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Conserved domains on  [gi|446195454|ref|WP_000273309|]
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MULTISPECIES: fructose-1-phosphate/6-phosphogluconate phosphatase [Enterobacteriaceae]

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 5.77e-148

fructose-1-phosphate/6-phosphogluconate phosphatase;


:

Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 407.92  E-value: 5.77e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   1 MYERYAGLIFDMDGTILDTEPTHRKAWREVLGHYGLQYDVQAMIALNGSPTWRIAQAIIELNQADLDPHALAREKTEAVR 80
Cdd:PRK10725   1 MYDRYAGLIFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVALNGSPTWRIAQAIIELNQADLDPHALAREKTEAVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  81 SMLLDSVEPLPLVEVVKSWHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPT 160
Cdd:PRK10725  81 SMLLDSVEPLPLIEVVKAWHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADDVQHHKPAPDTFLRCAQLMGVQPT 160

                        170       180
                 ....*....|....*....|....*...
gi 446195454 161 QCVVFEDADFGIQAARAAGMDAVDVRLL 188
Cdd:PRK10725 161 QCVVFEDADFGIQAARAAGMDAVDVRLL 188
 
Name Accession Description Interval E-value
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
1-188 5.77e-148

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 407.92  E-value: 5.77e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   1 MYERYAGLIFDMDGTILDTEPTHRKAWREVLGHYGLQYDVQAMIALNGSPTWRIAQAIIELNQADLDPHALAREKTEAVR 80
Cdd:PRK10725   1 MYDRYAGLIFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVALNGSPTWRIAQAIIELNQADLDPHALAREKTEAVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  81 SMLLDSVEPLPLVEVVKSWHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPT 160
Cdd:PRK10725  81 SMLLDSVEPLPLIEVVKAWHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADDVQHHKPAPDTFLRCAQLMGVQPT 160

                        170       180
                 ....*....|....*....|....*...
gi 446195454 161 QCVVFEDADFGIQAARAAGMDAVDVRLL 188
Cdd:PRK10725 161 QCVVFEDADFGIQAARAAGMDAVDVRLL 188
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 5-185 1.92e-89

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: 259.58  E-value: 1.92e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454    5 YAGLIFDMDGTILDTEPTHRKAWREVLGHYGLQYDVQAMIALNGSPTWRIAQAIIELNQADLDP---HALAREKTEAVRS 81
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDGLSLeeiHQLAERKNELYRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   82 ML-LDSVEPLPLVEVVKSWHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPT 160
Cdd:TIGR02009  81 LLrLTGVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRDYFDAIVDASEVKNGKPHPETFLLAAELLGVPPN 160

                         170       180
                  ....*....|....*....|....*
gi 446195454  161 QCVVFEDADFGIQAARAAGMDAVDV 185
Cdd:TIGR02009 161 ECIVFEDALAGVQAARAAGMFAVAV 185
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
4-185 4.26e-65

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 198.89  E-value: 4.26e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   4 RYAGLIFDMDGTILDTEPTHRKAWREVLGHYGLQYDVQAMIALNGSPTWRIAQAIIELNQADLDPHALAREKTEAVRSML 83
Cdd:COG0637    1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYRELL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  84 -LDSVEPLP-LVEVVKSWHGRR-PMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPT 160
Cdd:COG0637   81 aEEGLPLIPgVVELLEALKEAGiKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERLGVDPE 160

                        170       180
                 ....*....|....*....|....*
gi 446195454 161 QCVVFEDADFGIQAARAAGMDAVDV 185
Cdd:COG0637  161 ECVVFEDSPAGIRAAKAAGMRVVGV 185
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 7-186 3.41e-42

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: 138.52  E-value: 3.41e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   7 GLIFDMDGTILDTEPTHRKAWRevlghyglqydvqamialngsptwriaqaiielnqadldphaLAREKTEAVRSMLLDS 86
Cdd:cd07505    1 AVIFDMDGVLIDTEPLHRQAWQ------------------------------------------LLERKNALLLELIASE 38

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  87 VEPL--PLVEVVKSWHGRR-PMAVGTGSE-SAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPTQC 162
Cdd:cd07505   39 GLKLkpGVVELLDALKAAGiPVAVATSSSrRNVELLLLELGLLRGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERC 118

                        170       180
                 ....*....|....*....|....
gi 446195454 163 VVFEDADFGIQAARAAGMDAVDVR 186
Cdd:cd07505  119 LVFEDSLAGIEAAKAAGMTVVAVP 142
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
8-185 3.42e-34

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 119.23  E-value: 3.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454    8 LIFDMDGTILDTEPTHRKAWREVLGHYGL-QYDVQAMIALNGSPTWRIAQAIIELNQADLDPHALAREkteaVRSMLLD- 85
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYgELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFYLRK----YNEELHDk 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   86 SVEPLP-LVEVVKSWHGRR-PMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPTQCV 163
Cdd:pfam13419  77 LVKPYPgIKELLEELKEQGyKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVI 156

                         170       180
                  ....*....|....*....|..
gi 446195454  164 VFEDADFGIQAARAAGMDAVDV 185
Cdd:pfam13419 157 YVGDSPRDIEAAKNAGIKVIAV 178
 
Name Accession Description Interval E-value
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
1-188 5.77e-148

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 407.92  E-value: 5.77e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   1 MYERYAGLIFDMDGTILDTEPTHRKAWREVLGHYGLQYDVQAMIALNGSPTWRIAQAIIELNQADLDPHALAREKTEAVR 80
Cdd:PRK10725   1 MYDRYAGLIFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVALNGSPTWRIAQAIIELNQADLDPHALAREKTEAVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  81 SMLLDSVEPLPLVEVVKSWHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPT 160
Cdd:PRK10725  81 SMLLDSVEPLPLIEVVKAWHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADDVQHHKPAPDTFLRCAQLMGVQPT 160

                        170       180
                 ....*....|....*....|....*...
gi 446195454 161 QCVVFEDADFGIQAARAAGMDAVDVRLL 188
Cdd:PRK10725 161 QCVVFEDADFGIQAARAAGMDAVDVRLL 188
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 5-185 1.92e-89

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: 259.58  E-value: 1.92e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454    5 YAGLIFDMDGTILDTEPTHRKAWREVLGHYGLQYDVQAMIALNGSPTWRIAQAIIELNQADLDP---HALAREKTEAVRS 81
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDGLSLeeiHQLAERKNELYRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   82 ML-LDSVEPLPLVEVVKSWHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPT 160
Cdd:TIGR02009  81 LLrLTGVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRDYFDAIVDASEVKNGKPHPETFLLAAELLGVPPN 160

                         170       180
                  ....*....|....*....|....*
gi 446195454  161 QCVVFEDADFGIQAARAAGMDAVDV 185
Cdd:TIGR02009 161 ECIVFEDALAGVQAARAAGMFAVAV 185
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
4-185 4.26e-65

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 198.89  E-value: 4.26e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   4 RYAGLIFDMDGTILDTEPTHRKAWREVLGHYGLQYDVQAMIALNGSPTWRIAQAIIELNQADLDPHALAREKTEAVRSML 83
Cdd:COG0637    1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYRELL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  84 -LDSVEPLP-LVEVVKSWHGRR-PMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPT 160
Cdd:COG0637   81 aEEGLPLIPgVVELLEALKEAGiKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERLGVDPE 160

                        170       180
                 ....*....|....*....|....*
gi 446195454 161 QCVVFEDADFGIQAARAAGMDAVDV 185
Cdd:COG0637  161 ECVVFEDSPAGIRAAKAAGMRVVGV 185
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 7-186 3.41e-42

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: 138.52  E-value: 3.41e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   7 GLIFDMDGTILDTEPTHRKAWRevlghyglqydvqamialngsptwriaqaiielnqadldphaLAREKTEAVRSMLLDS 86
Cdd:cd07505    1 AVIFDMDGVLIDTEPLHRQAWQ------------------------------------------LLERKNALLLELIASE 38

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  87 VEPL--PLVEVVKSWHGRR-PMAVGTGSE-SAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPTQC 162
Cdd:cd07505   39 GLKLkpGVVELLDALKAAGiPVAVATSSSrRNVELLLLELGLLRGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERC 118

                        170       180
                 ....*....|....*....|....
gi 446195454 163 VVFEDADFGIQAARAAGMDAVDVR 186
Cdd:cd07505  119 LVFEDSLAGIEAAKAAGMTVVAVP 142
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
5-183 1.24e-37

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 128.89  E-value: 1.24e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   5 YAGLIFDMDGTILDTEPTHRKAWREVLGHYGLQ-YDVQAMIALNGSPTWRIAQAIIELNQADLDPHALAREKtEAVRSML 83
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPpLDLEELRALIGLGLRELLRRLLGEDPDEELEELLARFR-ELYEEEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  84 LDSVEPLPLV-EVVKSWHGRR-PMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPTQ 161
Cdd:COG0546   80 LDETRLFPGVrELLEALKARGiKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLDPEE 159

                        170       180
                 ....*....|....*....|..
gi 446195454 162 CVVFEDADFGIQAARAAGMDAV 183
Cdd:COG0546  160 VLMVGDSPHDIEAARAAGVPFI 181
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 8-186 1.73e-35

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: 121.98  E-value: 1.73e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   8 LIFDMDGTILDTEPTHRKAWREVLGHYglqydvqamialngspTWRIAQAIIELNqADLDPHALAREKTEAVRSMLLdsv 87
Cdd:cd16423    2 VIFDFDGVIVDTEPLWYEAWQELLNER----------------RNELIKRQFSEK-TDLPPIEGVKELLEFLKEKGI--- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  88 eplplvevvkswhgrrPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPTQCVVFED 167
Cdd:cd16423   62 ----------------KLAVASSSPRRWIEPHLERLGLLDYFEVIVTGDDVEKSKPDPDLYLEAAERLGVNPEECVVIED 125

                        170
                 ....*....|....*....
gi 446195454 168 ADFGIQAARAAGMDAVDVR 186
Cdd:cd16423  126 SRNGVLAAKAAGMKCVGVP 144
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
8-185 3.42e-34

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 119.23  E-value: 3.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454    8 LIFDMDGTILDTEPTHRKAWREVLGHYGL-QYDVQAMIALNGSPTWRIAQAIIELNQADLDPHALAREkteaVRSMLLD- 85
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYgELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFYLRK----YNEELHDk 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   86 SVEPLP-LVEVVKSWHGRR-PMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPTQCV 163
Cdd:pfam13419  77 LVKPYPgIKELLEELKEQGyKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVI 156

                         170       180
                  ....*....|....*....|..
gi 446195454  164 VFEDADFGIQAARAAGMDAVDV 185
Cdd:pfam13419 157 YVGDSPRDIEAAKNAGIKVIAV 178
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 7-185 2.13e-32

beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which catalyzes the interconverison of beta-D-glucose-1-phosphate and beta-D-glucose-6-phosphate. The 6-phosphate is capable of non-enzymatic anomerization (alpha <-> beta) while the 1-phosphate is not. A separate enzyme is responsible for the isomerization of the alpha anomers. Beta-D-glucose-1-phosphate results from the phosphorylysis of maltose (2.4.1.8), trehalose (2.4.1.64) or trehalose-6-phosphate (2.4.1.216). Alternatively, these reactions can be run in the synthetic direction to create the disaccharides. All sequenced genomes which contain a member of this family also appear to contain at least one putative maltose or trehalose phosphorylase. Three species, Lactococcus, Enterococcus and Neisseria appear to contain a pair of paralogous beta-PGM's. Beta-phosphoglucomutase is a member of the haloacid dehalogenase superfamily of hydrolase enzymes. These enzymes are characterized by a series of three catalytic motifs positioned within an alpha-beta (Rossman) fold. beta-PGM contains an inserted alpha helical domain in between the first and second conserved motifs and thus is a member of subfamily IA of the superfamily. The third catalytic motif comes in three variants, the third of which, containing a conserved DD or ED, is the only one found here as well as in several other related enzymes (TIGR01509). The enzyme from L. lactis has been extensively characterized including a remarkable crystal structure which traps the pentacoordinate transition state. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 213672 [Multi-domain]  Cd Length: 185  Bit Score: 114.71  E-value: 2.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454    7 GLIFDMDGTILDTEPTHRKAWREVLGHYGLQYDVQAMIALNGSPTWRIAQAIIELNQADLDP---HALAREKTEAVRSML 83
Cdd:TIGR01990   1 AVIFDLDGVITDTAEYHYLAWKHLADELGIPFDEEFNESLKGVSREESLERILDLGGKKYSEeekEELAERKNDYYVELL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   84 --LDSVEPLPLVEVVKSWHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPTQ 161
Cdd:TIGR01990  81 keLTPADVLPGIKSLLADLKKNNIKIALASASKNAPTILEKLELIDYFDAIVDPAELKKGKPDPEIFLAAAEGLGVSPSE 160

                         170       180
                  ....*....|....*....|....
gi 446195454  162 CVVFEDADFGIQAARAAGMDAVDV 185
Cdd:TIGR01990 161 CIGIEDAQAGIEAIKAAGMFAVGV 184
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 8-185 4.24e-31

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: 111.67  E-value: 4.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   8 LIFDMDGTILDTEPTHRKAWREVLGHYGLQYDVQAMIALNGSPTWRIAQAIIELNQADLDPHALAREKTEAVRSMLLDSV 87
Cdd:cd07529    4 CIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLEEEFDEQQEALAELFMGTA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  88 EPLPLVE-VVKSWHGRR-PMAVGTGSESAIAEALLA-HLGLRRYFDAVVAADH---VKHHKPAPDTFLLCAQRMG---VQ 158
Cdd:cd07529   84 KLMPGAErLLRHLHAHNiPIALATSSCTRHFKLKTSrHKELFSLFHHVVTGDDpevKGRGKPAPDIFLVAAKRFNeppKD 163

                        170       180
                 ....*....|....*....|....*..
gi 446195454 159 PTQCVVFEDADFGIQAARAAGMDAVDV 185
Cdd:cd07529  164 PSKCLVFEDSPNGVKAAKAAGMQVVMV 190
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 7-185 2.53e-30

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: 110.13  E-value: 2.53e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   7 GLIFDMDGTILDTEPTHRKAWREVLGHYGLQYDvQAMIALNGsptWRIAQAIIELNQADLDPHALAREKTEAVRSMLlDS 86
Cdd:cd07527    1 ALLFDMDGTLVDSTPAVERAWHKWAKEHGVDPE-EVLKVSHG---RRAIDVIRKLAPDDADIELVLALETEEPESYP-EG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  87 VEPLP----LVEVVKSwHGRRPMAVgTGSESAIAEALLAHLGLRRYfDAVVAADHVKHHKPAPDTFLLCAQRMGVQPTQC 162
Cdd:cd07527   76 VIAIPgavdLLASLPA-AGDRWAIV-TSGTRALAEARLEAAGLPHP-EVLVTADDVKNGKPDPEPYLLGAKLLGLDPSDC 152

                        170       180
                 ....*....|....*....|...
gi 446195454 163 VVFEDADFGIQAARAAGMDAVDV 185
Cdd:cd07527  153 VVFEDAPAGIKAGKAAGARVVAV 175
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 5-179 6.60e-27

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: 100.74  E-value: 6.60e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454    5 YAGLIFDMDGTILDTEPTHRKAWREVLGHYGLQYDVQAMI-------------ALNGSPTW-RIAQAIIELNQADLDPHA 70
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAedlpipvedftarLLLGKRDWlEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   71 LAREKTEAVRSMLLDSVEPLP-LVEVVKSWHGRR-PMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTF 148
Cdd:pfam00702  81 TVVLVELLGVIALADELKLYPgAAEALKALKERGiKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIY 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 446195454  149 LLCAQRMGVQPTQCVVFEDADFGIQAARAAG 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 1.29e-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: 99.80  E-value: 1.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454    8 LIFDMDGTILDTEPTHRK-AWREVLGHYGLQYDVQAMIALNGS-PTW------RIAQAIIELNQADLDPHALAREKTEAV 79
Cdd:TIGR01509   2 ILFDLDGVLVDTEFAIAKlINREELGLVPDELGVSAVGRLELAlRRFkaqygrTISPEDAQLLYKQLFYEQIEEEAKLKP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   80 RSMLLDSVEPLPLvevvkswHGRRpMAVGTGSEsAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQP 159
Cdd:TIGR01509  82 LPGVRALLEALRA-------RGKK-LALLTNSP-RAHKLVLALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLEP 152

                         170       180
                  ....*....|....*....|....
gi 446195454  160 TQCVVFEDADFGIQAARAAGMDAV 183
Cdd:TIGR01509 153 SECVFVDDSPAGIEAAKAAGMHTV 176
PLN02940 PLN02940
riboflavin kinase
 8-185 1.08e-25

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 101.45  E-value: 1.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   8 LIFDMDGTILDTEPTHRKAWREVLGHYGLQYDVQAMIALNGSPTWRIAQAIIELNQADLDPHALAREKTEAVrSMLLDSV 87
Cdd:PLN02940  14 VILDLDGTLLNTDGIVSDVLKAFLVKYGKQWDGREAQKIVGKTPLEAAATVVEDYGLPCSTDEFNSEITPLL-SEQWCNI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  88 EPLP----LVEVVKSwHGRrPMAVGTGSESAIAEALLA-HLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPTQC 162
Cdd:PLN02940  93 KALPganrLIKHLKS-HGV-PMALASNSPRANIEAKIScHQGWKESFSVIVGGDEVEKGKPSPDIFLEAAKRLNVEPSNC 170

                        170       180
                 ....*....|....*....|...
gi 446195454 163 VVFEDADFGIQAARAAGMDAVDV 185
Cdd:PLN02940 171 LVIEDSLPGVMAGKAAGMEVIAV 193
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 7-185 4.24e-25

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: 95.44  E-value: 4.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   7 GLIFDMDGTILDTEPTHRKAWRevlghyglqydvqamialngsptwriaqaiielNQADLDphALAREKTEAVRSML--L 84
Cdd:cd02598    1 GVIFDLDGVITDTAEYHYRAWK---------------------------------KLADKE--ELAARKNRIYVELIeeL 45

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  85 DSVEPLP-----LVEVVKswhgrRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQP 159
Cdd:cd02598   46 TPVDVLPgiaslLVDLKA-----KGIKIALASASKNAPKILEKLGLAEYFDAIVDGAVLAKGKPDPDIFLAAAEGLGLNP 120

                        170       180
                 ....*....|....*....|....*.
gi 446195454 160 TQCVVFEDADFGIQAARAAGMDAVDV 185
Cdd:cd02598  121 KDCIGVEDAQAGIRAIKAAGFLVVGV 146
PRK10826 PRK10826
hexitol phosphatase HxpB;
9-185 6.62e-25

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 96.17  E-value: 6.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   9 IFDMDGTILDTEPTHRKAWREVLGHYGL----QYDVQAMIALngsptwRIAQAIIELNQA----DLDPHALAREKTEAVR 80
Cdd:PRK10826  11 IFDMDGLLIDSEPLWDRAELDVMASLGVdisrREELPDTLGL------RIDQVVDLWYARqpwnGPSRQEVVQRIIARVI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  81 SMLLDSVEPLPLVEVVKSWHGRRPMAVG--TGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQ 158
Cdd:PRK10826  85 SLIEETRPLLPGVREALALCKAQGLKIGlaSASPLHMLEAVLTMFDLRDYFDALASAEKLPYSKPHPEVYLNCAAKLGVD 164

                        170       180
                 ....*....|....*....|....*..
gi 446195454 159 PTQCVVFEDADFGIQAARAAGMDAVDV 185
Cdd:PRK10826 165 PLTCVALEDSFNGMIAAKAARMRSIVV 191
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 8-183 9.36e-25

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: 95.87  E-value: 9.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   8 LIFDMDGTILDTEPTHRKAWREVLGHYGLQYDVQAMIAL---NGSPTWRIAQAIIELNQADLD------PHALAREKTEA 78
Cdd:COG1011    4 VLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAEAyraIEYALWRRYERGEITFAELLRrlleelGLDLAEELAEA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  79 VRSMLLDSVEPLP-LVEVVKSWHGR-RPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMG 156
Cdd:COG1011   84 FLAALPELVEPYPdALELLEALKARgYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIFELALERLG 163

                        170       180       190
                 ....*....|....*....|....*....|
gi 446195454 157 VQPTQCVVFED---ADfgIQAARAAGMDAV 183
Cdd:COG1011  164 VPPEEALFVGDspeTD--VAGARAAGMRTV 191
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 8-180 1.92e-23

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: 92.06  E-value: 1.92e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   8 LIFDMDGTILDTEPTHRKAWREVLGH-YGL--QYDVQAMIAL--NGSPTWRIAQAIIELNQADLDPHALA-------REK 75
Cdd:cd07528    2 LIFDVDGTLAETEELHRRAFNNAFFAeRGLdwYWDRELYGELlrVGGGKERIAAYFEKVGWPESAPKDLKeliadlhKAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  76 TEAVRSMLLD-SVEPLP----LVEVVKSwHGRRPMAVGTGSESAIAEALLAHLGLRRY--FDAVVAADHVKHHKPAPDTF 148
Cdd:cd07528   82 TERYAELIAAgLLPLRPgvarLIDEAKA-AGVRLAIATTTSPANVDALLSALLGPERRaiFDAIAAGDDVAEKKPDPDIY 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 446195454 149 LLCAQRMGVQPTQCVVFEDADFGIQAARAAGM 180
Cdd:cd07528  161 LLALERLGVSPSDCLAIEDSAIGLQAAKAAGL 192
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 8-181 3.27e-23

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: 89.69  E-value: 3.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   8 LIFDMDGTILDTEPTHRKAWREVLGHYGLqydvqamialngsptwRIAQAIielnQADLDPHALAREKTEAvrsmlldsv 87
Cdd:cd07526    3 VIFDCDGVLVDSEVIAARVLVEVLAELGA----------------RVLAAF----EAELQPIPGAAAALSA--------- 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  88 epLPLvevvkswhgrrPMAVGTGSESAIAEALLAHLGLRRYFDA-VVAADHVKHHKPAPDTFLLCAQRMGVQPTQCVVFE 166
Cdd:cd07526   54 --LTL-----------PFCVASNSSRERLTHSLGLAGLLAYFEGrIFSASDVGRGKPAPDLFLHAAAQMGVAPERCLVIE 120

                        170
                 ....*....|....*
gi 446195454 167 DADFGIQAARAAGMD 181
Cdd:cd07526  121 DSPTGVRAALAAGMT 135
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
1-186 1.26e-20

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 85.25  E-value: 1.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   1 MYERYAGLIFDMDGTILDTEPthrkawrevlghyGLQYDVQAMIALNGSPTW---RI-------AQAIIE----LNQADL 66
Cdd:PRK13222   2 KFMDIRAVAFDLDGTLVDSAP-------------DLAAAVNAALAALGLPPAgeeRVrtwvgngADVLVEraltWAGREP 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  67 DPHALAR---------EKTEAVRSMLLDSVEplplvEVVKSWHGRR-PMAVGTGSESAIAEALLAHLGLRRYFDAVVAAD 136
Cdd:PRK13222  69 DEELLEKlrelfdrhyAENVAGGSRLYPGVK-----ETLAALKAAGyPLAVVTNKPTPFVAPLLEALGIADYFSVVIGGD 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446195454 137 HVKHHKPAPDTFLLCAQRMGVQPTQCVVFEDADFGIQAARAAGMDAVDVR 186
Cdd:PRK13222 144 SLPNKKPDPAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPSVGVT 193
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 7-185 2.32e-20

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 87.60  E-value: 2.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454    7 GLIFDMDGTILDTEPTHRKAWREVLGHYGLQYDVQAMIALNGSPTWRIAQAIIELNQA-DLDPHALAREKTEavrsMLLD 85
Cdd:PLN02919   77 AVLFDMDGVLCNSEEPSRRAAVDVFAEMGVEVTVEDFVPFMGTGEANFLGGVASVKGVkGFDPDAAKKRFFE----IYLE 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   86 SVEP----------LPLVEVVKSwHGRRpMAVGTGSESAIAEALLAHLGL-RRYFDAVVAADHVKHHKPAPDTFLLCAQR 154
Cdd:PLN02919  153 KYAKpnsgigfpgaLELITQCKN-KGLK-VAVASSADRIKVDANLAAAGLpLSMFDAIVSADAFENLKPAPDIFLAAAKI 230

                         170       180       190
                  ....*....|....*....|....*....|.
gi 446195454  155 MGVQPTQCVVFEDADFGIQAARAAGMDAVDV 185
Cdd:PLN02919  231 LGVPTSECVVIEDALAGVQAARAAGMRCIAV 261
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 8-180 8.49e-20

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 83.99  E-value: 8.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   8 LIFDMDGTILDTEPT-HRKAWREVLGHYGLQ--------YDVQAMIA-----------LNGSPTWRIAQAIIELNQADLD 67
Cdd:PLN02779  43 LLFDCDGVLVETERDgHRVAFNDAFKEFGLRpvewdvelYDELLNIGggkermtwyfnENGWPTSTIEKAPKDEEERKEL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  68 PHALAREKTEAVRSMLLD-SVEPLP----LVEVVKSwhGRRPMAV-GTGSESAIAEALLAHLGLRRY--FDaVVAADHVK 139
Cdd:PLN02779 123 VDSLHDRKTELFKELIESgALPLRPgvlrLMDEALA--AGIKVAVcSTSNEKAVSKIVNTLLGPERAqgLD-VFAGDDVP 199

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446195454 140 HHKPAPDTFLLCAQRMGVQPTQCVVFEDADFGIQAARAAGM 180
Cdd:PLN02779 200 KKKPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAAKAAGM 240
PLN02811 PLN02811
hydrolase
 12-185 1.03e-19

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 82.50  E-value: 1.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  12 MDGTILDTEPTHRKAWREVLGHYGLQYDVQAMIALNGSPTWRIAQAIIELNQAD--LDPHALAREKTEAVRSMLLDSvEP 89
Cdd:PLN02811   1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSdsLSPEDFLVEREAMLQDLFPTS-DL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  90 LPLVE-VVKSWHGRR-PMAVGTGS-ESAIAEALLAHLGLRRYFDAVVAADH--VKHHKPAPDTFLLCAQRM---GVQPTQ 161
Cdd:PLN02811  80 MPGAErLVRHLHAKGiPIAIATGShKRHFDLKTQRHGELFSLMHHVVTGDDpeVKQGKPAPDIFLAAARRFedgPVDPGK 159

                        170       180
                 ....*....|....*....|....
gi 446195454 162 CVVFEDADFGIQAARAAGMDAVDV 185
Cdd:PLN02811 160 VLVFEDAPSGVEAAKNAGMSVVMV 183
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 7-186 3.56e-17

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: 75.73  E-value: 3.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   7 GLIFDMDGTILDTEPthrkawrevlghyGLQYDVQAMIALNGSPTWRIAQ-------------------AIIELNQADLD 67
Cdd:cd16417    1 LVAFDLDGTLVDSAP-------------DLAEAANAMLAALGLPPLPEETvrtwigngadvlveraltgAREAEPDEELF 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  68 PHALAR-----EKTEAVRSMLLDSVEplplvEVVKSWH-GRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHH 141
Cdd:cd16417   68 KEARALfdrhyAETLSVHSHLYPGVK-----EGLAALKaQGYPLACVTNKPERFVAPLLEALGISDYFSLVLGGDSLPEK 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446195454 142 KPAPDTFLLCAQRMGVQPTQCVVFEDADFGIQAARAAGMDAVDVR 186
Cdd:cd16417  143 KPDPAPLLHACEKLGIAPAQMLMVGDSRNDILAARAAGCPSVGLT 187
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 8-183 1.93e-16

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 74.49  E-value: 1.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   8 LIFDMDGTILDTEPTHRKAWREVLGHYGLQydvqamialNGSPtwrIAQAIIELNQAD---------LDPHALAR----- 73
Cdd:PLN02770  25 VLFDVDGTLCDSDPLHYYAFREMLQEINFN---------GGVP---ITEEFFVENIAGkhnedialgLFPDDLERglkft 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  74 -EKTEAVRSMLLDSVEPLPLVEVVKSW---HGRRPMAVgTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFL 149
Cdd:PLN02770  93 dDKEALFRKLASEQLKPLNGLYKLKKWiedRGLKRAAV-TNAPRENAELMISLLGLSDFFQAVIIGSECEHAKPHPDPYL 171

                        170       180       190
                 ....*....|....*....|....*....|....
gi 446195454 150 LCAQRMGVQPTQCVVFEDADFGIQAARAAGMDAV 183
Cdd:PLN02770 172 KALEVLKVSKDHTFVFEDSVSGIKAGVAAGMPVV 205
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 5-185 3.42e-16

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: 73.08  E-value: 3.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   5 YAGLIFDMDGTILDTEPTHRKAWREVLGHYGL----QYDVQAMIalnGSPTWRIAQAIIELNQADLdphalAREKTEAVR 80
Cdd:cd02616    1 ITTILFDLDGTLIDTNELIIKSFNHTLKEYGLegytREEVLPFI---GPPLRETFEKIDPDKLEDM-----VEEFRKYYR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  81 SMLLDSVEPLPLV-EVVKSWHGR-RPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQ 158
Cdd:cd02616   73 EHNDDLTKEYPGVyETLARLKSQgIKLGVVTTKLRETALKGLKLLGLDKYFDVIVGGDDVTHHKPDPEPVLKALELLGAE 152

                        170       180
                 ....*....|....*....|....*..
gi 446195454 159 PTQCVVFEDADFGIQAARAAGMDAVDV 185
Cdd:cd02616  153 PEEALMVGDSPHDILAGKNAGVKTVGV 179
PRK11587 PRK11587
putative phosphatase; Provisional
 7-179 2.28e-15

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 71.18  E-value: 2.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   7 GLIFDMDGTILDTEPTHRKAW-----------REVLGHYglqYDVQAMIALN----GSPTWRIAQAIIELNQadldphaL 71
Cdd:PRK11587   5 GFLFDLDGTLVDSLPAVERAWsnwadrhgiapDEVLNFI---HGKQAITSLRhfmaGASEAEIQAEFTRLEQ-------I 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  72 AREKTEAVRSM-----LLDSVEPLPLvevvkswhgrrPMAVGTGSESAIAEALLAHLGLRRYfDAVVAADHVKHHKPAPD 146
Cdd:PRK11587  75 EATDTEGITALpgaiaLLNHLNKLGI-----------PWAIVTSGSVPVASARHKAAGLPAP-EVFVTAERVKRGKPEPD 142

                        170       180       190
                 ....*....|....*....|....*....|...
gi 446195454 147 TFLLCAQRMGVQPTQCVVFEDADFGIQAARAAG 179
Cdd:PRK11587 143 AYLLGAQLLGLAPQECVVVEDAPAGVLSGLAAG 175
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 5-185 2.95e-14

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 68.91  E-value: 2.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   5 YAGLIFDMDGTILDTEPT-HRKAWREVLGHYGLQydVQAMIALNGSPTWRIAQAIIEL---NQADLDPHALAREKTEAVR 80
Cdd:PLN03243  24 WLGVVLEWEGVIVEDDSElERKAWRALAEEEGKR--PPPAFLLKRAEGMKNEQAISEVlcwSRDFLQMKRLAIRKEDLYE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  81 SMLLDSVEPLP----LVEVVKSWhgRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMG 156
Cdd:PLN03243 102 YMQGGLYRLRPgsreFVQALKKH--EIPIAVASTRPRRYLERAIEAVGMEGFFSVVLAAEDVYRGKPDPEMFMYAAERLG 179

                        170       180
                 ....*....|....*....|....*....
gi 446195454 157 VQPTQCVVFEDADFGIQAARAAGMDAVDV 185
Cdd:PLN03243 180 FIPERCIVFGNSNSSVEAAHDGCMKCVAV 208
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 92-185 4.10e-13

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: 62.41  E-value: 4.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  92 LVEVVKSWHGRR-PMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPTQCVVFEDADF 170
Cdd:cd01427   12 AVELLKRLRAAGiKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSEN 91

                         90
                 ....*....|....*
gi 446195454 171 GIQAARAAGMDAVDV 185
Cdd:cd01427   92 DIEAARAAGGRTVAV 106
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 93-183 4.63e-12

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: 59.86  E-value: 4.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  93 VEVVKSWHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPTQCVVFED---AD 169
Cdd:cd04305   15 KELLEELKKGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLMVGDsleSD 94

                         90
                 ....*....|....
gi 446195454 170 fgIQAARAAGMDAV 183
Cdd:cd04305   95 --ILGAKNAGIKTV 106
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 7-180 4.96e-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: 61.90  E-value: 4.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   7 GLIFDMDGTILDTEPTHRKAWREVLG------HYGLQYDVQAMIALNGSPTWRIAQaiiELNQADLDpHALAR---EKTE 77
Cdd:cd02588    2 ALVFDVYGTLIDWHSGLAAAERAFPGrgeelsRLWRQKQLEYTWLVTLMGPYVDFD---ELTRDALR-ATAAElglELDE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  78 AVRSMLLDSVEPLPL----VEVVKSWHGRR-PMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCA 152
Cdd:cd02588   78 SDLDELGDAYLRLPPfpdvVAGLRRLREAGyRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAEDVRAYKPAPAVYELAA 157

                        170       180
                 ....*....|....*....|....*...
gi 446195454 153 QRMGVQPTQCVVFEDADFGIQAARAAGM 180
Cdd:cd02588  158 ERLGVPPDEILHVASHAWDLAGARALGL 185
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 7-185 1.14e-11

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 62.19  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   7 GLIFDMDGTILDTEPT-HRKAWREVLGHYG-------LQYDVQAMialngsptwRIAQAIIELNQADLDPHALAREKT-- 76
Cdd:PLN02575 133 GAIFEWEGVIIEDNPDlENQAWLTLAQEEGkspppafILRRVEGM---------KNEQAISEVLCWSRDPAELRRMATrk 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  77 EAVRSMLLDSVEPL-----PLVEVVKswHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLC 151
Cdd:PLN02575 204 EEIYQALQGGIYRLrtgsqEFVNVLM--NYKIPMALVSTRPRKTLENAIGSIGIRGFFSVIVAAEDVYRGKPDPEMFIYA 281

                        170       180       190
                 ....*....|....*....|....*....|....
gi 446195454 152 AQRMGVQPTQCVVFEDADFGIQAARAAGMDAVDV 185
Cdd:PLN02575 282 AQLLNFIPERCIVFGNSNQTVEAAHDARMKCVAV 315
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 7-183 2.87e-11

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: 60.02  E-value: 2.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   7 GLIFDMDGTILDTEPTHRKAWREVLGHYGLQ----YDVQAMIAlNGSPTWrIAQAIIELnQADLDPHAlarekTEAVRSM 82
Cdd:cd07512    1 AVIFDLDGTLIDSAPDLHAALNAVLAAEGLAplslAEVRSFVG-HGAPAL-IRRAFAAA-GEDLDGPL-----HDALLAR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  83 LLDSVEPLPLVE------VVKSWHGRR----PMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCA 152
Cdd:cd07512   73 FLDHYEADPPGLtrpypgVIEALERLRaagwRLAICTNKPEAPARALLSALGLADLFAAVVGGDTLPQRKPDPAPLRAAI 152

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446195454 153 QRMGVQPTQCVVFEDADFGIQAARAAGMDAV 183
Cdd:cd07512  153 RRLGGDVSRALMVGDSETDAATARAAGVPFV 183
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 125-183 1.14e-10

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: 57.74  E-value: 1.14e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446195454 125 LRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPTQCVVFEDADFGIQAARAAGMDAV 183
Cdd:cd02603  124 RGDLFDGVVESCRLGVRKPDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGIHAI 182
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 7-179 1.82e-10

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: 56.64  E-value: 1.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454    7 GLIFDMDGTILDTEPTHRKAWREVL-GHYGLQYDVQAMIA---LNGSPTWRIAQAiiELNQADLDPHALAREKTEAVRSM 82
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFeEFGLDPASFKALKQaggLAEEEWYRIATS--ALEELQGRFWSEYDAEEAYIRGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   83 lldsveplplVEVVKSWHGR-RPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVkHHKPAPDTFLLCAQRMGVqPTQ 161
Cdd:TIGR01549  79 ----------ADLLARLKSAgIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEP-GSKPEPEIFLAALESLGV-PPE 146

                         170
                  ....*....|....*...
gi 446195454  162 CVVFEDADFGIQAARAAG 179
Cdd:TIGR01549 147 VLHVGDNLNDIEGARNAG 164
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 10-180 2.28e-10

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 57.40  E-value: 2.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  10 FDMDGTILDTEPTHRKAWREVLGHYGLQYDVQAMIA-LNGSPTWRIAQAI-----IELNQADLDPHAlareKTEAVRsmL 83
Cdd:PRK10563   9 FDCDGTLVDSEVICSRAYVTMFAEFGITLSLEEVFKrFKGVKLYEIIDIIskehgVTLAKAELEPVY----RAEVAR--L 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  84 LDS-VEPLP----LVEVVKSwhgrrPMAVGTGSESAIAEALLAHLGLRRYF-DAVVAADHVKHHKPAPDTFLLCAQRMGV 157
Cdd:PRK10563  83 FDSeLEPIAganaLLESITV-----PMCVVSNGPVSKMQHSLGKTGMLHYFpDKLFSGYDIQRWKPDPALMFHAAEAMNV 157

                        170       180
                 ....*....|....*....|...
gi 446195454 158 QPTQCVVFEDADFGIQAARAAGM 180
Cdd:PRK10563 158 NVENCILVDDSSAGAQSGIAAGM 180
PRK13226 PRK13226
phosphoglycolate phosphatase; Provisional
 8-183 1.24e-09

phosphoglycolate phosphatase; Provisional


Pssm-ID: 237311 [Multi-domain]  Cd Length: 229  Bit Score: 55.63  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   8 LIFDMDGTILDTEPThrkawrevlghygLQYDVQAMIALNGSPTWRIAQ----------AIIELNQADLD--------PH 69
Cdd:PRK13226  15 VLFDLDGTLLDSAPD-------------MLATVNAMLAARGRAPITLAQlrpvvskgarAMLAVAFPELDaaardaliPE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  70 ALAR-EKTEAVRSMLLDSVEPL--PLVEVVKSWhgrrpmAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPD 146
Cdd:PRK13226  82 FLQRyEALIGTQSQLFDGVEGMlqRLECAGCVW------GIVTNKPEYLARLILPQLGWEQRCAVLIGGDTLAERKPHPL 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446195454 147 TFLLCAQRMGVQPTQCVVFEDADFGIQAARAAGMDAV 183
Cdd:PRK13226 156 PLLVAAERIGVAPTDCVYVGDDERDILAARAAGMPSV 192
YjjG/YfnB TIGR02254
noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including ...
 5-183 2.45e-09

noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including YjjG from E. coli and YfnB from B. subtilis. YjjG has been shown to act as a house-cleaning enzyme, cleaving nucleotides with non-canonical nucleotide bases. This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterized by three conserved sequence motifs. By virtue of an alpha helical domain in-between the first and second conserved motif, this family is a member of subfamily IA (TIGR01549).


Pssm-ID: 162788 [Multi-domain]  Cd Length: 224  Bit Score: 54.80  E-value: 2.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454    5 YAGLIFDMDGTILDTEPTHRKAWREVLGHYGLQY--DVQAMIALNGSPTW----------------RIAQAIIELNqADL 66
Cdd:TIGR02254   1 YKTLLFDLDDTILDFQAAEALALRLLFEDQGIPLteDMFAQYKEINQGLWrayeegkitkdevvntRFSALLKEYN-TEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   67 DPHALAREkteaVRSMLLDSVEPLP-LVEVVKSWHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAP 145
Cdd:TIGR02254  80 DEALLNQK----YLRFLEEGHQLLPgAFELMENLQQKFRLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDK 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 446195454  146 DTFLLCAQRMGvQPTQ---CVVFEDADFGIQAARAAGMDAV 183
Cdd:TIGR02254 156 EIFNYALERMP-KFSKeevLMIGDSLTADIKGGQNAGLDTC 195
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 83-183 3.13e-09

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: 52.68  E-value: 3.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  83 LLDSVEPLPLVEVVKSWHGRR-PMAVGTGSESAIaEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPTQ 161
Cdd:cd16415    3 TFDVTGTLLAVETLKDLKEKGlKLAVVSNFDRRL-RELLEALGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPEE 81

                         90       100
                 ....*....|....*....|...
gi 446195454 162 CV-VFEDADFGIQAARAAGMDAV 183
Cdd:cd16415   82 ALhVGDDLKNDYLGARAVGWHAL 104
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 8-185 8.35e-09

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: 52.79  E-value: 8.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   8 LIFDMDGTILDTEPTHRKAWREVLGHYGL----QYDVQAMIALNgsptwrIAQAIIEL-NQADLDPHALAREKTEAVRSM 82
Cdd:cd07533    2 VIFDWDGTLADSQHNIVAAMTAAFADLGLpvpsAAEVRSIIGLS------LDEAIARLlPMATPALVAVAERYKEAFDIL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  83 LLDSVEPLPL----VEVVKSWHGRRPM-AVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHhKPAPDTFLLCAQRMGV 157
Cdd:cd07533   76 RLLPEHAEPLfpgvREALDALAAQGVLlAVATGKSRRGLDRVLEQHGLGGYFDATRTADDTPS-KPHPEMLREILAELGV 154

                        170       180
                 ....*....|....*....|....*...
gi 446195454 158 QPTQCVVFEDADFGIQAARAAGMDAVDV 185
Cdd:cd07533  155 DPSRAVMVGDTAYDMQMAANAGAHAVGV 182
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 9-181 1.08e-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: 51.99  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   9 IFDMDGTILDTEPTHRKAWREVLGHYGLQYD----VQAMIALNGSPTWRIAQAIIELNQadlDPHALAREKTEAVrsMLL 84
Cdd:cd07523    3 IWDLDGTLLDSYPAMTKALSETLADFGIPQDletvYKIIKESSVQFAIQYYAEVPDLEE---EYKELEAEYLAKP--ILF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  85 DSVEPLplVEVVKSWHGRRPMAVGTGSEsaiAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPTQCVV 164
Cdd:cd07523   78 PGAKAV--LRWIKEQGGKNFLMTHRDHS---ALTILKKDGIASYFTEIVTSDNGFPRKPNPEAINYLLNKYQLNPEETVM 152

                        170
                 ....*....|....*..
gi 446195454 165 FEDADFGIQAARAAGMD 181
Cdd:cd07523  153 IGDRELDIEAGHNAGIS 169
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 104-185 1.63e-08

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: 50.15  E-value: 1.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454 104 PMAVGTGSESAIAEALLAHLGLRRyFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPTQCVVFEDADFGIQAARAAGMDAV 183
Cdd:cd16421   25 KLAVLSNKPNEAVQVLVEELFPGS-FDFVLGEKEGIRRKPDPT*ALECAKVLGVPPDEVLYVGDSGVDMQTARNAGMDEI 103


                 ..
gi 446195454 184 DV 185
Cdd:cd16421  104 GV 105
Pyr-5-nucltdase TIGR01993
pyrimidine 5'-nucleotidase; This family of proteins includes the SDT1/SSM1 gene from yeast ...
 84-183 1.94e-08

pyrimidine 5'-nucleotidase; This family of proteins includes the SDT1/SSM1 gene from yeast which has been shown to code for a pyrimidine (UMP/CMP) 5'nucleotidase. The family spans plants, fungi and a small number of bacteria. These enzymes are members of the haloacid dehalogenase (HAD) superfamily of hydrolases, specifically the IA subfamily (variant 3, TIGR01509).


Pssm-ID: 273917 [Multi-domain]  Cd Length: 183  Bit Score: 51.58  E-value: 1.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   84 LDSVEPLP-LVEVVKSWHGRRpmAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHH---KPAPDTFLLCAQRMGVQP 159
Cdd:TIGR01993  80 YDKLKPDPeLRNLLLRLPGRK--IIFTNGDRAHARRALRRLGIEDCFDGIFCFDTANPDllpKPSPQAYEKALREAGVDP 157

                          90       100
                  ....*....|....*....|....
gi 446195454  160 TQCVVFEDADFGIQAARAAGMDAV 183
Cdd:TIGR01993 158 ERAIFFDDSARNIAAGKALGMKTV 181
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 5-186 2.20e-08

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: 51.57  E-value: 2.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454    5 YAGLIFDMDGTILDTEPTHRKAWREVLGhyglqyDVQAMIALngsptWRIAQ----AIIELNQA-----DLDPHALAR-- 73
Cdd:TIGR01428   1 IKALVFDVYGTLFDVHSVAERAAELYGG------RGEALSQL-----WRQKQleysWLRTLMGPykdfwDLTREALRYll 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   74 -----EKTEAVRSMLLDSVEPL-PLVEVVKSWHGRRPM----AVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKP 143
Cdd:TIGR01428  70 grlglEDDESAADRLAEAYLRLpPHPDVPAGLRALKERgyrlAILSNGSPAMLKSLVKHAGLDDPFDAVLSADAVRAYKP 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 446195454  144 APDTFLLCAQRMGVQPTQcVVFEDADFG-IQAARAAGMDAVDVR 186
Cdd:TIGR01428 150 APQVYQLALEALGVPPDE-VLFVASNPWdLGGAKKFGFKTAWIN 192
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 8-179 2.41e-08

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 51.57  E-value: 2.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   8 LIFDMDGTILDTEPTHRKAWREVLGHY-GLQYDVQAMIALNGSPTWRIAQAIielnqadlDPhalarEKTEAVRSMLL-- 84
Cdd:PRK13288   6 VLFDLDGTLINTNELIISSFLHTLKTYyPNQYKREDVLPFIGPSLHDTFSKI--------DE-----SKVEEMITTYRef 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  85 ------DSVEPLPLV-EVVKSWHGRR-PMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMG 156
Cdd:PRK13288  73 nhehhdELVTEYETVyETLKTLKKQGyKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPDPEPVLKALELLG 152

                        170       180
                 ....*....|....*....|...
gi 446195454 157 VQPTQCVVFEDADFGIQAARAAG 179
Cdd:PRK13288 153 AKPEEALMVGDNHHDILAGKNAG 175
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 8-186 1.64e-06

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: 46.43  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   8 LIFDMDGTILDTEPTHRKAWREVLGHYGLQY-DVQAMIALNGSPtwrIAQAIIELNQADLDphaLAREKTEAVRS----- 81
Cdd:cd04302    2 ILFDLDGTLTDSAEGITASVQYALEELGIPVpDESELRRFIGPP---LEDSFRELLPFDEE---EAQRAVDAYREyykek 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  82 -MLLDSVEP--LPLVEVVKSwHGRRpMAVGTGSESAIAEALLAHLGLRRYFDAVVAA--DHVKHHKPAPDTFLLcaQRMG 156
Cdd:cd04302   76 gLFENEVYPgiPELLEKLKA-AGYR-LYVATSKPEVFARRILEHFGLDEYFDGIAGAslDGSRVHKADVIRYAL--DTLG 151

                        170       180       190
                 ....*....|....*....|....*....|
gi 446195454 157 VQPTQCVVFEDADFGIQAARAAGMDAVDVR 186
Cdd:cd04302  152 IAPEQAVMIGDRKHDIIGARANGIDSIGVL 181
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 83-186 4.39e-06

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: 44.93  E-value: 4.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  83 LLDSVEPLP-LVEVVKSWHGRRpmAVGTGSESAIAEALLAHLGLRRYFDAVVA-ADHVKHHKPAPDTFLLCAQRMGVQPT 160
Cdd:cd02604   78 LYDHLKPDPkLRNLLLALPGRK--IIFTNASKNHAIRVLKRLGLADLFDGIFDiEYAGPDPKPHPAAFEKAIREAGLDPK 155

                         90       100
                 ....*....|....*....|....*.
gi 446195454 161 QCVVFEDADFGIQAARAAGMDAVDVR 186
Cdd:cd02604  156 RAAFFDDSIRNLLAAKALGMKTVLVG 181
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
 8-183 3.34e-05

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 42.93  E-value: 3.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   8 LIFDMDGTILDTEPTHRKAWREVLGHYGLQ----YDVQAMIAlNGSPTW--RIAQAIIELNQAD--LDPHALAREKTEAV 79
Cdd:PRK13223  16 VMFDLDGTLVDSVPDLAAAVDRMLLELGRPpaglEAVRHWVG-NGAPVLvrRALAGSIDHDGVDdeLAEQALALFMEAYA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  80 RSMLLDSVEPlPLVEVVKsWHGRR--PMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGV 157
Cdd:PRK13223  95 DSHELTVVYP-GVRDTLK-WLKKQgvEMALITNKPERFVAPLLDQMKIGRYFRWIIGGDTLPQKKPDPAALLFVMKMAGV 172

                        170       180
                 ....*....|....*....|....*.
gi 446195454 158 QPTQCVVFEDADFGIQAARAAGMDAV 183
Cdd:PRK13223 173 PPSQSLFVGDSRSDVLAAKAAGVQCV 198
Hydrolase_like pfam13242
HAD-hyrolase-like;
142-186 8.95e-04

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 36.44  E-value: 8.95e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 446195454  142 KPAPDTFLLCAQRMGVQPTQCVVFED-ADFGIQAARAAGMDAVDVR 186
Cdd:pfam13242   4 KPNPGMLERALARLGLDPERTVMIGDrLDTDILGAREAGARTILVL 49
PRK13478 PRK13478
phosphonoacetaldehyde hydrolase; Provisional
 7-185 2.29e-03

phosphonoacetaldehyde hydrolase; Provisional


Pssm-ID: 184075 [Multi-domain]  Cd Length: 267  Bit Score: 37.53  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454   7 GLIFDMDGTILD---TEPTHrkAWREVLGHYGLQYDVQAMIALNGSPTW----------RIAQAIIELNQA---DLDPHA 70
Cdd:PRK13478   6 AVIFDWAGTTVDfgsFAPTQ--AFVEAFAQFGVEITLEEARGPMGLGKWdhirallkmpRVAARWQAVFGRlptEADVDA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  71 LAREKTEAVRSMLLDSVEPLP-LVEVVkSWHGRRPMAVG--TGSESAIAEALLAHLGLRRYF-DAVVAADHVKHHKPAPD 146
Cdd:PRK13478  84 LYAAFEPLQIAKLADYATPIPgVLEVI-AALRARGIKIGstTGYTREMMDVVVPLAAAQGYRpDHVVTTDDVPAGRPYPW 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446195454 147 TFLLCAQRMGVQPTQ-CVVFEDADFGIQAARAAGMDAVDV 185
Cdd:PRK13478 163 MALKNAIELGVYDVAaCVKVDDTVPGIEEGLNAGMWTVGV 202
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 142-186 3.75e-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: 36.87  E-value: 3.75e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446195454 142 KPAPDTFLLCAQRMGVQPTQCVVF-EDADFGIQAARAAGMDAVDVR 186
Cdd:cd07509  172 KPSPEFFLSALRSLGVDPEEAVMIgDDLRDDVGGAQACGMRGILVR 217
PRK09449 PRK09449
dUMP phosphatase; Provisional
 88-181 3.76e-03

dUMP phosphatase; Provisional


Pssm-ID: 181865 [Multi-domain]  Cd Length: 224  Bit Score: 36.80  E-value: 3.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446195454  88 EPLP-LVEVVKSWHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPTQCV--V 164
Cdd:PRK09449  95 TPLPgAVELLNALRGKVKMGIITNGFTELQQVRLERTGLRDYFDLLVISEQVGVAKPDVAIFDYALEQMGNPDRSRVlmV 174

                         90
                 ....*....|....*..
gi 446195454 165 FEDADFGIQAARAAGMD 181
Cdd:PRK09449 175 GDNLHSDILGGINAGID 191
PRK08238 PRK08238
UbiA family prenyltransferase;
62-136 5.46e-03

UbiA family prenyltransferase;


Pssm-ID: 236195 [Multi-domain]  Cd Length: 479  Bit Score: 36.78  E-value: 5.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446195454  62 NQADLDPHAL-AREkteavrsmlldsveplPLVEVVKSWHGR-RPMAVGTGSESAIAEALLAHLGLrryFDAVVAAD 136
Cdd:PRK08238  62 RRVDLDVATLpYNE----------------EVLDYLRAERAAgRKLVLATASDERLAQAVAAHLGL---FDGVFASD 119
 
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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