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Conserved domains on  [gi|727167864|ref|WP_033637176|]
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MULTISPECIES: fructose-1-phosphate/6-phosphogluconate phosphatase [Serratia]

Protein Classification

fructose-1-phosphate/6-phosphogluconate phosphatase( domain architecture ID 10793455)

fructose-1-phosphate/6-phosphogluconate phosphatase catalyzes strongly the dephosphorylation of fructose-1-phosphate (Fru1P) and slightly the dephosphorylation of 6-phosphogluconate (6P-Glu)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
1-188 2.48e-147

fructose-1-phosphate/6-phosphogluconate phosphatase;


:

Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 406.00  E-value: 2.48e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   1 MYDRYQGLIFDMDGTILDTEPTHRKAWREVLSRYGMTFDEAAMVALSGSPTWRIAQAIIASHQADLDPHHLAAEKTRAVE 80
Cdd:PRK10725   1 MYDRYAGLIFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVALNGSPTWRIAQAIIELNQADLDPHALAREKTEAVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  81 AMLLDSVRPLPLIEVVKSYHGRRPMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPPE 160
Cdd:PRK10725  81 SMLLDSVEPLPLIEVVKAWHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADDVQHHKPAPDTFLRCAQLMGVQPT 160

                        170       180
                 ....*....|....*....|....*...
gi 727167864 161 KCVVFEDADFGIQAAKSAGMAVVDVRTL 188
Cdd:PRK10725 161 QCVVFEDADFGIQAARAAGMDAVDVRLL 188
 
Name Accession Description Interval E-value
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
1-188 2.48e-147

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 406.00  E-value: 2.48e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   1 MYDRYQGLIFDMDGTILDTEPTHRKAWREVLSRYGMTFDEAAMVALSGSPTWRIAQAIIASHQADLDPHHLAAEKTRAVE 80
Cdd:PRK10725   1 MYDRYAGLIFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVALNGSPTWRIAQAIIELNQADLDPHALAREKTEAVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  81 AMLLDSVRPLPLIEVVKSYHGRRPMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPPE 160
Cdd:PRK10725  81 SMLLDSVEPLPLIEVVKAWHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADDVQHHKPAPDTFLRCAQLMGVQPT 160

                        170       180
                 ....*....|....*....|....*...
gi 727167864 161 KCVVFEDADFGIQAAKSAGMAVVDVRTL 188
Cdd:PRK10725 161 QCVVFEDADFGIQAARAAGMDAVDVRLL 188
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 5-185 1.55e-75

beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509).


Pssm-ID: 213673 [Multi-domain]  Cd Length: 185  Bit Score: 224.53  E-value: 1.55e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864    5 YQGLIFDMDGTILDTEPTHRKAWREVLSRYGMTFDEAAMVALSGSPTWRIAQAIIASHQADLDP---HHLAAEKTRAVEA 81
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDGLSLeeiHQLAERKNELYRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   82 ML-LDSVRPLPLIEVVKSYHGRRPMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPPE 160
Cdd:TIGR02009  81 LLrLTGVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRDYFDAIVDASEVKNGKPHPETFLLAAELLGVPPN 160

                         170       180
                  ....*....|....*....|....*
gi 727167864  161 KCVVFEDADFGIQAAKSAGMAVVDV 185
Cdd:TIGR02009 161 ECIVFEDALAGVQAARAAGMFAVAV 185
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
4-187 1.64e-68

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 207.37  E-value: 1.64e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   4 RYQGLIFDMDGTILDTEPTHRKAWREVLSRYGMTFDEAAMVALSGSPTWRIAQAIIASHQADLDPHHLAAEKTRAVEAML 83
Cdd:COG0637    1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYRELL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  84 -LDSVRPLP-LIEVVKSYHGRR-PMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPPE 160
Cdd:COG0637   81 aEEGLPLIPgVVELLEALKEAGiKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERLGVDPE 160

                        170       180
                 ....*....|....*....|....*..
gi 727167864 161 KCVVFEDADFGIQAAKSAGMAVVDVRT 187
Cdd:COG0637  161 ECVVFEDSPAGIRAAKAAGMRVVGVPD 187
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 7-187 4.70e-45

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: 145.84  E-value: 4.70e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   7 GLIFDMDGTILDTEPTHRKAWRevlsrygmtfdeaamvalsgsptwriaqaiiashqadldphhLAAEKTRAVEAMLLDS 86
Cdd:cd07505    1 AVIFDMDGVLIDTEPLHRQAWQ------------------------------------------LLERKNALLLELIASE 38

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  87 VRPL--PLIEVVKSYHGRR-PMAVGTGSEHR-MAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPPEKC 162
Cdd:cd07505   39 GLKLkpGVVELLDALKAAGiPVAVATSSSRRnVELLLLELGLLRGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERC 118

                        170       180
                 ....*....|....*....|....*
gi 727167864 163 VVFEDADFGIQAAKSAGMAVVDVRT 187
Cdd:cd07505  119 LVFEDSLAGIEAAKAAGMTVVAVPD 143
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
8-185 1.30e-32

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 114.99  E-value: 1.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864    8 LIFDMDGTILDTEPTHRKAWREVLSRYGM-TFDEAAMVALSGSPTWRIAQAIIASHQADLDPhhlaAEKTRAVEAMLLD- 85
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYgELSEEEILKFIGLPLREIFRYLGVSEDEEEKI----EFYLRKYNEELHDk 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   86 SVRPLP-LIEVVKS-YHGRRPMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPPEKCV 163
Cdd:pfam13419  77 LVKPYPgIKELLEElKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVI 156

                         170       180
                  ....*....|....*....|..
gi 727167864  164 VFEDADFGIQAAKSAGMAVVDV 185
Cdd:pfam13419 157 YVGDSPRDIEAAKNAGIKVIAV 178
 
Name Accession Description Interval E-value
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
1-188 2.48e-147

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 406.00  E-value: 2.48e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   1 MYDRYQGLIFDMDGTILDTEPTHRKAWREVLSRYGMTFDEAAMVALSGSPTWRIAQAIIASHQADLDPHHLAAEKTRAVE 80
Cdd:PRK10725   1 MYDRYAGLIFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVALNGSPTWRIAQAIIELNQADLDPHALAREKTEAVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  81 AMLLDSVRPLPLIEVVKSYHGRRPMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPPE 160
Cdd:PRK10725  81 SMLLDSVEPLPLIEVVKAWHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADDVQHHKPAPDTFLRCAQLMGVQPT 160

                        170       180
                 ....*....|....*....|....*...
gi 727167864 161 KCVVFEDADFGIQAAKSAGMAVVDVRTL 188
Cdd:PRK10725 161 QCVVFEDADFGIQAARAAGMDAVDVRLL 188
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 5-185 1.55e-75

beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509).


Pssm-ID: 213673 [Multi-domain]  Cd Length: 185  Bit Score: 224.53  E-value: 1.55e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864    5 YQGLIFDMDGTILDTEPTHRKAWREVLSRYGMTFDEAAMVALSGSPTWRIAQAIIASHQADLDP---HHLAAEKTRAVEA 81
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDGLSLeeiHQLAERKNELYRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   82 ML-LDSVRPLPLIEVVKSYHGRRPMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPPE 160
Cdd:TIGR02009  81 LLrLTGVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRDYFDAIVDASEVKNGKPHPETFLLAAELLGVPPN 160

                         170       180
                  ....*....|....*....|....*
gi 727167864  161 KCVVFEDADFGIQAAKSAGMAVVDV 185
Cdd:TIGR02009 161 ECIVFEDALAGVQAARAAGMFAVAV 185
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
4-187 1.64e-68

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 207.37  E-value: 1.64e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   4 RYQGLIFDMDGTILDTEPTHRKAWREVLSRYGMTFDEAAMVALSGSPTWRIAQAIIASHQADLDPHHLAAEKTRAVEAML 83
Cdd:COG0637    1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYRELL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  84 -LDSVRPLP-LIEVVKSYHGRR-PMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPPE 160
Cdd:COG0637   81 aEEGLPLIPgVVELLEALKEAGiKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERLGVDPE 160

                        170       180
                 ....*....|....*....|....*..
gi 727167864 161 KCVVFEDADFGIQAAKSAGMAVVDVRT 187
Cdd:COG0637  161 ECVVFEDSPAGIRAAKAAGMRVVGVPD 187
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 7-187 4.70e-45

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: 145.84  E-value: 4.70e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   7 GLIFDMDGTILDTEPTHRKAWRevlsrygmtfdeaamvalsgsptwriaqaiiashqadldphhLAAEKTRAVEAMLLDS 86
Cdd:cd07505    1 AVIFDMDGVLIDTEPLHRQAWQ------------------------------------------LLERKNALLLELIASE 38

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  87 VRPL--PLIEVVKSYHGRR-PMAVGTGSEHR-MAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPPEKC 162
Cdd:cd07505   39 GLKLkpGVVELLDALKAAGiPVAVATSSSRRnVELLLLELGLLRGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERC 118

                        170       180
                 ....*....|....*....|....*
gi 727167864 163 VVFEDADFGIQAAKSAGMAVVDVRT 187
Cdd:cd07505  119 LVFEDSLAGIEAAKAAGMTVVAVPD 143
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 8-186 5.88e-41

uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized Bacillus subtilis YhcW; This subfamily includes the uncharacterized Bacillus subtilis YhcW. It belongs to the beta-phosphoglucomutase-like family whose other 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. 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: 319859 [Multi-domain]  Cd Length: 169  Bit Score: 136.23  E-value: 5.88e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   8 LIFDMDGTILDTEPTHRKAWREVLSRYGmtfdeaamvalsgsptwriaqaiiashqadldpHHLAAEktraveamLLDSV 87
Cdd:cd16423    2 VIFDFDGVIVDTEPLWYEAWQELLNERR---------------------------------NELIKR--------QFSEK 40

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  88 RPLPLIEVVKSY----HGRR-PMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPPEKC 162
Cdd:cd16423   41 TDLPPIEGVKELleflKEKGiKLAVASSSPRRWIEPHLERLGLLDYFEVIVTGDDVEKSKPDPDLYLEAAERLGVNPEEC 120

                        170       180
                 ....*....|....*....|....
gi 727167864 163 VVFEDADFGIQAAKSAGMAVVDVR 186
Cdd:cd16423  121 VVIEDSRNGVLAAKAAGMKCVGVP 144
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
5-183 3.42e-37

Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 127.74  E-value: 3.42e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   5 YQGLIFDMDGTILDTEPTHRKAWREVLSRYGM-TFDEAAMVALSGSPTWRIAQAIIASHQADLDPHHLAAEKtRAVEAML 83
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLpPLDLEELRALIGLGLRELLRRLLGEDPDEELEELLARFR-ELYEEEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  84 LDSVRPLPLI-EVVKSYHGRR-PMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPPEK 161
Cdd:COG0546   80 LDETRLFPGVrELLEALKARGiKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLDPEE 159

                        170       180
                 ....*....|....*....|..
gi 727167864 162 CVVFEDADFGIQAAKSAGMAVV 183
Cdd:COG0546  160 VLMVGDSPHDIEAARAAGVPFI 181
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 8-185 2.17e-34

subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and Gpp2; This subfamily includes Arabidopsis thaliana AtGpp1 and AtGpp2, and Drosophila GS1-like protein (Dmel\Gs1l) of unknown function. AtGpp1 and AtGpp2 are constitutively expressed in all the Arabidopsis tissues and unaffected under abiotic stress. Overexpression of AtGpp2 in transgenic Arabidopsis plants increases the specific DL-glycerol-3-phosphatase activity and improves the plants tolerance to salt, osmotic and oxidative stress. It belongs to the beta-phosphoglucomutase-like family whose other 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. 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: 319831 [Multi-domain]  Cd Length: 192  Bit Score: 120.14  E-value: 2.17e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   8 LIFDMDGTILDTEPTHRKAWREVLSRYGMTFDEAAMVALSGSPTWRIAQAIIASHQADLDPHHLAAEKTRAVEAMLLDSV 87
Cdd:cd07529    4 CIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLEEEFDEQQEALAELFMGTA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  88 RPLPLIE-VVKSYHGRR-PMAVGTGSEHRMAEM-LLRHLGLFNCFDAIVGADD---VQRHKPEPDTFLRCAELIGVP--- 158
Cdd:cd07529   84 KLMPGAErLLRHLHAHNiPIALATSSCTRHFKLkTSRHKELFSLFHHVVTGDDpevKGRGKPAPDIFLVAAKRFNEPpkd 163

                        170       180
                 ....*....|....*....|....*..
gi 727167864 159 PEKCVVFEDADFGIQAAKSAGMAVVDV 185
Cdd:cd07529  164 PSKCLVFEDSPNGVKAAKAAGMQVVMV 190
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 7-187 2.63e-33

subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p); This subfamily includes Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). GPP1p and GPP2p are involved in glycerol biosynthesis, GPP1 is induced in response to both anaerobic and hyperosmotic stress, GPP2 is induced in response to hyperosmotic or oxidative stress, and during diauxic shift; overexpression of DOG1 or DOG2 confers 2-deoxyglucose resistance. These belong to the beta-phosphoglucomutase-like family whose other 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), 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: 319829 [Multi-domain]  Cd Length: 205  Bit Score: 117.44  E-value: 2.63e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   7 GLIFDMDGTILDTEPTHRKAWREVLSRYGMTFDEAaMVALSGsptWRIAQAIIASHQADLDPHHLAAEKTRAVEAMLlDS 86
Cdd:cd07527    1 ALLFDMDGTLVDSTPAVERAWHKWAKEHGVDPEEV-LKVSHG---RRAIDVIRKLAPDDADIELVLALETEEPESYP-EG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  87 VRPLP----LIEVVKSyHGRRPMAVgTGSEHRMAEMLLRHLGLFNCfDAIVGADDVQRHKPEPDTFLRCAELIGVPPEKC 162
Cdd:cd07527   76 VIAIPgavdLLASLPA-AGDRWAIV-TSGTRALAEARLEAAGLPHP-EVLVTADDVKNGKPDPEPYLLGAKLLGLDPSDC 152

                        170       180
                 ....*....|....*....|....*
gi 727167864 163 VVFEDADFGIQAAKSAGMAVVDVRT 187
Cdd:cd07527  153 VVFEDAPAGIKAGKAAGARVVAVNT 177
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
8-185 1.30e-32

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 114.99  E-value: 1.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864    8 LIFDMDGTILDTEPTHRKAWREVLSRYGM-TFDEAAMVALSGSPTWRIAQAIIASHQADLDPhhlaAEKTRAVEAMLLD- 85
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYgELSEEEILKFIGLPLREIFRYLGVSEDEEEKI----EFYLRKYNEELHDk 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   86 SVRPLP-LIEVVKS-YHGRRPMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPPEKCV 163
Cdd:pfam13419  77 LVKPYPgIKELLEElKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVI 156

                         170       180
                  ....*....|....*....|..
gi 727167864  164 VFEDADFGIQAAKSAGMAVVDV 185
Cdd:pfam13419 157 YVGDSPRDIEAAKNAGIKVIAV 178
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 5-179 5.04e-28

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: 103.82  E-value: 5.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864    5 YQGLIFDMDGTILDTEPTHRKAWREVLSR-------------YGMTFDEAAMVALSGSPTWRIAQAIIASHQADLDPHHL 71
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEhplakaivaaaedLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   72 AAEKTRAVEAMLL-DSVRPLP-LIEVVKSYHGRR-PMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTF 148
Cdd:pfam00702  81 TVVLVELLGVIALaDELKLYPgAAEALKALKERGiKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIY 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 727167864  149 LRCAELIGVPPEKCVVFEDADFGIQAAKSAG 179
Cdd:pfam00702 161 LAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 8-183 2.51e-26

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: 99.03  E-value: 2.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864    8 LIFDMDGTILDTEPTHrkaWREVLSRYGMTFDEAAMVALSGSPTWRIAQAIIASHQADLDPHHLAAEKTRAVEAML-LDS 86
Cdd:TIGR01509   2 ILFDLDGVLVDTEFAI---AKLINREELGLVPDELGVSAVGRLELALRRFKAQYGRTISPEDAQLLYKQLFYEQIEeEAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   87 VRPLP-LIEVVKSYHGR-RPMAVGTGSEHRMaEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPPEKCVV 164
Cdd:TIGR01509  79 LKPLPgVRALLEALRARgKKLALLTNSPRAH-KLVLALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLEPSECVF 157

                         170
                  ....*....|....*....
gi 727167864  165 FEDADFGIQAAKSAGMAVV 183
Cdd:TIGR01509 158 VDDSPAGIEAAKAAGMHTV 176
PLN02940 PLN02940
riboflavin kinase
 8-185 1.62e-25

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 101.06  E-value: 1.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   8 LIFDMDGTILDTEPTHRKAWREVLSRYGMTFDEAAMVALSGSPTWRIAQAIIASHQADLDPHHLAAEKTRAVEAmLLDSV 87
Cdd:PLN02940  14 VILDLDGTLLNTDGIVSDVLKAFLVKYGKQWDGREAQKIVGKTPLEAAATVVEDYGLPCSTDEFNSEITPLLSE-QWCNI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  88 RPLP----LIEVVKSyHGRrPMAVGTGSEHRMAEMLLR-HLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPPEKC 162
Cdd:PLN02940  93 KALPganrLIKHLKS-HGV-PMALASNSPRANIEAKIScHQGWKESFSVIVGGDEVEKGKPSPDIFLEAAKRLNVEPSNC 170

                        170       180
                 ....*....|....*....|...
gi 727167864 163 VVFEDADFGIQAAKSAGMAVVDV 185
Cdd:PLN02940 171 LVIEDSLPGVMAGKAAGMEVIAV 193
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 7-185 1.47e-24

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: 94.28  E-value: 1.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   7 GLIFDMDGTILDTEPTHRKAWRevlsrygmtfdeaamvalsgsptwriaqaiiasHQADLDphHLAAEKTR----AVEAM 82
Cdd:cd02598    1 GVIFDLDGVITDTAEYHYRAWK---------------------------------KLADKE--ELAARKNRiyveLIEEL 45

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  83 LLDSVRP--LPLIEVVKSYHgrrpMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPPE 160
Cdd:cd02598   46 TPVDVLPgiASLLVDLKAKG----IKIALASASKNAPKILEKLGLAEYFDAIVDGAVLAKGKPDPDIFLAAAEGLGLNPK 121

                        170       180
                 ....*....|....*....|....*
gi 727167864 161 KCVVFEDADFGIQAAKSAGMAVVDV 185
Cdd:cd02598  122 DCIGVEDAQAGIRAIKAAGFLVVGV 146
PLN02811 PLN02811
hydrolase
 12-185 2.04e-24

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 95.21  E-value: 2.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  12 MDGTILDTEPTHRKAWREVLSRYGMTFDEAAMVALSGSPTWRIAQAIIASHQAD--LDPHHLAAEKTRAVEAMLLDSVRp 89
Cdd:PLN02811   1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSdsLSPEDFLVEREAMLQDLFPTSDL- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  90 LPLIE-VVKSYHGRR-PMAVGTGSEHRMAEM-LLRHLGLFNCFDAIVGADD--VQRHKPEPDTFLRCA---ELIGVPPEK 161
Cdd:PLN02811  80 MPGAErLVRHLHAKGiPIAIATGSHKRHFDLkTQRHGELFSLMHHVVTGDDpeVKQGKPAPDIFLAAArrfEDGPVDPGK 159

                        170       180
                 ....*....|....*....|....
gi 727167864 162 CVVFEDADFGIQAAKSAGMAVVDV 185
Cdd:PLN02811 160 VLVFEDAPSGVEAAKNAGMSVVMV 183
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 5-183 7.77e-23

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 90.86  E-value: 7.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   5 YQGLIFDMDGTILDTEPTHRKAWREVLSRYGMTFDEAAMVAL---SGSPTWRIAQAIIASHQADLD------PHHLAAEK 75
Cdd:COG1011    1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAEAyraIEYALWRRYERGEITFAELLRrlleelGLDLAEEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  76 TRAVEAMLLDSVRPLP-LIEVVKSYHGR-RPMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAE 153
Cdd:COG1011   81 AEAFLAALPELVEPYPdALELLEALKARgYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIFELALE 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 727167864 154 LIGVPPEKCVVFED---ADfgIQAAKSAGMAVV 183
Cdd:COG1011  161 RLGVPPEEALFVGDspeTD--VAGARAAGMRTV 191
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 8-182 2.85e-22

subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli 6-phosphogluconate phosphatase YieH; This subfamily includes Escherichia coli YieH/HAD3 an 6-phosphogluconate phosphatase, which can hydrolyzed purines and pyrimidines as secondary substrates. It belongs to the beta-phosphoglucomutase-like family whose other 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. 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: 319828 [Multi-domain]  Cd Length: 141  Bit Score: 87.37  E-value: 2.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   8 LIFDMDGTILDTEPTHRKAWREVLSRYGMTFDEAAMvalsgsptwriaqaiiashqADLDPHHLAAEKTRAVEAmlldsv 87
Cdd:cd07526    3 VIFDCDGVLVDSEVIAARVLVEVLAELGARVLAAFE--------------------AELQPIPGAAAALSALTL------ 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  88 rplplievvksyhgrrPMAVGTGSEHRMAEMLLRHLGLFNCFDA-IVGADDVQRHKPEPDTFLRCAELIGVPPEKCVVFE 166
Cdd:cd07526   57 ----------------PFCVASNSSRERLTHSLGLAGLLAYFEGrIFSASDVGRGKPAPDLFLHAAAQMGVAPERCLVIE 120

                        170
                 ....*....|....*.
gi 727167864 167 DADFGIQAAKSAGMAV 182
Cdd:cd07526  121 DSPTGVRAALAAGMTV 136
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 8-183 2.72e-21

subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides xylulose-1,5-bisphosphate phosphatase CbbY; This family includes Rhodobacter sphaeroides and Arabidopsis thaliana xylulose-1,5-bisphosphate phosphatase CbbY which convert xylulose-1,5-bisphosphate (a potent inhibitor of Ribulose-1,5-bisphosphate carboxylase/oxygenase, Rubisco), to the non-inhibitory compound xylulose-5-phosphate. It belongs to the beta-phosphoglucomutase-like family whose other 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. 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: 319830 [Multi-domain]  Cd Length: 199  Bit Score: 86.28  E-value: 2.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   8 LIFDMDGTILDTEPTHRKAwrevlsrygmtFDEAAMVALSGSPTWRIAQAI-----------IASHQADLDPHH------ 70
Cdd:cd07528    2 LIFDVDGTLAETEELHRRA-----------FNNAFFAERGLDWYWDRELYGellrvgggkerIAAYFEKVGWPEsapkdl 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  71 ------LAAEKT-RAVEAMLLDSVRPLP----LIEVVKSyHGRRPMAVGTGSEHRMAEMLLRHLGL--FNCFDAIVGADD 137
Cdd:cd07528   71 keliadLHKAKTeRYAELIAAGLLPLRPgvarLIDEAKA-AGVRLAIATTTSPANVDALLSALLGPerRAIFDAIAAGDD 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 727167864 138 VQRHKPEPDTFLRCAELIGVPPEKCVVFEDADFGIQAAKSAGMAVV 183
Cdd:cd07528  150 VAEKKPDPDIYLLALERLGVSPSDCLAIEDSAIGLQAAKAAGLPCI 195
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 7-187 3.76e-21

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 89.91  E-value: 3.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864    7 GLIFDMDGTILDTEPTHRKAWREVLSRYGMTFDEAAMVALSGSPTWRIAQAIIASHQA-DLDPhhlAAEKTRAVEAMLLD 85
Cdd:PLN02919   77 AVLFDMDGVLCNSEEPSRRAAVDVFAEMGVEVTVEDFVPFMGTGEANFLGGVASVKGVkGFDP---DAAKKRFFEIYLEK 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   86 SVRP---------LPLIEVVKSyHGRRpMAVGTGSEHRMAEMLLRHLGL-FNCFDAIVGADDVQRHKPEPDTFLRCAELI 155
Cdd:PLN02919  154 YAKPnsgigfpgaLELITQCKN-KGLK-VAVASSADRIKVDANLAAAGLpLSMFDAIVSADAFENLKPAPDIFLAAAKIL 231

                         170       180       190
                  ....*....|....*....|....*....|..
gi 727167864  156 GVPPEKCVVFEDADFGIQAAKSAGMAVVDVRT 187
Cdd:PLN02919  232 GVPTSECVVIEDALAGVQAARAAGMRCIAVTT 263
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 5-185 5.42e-19

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. 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: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 80.40  E-value: 5.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   5 YQGLIFDMDGTILDTEPTHRKAWREVLSRYGMT-FDEAAMVALSGSPTWRIAQAIIASHQADLdphhlAAEKTRAVEAML 83
Cdd:cd02616    1 ITTILFDLDGTLIDTNELIIKSFNHTLKEYGLEgYTREEVLPFIGPPLRETFEKIDPDKLEDM-----VEEFRKYYREHN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  84 LDSVRPLPLI-EVVKSYHGR-RPMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPPEK 161
Cdd:cd02616   76 DDLTKEYPGVyETLARLKSQgIKLGVVTTKLRETALKGLKLLGLDKYFDVIVGGDDVTHHKPDPEPVLKALELLGAEPEE 155

                        170       180
                 ....*....|....*....|....
gi 727167864 162 CVVFEDADFGIQAAKSAGMAVVDV 185
Cdd:cd02616  156 ALMVGDSPHDILAGKNAGVKTVGV 179
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 6-187 1.12e-17

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 77.96  E-value: 1.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   6 QGLIFDMDGTILDTEPTHRKAWREVLSRY----GMTFDEAAMVA-LSGSPTWRIAQAIIAShqaDLDPH-HLAAEKTRAV 79
Cdd:PLN02770  23 EAVLFDVDGTLCDSDPLHYYAFREMLQEInfngGVPITEEFFVEnIAGKHNEDIALGLFPD---DLERGlKFTDDKEALF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  80 EAMLLDSVRPLPLIEVVKSY---HGRRPMAVgTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIG 156
Cdd:PLN02770 100 RKLASEQLKPLNGLYKLKKWiedRGLKRAAV-TNAPRENAELMISLLGLSDFFQAVIIGSECEHAKPHPDPYLKALEVLK 178

                        170       180       190
                 ....*....|....*....|....*....|.
gi 727167864 157 VPPEKCVVFEDADFGIQAAKSAGMAVVDVRT 187
Cdd:PLN02770 179 VSKDHTFVFEDSVSGIKAGVAAGMPVVGLTT 209
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 7-185 1.67e-17

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 77.76  E-value: 1.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   7 GLIFDMDGTILDTEPT-HRKAWREVLSRYGMTFDEAAMvaLSGSPTWRIAQAIIASHQADLDPHH---LAAEKTRAVEAM 82
Cdd:PLN03243  26 GVVLEWEGVIVEDDSElERKAWRALAEEEGKRPPPAFL--LKRAEGMKNEQAISEVLCWSRDFLQmkrLAIRKEDLYEYM 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  83 LLDSVRPLP----LIEVVKSYhgRRPMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVP 158
Cdd:PLN03243 104 QGGLYRLRPgsreFVQALKKH--EIPIAVASTRPRRYLERAIEAVGMEGFFSVVLAAEDVYRGKPDPEMFMYAAERLGFI 181

                        170       180
                 ....*....|....*....|....*..
gi 727167864 159 PEKCVVFEDADFGIQAAKSAGMAVVDV 185
Cdd:PLN03243 182 PERCIVFGNSNSSVEAAHDGCMKCVAV 208
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 8-183 8.52e-17

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 75.90  E-value: 8.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   8 LIFDMDGTILDTEPT-HRKAWREVLSRYGMT--------FDEAAMVA-----------LSGSPTWRIA---------QAI 58
Cdd:PLN02779  43 LLFDCDGVLVETERDgHRVAFNDAFKEFGLRpvewdvelYDELLNIGggkermtwyfnENGWPTSTIEkapkdeeerKEL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  59 IASHQADLDPHHLAAEKTRAVEAmlldsvRP--LPLIEVVKSyhGRRPMAVGTGSEHRMAEMLLRHL---GLFNCFDAIV 133
Cdd:PLN02779 123 VDSLHDRKTELFKELIESGALPL------RPgvLRLMDEALA--AGIKVAVCSTSNEKAVSKIVNTLlgpERAQGLDVFA 194

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 727167864 134 GaDDVQRHKPEPDTFLRCAELIGVPPEKCVVFEDADFGIQAAKSAGMAVV 183
Cdd:PLN02779 195 G-DDVPKKKPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAAKAAGMRCI 243
PRK10826 PRK10826
hexitol phosphatase HxpB;
9-180 2.04e-16

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 73.83  E-value: 2.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   9 IFDMDGTILDTEPTHRKAWREVLSRYGM--TFDEA----------AMVAL-------SGSPTWRIAQAIIashqadldph 69
Cdd:PRK10826  11 IFDMDGLLIDSEPLWDRAELDVMASLGVdiSRREElpdtlglridQVVDLwyarqpwNGPSRQEVVQRII---------- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  70 hlaaekTRAVEaMLLDSVRPLPLIEVVKSYHGRRPMAVG--TGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDT 147
Cdd:PRK10826  81 ------ARVIS-LIEETRPLLPGVREALALCKAQGLKIGlaSASPLHMLEAVLTMFDLRDYFDALASAEKLPYSKPHPEV 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 727167864 148 FLRCAELIGVPPEKCVVFEDADFGIQAAKSAGM 180
Cdd:PRK10826 154 YLNCAAKLGVDPLTCVALEDSFNGMIAAKAARM 186
PRK11587 PRK11587
putative phosphatase; Provisional
 4-185 2.85e-16

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 73.49  E-value: 2.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   4 RYQGLIFDMDGTILDTEPTHRKAWREVLSRYGMTFDEA--------AMVAL----SGSPTWRIAQAIIASHQadldphhL 71
Cdd:PRK11587   2 RCKGFLFDLDGTLVDSLPAVERAWSNWADRHGIAPDEVlnfihgkqAITSLrhfmAGASEAEIQAEFTRLEQ-------I 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  72 AAEKTRAVEAM-----LLDSVRPLPL-IEVVKSyhGRRPMAvgtGSEHRMAEMLLRhlglfncfDAIVGADDVQRHKPEP 145
Cdd:PRK11587  75 EATDTEGITALpgaiaLLNHLNKLGIpWAIVTS--GSVPVA---SARHKAAGLPAP--------EVFVTAERVKRGKPEP 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 727167864 146 DTFLRCAELIGVPPEKCVVFEDADFGIQAAKSAGMAVVDV 185
Cdd:PRK11587 142 DAYLLGAQLLGLAPQECVVVEDAPAGVLSGLAAGCHVIAV 181
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 4-182 1.52e-13

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 66.26  E-value: 1.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   4 RYQGLIFDMDGTILDTEPTHRKAWREVLSRYGMTFD-EAAMVALSGSPTWRIAQAIIASH-----QADLDPHHlaaektR 77
Cdd:PRK10563   3 QIEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLSlEEVFKRFKGVKLYEIIDIISKEHgvtlaKAELEPVY------R 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  78 AVEAMLLDS-VRPLP----LIEVVKSyhgrrPMA-VGTGSEHRMAEMLLRhLGLFNCF-DAIVGADDVQRHKPEPDTFLR 150
Cdd:PRK10563  77 AEVARLFDSeLEPIAganaLLESITV-----PMCvVSNGPVSKMQHSLGK-TGMLHYFpDKLFSGYDIQRWKPDPALMFH 150

                        170       180       190
                 ....*....|....*....|....*....|..
gi 727167864 151 CAELIGVPPEKCVVFEDADFGIQAAKSAGMAV 182
Cdd:PRK10563 151 AAEAMNVNVENCILVDDSSAGAQSGIAAGMEV 182
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 7-186 2.28e-13

Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGP; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and 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 (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) 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: 319854 [Multi-domain]  Cd Length: 212  Bit Score: 65.33  E-value: 2.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   7 GLIFDMDGTILDTEPTHRKAWREVLSRYGM-TFDEA--------------------AMVALSGSPTWRIAQAIIASHQAD 65
Cdd:cd16417    1 LVAFDLDGTLVDSAPDLAEAANAMLAALGLpPLPEEtvrtwigngadvlveraltgAREAEPDEELFKEARALFDRHYAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  66 ldphhlaaekTRAVEAMLLDSVRplpliEVVKSYH-GRRPMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPE 144
Cdd:cd16417   81 ----------TLSVHSHLYPGVK-----EGLAALKaQGYPLACVTNKPERFVAPLLEALGISDYFSLVLGGDSLPEKKPD 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 727167864 145 PDTFLRCAELIGVPPEKCVVFEDADFGIQAAKSAGMAVVDVR 186
Cdd:cd16417  146 PAPLLHACEKLGIAPAQMLMVGDSRNDILAARAAGCPSVGLT 187
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 7-183 1.10e-12

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. 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: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 63.83  E-value: 1.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   7 GLIFDMDGTILDTEPTHRKAWREVLSRYGMTFDEA------AMVALSGSPTWRIAQAIiasHQADLD--PHHLAAEKTRA 78
Cdd:cd02588    2 ALVFDVYGTLIDWHSGLAAAERAFPGRGEELSRLWrqkqleYTWLVTLMGPYVDFDEL---TRDALRatAAELGLELDES 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  79 VEAMLLDSVRPLPL----IEVVKSYHGRR-PMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAE 153
Cdd:cd02588   79 DLDELGDAYLRLPPfpdvVAGLRRLREAGyRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAEDVRAYKPAPAVYELAAE 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 727167864 154 LIGVPPEKCVVFEDADFGIQAAKSAGMAVV 183
Cdd:cd02588  159 RLGVPPDEILHVASHAWDLAGARALGLRTA 188
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 7-183 1.38e-12

haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter sphaeroides CbbZ; Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. 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: 319815 [Multi-domain]  Cd Length: 214  Bit Score: 63.49  E-value: 1.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   7 GLIFDMDGTILDTEPTHRKAWREVLSRYG---MTFDEAAMVALSGSPTWrIAQAIIAShQADLDPHHLAAEKTR---AVE 80
Cdd:cd07512    1 AVIFDLDGTLIDSAPDLHAALNAVLAAEGlapLSLAEVRSFVGHGAPAL-IRRAFAAA-GEDLDGPLHDALLARfldHYE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  81 AMLLDSVRPLP-LIEVVKSYHGR-RPMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVP 158
Cdd:cd07512   79 ADPPGLTRPYPgVIEALERLRAAgWRLAICTNKPEAPARALLSALGLADLFAAVVGGDTLPQRKPDPAPLRAAIRRLGGD 158

                        170       180
                 ....*....|....*....|....*
gi 727167864 159 PEKCVVFEDADFGIQAAKSAGMAVV 183
Cdd:cd07512  159 VSRALMVGDSETDAATARAAGVPFV 183
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 100-185 1.49e-12

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 64.89  E-value: 1.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864 100 HGRRPMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPPEKCVVFEDADFGIQAAKSAG 179
Cdd:PLN02575 230 NYKIPMALVSTRPRKTLENAIGSIGIRGFFSVIVAAEDVYRGKPDPEMFIYAAQLLNFIPERCIVFGNSNQTVEAAHDAR 309


                 ....*.
gi 727167864 180 MAVVDV 185
Cdd:PLN02575 310 MKCVAV 315
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
4-186 1.97e-12

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 63.29  E-value: 1.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   4 RYQGLIFDMDGTILDTEPthrkawrevlsryGMTFDEAAMVALSGSPTWRIAQAI--------------IASHQADLDPH 69
Cdd:PRK13222   5 DIRAVAFDLDGTLVDSAP-------------DLAAAVNAALAALGLPPAGEERVRtwvgngadvlveraLTWAGREPDEE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  70 hlAAEKTRAV------EAMLLDSvRPLP-LIEVVKSYHGRR-PMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRH 141
Cdd:PRK13222  72 --LLEKLRELfdrhyaENVAGGS-RLYPgVKETLAALKAAGyPLAVVTNKPTPFVAPLLEALGIADYFSVVIGGDSLPNK 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 727167864 142 KPEPDTFLRCAELIGVPPEKCVVFEDADFGIQAAKSAGMAVVDVR 186
Cdd:PRK13222 149 KPDPAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPSVGVT 193
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 92-185 6.16e-12

Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGPase; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and 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 (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) 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: 319857 [Multi-domain]  Cd Length: 105  Bit Score: 59.39  E-value: 6.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  92 LIEVVKSYHGRR--PMAVGTGSEHRMAEMLLRHLGLFNcFDAIVGADDVQRHKPEPDTFLRCAELIGVPPEKCVVFEDAD 169
Cdd:cd16421   11 LILELLKALRQKgiKLAVLSNKPNEAVQVLVEELFPGS-FDFVLGEKEGIRRKPDPT*ALECAKVLGVPPDEVLYVGDSG 89

                         90
                 ....*....|....*.
gi 727167864 170 FGIQAAKSAGMAVVDV 185
Cdd:cd16421   90 VDMQTARNAGMDEIGV 105
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 104-185 1.11e-11

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: 58.56  E-value: 1.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864 104 PMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPPEKCVVFEDADFGIQAAKSAGMAVV 183
Cdd:cd01427   25 KLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSENDIEAARAAGGRTV 104


                 ..
gi 727167864 184 DV 185
Cdd:cd01427  105 AV 106
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 7-179 1.31e-11

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; 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/E), (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 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe 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 relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 59.72  E-value: 1.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864    7 GLIFDMDGTILDTEPTHRKAWREVLSRYGM---TFDEA-AMVALSGSPTWRIAQAIIASHQADLDPHHLAAEKTRAveam 82
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFGLdpaSFKALkQAGGLAEEEWYRIATSALEELQGRFWSEYDAEEAYIR---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   83 lldsvrplPLIEVVKSYHGR-RPMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVqRHKPEPDTFLRCAELIGVPPEk 161
Cdd:TIGR01549  77 --------GAADLLARLKSAgIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEP-GSKPEPEIFLAALESLGVPPE- 146

                         170
                  ....*....|....*...
gi 727167864  162 CVVFEDADFGIQAAKSAG 179
Cdd:TIGR01549 147 VLHVGDNLNDIEGARNAG 164
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 105-179 5.66e-11

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 58.89  E-value: 5.66e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 727167864 105 MAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPPEKCVVFEDADFGIQAAKSAG 179
Cdd:PRK13288 101 LGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPDPEPVLKALELLGAKPEEALMVGDNHHDILAGKNAG 175
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 5-186 1.16e-09

2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Belongs to the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases (pfam00702), class (subfamily) I. Note that the Type I HAD enzymes have not yet been fully characterized, but clearly utilize a substantially different catalytic mechanism and are thus unlikely to be related.


Pssm-ID: 130495 [Multi-domain]  Cd Length: 198  Bit Score: 55.04  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864    5 YQGLIFDMDGTILDTEPT---HRKAWREVLSRYGM-----TFDEAAMVALSG--SPTWRIAQAIIAshqADLDPHHLAAE 74
Cdd:TIGR01428   1 IKALVFDVYGTLFDVHSVaerAAELYGGRGEALSQlwrqkQLEYSWLRTLMGpyKDFWDLTREALR---YLLGRLGLEDD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   75 KtrAVEAMLLDSVRPL-PLIEVVKSYHGRRPM----AVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFL 149
Cdd:TIGR01428  78 E--SAADRLAEAYLRLpPHPDVPAGLRALKERgyrlAILSNGSPAMLKSLVKHAGLDDPFDAVLSADAVRAYKPAPQVYQ 155

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 727167864  150 RCAELIGVPPEKcVVFEDADFG-IQAAKSAGMAVVDVR 186
Cdd:TIGR01428 156 LALEALGVPPDE-VLFVASNPWdLGGAKKFGFKTAWIN 192
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 55-187 1.23e-08

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p; This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and CMP. 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: 319791 [Multi-domain]  Cd Length: 182  Bit Score: 52.25  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  55 AQAIIASHQADLDPHHlaaekTRAVEAMLLDSVRPLP-LIEVVKSYHGRRpmAVGTGSEHRMAEMLLRHLGLFNCFDAIV 133
Cdd:cd02604   55 LRGLMAEHGIDPDEFL-----DRVVHLILYDHLKPDPkLRNLLLALPGRK--IIFTNASKNHAIRVLKRLGLADLFDGIF 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 727167864 134 GADDVQ-RHKPEPDTFLRCAELIGVPPEKCVVFEDADFGIQAAKSAGMAVVDVRT 187
Cdd:cd02604  128 DIEYAGpDPKPHPAAFEKAIREAGLDPKRAAFFDDSIRNLLAAKALGMKTVLVGP 182
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 8-185 1.33e-08

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1; 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: 319835 [Multi-domain]  Cd Length: 207  Bit Score: 52.40  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   8 LIFDMDGTILDTE----PTHRKAWR----------EVLSRYGMTFDEAAMVALSGSPTWRIAQAIiaSHQADLDPHHLAa 73
Cdd:cd07533    2 VIFDWDGTLADSQhnivAAMTAAFAdlglpvpsaaEVRSIIGLSLDEAIARLLPMATPALVAVAE--RYKEAFDILRLL- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  74 ektRAVEAMLLDSVRPLplIEVVKSYHGRrpMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDvQRHKPEPDTFLRCAE 153
Cdd:cd07533   79 ---PEHAEPLFPGVREA--LDALAAQGVL--LAVATGKSRRGLDRVLEQHGLGGYFDATRTADD-TPSKPHPEMLREILA 150

                        170       180       190
                 ....*....|....*....|....*....|..
gi 727167864 154 LIGVPPEKCVVFEDADFGIQAAKSAGMAVVDV 185
Cdd:cd07533  151 ELGVDPSRAVMVGDTAYDMQMAANAGAHAVGV 182
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 93-183 1.67e-08

human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. 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: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 50.23  E-value: 1.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  93 IEVVKSYHGRRPMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPPEKCVVFED---AD 169
Cdd:cd04305   15 KELLEELKKGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLMVGDsleSD 94

                         90
                 ....*....|....
gi 727167864 170 fgIQAAKSAGMAVV 183
Cdd:cd04305   95 --ILGAKNAGIKTV 106
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 9-181 3.89e-08

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the uncharacterized Lactococcus lactis YsbA; The specific function of Lactococcus lactis YsbA is unknown. 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: 319825 [Multi-domain]  Cd Length: 173  Bit Score: 50.45  E-value: 3.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   9 IFDMDGTILDTEPTHRKAWREVLSRYGMTFDEAAMVALSGSPTWRIAQAIIA-SHQADLDPHHLAAEKTRAVeaMLLDSV 87
Cdd:cd07523    3 IWDLDGTLLDSYPAMTKALSETLADFGIPQDLETVYKIIKESSVQFAIQYYAeVPDLEEEYKELEAEYLAKP--ILFPGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  88 RplPLIEVVKSYHGRRPMAVgtgseHRMAEML--LRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPPEKCVVF 165
Cdd:cd07523   81 K--AVLRWIKEQGGKNFLMT-----HRDHSALtiLKKDGIASYFTEIVTSDNGFPRKPNPEAINYLLNKYQLNPEETVMI 153

                        170
                 ....*....|....*.
gi 727167864 166 EDADFGIQAAKSAGMA 181
Cdd:cd07523  154 GDRELDIEAGHNAGIS 169
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 81-180 4.03e-08

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to uncharacterized Drosophila melanogaster rhythmically expressed gene 2 protein and human haloacid dehalogenase-like hydrolase domain-containing protein 3; The haloacid dehalogenase-like (HAD) hydrolases are 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 include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members 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: 319852 [Multi-domain]  Cd Length: 128  Bit Score: 49.60  E-value: 4.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  81 AMLLDSVRPLPLIEVVKSYHGRR-PMAVGTGSEHRMaEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPP 159
Cdd:cd16415    1 LITFDVTGTLLAVETLKDLKEKGlKLAVVSNFDRRL-RELLEALGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSP 79

                         90       100
                 ....*....|....*....|..
gi 727167864 160 EKCV-VFEDADFGIQAAKSAGM 180
Cdd:cd16415   80 EEALhVGDDLKNDYLGARAVGW 101
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 8-186 2.05e-07

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; 5'-nucleotidases dephosphorylate nucleoside 5'-monophosphates to nucleosides and inorganic phosphate. Purified Pseudomonas aeruginosa PA0065 displayed high activity toward 5'-UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low activity against 5'-CMP. 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: 319798 [Multi-domain]  Cd Length: 209  Bit Score: 49.13  E-value: 2.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   8 LIFDMDGTILDTEPTHRKAWREVLSRYGmtFDEAAMVALsgspTWRIAQAIIASHQADLDPHHLAAEktRAVEA------ 81
Cdd:cd04302    2 ILFDLDGTLTDSAEGITASVQYALEELG--IPVPDESEL----RRFIGPPLEDSFRELLPFDEEEAQ--RAVDAyreyyk 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  82 ---MLLDSVRP--LPLIEVVKsYHGRRpMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGA--DDVQRHKpePDTFLRCAEL 154
Cdd:cd04302   74 ekgLFENEVYPgiPELLEKLK-AAGYR-LYVATSKPEVFARRILEHFGLDEYFDGIAGAslDGSRVHK--ADVIRYALDT 149

                        170       180       190
                 ....*....|....*....|....*....|..
gi 727167864 155 IGVPPEKCVVFEDADFGIQAAKSAGMAVVDVR 186
Cdd:cd04302  150 LGIAPEQAVMIGDRKHDIIGARANGIDSIGVL 181
PRK13226 PRK13226
phosphoglycolate phosphatase; Provisional
 8-183 2.56e-07

phosphoglycolate phosphatase; Provisional


Pssm-ID: 237311 [Multi-domain]  Cd Length: 229  Bit Score: 49.08  E-value: 2.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   8 LIFDMDGTILDTEPTHRKAWREVLSRYGmtfdEAAMVALSGSPTWRI-AQAIIASHQADLDPHHLAA---------EKTR 77
Cdd:PRK13226  15 VLFDLDGTLLDSAPDMLATVNAMLAARG----RAPITLAQLRPVVSKgARAMLAVAFPELDAAARDAlipeflqryEALI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  78 AVEAMLLDSVRP-LPLIEVVKSYHGrrpmaVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIG 156
Cdd:PRK13226  91 GTQSQLFDGVEGmLQRLECAGCVWG-----IVTNKPEYLARLILPQLGWEQRCAVLIGGDTLAERKPHPLPLLVAAERIG 165

                        170       180
                 ....*....|....*....|....*..
gi 727167864 157 VPPEKCVVFEDADFGIQAAKSAGMAVV 183
Cdd:PRK13226 166 VAPTDCVYVGDDERDILAARAAGMPSV 192
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
 105-183 5.31e-06

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 45.62  E-value: 5.31e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727167864 105 MAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADDVQRHKPEPDTFLRCAELIGVPPEKCVVFEDADFGIQAAKSAGMAVV 183
Cdd:PRK13223 120 MALITNKPERFVAPLLDQMKIGRYFRWIIGGDTLPQKKPDPAALLFVMKMAGVPPSQSLFVGDSRSDVLAAKAAGVQCV 198
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 8-183 1.67e-05

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. 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: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 43.49  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   8 LIFDMDGTILDTEPTHrkawreVLSRYGMTFDEAAMVALSGSPTWRIAQ----AIIASHQ-----ADLDPHHLAAEKTra 78
Cdd:cd02603    4 VLFDFGGVLIDPDPAA------AVARFEALTGEPSEFVLDTEGLAGAFLelerGRITEEEfweelREELGRPLSAELF-- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  79 vEAMLLDSVRPLP-LIEVVKSYHGRR-PMAVGTGSEHRMAEMLLRHL-GLFNCFDAIVGADDVQRHKPEPDTFLRCAELI 155
Cdd:cd02603   76 -EELVLAAVDPNPeMLDLLEALRAKGyKVYLLSNTWPDHFKFQLELLpRRGDLFDGVVESCRLGVRKPDPEIYQLALERL 154

                        170       180
                 ....*....|....*....|....*...
gi 727167864 156 GVPPEKCVVFEDADFGIQAAKSAGMAVV 183
Cdd:cd02603  155 GVKPEEVLFIDDREENVEAARALGIHAI 182
Hydrolase_like pfam13242
HAD-hyrolase-like;
140-187 2.69e-05

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 40.68  E-value: 2.69e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 727167864  140 RHKPEPDTFLRCAELIGVPPEKCVVFED-ADFGIQAAKSAGMAVVDVRT 187
Cdd:pfam13242   2 CGKPNPGMLERALARLGLDPERTVMIGDrLDTDILGAREAGARTILVLT 50
PRK13478 PRK13478
phosphonoacetaldehyde hydrolase; Provisional
 6-185 2.57e-04

phosphonoacetaldehyde hydrolase; Provisional


Pssm-ID: 184075 [Multi-domain]  Cd Length: 267  Bit Score: 40.23  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   6 QGLIFDMDGTILD---TEPTHrkAWREVLSRYG--MTFDEA-------------AMVALSgsptwRIAQAIIASHQA--- 64
Cdd:PRK13478   5 QAVIFDWAGTTVDfgsFAPTQ--AFVEAFAQFGveITLEEArgpmglgkwdhirALLKMP-----RVAARWQAVFGRlpt 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  65 DLDPHHLAAEktraVEAMLLDSVR----PLP-LIEVVKSYHGRRpMAVG--TGSEHRMAEMLLRhLGLFNCF--DAIVGA 135
Cdd:PRK13478  78 EADVDALYAA----FEPLQIAKLAdyatPIPgVLEVIAALRARG-IKIGstTGYTREMMDVVVP-LAAAQGYrpDHVVTT 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 727167864 136 DDVQRHKPEPDTFLRCAELIGV-PPEKCVVFEDADFGIQAAKSAGMAVVDV 185
Cdd:PRK13478 152 DDVPAGRPYPWMALKNAIELGVyDVAACVKVDDTVPGIEEGLNAGMWTVGV 202
HAD_PHN cd02586
Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; ...
 6-185 4.77e-03

Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; Degradation of the ubiquitous natural phosphonate 2-aminoethylphosphonate (AEP) into useable forms of nitrogen, carbon, and phosphorus is a two-step metabolic pathway. The first step, catalyzed by AEP transaminase, involves the transfer of NH3 from AEP to pyruvate, yielding phosphonoacetaldehyde (P-Ald) and alanine. In the second step, phosphonatase catalyzes the hydrolytic P-C bond cleavage of P-Ald to form orthophosphate and acetaldehyde. 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: 319785 [Multi-domain]  Cd Length: 242  Bit Score: 36.51  E-value: 4.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864   6 QGLIFDMDGTILD---TEPThrKAWREVLSRYGMTFDEAAMVALSGSPTW----------RIAQAIIASHQ-----ADLD 67
Cdd:cd02586    2 EAVIFDWAGTTVDygsFAPV--NAFVEAFAQRGVQITLEEARKPMGLLKIdhirallempRVAEAWRAVFGrlpteADVD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864  68 phhlaaEKTRAVEAMLLDSV----RPLP-LIEVVkSYHGRRPMAVG--TGSEHRMAEMLLRHLGLfNCF--DAIVGADDV 138
Cdd:cd02586   80 ------ALYEEFEPILIASLaeysSPIPgVLEVI-AKLRARGIKIGstTGYTREMMDIVLPEAAA-QGYrpDSLVTPDDV 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 727167864 139 QRHKPEPDTFLRCAELIGV-PPEKCVVFEDADFGIQAAKSAGMAVVDV 185
Cdd:cd02586  152 PAGRPYPWMCYKNAIELGVyDVAAVVKVGDTVPDIKEGLNAGMWTVGV 199
HAD pfam12710
haloacid dehalogenase-like hydrolase;
8-137 5.17e-03

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 36.36  E-value: 5.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727167864    8 LIFDMDGTILDTEPTH-----------RKAWREVLSRYGMTFDEAAMvALSGSPTWRIAQAIIASHqadldPHHLAAEKT 76
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFllirallrrggPDLWRALLVLLLLALLRLLG-RLSRAGARELLRALLAGL-----PEEDAAELE 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727167864   77 RAVEAMLLDSVRP--LPLIEVVKSYHGRrpMAVGTGSEHRMAEMLLRHLGLFNCFDAIVGADD 137
Cdd:pfam12710  75 RFVAEVALPRLHPgaLELLAAHRAAGDR--VVVVTGGLRPLVEPVLAELGFDEVLATELEVDD 135
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 142-187 7.40e-03

inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP); LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. 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: 319812 [Multi-domain]  Cd Length: 248  Bit Score: 36.10  E-value: 7.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 727167864 142 KPEPDTFLRCAELIGVPPEKCVVF-EDADFGIQAAKSAGMAVVDVRT 187
Cdd:cd07509  172 KPSPEFFLSALRSLGVDPEEAVMIgDDLRDDVGGAQACGMRGILVRT 218
 
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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