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Conserved domains on  [gi|891174165|ref|WP_048917104|]
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MULTISPECIES: fructose-1-phosphate/6-phosphogluconate phosphatase [Erwinia]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
1-188 2.93e-141

fructose-1-phosphate/6-phosphogluconate phosphatase;


:

Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 390.97  E-value: 2.93e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   1 MYDAYDGLIFDMDGTILDTEPTHRKAWHQVLAQYGMTFDETAIIGLNGSPTWRIAQVIIANHHSDLDPHRLAAEKTALLK 80
Cdd:PRK10725   1 MYDRYAGLIFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVALNGSPTWRIAQAIIELNQADLDPHALAREKTEAVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  81 TMLFDTVQPLPLIDVVKSYKGRRPMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAA 160
Cdd:PRK10725  81 SMLLDSVEPLPLIEVVKAWHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADDVQHHKPAPDTFLRCAQLMGVQPT 160

                        170       180
                 ....*....|....*....|....*...
gi 891174165 161 RCVVFEDADFGIQAAKAAGMDAVDVRLL 188
Cdd:PRK10725 161 QCVVFEDADFGIQAARAAGMDAVDVRLL 188
 
Name Accession Description Interval E-value
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
1-188 2.93e-141

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 390.97  E-value: 2.93e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   1 MYDAYDGLIFDMDGTILDTEPTHRKAWHQVLAQYGMTFDETAIIGLNGSPTWRIAQVIIANHHSDLDPHRLAAEKTALLK 80
Cdd:PRK10725   1 MYDRYAGLIFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVALNGSPTWRIAQAIIELNQADLDPHALAREKTEAVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  81 TMLFDTVQPLPLIDVVKSYKGRRPMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAA 160
Cdd:PRK10725  81 SMLLDSVEPLPLIEVVKAWHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADDVQHHKPAPDTFLRCAQLMGVQPT 160

                        170       180
                 ....*....|....*....|....*...
gi 891174165 161 RCVVFEDADFGIQAAKAAGMDAVDVRLL 188
Cdd:PRK10725 161 QCVVFEDADFGIQAARAAGMDAVDVRLL 188
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 5-185 1.73e-70

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: 211.82  E-value: 1.73e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165    5 YDGLIFDMDGTILDTEPTHRKAWHQVLAQYGMTFDETAIIGLNGSPTWRIAQVIIANHHSDLDP---HRLAAEKTALLKT 81
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDGLSLeeiHQLAERKNELYRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   82 MLFDT-VQPLPLIDVVKSYKGRRPMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAA 160
Cdd:TIGR02009  81 LLRLTgVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRDYFDAIVDASEVKNGKPHPETFLLAAELLGVPPN 160

                         170       180
                  ....*....|....*....|....*
gi 891174165  161 RCVVFEDADFGIQAAKAAGMDAVDV 185
Cdd:TIGR02009 161 ECIVFEDALAGVQAARAAGMFAVAV 185
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
5-185 2.75e-62

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 191.58  E-value: 2.75e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   5 YDGLIFDMDGTILDTEPTHRKAWHQVLAQYGMTFDETAIIGLNGSPTWRIAQVIIANHHSDLDPHRLAAEKTALLKTMLF 84
Cdd:COG0637    2 IKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYRELLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  85 DT-VQPLP-LIDVVKSYKGRR-PMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAAR 161
Cdd:COG0637   82 EEgLPLIPgVVELLEALKEAGiKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERLGVDPEE 161

                        170       180
                 ....*....|....*....|....
gi 891174165 162 CVVFEDADFGIQAAKAAGMDAVDV 185
Cdd:COG0637  162 CVVFEDSPAGIRAAKAAGMRVVGV 185
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 7-186 6.82e-40

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: 132.35  E-value: 6.82e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   7 GLIFDMDGTILDTEPTHRKAWhqvlaqygmtfdetaiiglngsptwriaqviianhhsdldphRLAAEKTALLKTMLFDT 86
Cdd:cd07505    1 AVIFDMDGVLIDTEPLHRQAW------------------------------------------QLLERKNALLLELIASE 38

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  87 VQPL--PLIDVVKSYKGRR-PMAVGTGSEHAMAV-GLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAARC 162
Cdd:cd07505   39 GLKLkpGVVELLDALKAAGiPVAVATSSSRRNVElLLLELGLLRGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERC 118

                        170       180
                 ....*....|....*....|....
gi 891174165 163 VVFEDADFGIQAAKAAGMDAVDVR 186
Cdd:cd07505  119 LVFEDSLAGIEAAKAAGMTVVAVP 142
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
8-185 2.06e-31

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 111.91  E-value: 2.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165    8 LIFDMDGTILDTEPTHRKAWHQVLAQYGM-TFDETAIIGLNGSPTWRIAQVIIANHHSDLDPHRLAAE-KTALLKtmlfD 85
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYgELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFYLRKyNEELHD----K 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   86 TVQPLP-LIDVVKSYKGRR-PMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAARCV 163
Cdd:pfam13419  77 LVKPYPgIKELLEELKEQGyKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVI 156

                         170       180
                  ....*....|....*....|..
gi 891174165  164 VFEDADFGIQAAKAAGMDAVDV 185
Cdd:pfam13419 157 YVGDSPRDIEAAKNAGIKVIAV 178
 
Name Accession Description Interval E-value
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
1-188 2.93e-141

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 390.97  E-value: 2.93e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   1 MYDAYDGLIFDMDGTILDTEPTHRKAWHQVLAQYGMTFDETAIIGLNGSPTWRIAQVIIANHHSDLDPHRLAAEKTALLK 80
Cdd:PRK10725   1 MYDRYAGLIFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVALNGSPTWRIAQAIIELNQADLDPHALAREKTEAVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  81 TMLFDTVQPLPLIDVVKSYKGRRPMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAA 160
Cdd:PRK10725  81 SMLLDSVEPLPLIEVVKAWHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADDVQHHKPAPDTFLRCAQLMGVQPT 160

                        170       180
                 ....*....|....*....|....*...
gi 891174165 161 RCVVFEDADFGIQAAKAAGMDAVDVRLL 188
Cdd:PRK10725 161 QCVVFEDADFGIQAARAAGMDAVDVRLL 188
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 5-185 1.73e-70

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: 211.82  E-value: 1.73e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165    5 YDGLIFDMDGTILDTEPTHRKAWHQVLAQYGMTFDETAIIGLNGSPTWRIAQVIIANHHSDLDP---HRLAAEKTALLKT 81
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDGLSLeeiHQLAERKNELYRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   82 MLFDT-VQPLPLIDVVKSYKGRRPMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAA 160
Cdd:TIGR02009  81 LLRLTgVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRDYFDAIVDASEVKNGKPHPETFLLAAELLGVPPN 160

                         170       180
                  ....*....|....*....|....*
gi 891174165  161 RCVVFEDADFGIQAAKAAGMDAVDV 185
Cdd:TIGR02009 161 ECIVFEDALAGVQAARAAGMFAVAV 185
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
5-185 2.75e-62

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 191.58  E-value: 2.75e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   5 YDGLIFDMDGTILDTEPTHRKAWHQVLAQYGMTFDETAIIGLNGSPTWRIAQVIIANHHSDLDPHRLAAEKTALLKTMLF 84
Cdd:COG0637    2 IKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYRELLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  85 DT-VQPLP-LIDVVKSYKGRR-PMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAAR 161
Cdd:COG0637   82 EEgLPLIPgVVELLEALKEAGiKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERLGVDPEE 161

                        170       180
                 ....*....|....*....|....
gi 891174165 162 CVVFEDADFGIQAAKAAGMDAVDV 185
Cdd:COG0637  162 CVVFEDSPAGIRAAKAAGMRVVGV 185
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 7-186 6.82e-40

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: 132.35  E-value: 6.82e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   7 GLIFDMDGTILDTEPTHRKAWhqvlaqygmtfdetaiiglngsptwriaqviianhhsdldphRLAAEKTALLKTMLFDT 86
Cdd:cd07505    1 AVIFDMDGVLIDTEPLHRQAW------------------------------------------QLLERKNALLLELIASE 38

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  87 VQPL--PLIDVVKSYKGRR-PMAVGTGSEHAMAV-GLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAARC 162
Cdd:cd07505   39 GLKLkpGVVELLDALKAAGiPVAVATSSSRRNVElLLLELGLLRGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERC 118

                        170       180
                 ....*....|....*....|....
gi 891174165 163 VVFEDADFGIQAAKAAGMDAVDVR 186
Cdd:cd07505  119 LVFEDSLAGIEAAKAAGMTVVAVP 142
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 8-186 7.43e-36

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: 123.13  E-value: 7.43e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   8 LIFDMDGTILDTEPTHRKAWHQVLAQYgmtfdetaiiglngsptwriaqviianhhsdlDPHRLAAektallktmLFDTV 87
Cdd:cd16423    2 VIFDFDGVIVDTEPLWYEAWQELLNER--------------------------------RNELIKR---------QFSEK 40

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  88 QPLPLIDVVKSY----KGRR-PMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAARC 162
Cdd:cd16423   41 TDLPPIEGVKELleflKEKGiKLAVASSSPRRWIEPHLERLGLLDYFEVIVTGDDVEKSKPDPDLYLEAAERLGVNPEEC 120

                        170       180
                 ....*....|....*....|....
gi 891174165 163 VVFEDADFGIQAAKAAGMDAVDVR 186
Cdd:cd16423  121 VVIEDSRNGVLAAKAAGMKCVGVP 144
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
5-183 6.52e-34

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 119.26  E-value: 6.52e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   5 YDGLIFDMDGTILDTEPTHRKAWHQVLAQYGM-TFDETAIIGLNGSPTWRIAQVIIANHHSDLDPhRLAAEKTALLKTML 83
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLpPLDLEELRALIGLGLRELLRRLLGEDPDEELE-ELLARFRELYEEEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  84 FDTVQPLPLI-DVVKSYKGRR-PMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAAR 161
Cdd:COG0546   80 LDETRLFPGVrELLEALKARGiKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLDPEE 159

                        170       180
                 ....*....|....*....|..
gi 891174165 162 CVVFEDADFGIQAAKAAGMDAV 183
Cdd:COG0546  160 VLMVGDSPHDIEAARAAGVPFI 181
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 7-185 1.34e-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: 115.10  E-value: 1.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165    7 GLIFDMDGTILDTEPTHRKAWHQVLAQYGMTFDETAIIGLNGSPTWRIAQVIIANHHSDLDPHR---LAAEKT----ALL 79
Cdd:TIGR01990   1 AVIFDLDGVITDTAEYHYLAWKHLADELGIPFDEEFNESLKGVSREESLERILDLGGKKYSEEEkeeLAERKNdyyvELL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   80 KTMLFDTVQP--LPLIDVVKSYKgrRPMAVGTGSEHAMAVglLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGV 157
Cdd:TIGR01990  81 KELTPADVLPgiKSLLADLKKNN--IKIALASASKNAPTI--LEKLELIDYFDAIVDPAELKKGKPDPEIFLAAAEGLGV 156

                         170       180
                  ....*....|....*....|....*...
gi 891174165  158 PAARCVVFEDADFGIQAAKAAGMDAVDV 185
Cdd:TIGR01990 157 SPSECIGIEDAQAGIEAIKAAGMFAVGV 184
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 7-185 1.73e-32

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: 115.52  E-value: 1.73e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   7 GLIFDMDGTILDTEPTHRKAWHQVLAQYGMTFDETAIIgLNGsptWRIAQVIIANHHSDLDPHRLAAEKTALLKTMLfDT 86
Cdd:cd07527    1 ALLFDMDGTLVDSTPAVERAWHKWAKEHGVDPEEVLKV-SHG---RRAIDVIRKLAPDDADIELVLALETEEPESYP-EG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  87 VQPLP----LIDVVKSYKGRrpMAVGTGSEHAMAVGLLQHLGLlAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAARC 162
Cdd:cd07527   76 VIAIPgavdLLASLPAAGDR--WAIVTSGTRALAEARLEAAGL-PHPEVLVTADDVKNGKPDPEPYLLGAKLLGLDPSDC 152

                        170       180
                 ....*....|....*....|...
gi 891174165 163 VVFEDADFGIQAAKAAGMDAVDV 185
Cdd:cd07527  153 VVFEDAPAGIKAGKAAGARVVAV 175
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
8-185 2.06e-31

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 111.91  E-value: 2.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165    8 LIFDMDGTILDTEPTHRKAWHQVLAQYGM-TFDETAIIGLNGSPTWRIAQVIIANHHSDLDPHRLAAE-KTALLKtmlfD 85
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYgELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFYLRKyNEELHD----K 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   86 TVQPLP-LIDVVKSYKGRR-PMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAARCV 163
Cdd:pfam13419  77 LVKPYPgIKELLEELKEQGyKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVI 156

                         170       180
                  ....*....|....*....|..
gi 891174165  164 VFEDADFGIQAAKAAGMDAVDV 185
Cdd:pfam13419 157 YVGDSPRDIEAAKNAGIKVIAV 178
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 8-185 1.01e-28

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: 105.51  E-value: 1.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   8 LIFDMDGTILDTEPTHRKAWHQVLAQYGMTFDETAIIGLNGSPTWRIAQVIIANHHSDLDPHRLAAEKTALLKTMLFDTV 87
Cdd:cd07529    4 CIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLEEEFDEQQEALAELFMGTA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  88 QPLP----LIDVVKSYkgRRPMAVGTGSEHAM-AVGLLQHLGLLAHFDAIVGADD---VKRHKPEPDTFLRCAELIGVPA 159
Cdd:cd07529   84 KLMPgaerLLRHLHAH--NIPIALATSSCTRHfKLKTSRHKELFSLFHHVVTGDDpevKGRGKPAPDIFLVAAKRFNEPP 161

                        170       180
                 ....*....|....*....|....*....
gi 891174165 160 A---RCVVFEDADFGIQAAKAAGMDAVDV 185
Cdd:cd07529  162 KdpsKCLVFEDSPNGVKAAKAAGMQVVMV 190
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 5-179 1.41e-24

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: 94.58  E-value: 1.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165    5 YDGLIFDMDGTILDTEPTHRKAWHQV-------------LAQYGMTFDETAIIGLNGSPTWRIAQVIIANHHSDL-DPHR 70
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELasehplakaivaaAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLeAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   71 LAAEKTALLKTMLFDTVQPLP-LIDVVKSYKGRR-PMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTF 148
Cdd:pfam00702  81 TVVLVELLGVIALADELKLYPgAAEALKALKERGiKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIY 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 891174165  149 LRCAELIGVPAARCVVFEDADFGIQAAKAAG 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 1.44e-23

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: 91.71  E-value: 1.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165    8 LIFDMDGTILDTEPTHRKawhQVLAQYGMTFDETAIIGLNGSPTWRIAQvIIANHHSDLDPHRLAAEKTALLKTMLFD-- 85
Cdd:TIGR01509   2 ILFDLDGVLVDTEFAIAK---LINREELGLVPDELGVSAVGRLELALRR-FKAQYGRTISPEDAQLLYKQLFYEQIEEea 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   86 TVQPLP-LIDVVKSYKGR-RPMAVGTGSEHAMAVGLLqHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAARCV 163
Cdd:TIGR01509  78 KLKPLPgVRALLEALRARgKKLALLTNSPRAHKLVLA-LLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLEPSECV 156

                         170       180
                  ....*....|....*....|
gi 891174165  164 VFEDADFGIQAAKAAGMDAV 183
Cdd:TIGR01509 157 FVDDSPAGIEAAKAAGMHTV 176
PLN02811 PLN02811
hydrolase
 12-185 1.30e-22

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 90.20  E-value: 1.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  12 MDGTILDTEPTHRKAWHQVLAQYGMTFDETAIIGLNGSPTWRIAQVIIanHHSDLD----PHRLAAEKTALLKtMLFDTV 87
Cdd:PLN02811   1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFV--EESGLSdslsPEDFLVEREAMLQ-DLFPTS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  88 QPLPLID-VVKSYKGRR-PMAVGTGS-EHAMAVGLLQHLGLLAHFDAIVGADD--VKRHKPEPDTFLRCA---ELIGVPA 159
Cdd:PLN02811  78 DLMPGAErLVRHLHAKGiPIAIATGShKRHFDLKTQRHGELFSLMHHVVTGDDpeVKQGKPAPDIFLAAArrfEDGPVDP 157

                        170       180
                 ....*....|....*....|....*.
gi 891174165 160 ARCVVFEDADFGIQAAKAAGMDAVDV 185
Cdd:PLN02811 158 GKVLVFEDAPSGVEAAKNAGMSVVMV 183
PLN02940 PLN02940
riboflavin kinase
 8-185 6.79e-22

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 91.05  E-value: 6.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   8 LIFDMDGTILDTEPTHRKAWHQVLAQYGMTFDETAIIGLNGSPTWRIAQVIIANHHSDLDPHRLAAEKTALLKTmLFDTV 87
Cdd:PLN02940  14 VILDLDGTLLNTDGIVSDVLKAFLVKYGKQWDGREAQKIVGKTPLEAAATVVEDYGLPCSTDEFNSEITPLLSE-QWCNI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  88 QPLP----LIDVVKSYKgrRPMAVGTGSEHA-MAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAARC 162
Cdd:PLN02940  93 KALPganrLIKHLKSHG--VPMALASNSPRAnIEAKISCHQGWKESFSVIVGGDEVEKGKPSPDIFLEAAKRLNVEPSNC 170

                        170       180
                 ....*....|....*....|...
gi 891174165 163 VVFEDADFGIQAAKAAGMDAVDV 185
Cdd:PLN02940 171 LVIEDSLPGVMAGKAAGMEVIAV 193
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 7-185 2.57e-21

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: 85.81  E-value: 2.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   7 GLIFDMDGTILDTEPTHRKAWHQVLaqygmtfdetaiiglngsptwriaqviianhhsdlDPHRLAAEKT----ALLKTM 82
Cdd:cd02598    1 GVIFDLDGVITDTAEYHYRAWKKLA-----------------------------------DKEELAARKNriyvELIEEL 45

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  83 LFDTVQP--LPLIDVVKSykgrRPMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAA 160
Cdd:cd02598   46 TPVDVLPgiASLLVDLKA----KGIKIALASASKNAPKILEKLGLAEYFDAIVDGAVLAKGKPDPDIFLAAAEGLGLNPK 121

                        170       180
                 ....*....|....*....|....*
gi 891174165 161 RCVVFEDADFGIQAAKAAGMDAVDV 185
Cdd:cd02598  122 DCIGVEDAQAGIRAIKAAGFLVVGV 146
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 6-181 8.03e-21

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: 83.52  E-value: 8.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   6 DGLIFDMDGTILDTEPTHRKAWHQVLAQYGMTfdetaiiglngsptwriaqviianhhsdldphRLAAektallktmlFD 85
Cdd:cd07526    1 DLVIFDCDGVLVDSEVIAARVLVEVLAELGAR--------------------------------VLAA----------FE 38

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  86 T-VQPLPLIDVVKSYKGRrPMAVGT-GSEHAMAVGLLQHlGLLAHFDA-IVGADDVKRHKPEPDTFLRCAELIGVPAARC 162
Cdd:cd07526   39 AeLQPIPGAAAALSALTL-PFCVASnSSRERLTHSLGLA-GLLAYFEGrIFSASDVGRGKPAPDLFLHAAAQMGVAPERC 116

                        170
                 ....*....|....*....
gi 891174165 163 VVFEDADFGIQAAKAAGMD 181
Cdd:cd07526  117 LVIEDSPTGVRAALAAGMT 135
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 3-180 1.03e-20

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 86.69  E-value: 1.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   3 DAYDGLIFDMDGTILDTEPT-HRKAWHQVLAQYGMT--------FDETAIIG-----------LNGSPTWRIAQVIianh 62
Cdd:PLN02779  38 ALPEALLFDCDGVLVETERDgHRVAFNDAFKEFGLRpvewdvelYDELLNIGggkermtwyfnENGWPTSTIEKAP---- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  63 HSDLDPHRLAAE----KTALLKTMLFD-TVQPLP----LIDVVKSyKGRRpMAVGTGSEHAMAVGLLQHL---GLLAHFD 130
Cdd:PLN02779 114 KDEEERKELVDSlhdrKTELFKELIESgALPLRPgvlrLMDEALA-AGIK-VAVCSTSNEKAVSKIVNTLlgpERAQGLD 191

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 891174165 131 AIVGaDDVKRHKPEPDTFLRCAELIGVPAARCVVFEDADFGIQAAKAAGM 180
Cdd:PLN02779 192 VFAG-DDVPKKKPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAAKAAGM 240
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 5-183 1.61e-20

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: 84.69  E-value: 1.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   5 YDGLIFDMDGTILDTEPTHRKAWHQVLAQYGMTFDETAIIGLNGSPTWRIAQVIIANHHSDLD---------PHRLAAEK 75
Cdd:COG1011    1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAEAYRAIEYALWRRYERGEITFAEllrrlleelGLDLAEEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  76 TALLKTMLFDTVQPLP-LIDVVKSYKGR-RPMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAE 153
Cdd:COG1011   81 AEAFLAALPELVEPYPdALELLEALKARgYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIFELALE 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 891174165 154 LIGVPAARCVVFED---ADfgIQAAKAAGMDAV 183
Cdd:COG1011  161 RLGVPPEEALFVGDspeTD--VAGARAAGMRTV 191
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 8-180 2.03e-20

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: 83.97  E-value: 2.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   8 LIFDMDGTILDTEPTHRKAW-HQVLAQYGMT-------FDETAIIGLNGSPtwriaqviIANHHSDLDPHRLA----AEK 75
Cdd:cd07528    2 LIFDVDGTLAETEELHRRAFnNAFFAERGLDwywdrelYGELLRVGGGKER--------IAAYFEKVGWPESApkdlKEL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  76 TALL---KTMLFDT------VQPLP----LIDVVKSyKGRRpMAVGTGSEHAMAVGLLQhlGLLAH-----FDAIVGADD 137
Cdd:cd07528   74 IADLhkaKTERYAEliaaglLPLRPgvarLIDEAKA-AGVR-LAIATTTSPANVDALLS--ALLGPerraiFDAIAAGDD 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 891174165 138 VKRHKPEPDTFLRCAELIGVPAARCVVFEDADFGIQAAKAAGM 180
Cdd:cd07528  150 VAEKKPDPDIYLLALERLGVSPSDCLAIEDSAIGLQAAKAAGL 192
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 7-185 3.38e-19

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 84.52  E-value: 3.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165    7 GLIFDMDGTILDTEPTHRKAWHQVLAQYGMTFDETAIIGLNGSPTWR-IAQVIIANHHSDLDPhrlAAEKTALLKTMLFD 85
Cdd:PLN02919   77 AVLFDMDGVLCNSEEPSRRAAVDVFAEMGVEVTVEDFVPFMGTGEANfLGGVASVKGVKGFDP---DAAKKRFFEIYLEK 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   86 TVQP---------LPLIDVVKSyKGRRpMAVGTGSEHAMAVGLLQHLGL-LAHFDAIVGADDVKRHKPEPDTFLRCAELI 155
Cdd:PLN02919  154 YAKPnsgigfpgaLELITQCKN-KGLK-VAVASSADRIKVDANLAAAGLpLSMFDAIVSADAFENLKPAPDIFLAAAKIL 231

                         170       180       190
                  ....*....|....*....|....*....|
gi 891174165  156 GVPAARCVVFEDADFGIQAAKAAGMDAVDV 185
Cdd:PLN02919  232 GVPTSECVVIEDALAGVQAARAAGMRCIAV 261
PRK10826 PRK10826
hexitol phosphatase HxpB;
9-185 1.97e-18

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 79.22  E-value: 1.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   9 IFDMDGTILDTEPTHRKAWHQVLAQYGM--TFDETA--IIGLngsptwRIAQVIIANHH----SDLDPHRLAAEKTALLK 80
Cdd:PRK10826  11 IFDMDGLLIDSEPLWDRAELDVMASLGVdiSRREELpdTLGL------RIDQVVDLWYArqpwNGPSRQEVVQRIIARVI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  81 TMLFDTVQPLPLIDVVKSYKGRRPMAVG--TGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVP 158
Cdd:PRK10826  85 SLIEETRPLLPGVREALALCKAQGLKIGlaSASPLHMLEAVLTMFDLRDYFDALASAEKLPYSKPHPEVYLNCAAKLGVD 164

                        170       180
                 ....*....|....*....|....*..
gi 891174165 159 AARCVVFEDADFGIQAAKAAGMDAVDV 185
Cdd:PRK10826 165 PLTCVALEDSFNGMIAAKAARMRSIVV 191
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
7-186 4.99e-16

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 72.92  E-value: 4.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   7 GLIFDMDGTILDTEPTHRKAWHQVLAQYGM-TFDETAIIGL--NGSPtwRIAQVIIANHHSDLDPHRLAA---------E 74
Cdd:PRK13222   8 AVAFDLDGTLVDSAPDLAAAVNAALAALGLpPAGEERVRTWvgNGAD--VLVERALTWAGREPDEELLEKlrelfdrhyA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  75 KTALLKTMLFDTVqplplIDVVKSYKGRR-PMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAE 153
Cdd:PRK13222  86 ENVAGGSRLYPGV-----KETLAALKAAGyPLAVVTNKPTPFVAPLLEALGIADYFSVVIGGDSLPNKKPDPAPLLLACE 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 891174165 154 LIGVPAARCVVFEDADFGIQAAKAAGMDAVDVR 186
Cdd:PRK13222 161 KLGLDPEEMLFVGDSRNDIQAARAAGCPSVGVT 193
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 7-186 9.10e-16

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: 71.88  E-value: 9.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   7 GLIFDMDGTILDTEPTHRKAWHQVLAQYGM-TFDETAI---IGlNGSPTWrIAQVIIANHHSDLDPHRLAA--------- 73
Cdd:cd16417    1 LVAFDLDGTLVDSAPDLAEAANAMLAALGLpPLPEETVrtwIG-NGADVL-VERALTGAREAEPDEELFKEaralfdrhy 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  74 EKTALLKTMLFDTVQplpliDVVKSYK-GRRPMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCA 152
Cdd:cd16417   79 AETLSVHSHLYPGVK-----EGLAALKaQGYPLACVTNKPERFVAPLLEALGISDYFSLVLGGDSLPEKKPDPAPLLHAC 153

                        170       180       190
                 ....*....|....*....|....*....|....
gi 891174165 153 ELIGVPAARCVVFEDADFGIQAAKAAGMDAVDVR 186
Cdd:cd16417  154 EKLGIAPAQMLMVGDSRNDILAARAAGCPSVGLT 187
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 10-180 1.40e-15

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 71.65  E-value: 1.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  10 FDMDGTILDTEPTHRKAWHQVLAQYGMTFDETAIIG-LNGSPTWRIAQVIIANHH-----SDLDPHRLAAEKTallktmL 83
Cdd:PRK10563   9 FDCDGTLVDSEVICSRAYVTMFAEFGITLSLEEVFKrFKGVKLYEIIDIISKEHGvtlakAELEPVYRAEVAR------L 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  84 FDT-VQPLP----LIDVVKSykgrrPMAV---GTGSEHAMAVGLLqhlGLLAHF-DAIVGADDVKRHKPEPDTFLRCAEL 154
Cdd:PRK10563  83 FDSeLEPIAganaLLESITV-----PMCVvsnGPVSKMQHSLGKT---GMLHYFpDKLFSGYDIQRWKPDPALMFHAAEA 154

                        170       180
                 ....*....|....*....|....*.
gi 891174165 155 IGVPAARCVVFEDADFGIQAAKAAGM 180
Cdd:PRK10563 155 MNVNVENCILVDDSSAGAQSGIAAGM 180
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 5-185 8.51e-15

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: 69.23  E-value: 8.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   5 YDGLIFDMDGTILDTEPTHRKAWHQVLAQYGMT-FDETAIIGLNGSPTWRIAQVIIANHHSD-LDPHRLAAEKTALLKTM 82
Cdd:cd02616    1 ITTILFDLDGTLIDTNELIIKSFNHTLKEYGLEgYTREEVLPFIGPPLRETFEKIDPDKLEDmVEEFRKYYREHNDDLTK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  83 LFDTVqpLPLIDVVKSyKGRRpMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAARC 162
Cdd:cd02616   81 EYPGV--YETLARLKS-QGIK-LGVVTTKLRETALKGLKLLGLDKYFDVIVGGDDVTHHKPDPEPVLKALELLGAEPEEA 156

                        170       180
                 ....*....|....*....|...
gi 891174165 163 VVFEDADFGIQAAKAAGMDAVDV 185
Cdd:cd02616  157 LMVGDSPHDILAGKNAGVKTVGV 179
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 6-183 1.21e-14

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 69.48  E-value: 1.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   6 DGLIFDMDGTILDTEPTHRKAWHQVLAQY----GMTFDETAII-GLNGSPTWRIAQVIIANhhsDLDPH-RLAAEKTALL 79
Cdd:PLN02770  23 EAVLFDVDGTLCDSDPLHYYAFREMLQEInfngGVPITEEFFVeNIAGKHNEDIALGLFPD---DLERGlKFTDDKEALF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  80 KTMLFDTVQPLPLIDVVKSY---KGRRPMAVgTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIG 156
Cdd:PLN02770 100 RKLASEQLKPLNGLYKLKKWiedRGLKRAAV-TNAPRENAELMISLLGLSDFFQAVIIGSECEHAKPHPDPYLKALEVLK 178

                        170       180
                 ....*....|....*....|....*..
gi 891174165 157 VPAARCVVFEDADFGIQAAKAAGMDAV 183
Cdd:PLN02770 179 VSKDHTFVFEDSVSGIKAGVAAGMPVV 205
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 7-185 2.92e-14

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 68.91  E-value: 2.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   7 GLIFDMDGTILDTEPT-HRKAWHQVLAQYGMTFDETAII----GLNGSPTwrIAQVIIANHHSdLDPHRLAAEKTALLKT 81
Cdd:PLN03243  26 GVVLEWEGVIVEDDSElERKAWRALAEEEGKRPPPAFLLkraeGMKNEQA--ISEVLCWSRDF-LQMKRLAIRKEDLYEY 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  82 MLFDTVQPLP----LIDVVKSYKgrRPMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGV 157
Cdd:PLN03243 103 MQGGLYRLRPgsreFVQALKKHE--IPIAVASTRPRRYLERAIEAVGMEGFFSVVLAAEDVYRGKPDPEMFMYAAERLGF 180

                        170       180
                 ....*....|....*....|....*...
gi 891174165 158 PAARCVVFEDADFGIQAAKAAGMDAVDV 185
Cdd:PLN03243 181 IPERCIVFGNSNSSVEAAHDGCMKCVAV 208
PRK11587 PRK11587
putative phosphatase; Provisional
 7-179 5.16e-14

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 67.33  E-value: 5.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   7 GLIFDMDGTILDTEPTHRKAWHQVLAQYGMTFDETA--IIGlngsptwriAQVIIANHH--SDLDPHRLAAEKTALLKTM 82
Cdd:PRK11587   5 GFLFDLDGTLVDSLPAVERAWSNWADRHGIAPDEVLnfIHG---------KQAITSLRHfmAGASEAEIQAEFTRLEQIE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  83 LFDT--VQPLP----LID----------VVKSykGRRPMAvgtGSEHAMAvgllqHLGLLAHFdaiVGADDVKRHKPEPD 146
Cdd:PRK11587  76 ATDTegITALPgaiaLLNhlnklgipwaIVTS--GSVPVA---SARHKAA-----GLPAPEVF---VTAERVKRGKPEPD 142

                        170       180       190
                 ....*....|....*....|....*....|...
gi 891174165 147 TFLRCAELIGVPAARCVVFEDADFGIQAAKAAG 179
Cdd:PRK11587 143 AYLLGAQLLGLAPQECVVVEDAPAGVLSGLAAG 175
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 7-183 1.65e-13

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: 65.80  E-value: 1.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   7 GLIFDMDGTILDTEPTHRKAWHQVLAQYGMT-FDETAIIGL--NGSPTWrIAQVIIAnHHSDLDPHRLAAEKTALLK--- 80
Cdd:cd07512    1 AVIFDLDGTLIDSAPDLHAALNAVLAAEGLApLSLAEVRSFvgHGAPAL-IRRAFAA-AGEDLDGPLHDALLARFLDhye 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  81 ------TMLFDTVqpLPLIDVVKSyKGRRpMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAEL 154
Cdd:cd07512   79 adppglTRPYPGV--IEALERLRA-AGWR-LAICTNKPEAPARALLSALGLADLFAAVVGGDTLPQRKPDPAPLRAAIRR 154

                        170       180
                 ....*....|....*....|....*....
gi 891174165 155 IGVPAARCVVFEDADFGIQAAKAAGMDAV 183
Cdd:cd07512  155 LGGDVSRALMVGDSETDAATARAAGVPFV 183
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 104-185 7.54e-11

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


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 56.64  E-value: 7.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165 104 PMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAARCVVFEDADFGIQAAKAAGMDAV 183
Cdd:cd01427   25 KLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSENDIEAARAAGGRTV 104


                 ..
gi 891174165 184 DV 185
Cdd:cd01427  105 AV 106
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 93-185 1.61e-10

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 58.73  E-value: 1.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  93 IDVVKSYKgrRPMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAARCVVFEDADFGI 172
Cdd:PLN02575 225 VNVLMNYK--IPMALVSTRPRKTLENAIGSIGIRGFFSVIVAAEDVYRGKPDPEMFIYAAQLLNFIPERCIVFGNSNQTV 302

                         90
                 ....*....|...
gi 891174165 173 QAAKAAGMDAVDV 185
Cdd:PLN02575 303 EAAHDARMKCVAV 315
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 104-185 4.03e-10

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: 54.39  E-value: 4.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165 104 PMAVGTGSEHAmAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAARCVVFEDADFGIQAAKAAGMDAV 183
Cdd:cd16421   25 KLAVLSNKPNE-AVQVLVEELFPGSFDFVLGEKEGIRRKPDPT*ALECAKVLGVPPDEVLYVGDSGVDMQTARNAGMDEI 103


                 ..
gi 891174165 184 DV 185
Cdd:cd16421  104 GV 105
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 9-181 2.86e-09

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: 53.54  E-value: 2.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   9 IFDMDGTILDTEPTHRKAWHQVLAQYGMTFDETAIIGLNGSPTWRIAQVIIANHHSDL-DPHRLAAEKTAllKTMLFDTV 87
Cdd:cd07523    3 IWDLDGTLLDSYPAMTKALSETLADFGIPQDLETVYKIIKESSVQFAIQYYAEVPDLEeEYKELEAEYLA--KPILFPGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  88 QplPLIDVVKSYKGRRPMAVgtgSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAARCVVFED 167
Cdd:cd07523   81 K--AVLRWIKEQGGKNFLMT---HRDHSALTILKKDGIASYFTEIVTSDNGFPRKPNPEAINYLLNKYQLNPEETVMIGD 155

                        170
                 ....*....|....
gi 891174165 168 ADFGIQAAKAAGMD 181
Cdd:cd07523  156 RELDIEAGHNAGIS 169
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 7-179 5.05e-09

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: 52.78  E-value: 5.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165    7 GLIFDMDGTILDTEPTHRKAWHQVLAQYGM------TFDETAIIGLNGspTWRIAqviianhHSDLDPHRLAAEKTALLK 80
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFGLdpasfkALKQAGGLAEEE--WYRIA-------TSALEELQGRFWSEYDAE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   81 TMLFDTVqplplIDVVKSYKGR-RPMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVkRHKPEPDTFLRCAELIGVPa 159
Cdd:TIGR01549  72 EAYIRGA-----ADLLARLKSAgIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEP-GSKPEPEIFLAALESLGVP- 144

                         170       180
                  ....*....|....*....|
gi 891174165  160 ARCVVFEDADFGIQAAKAAG 179
Cdd:TIGR01549 145 PEVLHVGDNLNDIEGARNAG 164
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 8-185 4.11e-08

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1; This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319835 [Multi-domain]  Cd Length: 207  Bit Score: 50.86  E-value: 4.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   8 LIFDMDGTILDTE----PTHRKAWH----------QVLAQYGMTFDEtAIIGLNGSPTWRIAQVIIANHHsDLDPHRLAA 73
Cdd:cd07533    2 VIFDWDGTLADSQhnivAAMTAAFAdlglpvpsaaEVRSIIGLSLDE-AIARLLPMATPALVAVAERYKE-AFDILRLLP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  74 EKTallkTMLFDTVqpLPLIDVVKSYKGRrpMAVGTG-SEHAMAVGLLQHlGLLAHFDAIVGADDvKRHKPEPDTFLRCA 152
Cdd:cd07533   80 EHA----EPLFPGV--REALDALAAQGVL--LAVATGkSRRGLDRVLEQH-GLGGYFDATRTADD-TPSKPHPEMLREIL 149

                        170       180       190
                 ....*....|....*....|....*....|...
gi 891174165 153 ELIGVPAARCVVFEDADFGIQAAKAAGMDAVDV 185
Cdd:cd07533  150 AELGVDPSRAVMVGDTAYDMQMAANAGAHAVGV 182
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 118-183 7.98e-08

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to uncharacterized Drosophila melanogaster rhythmically expressed gene 2 protein and human haloacid dehalogenase-like hydrolase domain-containing protein 3; The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319852 [Multi-domain]  Cd Length: 128  Bit Score: 48.83  E-value: 7.98e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 891174165 118 GLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAARCV-VFEDADFGIQAAKAAGMDAV 183
Cdd:cd16415   38 ELLEALGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPEEALhVGDDLKNDYLGARAVGWHAL 104
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 120-183 1.33e-07

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: 47.92  E-value: 1.33e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 891174165 120 LQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELIGVPAARCVVFED---ADfgIQAAKAAGMDAV 183
Cdd:cd04305   42 LEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLMVGDsleSD--ILGAKNAGIKTV 106
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 6-180 1.36e-07

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: 49.57  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   6 DGLIFDMDGTILDTEPTHRKA--------------WHQVLAQYGMTfdetaiigLNGSPTWRIAQVIIAN--------HH 63
Cdd:cd02588    1 KALVFDVYGTLIDWHSGLAAAerafpgrgeelsrlWRQKQLEYTWL--------VTLMGPYVDFDELTRDalrataaeLG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  64 SDLDPHRLAAEKTALLKTMLF-DTVQPLplidvVKSYKGRRPMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHK 142
Cdd:cd02588   73 LELDESDLDELGDAYLRLPPFpDVVAGL-----RRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAEDVRAYK 147

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 891174165 143 PEPDTFLRCAELIGVPAARCVVFEDADFGIQAAKAAGM 180
Cdd:cd02588  148 PAPAVYELAAERLGVPPDEILHVASHAWDLAGARALGL 185
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 113-186 2.30e-07

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: 48.40  E-value: 2.30e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 891174165 113 HAMAVglLQHLGLLAHFDAIVGADDV-KRHKPEPDTFLRCAELIGVPAARCVVFEDADFGIQAAKAAGMDAVDVR 186
Cdd:cd02604  109 HAIRV--LKRLGLADLFDGIFDIEYAgPDPKPHPAAFEKAIREAGLDPKRAAFFDDSIRNLLAAKALGMKTVLVG 181
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 8-183 3.78e-07

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: 48.11  E-value: 3.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   8 LIFDMDGTILDTepthrkAWHQVLAQYGMTFDETAIIGLNGSPTW---------RIAQVIIANHHSDLDPHRLAAEKTAl 78
Cdd:cd02603    4 VLFDFGGVLIDP------DPAAAVARFEALTGEPSEFVLDTEGLAgaflelergRITEEEFWEELREELGRPLSAELFE- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  79 lKTMLFDTVQPLPLIDVVKSYKGRRpMAVGTGSEHAMAVGLLQHLGL---LAHFDAIVGADDVKRHKPEPDTFLRCAELI 155
Cdd:cd02603   77 -ELVLAAVDPNPEMLDLLEALRAKG-YKVYLLSNTWPDHFKFQLELLprrGDLFDGVVESCRLGVRKPDPEIYQLALERL 154

                        170       180
                 ....*....|....*....|....*...
gi 891174165 156 GVPAARCVVFEDADFGIQAAKAAGMDAV 183
Cdd:cd02603  155 GVKPEEVLFIDDREENVEAARALGIHAI 182
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
 8-183 5.59e-07

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 48.32  E-value: 5.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   8 LIFDMDGTILDTEPTHRKAWHQVLAQYGmtfdeTAIIGLNGSPTW--RIAQVII----ANH--HSDLD----PHRLAAEK 75
Cdd:PRK13223  16 VMFDLDGTLVDSVPDLAAAVDRMLLELG-----RPPAGLEAVRHWvgNGAPVLVrralAGSidHDGVDdelaEQALALFM 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  76 TALLKTMLFDTVQPlPLIDVVK-SYKGRRPMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAEL 154
Cdd:PRK13223  91 EAYADSHELTVVYP-GVRDTLKwLKKQGVEMALITNKPERFVAPLLDQMKIGRYFRWIIGGDTLPQKKPDPAALLFVMKM 169

                        170       180
                 ....*....|....*....|....*....
gi 891174165 155 IGVPAARCVVFEDADFGIQAAKAAGMDAV 183
Cdd:PRK13223 170 AGVPPSQSLFVGDSRSDVLAAKAAGVQCV 198
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 8-186 6.51e-07

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: 47.33  E-value: 6.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165    8 LIFDMDGTILDtepthrkaWHQVLAQYGMTFDETaiiGLNGSPTWRIAQ------VIIANHHSDLDP-HRLAAEKTA--- 77
Cdd:TIGR01428   4 LVFDVYGTLFD--------VHSVAERAAELYGGR---GEALSQLWRQKQleyswlRTLMGPYKDFWDlTREALRYLLgrl 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   78 ------LLKTMLFDTVQPLP----LIDVVKSYKGRR-PMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPD 146
Cdd:TIGR01428  73 gleddeSAADRLAEAYLRLPphpdVPAGLRALKERGyRLAILSNGSPAMLKSLVKHAGLDDPFDAVLSADAVRAYKPAPQ 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 891174165  147 TFLRCAELIGVPAARcVVFEDADFG-IQAAKAAGMDAVDVR 186
Cdd:TIGR01428 153 VYQLALEALGVPPDE-VLFVASNPWdLGGAKKFGFKTAWIN 192
PRK13226 PRK13226
phosphoglycolate phosphatase; Provisional
 8-183 5.40e-06

phosphoglycolate phosphatase; Provisional


Pssm-ID: 237311 [Multi-domain]  Cd Length: 229  Bit Score: 45.23  E-value: 5.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   8 LIFDMDGTILDTEPTHRKAWHQVLAQYGMTFDETAIIglngSPTWRI-AQVIIANHHSDLDphrlAAEKTALL------- 79
Cdd:PRK13226  15 VLFDLDGTLLDSAPDMLATVNAMLAARGRAPITLAQL----RPVVSKgARAMLAVAFPELD----AAARDALIpeflqry 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  80 ------KTMLFDTV-QPLPLIDVVKSYKGrrpmaVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCA 152
Cdd:PRK13226  87 ealigtQSQLFDGVeGMLQRLECAGCVWG-----IVTNKPEYLARLILPQLGWEQRCAVLIGGDTLAERKPHPLPLLVAA 161

                        170       180       190
                 ....*....|....*....|....*....|.
gi 891174165 153 ELIGVPAARCVVFEDADFGIQAAKAAGMDAV 183
Cdd:PRK13226 162 ERIGVAPTDCVYVGDDERDILAARAAGMPSV 192
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 104-186 1.86e-05

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: 43.35  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165 104 PMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGA--DDVKRHKpePDTFLRCAELIGVPAARCVVFEDADFGIQAAKAAGMD 181
Cdd:cd04302   99 RLYVATSKPEVFARRILEHFGLDEYFDGIAGAslDGSRVHK--ADVIRYALDTLGIAPEQAVMIGDRKHDIIGARANGID 176


                 ....*
gi 891174165 182 AVDVR 186
Cdd:cd04302  177 SIGVL 181
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 8-179 2.08e-05

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 43.48  E-value: 2.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   8 LIFDMDGTILDTEPTHRKAW-HQVLAQYGMTFDETAIIGLNGSPTWRIaqviianhHSDLDPHRLA-----------AEK 75
Cdd:PRK13288   6 VLFDLDGTLINTNELIISSFlHTLKTYYPNQYKREDVLPFIGPSLHDT--------FSKIDESKVEemittyrefnhEHH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  76 TALLKtmLFDTVqpLPLIDVVKSyKGRRpMAVGTGSEHAMAVGLLQHLGLLAHFDAIVGADDVKRHKPEPDTFLRCAELI 155
Cdd:PRK13288  78 DELVT--EYETV--YETLKTLKK-QGYK-LGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPDPEPVLKALELL 151

                        170       180
                 ....*....|....*....|....
gi 891174165 156 GVPAARCVVFEDADFGIQAAKAAG 179
Cdd:PRK13288 152 GAKPEEALMVGDNHHDILAGKNAG 175
Hydrolase_like pfam13242
HAD-hyrolase-like;
140-186 2.25e-04

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 38.37  E-value: 2.25e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 891174165  140 RHKPEPDTFLRCAELIGVPAARCVVFED-ADFGIQAAKAAGMDAVDVR 186
Cdd:pfam13242   2 CGKPNPGMLERALARLGLDPERTVMIGDrLDTDILGAREAGARTILVL 49
PRK13478 PRK13478
phosphonoacetaldehyde hydrolase; Provisional
 130-185 9.98e-04

phosphonoacetaldehyde hydrolase; Provisional


Pssm-ID: 184075 [Multi-domain]  Cd Length: 267  Bit Score: 38.69  E-value: 9.98e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 891174165 130 DAIVGADDVKRHKPEPDTFLRCAELIGV-PAARCVVFEDADFGIQAAKAAGMDAVDV 185
Cdd:PRK13478 146 DHVVTTDDVPAGRPYPWMALKNAIELGVyDVAACVKVDDTVPGIEEGLNAGMWTVGV 202
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 8-185 3.79e-03

phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase PGP/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: 319799 [Multi-domain]  Cd Length: 201  Bit Score: 36.57  E-value: 3.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165   8 LIFDMDGTILDTEPTHRKAWHQVLAQYGM-TFDETAIIGLNGsptWRIAQVIianHHSDLDPHRLAAEKTALLKTMLfDT 86
Cdd:cd04303    2 IIFDFDGTLADSFPWFLSILNQLAARHGFkTVDEEEIEQLRQ---LSSREIL---KQLGVPLWKLPLIAKDFRRLMA-EA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891174165  87 VQPLPLIDVVKSY------KGRRPMAVGTGS-EHAMAVglLQHLGLLAHFDAIVGADDVKRHKpepdTFLRCAELIGVPA 159
Cdd:cd04303   75 APELALFPGVEDMlralhaRGVRLAVVSSNSeENIRRV--LGPEELISLFAVIEGSSLFGKAK----KIRRVLRRTKITA 148

                        170       180
                 ....*....|....*....|....*.
gi 891174165 160 ARCVVFEDADFGIQAAKAAGMDAVDV 185
Cdd:cd04303  149 AQVIYVGDETRDIEAARKVGLAFAAV 174
PRK09456 PRK09456
?-D-glucose-1-phosphatase; Provisional
 130-185 6.92e-03

?-D-glucose-1-phosphatase; Provisional


Pssm-ID: 181872 [Multi-domain]  Cd Length: 199  Bit Score: 35.78  E-value: 6.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 891174165 130 DAIVGADDVKRHKPEPDTFLRCAELIGVPAARCVVFEDADFGIQAAKAAGMDAVDV 185
Cdd:PRK09456 129 DHIYLSQDLGMRKPEARIYQHVLQAEGFSAADAVFFDDNADNIEAANALGITSILV 184
 
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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