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Conserved domains on  [gi|1801175961|ref|WP_160838178|]
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MULTISPECIES: HAD family phosphatase [Aeromonas]

Protein Classification

HAD family hydrolase( domain architecture ID 11428160)

haloacid dehalogenase (HAD) family hydrolase uses a nucleophilic aspartate in the phosphoryl transfer reaction; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

CATH:  3.30.1240.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|15337123|33940035|37786806

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
20-198 1.40e-69

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


:

Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 210.84  E-value: 1.40e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  20 YDALIFDMDGTLVDSMPLHLDAWEITSAEFGLPFDRAQLNEYGGIPTRKIVTMLAEQHGMTVDVEAFARRKVALYLA--R 97
Cdd:COG0637     2 IKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYREllA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  98 TDDVRVFPAMWELVRQYHGK-VPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANPAN 176
Cdd:COG0637    82 EEGLPLIPGVVELLEALKEAgIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERLGVDPEE 161

                         170       180
                  ....*....|....*....|..
gi 1801175961 177 CLVFEDTRIGIQAGKAAGMTTL 198
Cdd:COG0637   162 CVVFEDSPAGIRAAKAAGMRVV 183
 
Name Accession Description Interval E-value
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
20-198 1.40e-69

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 210.84  E-value: 1.40e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  20 YDALIFDMDGTLVDSMPLHLDAWEITSAEFGLPFDRAQLNEYGGIPTRKIVTMLAEQHGMTVDVEAFARRKVALYLA--R 97
Cdd:COG0637     2 IKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYREllA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  98 TDDVRVFPAMWELVRQYHGK-VPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANPAN 176
Cdd:COG0637    82 EEGLPLIPGVVELLEALKEAgIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERLGVDPEE 161

                         170       180
                  ....*....|....*....|..
gi 1801175961 177 CLVFEDTRIGIQAGKAAGMTTL 198
Cdd:COG0637   162 CVVFEDSPAGIRAAKAAGMRVV 183
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 20-195 1.09e-57

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: 180.23  E-value: 1.09e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  20 YDALIFDMDGTLVDSMPLHLDAWEITSAEFGLPFDRAQLNEYGGIPTRKIVTMLAEQHGMTVD---VEAFARRKVALY-- 94
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDGLSleeIHQLAERKNELYre 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  95 LARTDDVRVFPAMwELVRQYHGKVPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANP 174
Cdd:TIGR02009  81 LLRLTGVAVLPGI-RNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRDYFDAIVDASEVKNGKPHPETFLLAAELLGVPP 159

                         170       180
                  ....*....|....*....|.
gi 1801175961 175 ANCLVFEDTRIGIQAGKAAGM 195
Cdd:TIGR02009 160 NECIVFEDALAGVQAARAAGM 180
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
17-195 1.73e-53

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 169.49  E-value: 1.73e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  17 FDEYDALIFDMDGTLVDSMPLHLDAWEITSAEFGLPFDRAQLNEYGGIPTRKIVTMLAEQHGMTVDVEAFARRKVALYLA 96
Cdd:PRK10725    2 YDRYAGLIFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVALNGSPTWRIAQAIIELNQADLDPHALAREKTEAVKS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  97 RT-DDVRVFPAMwELVRQYHGKVPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANPA 175
Cdd:PRK10725   82 MLlDSVEPLPLI-EVVKAWHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADDVQHHKPAPDTFLRCAQLMGVQPT 160

                         170       180
                  ....*....|....*....|
gi 1801175961 176 NCLVFEDTRIGIQAGKAAGM 195
Cdd:PRK10725  161 QCVVFEDADFGIQAARAAGM 180
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 22-197 1.47e-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: 135.05  E-value: 1.47e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  22 ALIFDMDGTLVDSMPLHLDAWEitsaefglpfdraqlneyggiptrkivtmlaeqhgmtvdveaFARRKVALY--LARTD 99
Cdd:cd07505     1 AVIFDMDGVLIDTEPLHRQAWQ------------------------------------------LLERKNALLleLIASE 38

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961 100 DVRVFPAMWELVRQYHG-KVPMGIGTGSTREHAAHILRQTGLDA-FISVLVSADDVVNHKPHPDTFLKVAEQLGANPANC 177
Cdd:cd07505    39 GLKLKPGVVELLDALKAaGIPVAVATSSSRRNVELLLLELGLLRgYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERC 118

                         170       180
                  ....*....|....*....|
gi 1801175961 178 LVFEDTRIGIQAGKAAGMTT 197
Cdd:cd07505   119 LVFEDSLAGIEAAKAAGMTV 138
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
23-200 1.35e-39

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 133.48  E-value: 1.35e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  23 LIFDMDGTLVDSMPLHLDAWEITSAEFGL-PFDRAQLNEYGGIPTRKIVTMLAEQHGMTVDVEAFaRRKVALYLARtDDV 101
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYgELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFY-LRKYNEELHD-KLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961 102 RVFPAMWELVRQ-YHGKVPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANPANCLVF 180
Cdd:pfam13419  79 KPYPGIKELLEElKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVIYV 158

                         170       180
                  ....*....|....*....|
gi 1801175961 181 EDTRIGIQAGKAAGMTTLLA 200
Cdd:pfam13419 159 GDSPRDIEAAKNAGIKVIAV 178
 
Name Accession Description Interval E-value
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
20-198 1.40e-69

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 210.84  E-value: 1.40e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  20 YDALIFDMDGTLVDSMPLHLDAWEITSAEFGLPFDRAQLNEYGGIPTRKIVTMLAEQHGMTVDVEAFARRKVALYLA--R 97
Cdd:COG0637     2 IKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYREllA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  98 TDDVRVFPAMWELVRQYHGK-VPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANPAN 176
Cdd:COG0637    82 EEGLPLIPGVVELLEALKEAgIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERLGVDPEE 161

                         170       180
                  ....*....|....*....|..
gi 1801175961 177 CLVFEDTRIGIQAGKAAGMTTL 198
Cdd:COG0637   162 CVVFEDSPAGIRAAKAAGMRVV 183
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 20-195 1.09e-57

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: 180.23  E-value: 1.09e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  20 YDALIFDMDGTLVDSMPLHLDAWEITSAEFGLPFDRAQLNEYGGIPTRKIVTMLAEQHGMTVD---VEAFARRKVALY-- 94
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDGLSleeIHQLAERKNELYre 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  95 LARTDDVRVFPAMwELVRQYHGKVPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANP 174
Cdd:TIGR02009  81 LLRLTGVAVLPGI-RNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRDYFDAIVDASEVKNGKPHPETFLLAAELLGVPP 159

                         170       180
                  ....*....|....*....|.
gi 1801175961 175 ANCLVFEDTRIGIQAGKAAGM 195
Cdd:TIGR02009 160 NECIVFEDALAGVQAARAAGM 180
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
17-195 1.73e-53

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 169.49  E-value: 1.73e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  17 FDEYDALIFDMDGTLVDSMPLHLDAWEITSAEFGLPFDRAQLNEYGGIPTRKIVTMLAEQHGMTVDVEAFARRKVALYLA 96
Cdd:PRK10725    2 YDRYAGLIFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVALNGSPTWRIAQAIIELNQADLDPHALAREKTEAVKS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  97 RT-DDVRVFPAMwELVRQYHGKVPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANPA 175
Cdd:PRK10725   82 MLlDSVEPLPLI-EVVKAWHGRRPMAVGTGSESAIAEALLAHLGLRRYFDAVVAADDVQHHKPAPDTFLRCAQLMGVQPT 160

                         170       180
                  ....*....|....*....|
gi 1801175961 176 NCLVFEDTRIGIQAGKAAGM 195
Cdd:PRK10725  161 QCVVFEDADFGIQAARAAGM 180
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
20-203 1.37e-43

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 145.07  E-value: 1.37e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  20 YDALIFDMDGTLVDSMPLHLDAWEITSAEFGLP-FDRAQLNEYGGIPTRKIVTMLAEqHGMTVDVEAFARRKVALYLAR- 97
Cdd:COG0546     1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPpLDLEELRALIGLGLRELLRRLLG-EDPDEELEELLARFRELYEEEl 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  98 TDDVRVFPAMWELVRQYHGK-VPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANPAN 176
Cdd:COG0546    80 LDETRLFPGVRELLEALKARgIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLDPEE 159

                         170       180
                  ....*....|....*....|....*..
gi 1801175961 177 CLVFEDTRIGIQAGKAAGMTTLLATEG 203
Cdd:COG0546   160 VLMVGDSPHDIEAARAAGVPFIGVTWG 186
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 22-197 1.47e-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: 135.05  E-value: 1.47e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  22 ALIFDMDGTLVDSMPLHLDAWEitsaefglpfdraqlneyggiptrkivtmlaeqhgmtvdveaFARRKVALY--LARTD 99
Cdd:cd07505     1 AVIFDMDGVLIDTEPLHRQAWQ------------------------------------------LLERKNALLleLIASE 38

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961 100 DVRVFPAMWELVRQYHG-KVPMGIGTGSTREHAAHILRQTGLDA-FISVLVSADDVVNHKPHPDTFLKVAEQLGANPANC 177
Cdd:cd07505    39 GLKLKPGVVELLDALKAaGIPVAVATSSSRRNVELLLLELGLLRgYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERC 118

                         170       180
                  ....*....|....*....|
gi 1801175961 178 LVFEDTRIGIQAGKAAGMTT 197
Cdd:cd07505   119 LVFEDSLAGIEAAKAAGMTV 138
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
23-200 1.35e-39

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 133.48  E-value: 1.35e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  23 LIFDMDGTLVDSMPLHLDAWEITSAEFGL-PFDRAQLNEYGGIPTRKIVTMLAEQHGMTVDVEAFaRRKVALYLARtDDV 101
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYgELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFY-LRKYNEELHD-KLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961 102 RVFPAMWELVRQ-YHGKVPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANPANCLVF 180
Cdd:pfam13419  79 KPYPGIKELLEElKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVIYV 158

                         170       180
                  ....*....|....*....|
gi 1801175961 181 EDTRIGIQAGKAAGMTTLLA 200
Cdd:pfam13419 159 GDSPRDIEAAKNAGIKVIAV 178
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 22-196 5.98e-32

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: 113.89  E-value: 5.98e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  22 ALIFDMDGTLVDSMPLHLDAWEitsaefglpfdraqlneyggiptrkivtmlaeqhgmtvdvEAFARRKVALYLAR---T 98
Cdd:cd16423     1 AVIFDFDGVIVDTEPLWYEAWQ----------------------------------------ELLNERRNELIKRQfseK 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  99 DDVRVFPAMWELVRQYHGK-VPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANPANC 177
Cdd:cd16423    41 TDLPPIEGVKELLEFLKEKgIKLAVASSSPRRWIEPHLERLGLLDYFEVIVTGDDVEKSKPDPDLYLEAAERLGVNPEEC 120

                         170
                  ....*....|....*....
gi 1801175961 178 LVFEDTRIGIQAGKAAGMT 196
Cdd:cd16423   121 VVIEDSRNGVLAAKAAGMK 139
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 20-194 1.42e-30

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: 110.75  E-value: 1.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  20 YDALIFDMDGTLVDSMPLHLDAWEITSAEFGLPFD--------RAQLNEYGGIPTRKIVTMLAEQHGMTVDVEAFARRKV 91
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAKAivaaaedlPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  92 ALYLAR-------TDDVRVFPAMWELVRQYHGK-VPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTF 163
Cdd:pfam00702  81 TVVLVEllgvialADELKLYPGAAEALKALKERgIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIY 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1801175961 164 LKVAEQLGANPANCLVFEDTRIGIQAGKAAG 194
Cdd:pfam00702 161 LAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 22-198 2.11e-30

subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p); This subfamily includes Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). GPP1p and GPP2p are involved in glycerol biosynthesis, GPP1 is induced in response to both anaerobic and hyperosmotic stress, GPP2 is induced in response to hyperosmotic or oxidative stress, and during diauxic shift; overexpression of DOG1 or DOG2 confers 2-deoxyglucose resistance. These belong to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319829 [Multi-domain]  Cd Length: 205  Bit Score: 110.90  E-value: 2.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  22 ALIFDMDGTLVDSMPLHLDAWEITSAEFGLPFDRAQLNEYGgiptRKIVTMLAEQHGMTVDVEAFARRKVALYLARTDDV 101
Cdd:cd07527     1 ALLFDMDGTLVDSTPAVERAWHKWAKEHGVDPEEVLKVSHG----RRAIDVIRKLAPDDADIELVLALETEEPESYPEGV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961 102 RVFPAMWELVRQYHG-KVPMGIGTGSTREHAAHILRQTGLDAfISVLVSADDVVNHKPHPDTFLKVAEQLGANPANCLVF 180
Cdd:cd07527    77 IAIPGAVDLLASLPAaGDRWAIVTSGTRALAEARLEAAGLPH-PEVLVTADDVKNGKPDPEPYLLGAKLLGLDPSDCVVF 155

                         170
                  ....*....|....*...
gi 1801175961 181 EDTRIGIQAGKAAGMTTL 198
Cdd:cd07527   156 EDAPAGIKAGKAAGARVV 173
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 21-198 8.38e-29

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: 104.71  E-value: 8.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  21 DALIFDMDGTLVDSmplhldawEITSAefglpfdraqlneyggiptRKIVTMLAEqHGMTVdVEAFARrkvalylartdD 100
Cdd:cd07526     1 DLVIFDCDGVLVDS--------EVIAA-------------------RVLVEVLAE-LGARV-LAAFEA-----------E 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961 101 VRVFPAMWELVRQYhgKVPMGIGTGSTREHAAHILRQTGLDA-FISVLVSADDVVNHKPHPDTFLKVAEQLGANPANCLV 179
Cdd:cd07526    41 LQPIPGAAAALSAL--TLPFCVASNSSRERLTHSLGLAGLLAyFEGRIFSASDVGRGKPAPDLFLHAAAQMGVAPERCLV 118

                         170
                  ....*....|....*....
gi 1801175961 180 FEDTRIGIQAGKAAGMTTL 198
Cdd:cd07526   119 IEDSPTGVRAALAAGMTVF 137
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 20-199 1.97e-28

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: 106.27  E-value: 1.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  20 YDALIFDMDGTLVDSMPLHLDAWEITSAEFGLPFDRAQL--------------NEYGGIPTRKIVTMLAEQHGMTVDVEA 85
Cdd:COG1011     1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELaeayraieyalwrrYERGEITFAELLRRLLEELGLDLAEEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  86 FArrkvALYLARTDDVRVFPAMWELVRQYHGK-VPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFL 164
Cdd:COG1011    81 AE----AFLAALPELVEPYPDALELLEALKARgYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIFE 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1801175961 165 KVAEQLGANPANCLVFEDTRIG-IQAGKAAGMTTLL 199
Cdd:COG1011   157 LALERLGVPPEEALFVGDSPETdVAGARAAGMRTVW 192
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 22-199 1.97e-27

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: 102.50  E-value: 1.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  22 ALIFDMDGTLVDSMPLHldAWEITSAEFGLpFDRAQLNEYGGIPTRKIVTMLaEQHGMTVDVEAFAR---RKVALYLART 98
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAI--AKLINREELGL-VPDELGVSAVGRLELALRRFK-AQYGRTISPEDAQLlykQLFYEQIEEE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  99 DDVRVFPAMWELVRQYHGK-VPMGIGTGSTREHAAHiLRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANPANC 177
Cdd:TIGR01509  77 AKLKPLPGVRALLEALRARgKKLALLTNSPRAHKLV-LALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLEPSEC 155

                         170       180
                  ....*....|....*....|..
gi 1801175961 178 LVFEDTRIGIQAGKAAGMTTLL 199
Cdd:TIGR01509 156 VFVDDSPAGIEAAKAAGMHTVG 177
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 20-207 5.38e-26

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: 99.28  E-value: 5.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  20 YDALIFDMDGTLVDSMPLHLDAWEITSAEFGL-PFDRAQLNEYGGIPTRKIVTMLAEQHgmtvdVEAFARRKVALYLART 98
Cdd:cd02616     1 ITTILFDLDGTLIDTNELIIKSFNHTLKEYGLeGYTREEVLPFIGPPLRETFEKIDPDK-----LEDMVEEFRKYYREHN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  99 DD-VRVFPAMWELVRQYHGK-VPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANPAN 176
Cdd:cd02616    76 DDlTKEYPGVYETLARLKSQgIKLGVVTTKLRETALKGLKLLGLDKYFDVIVGGDDVTHHKPDPEPVLKALELLGAEPEE 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1801175961 177 CLVFEDTRIGIQAGKAAGMTTLLATEGTLQR 207
Cdd:cd02616   156 ALMVGDSPHDILAGKNAGVKTVGVTWGYKGR 186
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 22-198 1.03e-25

beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); Lactococcus lactis beta-PGM catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate as an intermediate. In the forward G6P-forming direction, this reaction links polysaccharide phosphorolysis to glycolysis, in the reverse direction, the reaction provides G1P for the biosynthesis of exo-polysaccharides. This subfamily belongs to the beta-phosphoglucomutase-like family whose other members include Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319788 [Multi-domain]  Cd Length: 174  Bit Score: 97.75  E-value: 1.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  22 ALIFDMDGTLVDSMPLHLDAWeitsaefglpfdraqlneyggiptrkivTMLAeqhgmtvDVEAFARRKVALYLA---RT 98
Cdd:cd02598     1 GVIFDLDGVITDTAEYHYRAW----------------------------KKLA-------DKEELAARKNRIYVElieEL 45

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  99 DDVRVFPAMWELVRQYHGKVpMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANPANCL 178
Cdd:cd02598    46 TPVDVLPGIASLLVDLKAKG-IKIALASASKNAPKILEKLGLAEYFDAIVDGAVLAKGKPDPDIFLAAAEGLGLNPKDCI 124

                         170       180
                  ....*....|....*....|
gi 1801175961 179 VFEDTRIGIQAGKAAGMTTL 198
Cdd:cd02598   125 GVEDAQAGIRAIKAAGFLVV 144
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
22-203 1.12e-24

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 96.42  E-value: 1.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  22 ALIFDMDGTLVDSMPLHLDAWEITSAEFGLP-FDRAQLNEYGGIPTRKIVTMLAEQHGMTVDVEAFaRRKVALYLAR--- 97
Cdd:PRK13222    8 AVAFDLDGTLVDSAPDLAAAVNAALAALGLPpAGEERVRTWVGNGADVLVERALTWAGREPDEELL-EKLRELFDRHyae 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  98 --TDDVRVFPAMWELVRQYHGK-VPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANP 174
Cdd:PRK13222   87 nvAGGSRLYPGVKETLAALKAAgYPLAVVTNKPTPFVAPLLEALGIADYFSVVIGGDSLPNKKPDPAPLLLACEKLGLDP 166

                         170       180
                  ....*....|....*....|....*....
gi 1801175961 175 ANCLVFEDTRIGIQAGKAAGMTTLLATEG 203
Cdd:PRK13222  167 EEMLFVGDSRNDIQAARAAGCPSVGVTYG 195
PGP_bact TIGR01449
2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate ...
 23-203 4.86e-24

2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate salvage pathway in higher organisms (photorespiration in plants). Phosphoglycolate results from the oxidase activity of RubisCO in the Calvin cycle when concentrations of carbon dioxide are low relative to oxygen. In Ralstonia (Alcaligenes) eutropha and Rhodobacter sphaeroides, the PGP gene (CbbZ) is located on an operon along with other Calvin cycle enzymes including RubisCO. The only other pertinent experimental evidence concerns the gene from E. coli. The in vitro activity of the Ralstonia and Escherichia enzymes was determined with crude cell extracts of strains containing PGP on expression plasmids and compared to controls. In E. coli, however, there does not appear to be a functional Calvin cycle (RubisCO is absent), although the E. coli PGP gene (gph) is on the same operon (dam) with ribulose-5-phosphate-3-epimerase (rpe), a gene in the pentose-phosphate pathway (along with other, unrelated genes). The E. coli enzyme is not expressed under normal laboratory conditions; the pathway to which it belongs has not been determined. In fact, the possibility exists, although unlikely, that the E. coli enzyme and others within this equivalog have as their physiological substrate another, closely related molecule. The other seed chosen for this model, from Xylella fastidiosa has no experimental evidence, but is a plant pathogen and thus may obtain phosphoglycolate from its host. This model has been restricted to encompass only proteobacteria as no related PGP has been verified outside of this clade. Sequences from Aquifex aeolicus and Treponema pallidum fall between the trusted and noise cutoffs. Just below the noise cutoff is a gene which is part of the operon for the biosynthesis of the blue pigment, indigoidine, from Erwinia (Pectobacterium) chrysanthemi, a plant pathogen. It does not seem likely, considering the proposed biosynthetic mechanism, that the dephosphorylation of phosphoglycolate or a closely related compound is required. Possibly, this gene is fortuitously located in this operon, or has an indirect relationship to the necessity for the biosynthesis of this compound. Sequences from 11 species have been annotated as PGP or putative PGP but fall below the noise cutoff. None of these have experimental validation. This enzyme is a member of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolase enzymes (pfam00702). [Energy metabolism, Sugars]


Pssm-ID: 130516 [Multi-domain]  Cd Length: 213  Bit Score: 94.50  E-value: 4.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  23 LIFDMDGTLVDSMPLHLDAWEITSAEFGLP-FDRAQLNEYGGIPTRKIVTMLAEQHGMTVDVEAfARRKVALYLARTDDV 101
Cdd:TIGR01449   1 VLFDLDGTLVDSAPDIAAAVNMALAALGLPpATLARVIGFIGNGVPVLMERVLAWAGQEPDAQR-VAELRKLFDRHYEEV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961 102 -----RVFPAMWELVRQYHGK-VPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANPA 175
Cdd:TIGR01449  80 ageltSVFPGVEATLGALRAKgLRLGLVTNKPTPLARPLLELLGLAKYFSVLIGGDSLAQRKPHPDPLLLAAERLGVAPQ 159

                         170       180
                  ....*....|....*....|....*...
gi 1801175961 176 NCLVFEDTRIGIQAGKAAGMTTLLATEG 203
Cdd:TIGR01449 160 QMVYVGDSRVDIQAARAAGCPSVLLTYG 187
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 22-203 1.64e-23

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: 93.07  E-value: 1.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  22 ALIFDMDGTLVDSMPLHLDAWEITSAEFGLP-FDRAQLNEYGGIPTRKIVTMLAEQHGMTVDVEAFARRKVALYLARTDD 100
Cdd:cd16417     1 LVAFDLDGTLVDSAPDLAEAANAMLAALGLPpLPEETVRTWIGNGADVLVERALTGAREAEPDEELFKEARALFDRHYAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961 101 V-----RVFPAMWELVRQYHGK-VPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANP 174
Cdd:cd16417    81 TlsvhsHLYPGVKEGLAALKAQgYPLACVTNKPERFVAPLLEALGISDYFSLVLGGDSLPEKKPDPAPLLHACEKLGIAP 160

                         170       180
                  ....*....|....*....|....*....
gi 1801175961 175 ANCLVFEDTRIGIQAGKAAGMTTLLATEG 203
Cdd:cd16417   161 AQMLMVGDSRNDILAARAAGCPSVGLTYG 189
PLN02940 PLN02940
riboflavin kinase
 22-195 2.43e-23

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 95.67  E-value: 2.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  22 ALIFDMDGTLVDSMPLHLDAWEITSAEFGLPFDRAQLNEYGGIPTRKIVTMLAEQHGMTVDVEAFARRKVALYLARTDDV 101
Cdd:PLN02940   13 HVILDLDGTLLNTDGIVSDVLKAFLVKYGKQWDGREAQKIVGKTPLEAAATVVEDYGLPCSTDEFNSEITPLLSEQWCNI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961 102 RVFPAMWELVRQY--HGkVPMGIGTGSTREH-AAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANPANCL 178
Cdd:PLN02940   93 KALPGANRLIKHLksHG-VPMALASNSPRANiEAKISCHQGWKESFSVIVGGDEVEKGKPSPDIFLEAAKRLNVEPSNCL 171

                         170
                  ....*....|....*..
gi 1801175961 179 VFEDTRIGIQAGKAAGM 195
Cdd:PLN02940  172 VIEDSLPGVMAGKAAGM 188
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 22-199 2.65e-23

subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides xylulose-1,5-bisphosphate phosphatase CbbY; This family includes Rhodobacter sphaeroides and Arabidopsis thaliana xylulose-1,5-bisphosphate phosphatase CbbY which convert xylulose-1,5-bisphosphate (a potent inhibitor of Ribulose-1,5-bisphosphate carboxylase/oxygenase, Rubisco), to the non-inhibitory compound xylulose-5-phosphate. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319830 [Multi-domain]  Cd Length: 199  Bit Score: 92.06  E-value: 2.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  22 ALIFDMDGTLVDSMPLHLDAW-EITSAEFGLPFD------RAQLNEYGGIPT-----RKIVTMLAEQHGMTVDVEAFARR 89
Cdd:cd07528     1 ALIFDVDGTLAETEELHRRAFnNAFFAERGLDWYwdrelyGELLRVGGGKERiaayfEKVGWPESAPKDLKELIADLHKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  90 KVALY--LARTDDVRVFPAMWELVRQ-YHGKVPMGIGTGSTREHAAHILRQT-GLDAF--ISVLVSADDVVNHKPHPDTF 163
Cdd:cd07528    81 KTERYaeLIAAGLLPLRPGVARLIDEaKAAGVRLAIATTTSPANVDALLSALlGPERRaiFDAIAAGDDVAEKKPDPDIY 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1801175961 164 LKVAEQLGANPANCLVFEDTRIGIQAGKAAGMTTLL 199
Cdd:cd07528   161 LLALERLGVSPSDCLAIEDSAIGLQAAKAAGLPCIV 196
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 22-195 8.76e-23

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: 90.48  E-value: 8.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  22 ALIFDMDGTLVDSMPLHLDAWEITSAEFGLPFDRAQLNEYGGIPT----RKIVTMLaeQHGMTVDvEAFARRKVALYLAR 97
Cdd:cd07529     3 HCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPAseaaRIIVDEL--KLPMSLE-EEFDEQQEALAELF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  98 TDDVRVFPAMWELVRQYHGK-VPMGIGTGSTREH----AAHILRQTGLDAFIsVLVSADDVVNH-KPHPDTFLKVAEQLG 171
Cdd:cd07529    80 MGTAKLMPGAERLLRHLHAHnIPIALATSSCTRHfklkTSRHKELFSLFHHV-VTGDDPEVKGRgKPAPDIFLVAAKRFN 158

                         170       180
                  ....*....|....*....|....*..
gi 1801175961 172 ---ANPANCLVFEDTRIGIQAGKAAGM 195
Cdd:cd07529   159 eppKDPSKCLVFEDSPNGVKAAKAAGM 185
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 21-196 2.77e-19

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 83.22  E-value: 2.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  21 DALIFDMDGTLVDS-MPLHLDAWEITSAEFGL--------------------PFDRAQLNEYGgIPTRKIVTMLAEQHGM 79
Cdd:PLN02779   41 EALLFDCDGVLVETeRDGHRVAFNDAFKEFGLrpvewdvelydellnigggkERMTWYFNENG-WPTSTIEKAPKDEEER 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  80 TVDVEAFARRKVALY--LARTDDVRVFPAMWELVRQYHGK-VPMGIGTGSTREHAAHIL-------RQTGLDAFisvlvS 149
Cdd:PLN02779  120 KELVDSLHDRKTELFkeLIESGALPLRPGVLRLMDEALAAgIKVAVCSTSNEKAVSKIVntllgpeRAQGLDVF-----A 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1801175961 150 ADDVVNHKPHPDTFLKVAEQLGANPANCLVFEDTRIGIQAGKAAGMT 196
Cdd:PLN02779  195 GDDVPKKKPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAAKAAGMR 241
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 21-195 2.35e-17

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 77.04  E-value: 2.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  21 DALIFDMDGTLVDSMPLHLDAWEITSAEFGLPFDRAQL-NEYGGIPTRKIVTMLAEQHGMTVDVEAFARrkvaLYlaRTD 99
Cdd:PRK10563    5 EAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLSLEEVfKRFKGVKLYEIIDIISKEHGVTLAKAELEP----VY--RAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961 100 DVRVF-------PAMWELVRQYHgkVPMGIGTGSTREHAAHILRQTG-LDAFISVLVSADDVVNHKPHPDTFLKVAEQLG 171
Cdd:PRK10563   79 VARLFdselepiAGANALLESIT--VPMCVVSNGPVSKMQHSLGKTGmLHYFPDKLFSGYDIQRWKPDPALMFHAAEAMN 156

                         170       180
                  ....*....|....*....|....
gi 1801175961 172 ANPANCLVFEDTRIGIQAGKAAGM 195
Cdd:PRK10563  157 VNVENCILVDDSSAGAQSGIAAGM 180
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 22-203 8.05e-17

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: 75.43  E-value: 8.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  22 ALIFDMDGTLVDSMPLHLDAWEITSAEFGL-PFDRAQLNEYGGIPTRKIVTMLAEQHGMTVDVEAFAR---RKVALYLAR 97
Cdd:cd07512     1 AVIFDLDGTLIDSAPDLHAALNAVLAAEGLaPLSLAEVRSFVGHGAPALIRRAFAAAGEDLDGPLHDAllaRFLDHYEAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  98 -TDDVRVFPAMWELVRQYHGK-VPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANPA 175
Cdd:cd07512    81 pPGLTRPYPGVIEALERLRAAgWRLAICTNKPEAPARALLSALGLADLFAAVVGGDTLPQRKPDPAPLRAAIRRLGGDVS 160

                         170       180
                  ....*....|....*....|....*...
gi 1801175961 176 NCLVFEDTRIGIQAGKAAGMTTLLATEG 203
Cdd:cd07512   161 RALMVGDSETDAATARAAGVPFVLVTFG 188
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 22-197 1.03e-16

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 75.07  E-value: 1.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  22 ALIFDMDGTLVDSMPLHLDAWEITSAEFgLP--FDRAQLNEYGGIPTRKIVTMLAEQHgmtvdVEAFARRKVALYLARTD 99
Cdd:PRK13288    5 TVLFDLDGTLINTNELIISSFLHTLKTY-YPnqYKREDVLPFIGPSLHDTFSKIDESK-----VEEMITTYREFNHEHHD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961 100 D-VRVFPAMWELVRQYHGK-VPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANPANC 177
Cdd:PRK13288   79 ElVTEYETVYETLKTLKKQgYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPDPEPVLKALELLGAKPEEA 158

                         170       180
                  ....*....|....*....|
gi 1801175961 178 LVFEDTRIGIQAGKAAGMTT 197
Cdd:PRK13288  159 LMVGDNHHDILAGKNAGTKT 178
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 22-202 2.32e-16

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 76.81  E-value: 2.32e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961   22 ALIFDMDGTLVDSMPLHLDA---------WEITSAEFgLPF-DRAQLNEYGGIPTRKIVTMLaeqhgmtvDVEAFARRKV 91
Cdd:PLN02919    77 AVLFDMDGVLCNSEEPSRRAavdvfaemgVEVTVEDF-VPFmGTGEANFLGGVASVKGVKGF--------DPDAAKKRFF 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961   92 ALYL---ARTDDVRVFPAMWELVRQYHGK-VPMGIGTGSTR-----EHAAHILRQTGLDAfisvLVSADDVVNHKPHPDT 162
Cdd:PLN02919   148 EIYLekyAKPNSGIGFPGALELITQCKNKgLKVAVASSADRikvdaNLAAAGLPLSMFDA----IVSADAFENLKPAPDI 223

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1801175961  163 FLKVAEQLGANPANCLVFEDTRIGIQAGKAAGM-----TTLLATE 202
Cdd:PLN02919   224 FLAAAKILGVPTSECVVIEDALAGVQAARAAGMrciavTTTLSEE 268
PRK10826 PRK10826
hexitol phosphatase HxpB;
22-198 2.72e-15

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 71.52  E-value: 2.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  22 ALIFDMDGTLVDSMPLHLDAWEITSAEFGLPFDRAQ-LNEYGGIPTRKIVTMLAEQHGMT-VDVEAFARRKVALYLARTD 99
Cdd:PRK10826    9 AAIFDMDGLLIDSEPLWDRAELDVMASLGVDISRREeLPDTLGLRIDQVVDLWYARQPWNgPSRQEVVQRIIARVISLIE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961 100 DVRvfPAM------WELVRQYHGKVpmGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGAN 173
Cdd:PRK10826   89 ETR--PLLpgvreaLALCKAQGLKI--GLASASPLHMLEAVLTMFDLRDYFDALASAEKLPYSKPHPEVYLNCAAKLGVD 164

                         170       180
                  ....*....|....*....|....*
gi 1801175961 174 PANCLVFEDTRIGIQAGKAAGMTTL 198
Cdd:PRK10826  165 PLTCVALEDSFNGMIAAKAARMRSI 189
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 21-195 3.05e-15

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 71.79  E-value: 3.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  21 DALIFDMDGTLVDSMPLHLDAWEitsaEFGLpfdraQLNEYGGIPTRK--IVTMLAEQHG-----------------MTV 81
Cdd:PLN02770   23 EAVLFDVDGTLCDSDPLHYYAFR----EMLQ-----EINFNGGVPITEefFVENIAGKHNedialglfpddlerglkFTD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  82 DVEAFARRKVAlylartDDVRVFPAMWELVR--QYHGKVPMGIgTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPH 159
Cdd:PLN02770   94 DKEALFRKLAS------EQLKPLNGLYKLKKwiEDRGLKRAAV-TNAPRENAELMISLLGLSDFFQAVIIGSECEHAKPH 166

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1801175961 160 PDTFLKVAEQLGANPANCLVFEDTRIGIQAGKAAGM 195
Cdd:PLN02770  167 PDPYLKALEVLKVSKDHTFVFEDSVSGIKAGVAAGM 202
PLN02811 PLN02811
hydrolase
 27-195 5.34e-15

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 70.56  E-value: 5.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  27 MDGTLVDSMPLHLDAWEITSAEFGLPFDRAQLNEYGGIPTRKIVTMLAEQHGMT--VDVEAFARRKVALYLARTDDVRVF 104
Cdd:PLN02811    1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSdsLSPEDFLVEREAMLQDLFPTSDLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961 105 PAMWELVRQYHGK-VPMGIGTGSTREH-AAHILRQTGLDAFISVLVSADD--VVNHKPHPDTFLKVAEQL---GANPANC 177
Cdd:PLN02811   81 PGAERLVRHLHAKgIPIAIATGSHKRHfDLKTQRHGELFSLMHHVVTGDDpeVKQGKPAPDIFLAAARRFedgPVDPGKV 160

                         170
                  ....*....|....*...
gi 1801175961 178 LVFEDTRIGIQAGKAAGM 195
Cdd:PLN02811  161 LVFEDAPSGVEAAKNAGM 178
PRK11587 PRK11587
putative phosphatase; Provisional
 24-194 6.16e-15

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 70.41  E-value: 6.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  24 IFDMDGTLVDSMPLHLDAWEITSAEFGLpfDRAQLNEYggIPTRKIVTMLaeQHGMTVDVEAFARRKVaLYLAR-----T 98
Cdd:PRK11587    7 LFDLDGTLVDSLPAVERAWSNWADRHGI--APDEVLNF--IHGKQAITSL--RHFMAGASEAEIQAEF-TRLEQieatdT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  99 DDVRVFPAMWELVRQYHG-KVPMGIGTGSTR--EHAAHilRQTGLDAfISVLVSADDVVNHKPHPDTFLKVAEQLGANPA 175
Cdd:PRK11587   80 EGITALPGAIALLNHLNKlGIPWAIVTSGSVpvASARH--KAAGLPA-PEVFVTAERVKRGKPEPDAYLLGAQLLGLAPQ 156

                         170
                  ....*....|....*....
gi 1801175961 176 NCLVFEDTRIGIQAGKAAG 194
Cdd:PRK11587  157 ECVVVEDAPAGVLSGLAAG 175
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 23-195 1.69e-14

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: 68.96  E-value: 1.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  23 LIFDMDGTLVDSMPLHLDAWEITSAEFGLPF-DRAQLNEYGGIP-TRKIVTMLAEQHGMTVDV-EAFARRKVALYLARTD 99
Cdd:cd07533     2 VIFDWDGTLADSQHNIVAAMTAAFADLGLPVpSAAEVRSIIGLSlDEAIARLLPMATPALVAVaERYKEAFDILRLLPEH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961 100 DVRVFPAMWELVRQYHGK-VPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNhKPHPDTFLKVAEQLGANPANCL 178
Cdd:cd07533    82 AEPLFPGVREALDALAAQgVLLAVATGKSRRGLDRVLEQHGLGGYFDATRTADDTPS-KPHPEMLREILAELGVDPSRAV 160

                         170
                  ....*....|....*..
gi 1801175961 179 VFEDTRIGIQAGKAAGM 195
Cdd:cd07533   161 MVGDTAYDMQMAANAGA 177
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 22-194 3.00e-14

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: 67.42  E-value: 3.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  22 ALIFDMDGTLVDSMPLHLDAWEITSAEFGLpfDRAQLNEYggiptrKIVTMLAEQHGMTVDVEAFAR-RKVALYLARTDD 100
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFGL--DPASFKAL------KQAGGLAEEEWYRIATSALEElQGRFWSEYDAEE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961 101 VRvFPAMWELVRQYHGK-VPMGIGTGSTREHAAHILRQTGLDAFiSVLVSADDVVNHKPHPDTFLKVAEQLGANPaNCLV 179
Cdd:TIGR01549  73 AY-IRGAADLLARLKSAgIKLGIISNGSLRAQKLLLRLFGLGDY-FELILVSDEPGSKPEPEIFLAALESLGVPP-EVLH 149

                         170
                  ....*....|....*
gi 1801175961 180 FEDTRIGIQAGKAAG 194
Cdd:TIGR01549 150 VGDNLNDIEGARNAG 164
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 109-199 4.36e-13

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


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 62.80  E-value: 4.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961 109 ELVRQYHGK-VPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANPANCLVFEDTRIGI 187
Cdd:cd01427    14 ELLKRLRAAgIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSENDI 93

                          90
                  ....*....|..
gi 1801175961 188 QAGKAAGMTTLL 199
Cdd:cd01427    94 EAARAAGGRTVA 105
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 83-204 6.98e-12

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 62.74  E-value: 6.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  83 VEAFARRKVALY-LARTDDVRVFPAMWELV---RQYhgKVPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKP 158
Cdd:PLN03243   89 MKRLAIRKEDLYeYMQGGLYRLRPGSREFVqalKKH--EIPIAVASTRPRRYLERAIEAVGMEGFFSVVLAAEDVYRGKP 166

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1801175961 159 HPDTFLKVAEQLGANPANCLVFEDTRIGIQAGKAAGMTTlLATEGT 204
Cdd:PLN03243  167 DPEMFMYAAERLGFIPERCIVFGNSNSSVEAAHDGCMKC-VAVAGK 211
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 24-199 1.80e-11

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: 60.08  E-value: 1.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  24 IFDMDGTLVDSMPLHLDAWEITSAEFGLPFDRAQLNEYggipTRKIVTMLAEQHGMTVDV--EAFARRKVALylarTDDV 101
Cdd:cd07523     3 IWDLDGTLLDSYPAMTKALSETLADFGIPQDLETVYKI----IKESSVQFAIQYYAEVPDleEEYKELEAEY----LAKP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961 102 RVFPAMWELVRqyhgKVPMGIGTG---STREHAA-HILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANPANC 177
Cdd:cd07523    75 ILFPGAKAVLR----WIKEQGGKNflmTHRDHSAlTILKKDGIASYFTEIVTSDNGFPRKPNPEAINYLLNKYQLNPEET 150

                         170       180
                  ....*....|....*....|..
gi 1801175961 178 LVFEDTRIGIQAGKAAGMTTLL 199
Cdd:cd07523   151 VMIGDRELDIEAGHNAGISTIL 172
PRK13226 PRK13226
phosphoglycolate phosphatase; Provisional
 22-203 2.56e-11

phosphoglycolate phosphatase; Provisional


Pssm-ID: 237311 [Multi-domain]  Cd Length: 229  Bit Score: 60.64  E-value: 2.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  22 ALIFDMDGTLVDSMPLHLDAWEITSAEFGL-PFDRAQLNEYGGIPTRKIVTMlaeqhgMTVDVEAFARRK-VALYLARTD 99
Cdd:PRK13226   14 AVLFDLDGTLLDSAPDMLATVNAMLAARGRaPITLAQLRPVVSKGARAMLAV------AFPELDAAARDAlIPEFLQRYE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961 100 DV-----RVFPAMWE-LVRQYHGKVPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGAN 173
Cdd:PRK13226   88 ALigtqsQLFDGVEGmLQRLECAGCVWGIVTNKPEYLARLILPQLGWEQRCAVLIGGDTLAERKPHPLPLLVAAERIGVA 167

                         170       180       190
                  ....*....|....*....|....*....|
gi 1801175961 174 PANCLVFEDTRIGIQAGKAAGMTTLLATEG 203
Cdd:PRK13226  168 PTDCVYVGDDERDILAARAAGMPSVAALWG 197
Pyr-5-nucltdase TIGR01993
pyrimidine 5'-nucleotidase; This family of proteins includes the SDT1/SSM1 gene from yeast ...
 21-199 3.27e-09

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


Pssm-ID: 273917 [Multi-domain]  Cd Length: 183  Bit Score: 54.28  E-value: 3.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  21 DALIFDMDGTLvdsMPLHLDAW--------EITSAEFGLPFDRAQ-LN-----EYGgiptrkiVTM--LAEQHGmtVDVE 84
Cdd:TIGR01993   1 DVWFFDLDNTL---YPHSAGIFlqidrnitEFVAARLKLSPEEARvLRkdyykEYG-------TTLagLMILHE--IDAD 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  85 AFARR--KVALYLARTDDvrvfPAMWELVRQYHGKvpMGIGTGSTREHAAHILRQTGL-DAF--ISVLVSADDVVNHKPH 159
Cdd:TIGR01993  69 EYLRYvhGRLPYDKLKPD----PELRNLLLRLPGR--KIIFTNGDRAHARRALRRLGIeDCFdgIFCFDTANPDLLPKPS 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1801175961 160 PDTFLKVAEQLGANPANCLVFEDTRIGIQAGKAAGMTTLL 199
Cdd:TIGR01993 143 PQAYEKALREAGVDPERAIFFDDSARNIAAGKALGMKTVL 182
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 21-178 3.86e-09

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: 54.58  E-value: 3.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  21 DALIFDMDGTLVD--SMPLHLDAWEITSAEFGLPFDRAQLNEYG------------GIPTRKIVTMLAEQHGMTVDVEAF 86
Cdd:cd02588     1 KALVFDVYGTLIDwhSGLAAAERAFPGRGEELSRLWRQKQLEYTwlvtlmgpyvdfDELTRDALRATAAELGLELDESDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  87 AR-RKVALYLARTDDVRvfPAMWELVRQYHGKVPMgigTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLK 165
Cdd:cd02588    81 DElGDAYLRLPPFPDVV--AGLRRLREAGYRLAIL---SNGSPDLIEDVVANAGLRDLFDAVLSAEDVRAYKPAPAVYEL 155

                         170
                  ....*....|...
gi 1801175961 166 VAEQLGANPANCL 178
Cdd:cd02588   156 AAERLGVPPDEIL 168
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 24-195 1.03e-08

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 54.10  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  24 IFDMDGTLVDSMP-LHLDAWEITSAEFGLPFDRAQLneyggipTRKIVTMLAEQHGMTV--------DVEAFARRKVALY 94
Cdd:PLN02575  135 IFEWEGVIIEDNPdLENQAWLTLAQEEGKSPPPAFI-------LRRVEGMKNEQAISEVlcwsrdpaELRRMATRKEEIY 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  95 LARTDDV-RVFPAMWELVRQY-HGKVPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGA 172
Cdd:PLN02575  208 QALQGGIyRLRTGSQEFVNVLmNYKIPMALVSTRPRKTLENAIGSIGIRGFFSVIVAAEDVYRGKPDPEMFIYAAQLLNF 287

                         170       180
                  ....*....|....*....|...
gi 1801175961 173 NPANCLVFEDTRIGIQAGKAAGM 195
Cdd:PLN02575  288 IPERCIVFGNSNQTVEAAHDARM 310
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 109-197 1.51e-08

human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 50.62  E-value: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961 109 ELVRQYHGKVPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANPANCLVFEDT-RIGI 187
Cdd:cd04305    16 ELLEELKKGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLMVGDSlESDI 95

                          90
                  ....*....|
gi 1801175961 188 QAGKAAGMTT 197
Cdd:cd04305    96 LGAKNAGIKT 105
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 22-195 1.57e-08

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: 52.36  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  22 ALIFDMDGTLVDSMPLHLDAWEITSAEFGlpFDRAQLNEYGGIPTRKIVTMLAEQHGMTVDVEAFARRKVALYLARTDDV 101
Cdd:cd04303     1 LIIFDFDGTLADSFPWFLSILNQLAARHG--FKTVDEEEIEQLRQLSSREILKQLGVPLWKLPLIAKDFRRLMAEAAPEL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961 102 RVFPAMWELVRQYHGK-VPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKphpdTFLKVAEQLGANPANCLVF 180
Cdd:cd04303    79 ALFPGVEDMLRALHARgVRLAVVSSNSEENIRRVLGPEELISLFAVIEGSSLFGKAK----KIRRVLRRTKITAAQVIYV 154

                         170
                  ....*....|....*
gi 1801175961 181 EDTRIGIQAGKAAGM 195
Cdd:cd04303   155 GDETRDIEAARKVGL 169
HAD_PHN cd02586
Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; ...
 22-197 2.46e-08

Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; Degradation of the ubiquitous natural phosphonate 2-aminoethylphosphonate (AEP) into useable forms of nitrogen, carbon, and phosphorus is a two-step metabolic pathway. The first step, catalyzed by AEP transaminase, involves the transfer of NH3 from AEP to pyruvate, yielding phosphonoacetaldehyde (P-Ald) and alanine. In the second step, phosphonatase catalyzes the hydrolytic P-C bond cleavage of P-Ald to form orthophosphate and acetaldehyde. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319785 [Multi-domain]  Cd Length: 242  Bit Score: 52.30  E-value: 2.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  22 ALIFDMDGTLVD--SM-PLHldAWEITSAEFGLPFDRAQLNEYGGIP----TRKIVTM--LAEQ------HGMT-VDVEA 85
Cdd:cd02586     3 AVIFDWAGTTVDygSFaPVN--AFVEAFAQRGVQITLEEARKPMGLLkidhIRALLEMprVAEAwravfgRLPTeADVDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  86 FARRKVALYLAR-TDDVRVFPAMWELV---RQYHGKVpmGIGTGSTREHAAHILRQTGLDAF-ISVLVSADDVVNHKPHP 160
Cdd:cd02586    81 LYEEFEPILIASlAEYSSPIPGVLEVIaklRARGIKI--GSTTGYTREMMDIVLPEAAAQGYrPDSLVTPDDVPAGRPYP 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1801175961 161 DTFLKVAEQLGANPAN-CLVFEDTRIGIQAGKAAGMTT 197
Cdd:cd02586   159 WMCYKNAIELGVYDVAaVVKVGDTVPDIKEGLNAGMWT 196
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 22-199 2.98e-08

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: 51.58  E-value: 2.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  22 ALIFDMDGTLVDsmplhLDAWEITSAEFGLPFDRAQLNEyggiptRKIVTMLAEQHGMT--VDVEAFaRRKVALYLARTD 99
Cdd:cd02603     3 AVLFDFGGVLID-----PDPAAAVARFEALTGEPSEFVL------DTEGLAGAFLELERgrITEEEF-WEELREELGRPL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961 100 D-----------VRVFPAMWELVRQYHGK-VPMGIGTGSTREHAAHILRQ--TGLDAFISVLVSADDVVnHKPHPDTFLK 165
Cdd:cd02603    71 SaelfeelvlaaVDPNPEMLDLLEALRAKgYKVYLLSNTWPDHFKFQLELlpRRGDLFDGVVESCRLGV-RKPDPEIYQL 149

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1801175961 166 VAEQLGANPANCLVFEDTRIGIQAGKAAGMTTLL 199
Cdd:cd02603   150 ALERLGVKPEEVLFIDDREENVEAARALGIHAIL 183
PRK13225 PRK13225
phosphoglycolate phosphatase; Provisional
 2-203 7.04e-08

phosphoglycolate phosphatase; Provisional


Pssm-ID: 106187 [Multi-domain]  Cd Length: 273  Bit Score: 51.25  E-value: 7.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961   2 PQSSPCDHHQSEQprfdeydALIFDMDGTLVDSMPLHLDAWEITSAEFGL-PFDR---AQLNEYGgipTRKIVtmlaEQH 77
Cdd:PRK13225   51 PQVFPQSYPQTLQ-------AIIFDFDGTLVDSLPTVVAIANAHAPDFGYdPIDErdyAQLRQWS---SRTIV----RRA 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  78 GMTVDVEAFARRKVALYLART-DDVRVFPAMWELVRQYHGK-VPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVN 155
Cdd:PRK13225  117 GLSPWQQARLLQRVQRQLGDClPALQLFPGVADLLAQLRSRsLCLGILSSNSRQNIEAFLQRQGLRSLFSVVQAGTPILS 196

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1801175961 156 HKphpDTFLKVAEQLGANPANCLVFEDTRIGIQAGKAAGMTTLLATEG 203
Cdd:PRK13225  197 KR---RALSQLVAREGWQPAAVMYVGDETRDVEAARQVGLIAVAVTWG 241
PRK13478 PRK13478
phosphonoacetaldehyde hydrolase; Provisional
 22-197 2.11e-07

phosphonoacetaldehyde hydrolase; Provisional


Pssm-ID: 184075 [Multi-domain]  Cd Length: 267  Bit Score: 49.86  E-value: 2.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  22 ALIFDMDGTLVD--SM-PLH--LDAWeitsAEFGLPFDRAQLNEYGGIPTRK-IVTMLA---------EQHG--MT-VDV 83
Cdd:PRK13478    6 AVIFDWAGTTVDfgSFaPTQafVEAF----AQFGVEITLEEARGPMGLGKWDhIRALLKmprvaarwqAVFGrlPTeADV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  84 EAFARRKVALYLARTDD-VRVFPAMWELVRQYHGKvPMGIG--TGSTREHAAHILRQTGLDAFI-SVLVSADDVVNHKPH 159
Cdd:PRK13478   82 DALYAAFEPLQIAKLADyATPIPGVLEVIAALRAR-GIKIGstTGYTREMMDVVVPLAAAQGYRpDHVVTTDDVPAGRPY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1801175961 160 PDTFLKVAEQLGANPAN-CLVFEDTRIGIQAGKAAGMTT 197
Cdd:PRK13478  161 PWMALKNAIELGVYDVAaCVKVDDTVPGIEEGLNAGMWT 199
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
 23-195 2.34e-07

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 49.86  E-value: 2.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  23 LIFDMDGTLVDSMPLHLDAWEITSAEFGLPFD-----RAQLNEYGGIPTRKIVTMLAEQHGmtVDvEAFARRKVALYLAR 97
Cdd:PRK13223   16 VMFDLDGTLVDSVPDLAAAVDRMLLELGRPPAgleavRHWVGNGAPVLVRRALAGSIDHDG--VD-DELAEQALALFMEA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  98 TDD----VRVFPAMWELVRQYHGK-VPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGA 172
Cdd:PRK13223   93 YADshelTVVYPGVRDTLKWLKKQgVEMALITNKPERFVAPLLDQMKIGRYFRWIIGGDTLPQKKPDPAALLFVMKMAGV 172

                         170       180
                  ....*....|....*....|...
gi 1801175961 173 NPANCLVFEDTRIGIQAGKAAGM 195
Cdd:PRK13223  173 PPSQSLFVGDSRSDVLAAKAAGV 195
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 122-199 3.98e-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: 3.98e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1801175961 122 IGTGSTREHAAHILRQTGL-DAFISVLVSADDVVNHKPHPDTFLKVAEQLGANPANCLVFEDTRIGIQAGKAAGMTTLL 199
Cdd:cd02604   101 IFTNASKNHAIRVLKRLGLaDLFDGIFDIEYAGPDPKPHPAAFEKAIREAGLDPKRAAFFDDSIRNLLAAKALGMKTVL 179
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 22-203 4.66e-07

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; 5'-nucleotidases dephosphorylate nucleoside 5'-monophosphates to nucleosides and inorganic phosphate. Purified Pseudomonas aeruginosa PA0065 displayed high activity toward 5'-UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low activity against 5'-CMP. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319798 [Multi-domain]  Cd Length: 209  Bit Score: 48.36  E-value: 4.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  22 ALIFDMDGTLVDSMPLHLDAWEITSAEFGLP-FDRAQLNEYGGIPtrkIVTMLAEQHGMTvdvEAFARRKVALYLARTDD 100
Cdd:cd04302     1 TILFDLDGTLTDSAEGITASVQYALEELGIPvPDESELRRFIGPP---LEDSFRELLPFD---EEEAQRAVDAYREYYKE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961 101 -----VRVFPAMWELVRQYHGK-VPMGIGTGSTREHAAHILRQTGLDAFISVLVSA--DDVVNHKphPDTFLKVAEQLGA 172
Cdd:cd04302    75 kglfeNEVYPGIPELLEKLKAAgYRLYVATSKPEVFARRILEHFGLDEYFDGIAGAslDGSRVHK--ADVIRYALDTLGI 152

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1801175961 173 NPANCLVFEDTRIGIQAGKAAGMTTLLATEG 203
Cdd:cd04302   153 APEQAVMIGDRKHDIIGARANGIDSIGVLYG 183
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 22-197 4.00e-06

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: 45.79  E-value: 4.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  22 ALIFDMDGTLVDSMPLHLDAWEITSAEFGLPFD--RAQLNEYG------------GIPTRKIVTMLAEQHGMTVDvEAFA 87
Cdd:TIGR01428   3 ALVFDVYGTLFDVHSVAERAAELYGGRGEALSQlwRQKQLEYSwlrtlmgpykdfWDLTREALRYLLGRLGLEDD-ESAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  88 RRKVALYLartdDVRVFPAMWELVRQY--HGkVPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVVNHKPHPDTFLK 165
Cdd:TIGR01428  82 DRLAEAYL----RLPPHPDVPAGLRALkeRG-YRLAILSNGSPAMLKSLVKHAGLDDPFDAVLSADAVRAYKPAPQVYQL 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1801175961 166 VAEQLGANPANCLVFEDTRIGIQAGKAAGMTT 197
Cdd:TIGR01428 157 ALEALGVPPDEVLFVASNPWDLGGAKKFGFKT 188
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 134-199 9.29e-06

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: 43.43  E-value: 9.29e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1801175961 134 ILRQTGLDAFISVLVSADDVVNHKPHPDTFLKVAEQLGANPANCL-VFEDTRIGIQAGKAAGMTTLL 199
Cdd:cd16415    39 LLEALGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPEEALhVGDDLKNDYLGARAVGWHALL 105
Hydrolase_like pfam13242
HAD-hyrolase-like;
154-199 4.00e-05

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 40.29  E-value: 4.00e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1801175961 154 VNHKPHPDTFLKVAEQLGANPANCLVFEDTRI-GIQAGKAAGMTTLL 199
Cdd:pfam13242   1 VCGKPNPGMLERALARLGLDPERTVMIGDRLDtDILGAREAGARTIL 47
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 24-153 4.41e-05

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). 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: 319796 [Multi-domain]  Cd Length: 195  Bit Score: 42.68  E-value: 4.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  24 IFDMDGTLVDSmplhlDAWEITSAEFGLPFDRAQLNEYGGIP--TRKIVTMLAEQH----------GMTVDVEAFARRKV 91
Cdd:cd02612     3 FFDLDGTLIAG-----DSFFAFLRFKGIAERRAPLEELLLLRlmALYALGRLDGAGmeallgfataGLAGELAALVEEFV 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1801175961  92 ALYLARtddvRVFPAMWELVRQYHGKVP-MGIGTGSTREHAAHILRQTGLDAFI-SVLVSADDV 153
Cdd:cd02612    78 EEYILR----VLYPEARELIAWHKAAGHdVVLISASPEELVAPIARKLGIDNVLgTQLETEDGR 137
HAD pfam12710
haloacid dehalogenase-like hydrolase;
23-154 7.50e-05

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 41.75  E-value: 7.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  23 LIFDMDGTLVDSMPLHLdaWEITSAEFGLPFDRAQLNEYGGIPTRKIVTMLAEQHGMTVDVEAFARRKVALY------LA 96
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFL--LIRALLRRGGPDLWRALLVLLLLALLRLLGRLSRAGARELLRALLAGLPEEDAaelerfVA 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1801175961  97 RTDDVRVFPAMWELVRQYHGK-VPMGIGTGSTREHAAHILRQTGLDAFISVLVSADDVV 154
Cdd:pfam12710  79 EVALPRLHPGALELLAAHRAAgDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDGR 137
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 157-198 9.82e-05

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: 40.13  E-value: 9.82e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1801175961 157 KPHPDTFLKVAEQLGANPANCLVFEDTRIGIQAGKAAGMTTL 198
Cdd:cd16421    62 KPDPT*ALECAKVLGVPPDEVLYVGDSGVDMQTARNAGMDEI 103
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 22-182 3.44e-04

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 40.21  E-value: 3.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  22 ALIFDMDGTLV--DSMplhlDAWeitsAEFglpfdraqLNEYGGIPTRKIVTMLAEQ--HGM--TVDVEAFARRKVALYL 95
Cdd:COG0560     5 LAVFDLDGTLIagESI----DEL----ARF--------LGRRGLVDRREVLEEVAAIteRAMagELDFEESLRFRVALLA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  96 ARTDDV-------------RVFPAMWELVRQYHGK-VPMGIGTGSTREHAAHILRQTGLDAFI-SVLVSADDVVNHKPH- 159
Cdd:COG0560    69 GLPEEEleelaerlfeevpRLYPGARELIAEHRAAgHKVAIVSGGFTFFVEPIAERLGIDHVIaNELEVEDGRLTGEVVg 148

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1801175961 160 --------PDTFLKVAEQLGANPANCLVFED 182
Cdd:COG0560   149 pivdgegkAEALRELAAELGIDLEQSYAYGD 179
PRK06769 PRK06769
HAD-IIIA family hydrolase;
157-203 1.33e-03

HAD-IIIA family hydrolase;


Pssm-ID: 180686 [Multi-domain]  Cd Length: 173  Bit Score: 38.17  E-value: 1.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1801175961 157 KPHPDTFLKVAEQLGANPANCLVFEDTRIGIQAGKAAGMTTLLATEG 203
Cdd:PRK06769   93 KPSTGMLLQAAEKHGLDLTQCAVIGDRWTDIVAAAKVNATTILVRTG 139
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 121-199 3.68e-03

histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal domain of the Escherichia coli bifunctional enzyme histidinol-phosphate phosphatase/imidazole-glycerol-phosphate dehydratase, HisB. The N-terminal histidinol-phosphate phosphatase domain catalyzes the dephosphorylation of histidinol phosphate, the eight step of L-histidine biosynthesis. This family also includes Escherichia coli GmhB phosphatase which is highly specific for D-glycero-D-manno-heptose-1,7-bisphosphate, it removes the C(7)phosphate and not the C(1)phosphate, and this is the third essential step of lipopolysaccharide heptose biosynthesis. 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: 319806 [Multi-domain]  Cd Length: 142  Bit Score: 36.36  E-value: 3.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961 121 GIGTGSTREHAAHILRQTGLDAFISVLVSADDVV--------NH---KPHPDTFLKVAEQLGANPANCLVFEDTRIGIQA 189
Cdd:cd07503    52 GIARGYFSEADFEALHDKMRELLASQGVEIDDIYycphhpddGCpcrKPKPGMLLDAAKELGIDLARSFVIGDRLSDIQA 131

                          90
                  ....*....|
gi 1801175961 190 GKAAGMTTLL 199
Cdd:cd07503   132 ARNAGCKGIL 141
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
 85-207 6.91e-03

haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this UmpH/NagD family include Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase , Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase, human PGP phosphoglycolate phosphatase, Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase, Bacillus AraL a putative sugar phosphatase, and Plasmodium falciparum para nitrophenyl phosphate phosphatase PNPase. 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: 319811 [Multi-domain]  Cd Length: 270  Bit Score: 36.57  E-value: 6.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801175961  85 AFARRKVALYLARTDDvRVFPAMWELVrqyhgkvpmGIGTGSTrehAAHILRQTGldafisvlvsADDVVNHKPHPDTFL 164
Cdd:cd07508   148 RYLRNPGCLFIATAPD-RIHPLKDGGP---------IPGTGAF---AAAVEAATG----------RQPLVLGKPSPWLGE 204

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1801175961 165 KVAEQLGANPANCLVFEDT-RIGIQAGKAAGMTTLLATEGTLQR 207
Cdd:cd07508   205 LALEKFGIDPERVLFVGDRlATDVLFGKACGFQTLLVLTGVTTL 248
 
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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