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Conserved domains on  [gi|818607423|gb|KKS56384|]
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MAG: cof-like protein hydrolase [Candidatus Magasanikbacteria bacterium GW2011_GWA2_42_32]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cof-subfamily super family cl36587
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 6-248 1.67e-29

Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity]


The actual alignment was detected with superfamily member TIGR00099:

Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 111.59  E-value: 1.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423    6 ILFLaDLDGTILGGDHRILEPTHKAILNLQDLGILFSVATGRSS---TCIEQcALPVNCPGVFDNGGAICQSDGKIISCF 82
Cdd:TIGR00099   1 LIFI-DLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYkevKNILK-ELGLDTPFITANGAAVIDDQGEILYKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423   83 AFSRQELKMLRSLIKRNRHNITYAfssssfssGYTMLFLNeKNPQAILKWFGISIGRVAPD--------ETNFLKEMEQG 154
Cdd:TIGR00099  79 PLDLDLVEEILNFLKKHGLDVILY--------GDDSIYAS-KNDPEYFTIFKKFLGEPKLEvvdiqylpDDILKILLLFL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423  155 SHrlslvGDIKDIPPELNHTTND------SSGVHFHEFTRRGVNKGKGVEILAKYLGIPRRRVIIAGNDVNDLSMFQLnF 228
Cdd:TIGR00099 150 DP-----EDLDLLIEALNKLELEenvsvvSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEA-A 223

                         250       260
                  ....*....|....*....|
gi 818607423  229 GVRIAVGpNCPEEIQRRATH 248
Cdd:TIGR00099 224 GYGVAMG-NADEELKALADY 242
 
Name Accession Description Interval E-value
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 6-248 1.67e-29

Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 111.59  E-value: 1.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423    6 ILFLaDLDGTILGGDHRILEPTHKAILNLQDLGILFSVATGRSS---TCIEQcALPVNCPGVFDNGGAICQSDGKIISCF 82
Cdd:TIGR00099   1 LIFI-DLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYkevKNILK-ELGLDTPFITANGAAVIDDQGEILYKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423   83 AFSRQELKMLRSLIKRNRHNITYAfssssfssGYTMLFLNeKNPQAILKWFGISIGRVAPD--------ETNFLKEMEQG 154
Cdd:TIGR00099  79 PLDLDLVEEILNFLKKHGLDVILY--------GDDSIYAS-KNDPEYFTIFKKFLGEPKLEvvdiqylpDDILKILLLFL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423  155 SHrlslvGDIKDIPPELNHTTND------SSGVHFHEFTRRGVNKGKGVEILAKYLGIPRRRVIIAGNDVNDLSMFQLnF 228
Cdd:TIGR00099 150 DP-----EDLDLLIEALNKLELEenvsvvSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEA-A 223

                         250       260
                  ....*....|....*....|
gi 818607423  229 GVRIAVGpNCPEEIQRRATH 248
Cdd:TIGR00099 224 GYGVAMG-NADEELKALADY 242
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 11-248 1.25e-28

haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes.


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 109.25  E-value: 1.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423   11 DLDGTILGGDHRILEPTHKAILNLQDLGILFSVATGRSSTCIEQCA--LPVNCPGVFDNGGAICQSDGKIISCFAFSRQE 88
Cdd:pfam08282   4 DLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIkeLGLDDPVICYNGALIYDENGKILYSNPISKEA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423   89 LKMLRSLIKRNRHNITYAFSSSsfssgytmLFLNEKNPQAILKWFGISIGRVAPDETNFLKEMEQGSHRLSLVGD----- 163
Cdd:pfam08282  84 VKEIIEYLKENNLEILLYTDDG--------VYILNDNELEKILKELNYTKSFVPEIDDFELLEDEDINKILILLDeedld 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423  164 --IKDIPPELNHTTN--DSSGVHFhEFTRRGVNKGKGVEILAKYLGIPRRRVIIAGNDVNDLSMFQLnFGVRIAVGpNCP 239
Cdd:pfam08282 156 elEKELKELFGSLITitSSGPGYL-EIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEA-AGLGVAMG-NAS 232


                  ....*....
gi 818607423  240 EEIQRRATH 248
Cdd:pfam08282 233 PEVKAAADY 241
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 7-248 2.15e-26

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-phosphate. Members of this family belong 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: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 103.44  E-value: 2.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423   7 LFLADLDGTILGGDHRILEPTHKAILNLQDLGILFSVATGRS----STCIEQcaLPVNCPGVFDNGGAICQSDGKIISCF 82
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPlrgaQPYLEE--LGLDSPLITFNGALVYDPTGKEILER 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423  83 AFSRQELKMLRSLIKRNRHNITYAFSSSSFSSGYTmlflnEKNPQAILKWFGISIGRVAPDETNFLKEMEQGSHRLSLVG 162
Cdd:cd07516   79 LISKEDVKELEEFLRKLGIGINIYTNDDWADTIYE-----ENEDDEIIKPAEILDDLLLPPDEDITKILFVGEDEELDEL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423 163 DIKDIPPELNHTTNDSSGVHFHEFTRRGVNKGKGVEILAKYLGIPRRRVIIAGNDVNDLSMFQLnFGVRIAVGpNCPEEI 242
Cdd:cd07516  154 IAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEY-AGLGVAMG-NAIDEV 231


                 ....*.
gi 818607423 243 QRRATH 248
Cdd:cd07516  232 KEAADY 237
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 7-248 6.96e-26

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 100.60  E-value: 6.96e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423   7 LFLADLDGTILGGDHRILEPTHKAILNLQDLGILFSVATGRSSTCIEQCA--LPVNCPGVFDNGGAICQSDGKIISCFAF 84
Cdd:COG0561    4 LIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLeeLGLDDPLITSNGALIYDPDGEVLYERPL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423  85 SRQELKMLRSLIKRnrhnityafssssfssgytmlflneknpqailkwFGISIGRVApdetnflkemeqgshrlslvgdi 164
Cdd:COG0561   84 DPEDVREILELLRE----------------------------------HGLHLQVVV----------------------- 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423 165 kdippelnhttndSSGVHFHEFTRRGVNKGKGVEILAKYLGIPRRRVIIAGNDVNDLSMFQLNfGVRIAVGpNCPEEIQR 244
Cdd:COG0561  107 -------------RSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAA-GLGVAMG-NAPPEVKA 171


                 ....
gi 818607423 245 RATH 248
Cdd:COG0561  172 AADY 175
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 10-254 1.34e-12

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 65.38  E-value: 1.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423  10 ADLDGTILGGDHRILEPTHKAILNLQDLGILFSVATGRSSTCIEQCA--LPVNCPGVFDNGGAIC-QSDGKIIscFAFSR 86
Cdd:PRK01158   8 IDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGNVLCFARAAAklIGTSGPVIAENGGVISvGFDGKRI--FLGDI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423  87 QELKMLRSLIKrNRHnityafssSSFSSGYTML-FLNEKNPQAILKWFGISIGRvapdetnflKEMEQGSHRLSLVgdik 165
Cdd:PRK01158  86 EECEKAYSELK-KRF--------PEASTSLTKLdPDYRKTEVALRRTVPVEEVR---------ELLEELGLDLEIV---- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423 166 dippelnhttndSSGVHFHeFTRRGVNKGKGVEILAKYLGIPRRRVIIAGNDVNDLSMFQLNfGVRIAVGpNCPEEIqRR 245
Cdd:PRK01158 144 ------------DSGFAIH-IKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVA-GFGVAVA-NADEEL-KE 207


                 ....*....
gi 818607423 246 ATHYVETME 254
Cdd:PRK01158 208 AADYVTEKS 216
 
Name Accession Description Interval E-value
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 6-248 1.67e-29

Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 111.59  E-value: 1.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423    6 ILFLaDLDGTILGGDHRILEPTHKAILNLQDLGILFSVATGRSS---TCIEQcALPVNCPGVFDNGGAICQSDGKIISCF 82
Cdd:TIGR00099   1 LIFI-DLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYkevKNILK-ELGLDTPFITANGAAVIDDQGEILYKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423   83 AFSRQELKMLRSLIKRNRHNITYAfssssfssGYTMLFLNeKNPQAILKWFGISIGRVAPD--------ETNFLKEMEQG 154
Cdd:TIGR00099  79 PLDLDLVEEILNFLKKHGLDVILY--------GDDSIYAS-KNDPEYFTIFKKFLGEPKLEvvdiqylpDDILKILLLFL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423  155 SHrlslvGDIKDIPPELNHTTND------SSGVHFHEFTRRGVNKGKGVEILAKYLGIPRRRVIIAGNDVNDLSMFQLnF 228
Cdd:TIGR00099 150 DP-----EDLDLLIEALNKLELEenvsvvSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEA-A 223

                         250       260
                  ....*....|....*....|
gi 818607423  229 GVRIAVGpNCPEEIQRRATH 248
Cdd:TIGR00099 224 GYGVAMG-NADEELKALADY 242
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 11-248 1.25e-28

haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes.


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 109.25  E-value: 1.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423   11 DLDGTILGGDHRILEPTHKAILNLQDLGILFSVATGRSSTCIEQCA--LPVNCPGVFDNGGAICQSDGKIISCFAFSRQE 88
Cdd:pfam08282   4 DLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIkeLGLDDPVICYNGALIYDENGKILYSNPISKEA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423   89 LKMLRSLIKRNRHNITYAFSSSsfssgytmLFLNEKNPQAILKWFGISIGRVAPDETNFLKEMEQGSHRLSLVGD----- 163
Cdd:pfam08282  84 VKEIIEYLKENNLEILLYTDDG--------VYILNDNELEKILKELNYTKSFVPEIDDFELLEDEDINKILILLDeedld 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423  164 --IKDIPPELNHTTN--DSSGVHFhEFTRRGVNKGKGVEILAKYLGIPRRRVIIAGNDVNDLSMFQLnFGVRIAVGpNCP 239
Cdd:pfam08282 156 elEKELKELFGSLITitSSGPGYL-EIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEA-AGLGVAMG-NAS 232


                  ....*....
gi 818607423  240 EEIQRRATH 248
Cdd:pfam08282 233 PEVKAAADY 241
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 7-248 2.15e-26

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-phosphate. Members of this family belong 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: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 103.44  E-value: 2.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423   7 LFLADLDGTILGGDHRILEPTHKAILNLQDLGILFSVATGRS----STCIEQcaLPVNCPGVFDNGGAICQSDGKIISCF 82
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPlrgaQPYLEE--LGLDSPLITFNGALVYDPTGKEILER 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423  83 AFSRQELKMLRSLIKRNRHNITYAFSSSSFSSGYTmlflnEKNPQAILKWFGISIGRVAPDETNFLKEMEQGSHRLSLVG 162
Cdd:cd07516   79 LISKEDVKELEEFLRKLGIGINIYTNDDWADTIYE-----ENEDDEIIKPAEILDDLLLPPDEDITKILFVGEDEELDEL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423 163 DIKDIPPELNHTTNDSSGVHFHEFTRRGVNKGKGVEILAKYLGIPRRRVIIAGNDVNDLSMFQLnFGVRIAVGpNCPEEI 242
Cdd:cd07516  154 IAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEY-AGLGVAMG-NAIDEV 231


                 ....*.
gi 818607423 243 QRRATH 248
Cdd:cd07516  232 KEAADY 237
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 7-248 6.96e-26

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 100.60  E-value: 6.96e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423   7 LFLADLDGTILGGDHRILEPTHKAILNLQDLGILFSVATGRSSTCIEQCA--LPVNCPGVFDNGGAICQSDGKIISCFAF 84
Cdd:COG0561    4 LIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLeeLGLDDPLITSNGALIYDPDGEVLYERPL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423  85 SRQELKMLRSLIKRnrhnityafssssfssgytmlflneknpqailkwFGISIGRVApdetnflkemeqgshrlslvgdi 164
Cdd:COG0561   84 DPEDVREILELLRE----------------------------------HGLHLQVVV----------------------- 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423 165 kdippelnhttndSSGVHFHEFTRRGVNKGKGVEILAKYLGIPRRRVIIAGNDVNDLSMFQLNfGVRIAVGpNCPEEIQR 244
Cdd:COG0561  107 -------------RSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAA-GLGVAMG-NAPPEVKA 171


                 ....
gi 818607423 245 RATH 248
Cdd:COG0561  172 AADY 175
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 6-250 1.96e-14

phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. Members of this family belong 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: 319819 [Multi-domain]  Cd Length: 213  Bit Score: 70.33  E-value: 1.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423   6 ILFLaDLDGTILGGDHRILEPTHKAILNLQDLGILFSVATGRSSTCIEQCALPVNCPGVFDNGGAICQSDGKIISCFAFS 85
Cdd:cd07517    2 IVFF-DIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGIDSYVSYNGQYVFFEGEVIYKNPLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423  86 RQELKMLRSLIKRNRHNITYafssssfssgYTMLFLneknpqailkwfgisigrvapdetnFLKEMEqgshrlslvgDIK 165
Cdd:cd07517   81 QELVERLTEFAKEQGHPVSF----------YGQLLL-------------------------FEDEEE----------EQK 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423 166 DIP--PELnhttndsSGVHFHEF----TRRGVNKGKGVEILAKYLGIPRRRVIIAGNDVNDLSMFQLnFGVRIAVGpNCP 239
Cdd:cd07517  116 YEElrPEL-------RFVRWHPLstdvIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEA-VGIGIAMG-NAH 186

                        250
                 ....*....|.
gi 818607423 240 EEIQRRAThYV 250
Cdd:cd07517  187 EELKEIAD-YV 196
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 6-246 9.55e-14

phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be phosphoglycolate phosphatases, is most closely related to the sucrose-phosphate phosphatases from plants and cyanobacteria (TIGR01485). Together, these two models comprise a subfamily model (TIGR01482). TIGR01482, in turn, is a member of the IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases.


Pssm-ID: 273652 [Multi-domain]  Cd Length: 215  Bit Score: 68.23  E-value: 9.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423    6 ILFLADLDGTILGGDHRILEPTHKAILNLQDLGILFSVATGRSSTCIEQCA--LPVNCPGVFDNGGAICQSDGKIIscfa 83
Cdd:TIGR01487   2 KLVAIDIDGTLTDPNRMISERAIEAIRKAEKKGIPVSLVTGNTVPFARALAvlIGTSGPVVAENGGVIFYNKEDIF---- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423   84 FSRQElkmlRSLIKRNRHNITYAFSSssfssgytmlfLNEKNPQAILKWFGISIgrvapdETNFLKEMEQGShRLSLVgd 163
Cdd:TIGR01487  78 LANME----EEWFLDEEKKKRFPRDR-----------LSNEYPRASLVIMREGK------DVDEVREIIKER-GLNLV-- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423  164 ikdippelnhttndSSGVHFHeFTRRGVNKGKGVEILAKYLGIPRRRVIIAGNDVNDLSMFQLnFGVRIAVGpNCPEEIQ 243
Cdd:TIGR01487 134 --------------ASGFAIH-IMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRV-VGFKVAVA-NADDQLK 196


                  ...
gi 818607423  244 RRA 246
Cdd:TIGR01487 197 EIA 199
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 10-254 1.34e-12

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 65.38  E-value: 1.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423  10 ADLDGTILGGDHRILEPTHKAILNLQDLGILFSVATGRSSTCIEQCA--LPVNCPGVFDNGGAIC-QSDGKIIscFAFSR 86
Cdd:PRK01158   8 IDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGNVLCFARAAAklIGTSGPVIAENGGVISvGFDGKRI--FLGDI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423  87 QELKMLRSLIKrNRHnityafssSSFSSGYTML-FLNEKNPQAILKWFGISIGRvapdetnflKEMEQGSHRLSLVgdik 165
Cdd:PRK01158  86 EECEKAYSELK-KRF--------PEASTSLTKLdPDYRKTEVALRRTVPVEEVR---------ELLEELGLDLEIV---- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423 166 dippelnhttndSSGVHFHeFTRRGVNKGKGVEILAKYLGIPRRRVIIAGNDVNDLSMFQLNfGVRIAVGpNCPEEIqRR 245
Cdd:PRK01158 144 ------------DSGFAIH-IKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVA-GFGVAVA-NADEEL-KE 207


                 ....*....
gi 818607423 246 ATHYVETME 254
Cdd:PRK01158 208 AADYVTEKS 216
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 11-247 1.08e-11

sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP equivalog model (TIGR01485), encompassing plants and cyanobacteria, as well as those archaeal sequences which are the closest relatives (TIGR01487). It remains to be shown whether these archaeal sequences catalyze the same reaction as SPP.


Pssm-ID: 273650 [Multi-domain]  Cd Length: 225  Bit Score: 62.87  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423   11 DLDGTILGgDHRILEptHKAILNL---QDLGILFSVATGRSSTCIEQCA--LPVNCPGVFDNGGAICQSDGKIISCFAFs 85
Cdd:TIGR01482   4 DIDGTLTD-PNRAIN--ESALEAIrkaESKGIPVVLVTGNSVQFARALAklIGTPDPVIAENGGEISYNEGLDDIFLAY- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423   86 rqelkMLRSLIKRNRHNITYafssssfssgytmlflneknPQAILKwfgisigrvapdetnFLKEMEQGSHRLSLVGDIK 165
Cdd:TIGR01482  80 -----LEEEWFLDIVIAKTF--------------------PFSRLK---------------VQYPRRASLVKMRYGIDVD 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423  166 DIPPELNHTT----NDSSGVHFHeFTRRGVNKGKGVEILAKYLGIPRRRVIIAGNDVNDLSMFQL-NFGVRIAvgpNCPE 240
Cdd:TIGR01482 120 TVREIIKELGlnlvAVDSGFDIH-ILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVpGFGVAVA---NAQP 195


                  ....*..
gi 818607423  241 EIQRRAT 247
Cdd:TIGR01482 196 ELKEWAD 202
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 7-234 1.08e-10

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: 59.70  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423    7 LFLADLDGTILG-GDHRILEPTHKAILNLQDLGILFSVATGRSSTCIEQCA--LPVNCPGVFDNGGAICQSDGKIiscFA 83
Cdd:TIGR01484   1 LLFFDLDGTLLDpNAHELSPETIEALERLREAGVKVVIVTGRSLAEIKELLkqLNLPLPLIAENGALIFYPGEIL---YI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423   84 FSRQELKmlrsLIKRNRHNITYAfssssfssgyTMLFLNEKNPQAILKW--FGISIG-RVAPDETNFLKEMEqgsHRLSL 160
Cdd:TIGR01484  78 EPSDVFE----EILGIKFEEIGA----------ELKSLSEHYVGTFIEDkaIAVAIHyVGAELGQELDSKMR---ERLEK 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818607423  161 vgdIKDIPPELNHTTndsSGVHFHEFTRRGVNKGKGVEILAKYLGIPRRRVIIAGNDVNDLSMFQLnFGVRIAV 234
Cdd:TIGR01484 141 ---IGRNDLELEAIY---SGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEV-AGLAVAV 207
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 190-248 6.28e-09

phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), and Pyrococcus horikoshii PH1421, a magnesium-dependent phosphatase; belongs to the haloacid dehalogenase-like superfamily; Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PGPase) catalyzes the magnesium-dependent dephosphorylation of phosphoglycolate. This family also includes Pyrococcus horikoshii OT3 PH1421, a magnesium-dependent phosphatase. 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: 319816 [Multi-domain]  Cd Length: 139  Bit Score: 53.36  E-value: 6.28e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 818607423 190 GVNKGKGVEILAKYLGIPRRRVIIAGNDVNDLSMFQLNfGVRIAVGpNCPEEIQRRATH 248
Cdd:cd07514   65 GVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVA-GFKVAVA-NADEELKEAADY 121
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 7-248 1.48e-08

Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli YbiV can act as both a sugar phosphatase and as a phosphotransferase. Members of this family belong 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: 319820 [Multi-domain]  Cd Length: 184  Bit Score: 52.97  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423   7 LFLADLDGTILGGDHRILEPTHKAILN-LQDLGILFSVATGRS-STCIEqcalpvNCPGVFDNggaicqsdgkiiscfaf 84
Cdd:cd07518    2 LIATDMDGTFLNDDKTYDHERFFAILDqLLKKGIKFVVASGRQyYQLIS------FFPEIKDE----------------- 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423  85 srqelkmlrslikrnrhnityafssssfssgytMLFLNEKNpqAILkWFGISIgrVAPDETnflkemeqgshrlslvgdI 164
Cdd:cd07518   59 ---------------------------------MSFVAENG--AVV-YFKFTL--NVPDEA------------------A 82

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423 165 KDIPPELNHTTND-----SSGVHFHEFTRRGVNKGKGVEILAKYLGIPRRRVIIAGNDVNDLSMFQlNFGVRIAVGpNCP 239
Cdd:cd07518   83 PDIIDELNQKFGGilravTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLK-YAGYSYAME-NAP 160


                 ....*....
gi 818607423 240 EEIQRRATH 248
Cdd:cd07518  161 EEVKAAAKY 169
PRK10976 PRK10976
putative hydrolase; Provisional
 10-223 5.12e-08

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 52.74  E-value: 5.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423  10 ADLDGTILGGDHRiLEPTHKAILN-LQDLGILFSVATGRSSTCIEQC--ALPVNCPGVFDNGGAICQSDGKIISCFAFSR 86
Cdd:PRK10976   7 SDLDGTLLSPDHT-LSPYAKETLKlLTARGIHFVFATGRHHVDVGQIrdNLEIKSYMITSNGARVHDTDGNLIFSHNLDR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423  87 QELKMLRSLIKRNRHNITYafssssfssgytmLFLNEknpqailKWFgisIGRVAPDETNFLKEME-------------Q 153
Cdd:PRK10976  86 DIASDLFGVVHDNPDIITN-------------VYRDD-------EWF---MNRHRPEEMRFFKEAVfkyqlyepgllepD 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818607423 154 GSHRLSLVGDIKD--IPPE--LNHTTNDSSGVHFH-----EFTRRGVNKGKGVEILAKYLGIPRRRVIIAGNDVNDLSM 223
Cdd:PRK10976 143 GVSKVFFTCDSHEklLPLEqaINARWGDRVNVSFStltclEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEM 221
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 164-255 4.28e-07

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 50.08  E-value: 4.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423 164 IKDIPPELNHT-TNDSSGVHFHEFTRRGVNKGKGVEILAKYLGIPRRRVIIAGNDVNDLSMFQLNfGVRIAVGpNCPEEI 242
Cdd:PRK10513 167 IARIPAEVKERyTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYA-GVGVAMG-NAIPSV 244

                         90
                 ....*....|...
gi 818607423 243 QRRATHYVETMEE 255
Cdd:PRK10513 245 KEVAQFVTKSNLE 257
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
 185-236 3.59e-06

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: 46.90  E-value: 3.59e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 818607423 185 EFTRRGVNKGKGVEILAKYLGIPRRRVIIAGNDVNDLSMFQ-LN----FGVRIAVGP 236
Cdd:cd01627  157 EVRPVGVNKGEAVERILGELPFAGDFVLCAGDDVTDEDAFRaLNgeggFSVKVGEGP 213
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 7-243 1.71e-04

Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate phosphohydrolase proteins found in plants and cyanobacteria. Sucrose-6(F)-phosphate phosphohydrolase catalyzes the final step in the pathway of sucrose biosynthesis.


Pssm-ID: 428314 [Multi-domain]  Cd Length: 246  Bit Score: 41.87  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423    7 LFLADLDGTILGGDHRILEpTHKAILNLQDLGILFSVATGRS----STCIEQCALPVncPGVfdnggAICqSDGKIIscf 82
Cdd:pfam05116   4 LLVSDLDNTLVDGDNEALA-RLNQLLEAYRPDVGLVFATGRSldsaKELLKEKPLPT--PDY-----LIT-SVGTEI--- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423   83 afsrqelkmlrslikrnrhnitYAFSSSSFSSGYTMLfLNEK-NPQAILkwfgisigrvapDETNFLKEM------EQGS 155
Cdd:pfam05116  72 ----------------------YYGPSLVPDQSWQEH-LDYHwDRQAVV------------EALAKFPGLtlqpeeEQRP 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423  156 HRLS-------LVGDIKDIPPELNHTTND-----SSGVHFHEFTRRGvNKGKGVEILAKYLGIPRRRVIIAGNDVNDLSM 223
Cdd:pfam05116 117 HKVSyfldpeaAAAVLAELEQLLRKRGLDvkviySSGRDLDILPLRA-SKGEALRYLALKLGLPLENTLVCGDSGNDEEL 195

                         250       260
                  ....*....|....*....|.
gi 818607423  224 FQLNF-GVriAVGPNCPEEIQ 243
Cdd:pfam05116 196 FIGGTrGV--VVGNAQPELLQ 214
PLN02887 PLN02887
hydrolase family protein
 185-235 1.53e-03

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 39.86  E-value: 1.53e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 818607423 185 EFTRRGVNKGKGVEILAKYLGIPRRRVIIAGNDVNDLSMFQL-NFGVRIAVG 235
Cdd:PLN02887 500 EIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGDGENDIEMLQLaSLGVALSNG 551
PRK15126 PRK15126
HMP-PP phosphatase;
11-47 1.89e-03

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 38.91  E-value: 1.89e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 818607423  11 DLDGTILGGDHRILEPTHKAILNLQDLGILFSVATGR 47
Cdd:PRK15126   8 DMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGR 44
PRK14502 PRK14502
bifunctional mannosyl-3-phosphoglycerate synthase/mannosyl-3 phosphoglycerate phosphatase; ...
 10-263 2.10e-03

bifunctional mannosyl-3-phosphoglycerate synthase/mannosyl-3 phosphoglycerate phosphatase; Provisional


Pssm-ID: 184713 [Multi-domain]  Cd Length: 694  Bit Score: 39.14  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423  10 ADLDGTILGGDHRILEPTHKAILNLQD--LGILFSVATGRSSTCIEQCALPVNCPGVFDNGGAICQSDGKIISCFAFSR- 86
Cdd:PRK14502 421 TDLDGTLLNPLTYSYSTALDALRLLKDkeLPLVFCSAKTMGEQDLYRNELGIKDPFITENGGAIFIPKDYFRLPFAYDRv 500

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423  87 ------QELKM----LRSLIKRNRHNITyafssssfssgyTMLFLNEKNPQAILKWFG-ISIGRVAPDETNFLKEMEQGS 155
Cdd:PRK14502 501 agnylvIELGMaykdIRHILKKALAEAC------------TEIENSEKAGNIFITSFGdMSVEDVSRLTDLNLKQAELAK 568

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423 156 HR-----LSLVGDIKDIPPELNHTTND----SSGVHFHEFTrRGVNKGKGVEILAKYLGIPRRRVII--AGNDVNDLSMF 224
Cdd:PRK14502 569 QReysetVHIEGDKRSTNIVLNHIQQSgleySFGGRFYEVT-GGNDKGKAIKILNELFRLNFGNIHTfgLGDSENDYSML 647

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 818607423 225 QlnfgvriAVgpNCPEEIQRRATHYVETMEELPLILRGL 263
Cdd:PRK14502 648 E-------TV--DSPILVQRPGNKWHKMRLRNPSYVKGV 677
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 193-259 2.58e-03

phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate. It catalyzes the last of three steps in the biosynthesis of serine from D-3-phosphoglycerate. Note that this enzyme acts on free phosphoserine, not on phosphoserine residues of phosphoproteins. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273022 [Multi-domain]  Cd Length: 219  Bit Score: 38.11  E-value: 2.58e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423  193 KGKGVEILAKYLGIPRRRVIIAGNDVNDLSMFQlnfGVRIAVGPNCPEEIQRRATHYVET---MEELPLI 259
Cdd:TIGR00338 153 KGKTLLILLRKEGISPENTVAVGDGANDLSMIK---AAGLGIAFNAKPKLQQKADICINKkdlTDILPLL 219
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 147-234 4.08e-03

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All 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. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 36.22  E-value: 4.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818607423 147 FLKEMEQGSHRLSLV--GDIKDIPPELNHTTNDSS--GVHFHEFTRRGVNKGKGVEILAKYLGIPRRRVIIAGNDVNDLS 222
Cdd:cd01427   15 LLKRLRAAGIKLAIVtnRSREALRALLEKLGLGDLfdGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSENDIE 94

                         90
                 ....*....|..
gi 818607423 223 MFQLNFGVRIAV 234
Cdd:cd01427   95 AARAAGGRTVAV 106
 
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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