdCAAALGAAGLGD 70
Cdd:cd07505     1 AVIFDMDGVLidtePLHRQawqllerknallleliaSEGLKLKPGVVELLDALKAAGIPVAVATSSS-RRNVELLLLELG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1806365104  71 LFAVHVDG-AAAEPGPSGEADPAALLEAARRLGVRPDRCVVVEN 113
Cdd:cd07505    80 LLRGYFDViVSGDDVERGKPAPDIYLLAAERLGVDPERCLVFED 123
PLN02205 PLN02205
alpha,alpha-trehalose-phosphate synthase [UDP-forming]
 186-429 1.81e-05

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


Pssm-ID: 177855 [Multi-domain]  Cd Length: 854  Bit Score: 47.33  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 186 TPAVFFDFDGTL--SEIVDDPGAARLVDGADAALRALAAVcpVAILSGRDLGDVVD------RVGVpglwyAGSHGFELR 257
Cdd:PLN02205  596 TRAILLDYDGTLmpQASIDKSPSSKSIDILNTLCRDKNNM--VFIVSARSRKTLADwfspceKLGI-----AAEHGYFLR 668

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 258 GPDGAHHQNETAAA--AIPVLAEAADELRSRlaSIDGVLVEHKRFAVAVHYRNA--------ARE---HVGAVTAavrea 324
Cdd:PLN02205  669 LKRDVEWETCVPVAdcSWKQIAEPVMQLYTE--TTDGSTIEDKETALVWCYEDAdpdfgscqAKElldHLESVLA----- 741

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104 325 grRDRLRVTTGREVIELRPdidwdKGKTLRWLTDRIGGAASER-LLPVFV---GDDITDEDAFAEISSDGIGIMVRHSDD 400
Cdd:PLN02205  742 --NEPVTVKSGQNIVEVKP-----QGVSKGLVAKRLLSIMQERgMLPDFVlciGDDRSDEDMFEVITSSMAGPSIAPRAE 814

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1806365104 401 ------GDRATSARFAVADPAAVRDFTEELARTLE 429
Cdd:PLN02205  815 vfactvGQKPSKAKYYLDDTAEIVRLMQGLASVSE 849
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
26-112 4.24e-05

Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 44.43  E-value: 4.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104  26 RDDGAPALSTTVSLVQRLRRLGVGTAVVSANRD--CAAALGAAGLGDLFAVHVDGAAAEPG-PsgeaDPAALLEAARRLG 102
Cdd:COG0637    81 AEEGLPLIPGVVELLEALKEAGIKIAVATSSPRenAEAVLEAAGLLDYFDVIVTGDDVARGkP----DPDIYLLAAERLG 156

                          90
                  ....*....|
gi 1806365104 103 VRPDRCVVVE 112
Cdd:COG0637   157 VDPEECVVFE 166
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 29-112 1.54e-03

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 39.33  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104  29 GAPALSTTVSLVQRLRRLGVGTAVVS-ANRDCAAALGAAGLGDLFAVHVDGAAAepgPSGEADPAALLEAARRLGVRPDR 107
Cdd:TIGR01509  78 KLKPLPGVRALLEALRARGKKLALLTnSPRAHKLVLALLGLRDLFDVVIDSSDV---GLGKPDPDIYLQALKALGLEPSE 154


                  ....*
gi 1806365104 108 CVVVE 112
Cdd:TIGR01509 155 CVFVD 159
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 11-112 2.03e-03

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 39.11  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806365104  11 DAVLFDLDAVVPVHrrdDGAPALSTTVSLVQRLRRLGVGTAVVSANRDCAAALGAAGLGDLFAVHVDgAAAEPGPSGEAD 90
Cdd:pfam00702  81 TVVLVELLGVIALA---DELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVV-ISGDDVGVGKPK 156

                          90       100
                  ....*....|....*....|..
gi 1806365104  91 PAALLEAARRLGVRPDRCVVVE 112
Cdd:pfam00702 157 PEIYLAALERLGVKPEEVLMVG 178
 
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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