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Conserved domains on  [gi|488238094|ref|WP_002309302|]
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MULTISPECIES: HAD family phosphatase [Enterococcus]

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

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List of domain hits

 Name Accession Description Interval E-value
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
6-201 4.85e-54

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


:

Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 171.55  E-value: 4.85e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   6 IFDMDGVLIDSENFYFDRRMQFFKEKNILPGSTNKLDFVGLTENGIWEVL-------VSEKDQRADLRKEYLAYREKHPI 78
Cdd:COG0637    6 IFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLleeygldLPEEELAARKEELYRELLAEEGL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  79 DfkiaLRKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNAL--DGRH 156
Cdd:COG0637   86 P----LIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERLgvDPEE 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 488238094 157 CIAVEDSPVGIASAKAANLYTIALKQDLPLDQ--AQADIVIDDLNDI 201
Cdd:COG0637  162 CVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEelAGADLVVDDLAEL 208
 
Name Accession Description Interval E-value
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
6-201 4.85e-54

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 171.55  E-value: 4.85e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   6 IFDMDGVLIDSENFYFDRRMQFFKEKNILPGSTNKLDFVGLTENGIWEVL-------VSEKDQRADLRKEYLAYREKHPI 78
Cdd:COG0637    6 IFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLleeygldLPEEELAARKEELYRELLAEEGL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  79 DfkiaLRKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNAL--DGRH 156
Cdd:COG0637   86 P----LIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERLgvDPEE 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 488238094 157 CIAVEDSPVGIASAKAANLYTIALKQDLPLDQ--AQADIVIDDLNDI 201
Cdd:COG0637  162 CVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEelAGADLVVDDLAEL 208
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 6-180 2.50e-35

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: 121.57  E-value: 2.50e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   6 IFDMDGVLIDSENFYFdRRMQFFKEKNILpgstnkldfvgltengiwevlvsekdqradlrkeylaYREKHPiDFKIALR 85
Cdd:cd07505    3 IFDMDGVLIDTEPLHR-QAWQLLERKNAL-------------------------------------LLELIA-SEGLKLK 43

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  86 KGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNAL-APYFDFVISGEKLSKSKPHPEIYQIAVNAL--DGRHCIAVED 162
Cdd:cd07505   44 PGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLlRGYFDVIVSGDDVERGKPAPDIYLLAAERLgvDPERCLVFED 123

                        170
                 ....*....|....*...
gi 488238094 163 SPVGIASAKAANLYTIAL 180
Cdd:cd07505  124 SLAGIEAAKAAGMTVVAV 141
PRK10826 PRK10826
hexitol phosphatase HxpB;
6-200 4.29e-30

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 110.42  E-value: 4.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   6 IFDMDGVLIDSENFYFDRRMQFFKEKNILPGSTNKL-DFVGLtengiwevlvsekdqRADLRKEYlaYREKHP------- 77
Cdd:PRK10826  11 IFDMDGLLIDSEPLWDRAELDVMASLGVDISRREELpDTLGL---------------RIDQVVDL--WYARQPwngpsrq 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  78 ------IDFKIAL-------RKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEI 144
Cdd:PRK10826  74 evvqriIARVISLieetrplLPGVREALALCKAQGLKIGLASASPLHMLEAVLTMFDLRDYFDALASAEKLPYSKPHPEV 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488238094 145 YQIAVNAL--DGRHCIAVEDSPVGIASAKAANLYTIALKQDLPLDQAQ---ADIVIDDLND 200
Cdd:PRK10826 154 YLNCAAKLgvDPLTCVALEDSFNGMIAAKAARMRSIVVPAPEQQNDPRwalADVKLESLTE 214
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
6-179 2.66e-29

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 107.29  E-value: 2.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094    6 IFDMDGVLIDSENFYFDRRMQFFKE-KNILPGSTNKLDFVGLT-ENGIWEVLVSEKDqrADLRKEYLAYREKHPIDFKIA 83
Cdd:pfam13419   2 IFDFDGTLLDTEELIIKSFNYLLEEfGYGELSEEEILKFIGLPlREIFRYLGVSEDE--EEKIEFYLRKYNEELHDKLVK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   84 LRKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNAL--DGRHCIAVE 161
Cdd:pfam13419  80 PYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLglKPEEVIYVG 159

                         170
                  ....*....|....*...
gi 488238094  162 DSPVGIASAKAANLYTIA 179
Cdd:pfam13419 160 DSPRDIEAAKNAGIKVIA 177
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 6-178 1.80e-26

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 99.80  E-value: 1.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094    6 IFDMDGVLIDSENFYFDRRMQFfkEKNILPGSTnKLDFVGLTENGI--WEVLVSEKDQRADLRKEY--LAYREKHPIDfK 81
Cdd:TIGR01509   3 LFDLDGVLVDTEFAIAKLINRE--ELGLVPDEL-GVSAVGRLELALrrFKAQYGRTISPEDAQLLYkqLFYEQIEEEA-K 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   82 IALRKGAEDILDYLKKKSIKIALASSSPQREIDKMLtQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNAL--DGRHCIA 159
Cdd:TIGR01509  79 LKPLPGVRALLEALRARGKKLALLTNSPRAHKLVLA-LLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALglEPSECVF 157

                         170
                  ....*....|....*....
gi 488238094  160 VEDSPVGIASAKAANLYTI 178
Cdd:TIGR01509 158 VDDSPAGIEAAKAAGMHTV 176
 
Name Accession Description Interval E-value
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
6-201 4.85e-54

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 171.55  E-value: 4.85e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   6 IFDMDGVLIDSENFYFDRRMQFFKEKNILPGSTNKLDFVGLTENGIWEVL-------VSEKDQRADLRKEYLAYREKHPI 78
Cdd:COG0637    6 IFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLleeygldLPEEELAARKEELYRELLAEEGL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  79 DfkiaLRKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNAL--DGRH 156
Cdd:COG0637   86 P----LIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERLgvDPEE 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 488238094 157 CIAVEDSPVGIASAKAANLYTIALKQDLPLDQ--AQADIVIDDLNDI 201
Cdd:COG0637  162 CVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEelAGADLVVDDLAEL 208
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
6-207 5.22e-37

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 128.12  E-value: 5.22e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   6 IFDMDGVLIDSENFYFDRRMQFFKEKNILPGSTNKL-DFVGLTENGIWEVLVSEK--DQRADLRKEYLAYREKHpIDFKI 82
Cdd:COG0546    5 LFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELrALIGLGLRELLRRLLGEDpdEELEELLARFRELYEEE-LLDET 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  83 ALRKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNAL--DGRHCIAV 160
Cdd:COG0546   84 RLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALERLglDPEEVLMV 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488238094 161 EDSPVGIASAKAANLYTIALK----QDLPLDQAQADIVIDDLNDIIQIIET 207
Cdd:COG0546  164 GDSPHDIEAARAAGVPFIGVTwgygSAEELEAAGADYVIDSLAELLALLAE 214
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 6-180 2.50e-35

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: 121.57  E-value: 2.50e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   6 IFDMDGVLIDSENFYFdRRMQFFKEKNILpgstnkldfvgltengiwevlvsekdqradlrkeylaYREKHPiDFKIALR 85
Cdd:cd07505    3 IFDMDGVLIDTEPLHR-QAWQLLERKNAL-------------------------------------LLELIA-SEGLKLK 43

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  86 KGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNAL-APYFDFVISGEKLSKSKPHPEIYQIAVNAL--DGRHCIAVED 162
Cdd:cd07505   44 PGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLlRGYFDVIVSGDDVERGKPAPDIYLLAAERLgvDPERCLVFED 123

                        170
                 ....*....|....*...
gi 488238094 163 SPVGIASAKAANLYTIAL 180
Cdd:cd07505  124 SLAGIEAAKAAGMTVVAV 141
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 6-201 6.93e-34

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: 118.90  E-value: 6.93e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   6 IFDMDGVLIDSENFYFDRRMQFFKEKNilpgstnkldfvgltengiWEVLVSEKDQRADLRkeylayrekhpidfkiaLR 85
Cdd:cd16423    3 IFDFDGVIVDTEPLWYEAWQELLNERR-------------------NELIKRQFSEKTDLP-----------------PI 46

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  86 KGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNALDGR--HCIAVEDS 163
Cdd:cd16423   47 EGVKELLEFLKEKGIKLAVASSSPRRWIEPHLERLGLLDYFEVIVTGDDVEKSKPDPDLYLEAAERLGVNpeECVVIEDS 126

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 488238094 164 PVGIASAKAANLYTIALKQDL--PLDQAQADIVIDDLNDI 201
Cdd:cd16423  127 RNGVLAAKAAGMKCVGVPNPVtgSQDFSKADLVLSSFAEK 166
PRK10826 PRK10826
hexitol phosphatase HxpB;
6-200 4.29e-30

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 110.42  E-value: 4.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   6 IFDMDGVLIDSENFYFDRRMQFFKEKNILPGSTNKL-DFVGLtengiwevlvsekdqRADLRKEYlaYREKHP------- 77
Cdd:PRK10826  11 IFDMDGLLIDSEPLWDRAELDVMASLGVDISRREELpDTLGL---------------RIDQVVDL--WYARQPwngpsrq 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  78 ------IDFKIAL-------RKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEI 144
Cdd:PRK10826  74 evvqriIARVISLieetrplLPGVREALALCKAQGLKIGLASASPLHMLEAVLTMFDLRDYFDALASAEKLPYSKPHPEV 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488238094 145 YQIAVNAL--DGRHCIAVEDSPVGIASAKAANLYTIALKQDLPLDQAQ---ADIVIDDLND 200
Cdd:PRK10826 154 YLNCAAKLgvDPLTCVALEDSFNGMIAAKAARMRSIVVPAPEQQNDPRwalADVKLESLTE 214
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
6-179 2.66e-29

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 107.29  E-value: 2.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094    6 IFDMDGVLIDSENFYFDRRMQFFKE-KNILPGSTNKLDFVGLT-ENGIWEVLVSEKDqrADLRKEYLAYREKHPIDFKIA 83
Cdd:pfam13419   2 IFDFDGTLLDTEELIIKSFNYLLEEfGYGELSEEEILKFIGLPlREIFRYLGVSEDE--EEKIEFYLRKYNEELHDKLVK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   84 LRKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNAL--DGRHCIAVE 161
Cdd:pfam13419  80 PYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLglKPEEVIYVG 159

                         170
                  ....*....|....*...
gi 488238094  162 DSPVGIASAKAANLYTIA 179
Cdd:pfam13419 160 DSPRDIEAAKNAGIKVIA 177
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 6-178 1.80e-26

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 99.80  E-value: 1.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094    6 IFDMDGVLIDSENFYFDRRMQFfkEKNILPGSTnKLDFVGLTENGI--WEVLVSEKDQRADLRKEY--LAYREKHPIDfK 81
Cdd:TIGR01509   3 LFDLDGVLVDTEFAIAKLINRE--ELGLVPDEL-GVSAVGRLELALrrFKAQYGRTISPEDAQLLYkqLFYEQIEEEA-K 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   82 IALRKGAEDILDYLKKKSIKIALASSSPQREIDKMLtQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNAL--DGRHCIA 159
Cdd:TIGR01509  79 LKPLPGVRALLEALRARGKKLALLTNSPRAHKLVLA-LLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALglEPSECVF 157

                         170
                  ....*....|....*....
gi 488238094  160 VEDSPVGIASAKAANLYTI 178
Cdd:TIGR01509 158 VDDSPAGIEAAKAAGMHTV 176
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 6-205 4.45e-25

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


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 97.41  E-value: 4.45e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   6 IFDMDGVLIDSENFYFDRRMQFFKEKNILPGSTNKLDFVGLTENGIWEVLVSEKDQRADLRKEYLayrEKHPIDFK---- 81
Cdd:COG1011    5 LFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAEAYRAIEYALWRRYERGEITFAELLRRLL---EELGLDLAeela 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  82 ----------IALRKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNA 151
Cdd:COG1011   82 eaflaalpelVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIFELALER 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488238094 152 L--DGRHCIAVEDSPVG-IASAKAANLYTIAL--KQDLPLDQAQADIVIDDLNDIIQII 205
Cdd:COG1011  162 LgvPPEEALFVGDSPETdVAGARAAGMRTVWVnrSGEPAPAEPRPDYVISDLAELLELL 220
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 4-201 1.44e-21

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: 87.78  E-value: 1.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   4 GMIFDMDGVLIDSENFYFDRRMQFFKEKNILPgstnklDFVGLTENGIWEVLVSEKDQRADLRKEYLAYREK---HPIDF 80
Cdd:cd07527    1 ALLFDMDGTLVDSTPAVERAWHKWAKEHGVDP------EEVLKVSHGRRAIDVIRKLAPDDADIELVLALETeepESYPE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  81 KIALRKGAEDILDYLKKKSIKIALASSSPQREIDKMLTqNALAPYFDFVISGEKLSKSKPHPEIYQIAVNAL--DGRHCI 158
Cdd:cd07527   75 GVIAIPGAVDLLASLPAAGDRWAIVTSGTRALAEARLE-AAGLPHPEVLVTADDVKNGKPDPEPYLLGAKLLglDPSDCV 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 488238094 159 AVEDSPVGIASAKAANLYTIAL--KQDLP-LDQAQADIVIDDLNDI 201
Cdd:cd07527  154 VFEDAPAGIKAGKAAGARVVAVntSHDLEqLEAAGADLVVEDLSDI 199
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 4-179 7.33e-21

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: 85.47  E-value: 7.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094    4 GMIFDMDGVLIDSENFYF--------DRRMQFFKEKNILPGSTNKLDFVG-LTENGIWEVLVSEKDQRADLRKEYlaYRE 74
Cdd:TIGR02009   3 AVIFDMDGVITDTAPLHAqawkhiaaKYGISFDKQYNESLKGLSREDILRaILKLRGDGLSLEEIHQLAERKNEL--YRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   75 KHPIDFKIALrKGAEDILDYLKKKSIKIALASSSpqREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNAL-- 152
Cdd:TIGR02009  81 LLRLTGVAVL-PGIRNLLKRLKAKGIAVGLGSSS--KNAPRILAKLGLRDYFDAIVDASEVKNGKPHPETFLLAAELLgv 157

                         170       180
                  ....*....|....*....|....*..
gi 488238094  153 DGRHCIAVEDSPVGIASAKAANLYTIA 179
Cdd:TIGR02009 158 PPNECIVFEDALAGVQAARAAGMFAVA 184
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 6-173 2.29e-20

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: 84.32  E-value: 2.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   6 IFDMDGVLIDSENFYFDRRMQFFKEKNILPGSTNKLDFVGLTENGIWEVLVSEKDQRADLRKEYLAYREKHPIDFK--IA 83
Cdd:cd07529    5 IFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLEEEFDEQQEALAELFMgtAK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  84 LRKGAEDILDYLKKKSIKIALASSSPQREIDkMLTQNALAPY--FDFVISG---EKLSKSKPHPEIYQIAVNAL-DGRH- 156
Cdd:cd07529   85 LMPGAERLLRHLHAHNIPIALATSSCTRHFK-LKTSRHKELFslFHHVVTGddpEVKGRGKPAPDIFLVAAKRFnEPPKd 163

                        170       180
                 ....*....|....*....|
gi 488238094 157 ---CIAVEDSPVGIASAKAA 173
Cdd:cd07529  164 pskCLVFEDSPNGVKAAKAA 183
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 6-174 5.96e-19

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: 80.71  E-value: 5.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094    6 IFDMDGVLIDSENFYFDRRMQFFKEKNILPGSTNKLDFVGLTENGIWEVLVSEKDQRADLRKEYLAYREKHPIDFKIA-- 83
Cdd:pfam00702   5 VFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGLTVvl 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   84 --------------LRKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAV 149
Cdd:pfam00702  85 vellgvialadelkLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIYLAAL 164

                         170       180
                  ....*....|....*....|....*..
gi 488238094  150 NAL--DGRHCIAVEDSPVGIASAKAAN 174
Cdd:pfam00702 165 ERLgvKPEEVLMVGDGVNDIPAAKAAG 191
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 4-201 7.23e-19

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: 80.03  E-value: 7.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   4 GMIFDMDGVLIDSENFYFDRRMQFFkeknilpgstnklDFVGLTENGIwevlvsekdqradlRKEYLAYREKHPIDfkia 83
Cdd:cd02598    1 GVIFDLDGVITDTAEYHYRAWKKLA-------------DKEELAARKN--------------RIYVELIEELTPVD---- 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  84 LRKGAEDILDYLKKKSIKIALASSSpqREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNAL--DGRHCIAVE 161
Cdd:cd02598   50 VLPGIASLLVDLKAKGIKIALASAS--KNAPKILEKLGLAEYFDAIVDGAVLAKGKPDPDIFLAAAEGLglNPKDCIGVE 127

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 488238094 162 DSPVGIASAKAANLYTIALKQDLPLDQAqADIVIDDLNDI 201
Cdd:cd02598  128 DAQAGIRAIKAAGFLVVGVGREEDLLGA-DIVVPDTTADL 166
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 6-204 9.58e-19

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 80.40  E-value: 9.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   6 IFDMDGVLIDS------------ENFYFDRrmqfFKEKNILPgstnkldFVGLTENGIWEVLvsEKDQRADLRKEYLAYR 73
Cdd:cd02616    5 LFDLDGTLIDTneliiksfnhtlKEYGLEG----YTREEVLP-------FIGPPLRETFEKI--DPDKLEDMVEEFRKYY 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  74 EKHPIDFkIALRKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNALD 153
Cdd:cd02616   72 REHNDDL-TKEYPGVYETLARLKSQGIKLGVVTTKLRETALKGLKLLGLDKYFDVIVGGDDVTHHKPDPEPVLKALELLG 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488238094 154 GR--HCIAVEDSPVGIASAKAANLYTIA----LKQDLPLDQAQADIVIDDLNDIIQI 204
Cdd:cd02616  151 AEpeEALMVGDSPHDILAGKNAGVKTVGvtwgYKGREYLKAFNPDFIIDKMSDLLTI 207
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 4-180 1.13e-18

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


Pssm-ID: 213672 [Multi-domain]  Cd Length: 185  Bit Score: 79.66  E-value: 1.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094    4 GMIFDMDGVLIDSENFYFDRRMQFFKEKNILPGSTNKLDFVGLT-ENGIWEVLVSEKDQRADLRKEYLAYR--------- 73
Cdd:TIGR01990   1 AVIFDLDGVITDTAEYHYLAWKHLADELGIPFDEEFNESLKGVSrEESLERILDLGGKKYSEEEKEELAERkndyyvell 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   74 -EKHPIDfkiaLRKGAEDILDYLKKKSIKIALASSSpqREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNAL 152
Cdd:TIGR01990  81 kELTPAD----VLPGIKSLLADLKKNNIKIALASAS--KNAPTILEKLELIDYFDAIVDPAELKKGKPDPEIFLAAAEGL 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 488238094  153 D--GRHCIAVEDSPVGIASAKAANLYTIAL 180
Cdd:TIGR01990 155 GvsPSECIGIEDAQAGIEAIKAAGMFAVGV 184
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
4-206 1.56e-18

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 80.24  E-value: 1.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   4 GMIFDMDGVLIDSE-------NfyfdrRMqfFKEKNILPGSTNKL-DFVGlteNGIwEVLVS----------EKDQRADL 65
Cdd:PRK13222   8 AVAFDLDGTLVDSApdlaaavN-----AA--LAALGLPPAGEERVrTWVG---NGA-DVLVEraltwagrepDEELLEKL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  66 RKEYLAYREKHpIDFKIALRKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIY 145
Cdd:PRK13222  77 RELFDRHYAEN-VAGGSRLYPGVKETLAALKAAGYPLAVVTNKPTPFVAPLLEALGIADYFSVVIGGDSLPNKKPDPAPL 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488238094 146 QIAVNALDGR--HCIAVEDSPVGIASAKAANLYTIALKQ----DLPLDQAQADIVIDDLNDIIQIIE 206
Cdd:PRK13222 156 LLACEKLGLDpeEMLFVGDSRNDIQAARAAGCPSVGVTYgynyGEPIALSEPDVVIDHFAELLPLLG 222
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 4-201 6.44e-16

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 75.66  E-value: 6.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094    4 GMIFDMDGVLIDSENFYFDRRMQFFKEKNILPGSTNKLDFVGLTE----NGIWEVL-VSEKDQRADLRKEYLAYREKH-P 77
Cdd:PLN02919   77 AVLFDMDGVLCNSEEPSRRAAVDVFAEMGVEVTVEDFVPFMGTGEanflGGVASVKgVKGFDPDAAKKRFFEIYLEKYaK 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   78 IDFKIALrKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALA-PYFDFVISGEKLSKSKPHPEIYQIAVNALD--G 154
Cdd:PLN02919  157 PNSGIGF-PGALELITQCKNKGLKVAVASSADRIKVDANLAAAGLPlSMFDAIVSADAFENLKPAPDIFLAAAKILGvpT 235

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 488238094  155 RHCIAVEDSPVGIASAKAANLYTIALKQDLP---LDQAQADIVIDDLNDI 201
Cdd:PLN02919  236 SECVVIEDALAGVQAARAAGMRCIAVTTTLSeeiLKDAGPSLIRKDIGNI 285
PLN02940 PLN02940
riboflavin kinase
 87-201 3.92e-15

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 72.94  E-value: 3.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  87 GAEDILDYLKKKSIKIALASSSPQREID-KMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNAL--DGRHCIAVEDS 163
Cdd:PLN02940  97 GANRLIKHLKSHGVPMALASNSPRANIEaKISCHQGWKESFSVIVGGDEVEKGKPSPDIFLEAAKRLnvEPSNCLVIEDS 176

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 488238094 164 PVGIASAKAANLYTIALKQdLPLDQAQ---ADIVIDDLNDI 201
Cdd:PLN02940 177 LPGVMAGKAAGMEVIAVPS-IPKQTHLyssADEVINSLLDL 216
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 5-178 9.91e-15

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: 69.72  E-value: 9.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   5 MIFDMDGVLIDSENF----YFDrrmQFFKEKNI-----LPGSTNKLDFVGLTENGI---------WEVLVSEKDQRADLR 66
Cdd:cd07528    2 LIFDVDGTLAETEELhrraFNN---AFFAERGLdwywdRELYGELLRVGGGKERIAayfekvgwpESAPKDLKELIADLH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  67 KEYLAYREKHPIDFKIALRKGAEDILDYLKKKSIKIALASSSPQREIDKMLtQNALAP----YFDFVISGEKLSKSKPHP 142
Cdd:cd07528   79 KAKTERYAELIAAGLLPLRPGVARLIDEAKAAGVRLAIATTTSPANVDALL-SALLGPerraIFDAIAAGDDVAEKKPDP 157

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 488238094 143 EIYQIAVNALD--GRHCIAVEDSPVGIASAKAANLYTI 178
Cdd:cd07528  158 DIYLLALERLGvsPSDCLAIEDSAIGLQAAKAAGLPCI 195
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 6-173 1.37e-14

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: 67.73  E-value: 1.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   6 IFDMDGVLIDSEnfyfdrrmqffkeknilpgstnkldfvgltenGIWEVLVSEKDQRADLRKEYLAYREKHPIDfkialr 85
Cdd:cd07526    4 IFDCDGVLVDSE--------------------------------VIAARVLVEVLAELGARVLAAFEAELQPIP------ 45

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  86 kGAEDILDYLkkkSIKIALASSSPQREIDKMLTQNALAPYFDFVI-SGEKLSKSKPHPEIYQIAVNAL--DGRHCIAVED 162
Cdd:cd07526   46 -GAAAALSAL---TLPFCVASNSSRERLTHSLGLAGLLAYFEGRIfSASDVGRGKPAPDLFLHAAAQMgvAPERCLVIED 121

                        170
                 ....*....|.
gi 488238094 163 SPVGIASAKAA 173
Cdd:cd07526  122 SPTGVRAALAA 132
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 6-202 1.66e-14

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: 69.19  E-value: 1.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   6 IFDMDGVLIDSE---NFYFDRRMQffkEKNILPGSTNKL-DFVGlteNGIwEVLVS-----------EKDQRADLRKEYL 70
Cdd:cd16417    3 AFDLDGTLVDSApdlAEAANAMLA---ALGLPPLPEETVrTWIG---NGA-DVLVEraltgareaepDEELFKEARALFD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  71 AYREKHpIDFKIALRKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPE--IYQIA 148
Cdd:cd16417   76 RHYAET-LSVHSHLYPGVKEGLAALKAQGYPLACVTNKPERFVAPLLEALGISDYFSLVLGGDSLPEKKPDPAplLHACE 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488238094 149 VNALDGRHCIAVEDSPVGIASAKAANLYTIALK----QDLPLDQAQADIVIDDLNDII 202
Cdd:cd16417  155 KLGIAPAQMLMVGDSRNDILAARAAGCPSVGLTygynYGEDIAASGPDAVIDSLAELL 212
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 6-201 3.79e-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: 68.19  E-value: 3.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   6 IFDMDGVLIDSENFYFDRRMQFFKEKNILPGSTNK-LDFVGLTENGIWEVLV--SEKDQRADLRKEYLAYREKHPI-DFK 81
Cdd:cd07533    3 IFDWDGTLADSQHNIVAAMTAAFADLGLPVPSAAEvRSIIGLSLDEAIARLLpmATPALVAVAERYKEAFDILRLLpEHA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  82 IALRKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKlSKSKPHPEIYQIAVNAL--DGRHCIA 159
Cdd:cd07533   83 EPLFPGVREALDALAAQGVLLAVATGKSRRGLDRVLEQHGLGGYFDATRTADD-TPSKPHPEMLREILAELgvDPSRAVM 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 488238094 160 VEDSPVGIASAKAANLYTIAL------KQDlpLDQAQADIVIDDLNDI 201
Cdd:cd07533  162 VGDTAYDMQMAANAGAHAVGVawgyhsLED--LRSAGADAVVDHFSEL 207
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 3-201 5.07e-14

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 68.91  E-value: 5.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   3 LGMIFDMDGVLIDsENFYFDRRM--QFFKEKNILPGSTNKLDFV-GL-TENGIWEVLVSEKD----QRADLRKEYLaYRE 74
Cdd:PLN03243  25 LGVVLEWEGVIVE-DDSELERKAwrALAEEEGKRPPPAFLLKRAeGMkNEQAISEVLCWSRDflqmKRLAIRKEDL-YEY 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  75 KHPIDFKiaLRKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNALD- 153
Cdd:PLN03243 103 MQGGLYR--LRPGSREFVQALKKHEIPIAVASTRPRRYLERAIEAVGMEGFFSVVLAAEDVYRGKPDPEMFMYAAERLGf 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 488238094 154 -GRHCIAVEDSPVGIASAKAANLYTIALKQDLPL-DQAQADIVIDDLNDI 201
Cdd:PLN03243 181 iPERCIVFGNSNSSVEAAHDGCMKCVAVAGKHPVyELSAGDLVVRRLDDL 230
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 6-174 5.82e-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: 66.65  E-value: 5.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094    6 IFDMDGVLIDSENFYFDRRMQFFKEKNILPGSTNKLDFVG-LTENGIWEVLVSEKDQ-RADLRKEYLAYRekhpidfkiA 83
Cdd:TIGR01549   3 LFDIDGTLVDIKFAIRRAFPQTFEEFGLDPASFKALKQAGgLAEEEWYRIATSALEElQGRFWSEYDAEE---------A 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   84 LRKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSkSKPHPEIYQIAVNALD-GRHCIAVED 162
Cdd:TIGR01549  74 YIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEPG-SKPEPEIFLAALESLGvPPEVLHVGD 152

                         170
                  ....*....|..
gi 488238094  163 SPVGIASAKAAN 174
Cdd:TIGR01549 153 NLNDIEGARNAG 164
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 88-180 8.53e-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: 62.03  E-value: 8.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  88 AEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVN--ALDGRHCIAVEDSPV 165
Cdd:cd01427   12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLklGVDPEEVLFVGDSEN 91

                         90
                 ....*....|....*
gi 488238094 166 GIASAKAANLYTIAL 180
Cdd:cd01427   92 DIEAARAAGGRTVAV 106
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 6-206 1.14e-12

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 64.28  E-value: 1.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   6 IFDMDGVLIDSE-----------NFYFDRRmqfFKEKNILPgstnkldFVGLTengIWEVLVSEKDQRAD-LRKEYLAYR 73
Cdd:PRK13288   7 LFDLDGTLINTNeliissflhtlKTYYPNQ---YKREDVLP-------FIGPS---LHDTFSKIDESKVEeMITTYREFN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  74 EKHPiDFKIALRKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNALD 153
Cdd:PRK13288  74 HEHH-DELVTEYETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPDPEPVLKALELLG 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488238094 154 GR--HCIAVEDSPVGIASAKAANLYTIALKQDLP----LDQAQADIVIDDLNDIIQIIE 206
Cdd:PRK13288 153 AKpeEALMVGDNHHDILAGKNAGTKTAGVAWTIKgreyLEQYKPDFMLDKMSDLLAIVG 211
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 5-200 1.55e-12

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 64.73  E-value: 1.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   5 MIFDMDGVLIDSENfyfD-RRMQF---FKEKNILP---------------GSTNKLDF----VGLTENGIWEVLVSEKDq 61
Cdd:PLN02779  43 LLFDCDGVLVETER---DgHRVAFndaFKEFGLRPvewdvelydellnigGGKERMTWyfneNGWPTSTIEKAPKDEEE- 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  62 radlRKEYLAYREKHPIDF--------KIALRKGAEDILDYLKKKSIKIALASSSPQREIDKMLtQNALAP----YFDfV 129
Cdd:PLN02779 119 ----RKELVDSLHDRKTELfkeliesgALPLRPGVLRLMDEALAAGIKVAVCSTSNEKAVSKIV-NTLLGPeraqGLD-V 192

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488238094 130 ISGEKLSKSKPHPEIYQIAVNAL--DGRHCIAVEDSPVGIASAKAANLYTIALKQDLPLDQA--QADIVIDDLND 200
Cdd:PLN02779 193 FAGDDVPKKKPDPDIYNLAAETLgvDPSRCVVVEDSVIGLQAAKAAGMRCIVTKSSYTADEDfsGADAVFDCLGD 267
PLN02811 PLN02811
hydrolase
 9-200 4.88e-12

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 62.47  E-value: 4.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   9 MDGVLIDSENFYFDrrMQffkEKnILPGSTNKLDF----------------VGLTENGIWEVLVSEK--DQRADLRKEYL 70
Cdd:PLN02811   1 MDGLLLDTEKFYTE--VQ---EK-ILARYGKTFDWslkakmmgkkaieaarIFVEESGLSDSLSPEDflVEREAMLQDLF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  71 AYREKHPidfkialrkGAEDILDYLKKKSIKIALASSSPQREIDkMLTQN--ALAPYFDFVISGE--KLSKSKPHPEIYQ 146
Cdd:PLN02811  75 PTSDLMP---------GAERLVRHLHAKGIPIAIATGSHKRHFD-LKTQRhgELFSLMHHVVTGDdpEVKQGKPAPDIFL 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488238094 147 IAVN-----ALDGRHCIAVEDSPVGIASAKAANLYTIALKqDLPLDQA---QADIVIDDLND 200
Cdd:PLN02811 145 AAARrfedgPVDPGKVLVFEDAPSGVEAAKNAGMSVVMVP-DPRLDKSyckGADQVLSSLLD 205
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 4-206 5.05e-12

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


Pssm-ID: 319815 [Multi-domain]  Cd Length: 214  Bit Score: 62.33  E-value: 5.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   4 GMIFDMDGVLIDSENFYFDRRMQFFKEKNILPGSTNKL-DFVGlteNG----IWEVLVSEKDQRADLRKE-----YLAYR 73
Cdd:cd07512    1 AVIFDLDGTLIDSAPDLHAALNAVLAAEGLAPLSLAEVrSFVG---HGapalIRRAFAAAGEDLDGPLHDallarFLDHY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  74 EKHPIDfKIALRKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNAL- 152
Cdd:cd07512   78 EADPPG-LTRPYPGVIEALERLRAAGWRLAICTNKPEAPARALLSALGLADLFAAVVGGDTLPQRKPDPAPLRAAIRRLg 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488238094 153 -DGRHCIAVEDSPVGIASAKAANL--------YTIALKQDLPldqaqADIVIDDLNDIIQIIE 206
Cdd:cd07512  157 gDVSRALMVGDSETDAATARAAGVpfvlvtfgYRHAPVAELP-----HDAVFSDFDALPDLLA 214
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 5-200 1.34e-11

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 61.78  E-value: 1.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   5 MIFDMDGVLIDSE--NFYFDRRM--------------QFFKEKniLPGSTNKLDFVGLTENGIWEVLVSEKDQRADLRKe 68
Cdd:PLN02770  25 VLFDVDGTLCDSDplHYYAFREMlqeinfnggvpiteEFFVEN--IAGKHNEDIALGLFPDDLERGLKFTDDKEALFRK- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  69 yLAYREKHPIDFKIALRKGAEDildylkkKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIA 148
Cdd:PLN02770 102 -LASEQLKPLNGLYKLKKWIED-------RGLKRAAVTNAPRENAELMISLLGLSDFFQAVIIGSECEHAKPHPDPYLKA 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488238094 149 VNALD--GRHCIAVEDSPVGIASAKAANLYTIALKQDLP---LDQAQADIVIDDLND 200
Cdd:PLN02770 174 LEVLKvsKDHTFVFEDSVSGIKAGVAAGMPVVGLTTRNPeslLMEAKPTFLIKDYED 230
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
 71-202 1.61e-11

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 61.80  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  71 AYREKHPIdfkIALRKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPE--IYQIA 148
Cdd:PRK13223  92 AYADSHEL---TVVYPGVRDTLKWLKKQGVEMALITNKPERFVAPLLDQMKIGRYFRWIIGGDTLPQKKPDPAalLFVMK 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488238094 149 VNALDGRHCIAVEDSPVGIASAKAANLYTIAL----KQDLPLDQAQADIVIDDLNDII 202
Cdd:PRK13223 169 MAGVPPSQSLFVGDSRSDVLAAKAAGVQCVALsygyNHGRPIAEESPALVIDDLRALL 226
CTE7 TIGR02253
HAD superfamily (subfamily IA) hydrolase, TIGR02253; This family of sequences from archaea and ...
 4-202 1.63e-11

HAD superfamily (subfamily IA) hydrolase, TIGR02253; This family of sequences from archaea and metazoans includes the human uncharacterized protein CTE7. Pyrococcus species appear to have three different forms of this enzyme, so it is unclear whether all members of this family have the same function. This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterized by three conserved sequence motifs. By virtue of an alpha helical domain in-between the first and second conserved motif, this family is a member of subfamily IA (TIGR01549).


Pssm-ID: 274057 [Multi-domain]  Cd Length: 221  Bit Score: 61.26  E-value: 1.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094    4 GMIFDMDGVLIDSENFYFDRRMQFFKeknILPGSTNKLDFVGLTE--NGIWEVLVSEKDQRAD--LRKEYLAYREKHPID 79
Cdd:TIGR02253   4 AIFFDLDDTLIDTSGLAEKARRNAIE---VLIEAGLNVDFEEAYEelLKLIKEYGSNYPTHFDylIRRLWEEYNPKLVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   80 FKIALRK----------GAEDILDYLKKKSIKIALASSS-PQREIDKMLTQNALaPYFDFVISGEKLSKSKPHPEIYQIA 148
Cdd:TIGR02253  81 FVYAYHKlkfaylrvypGVRDTLMELRESGYRLGIITDGlPVKQWEKLERLGVR-DFFDAVITSEEEGVEKPHPKIFYAA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488238094  149 VNAL--DGRHCIAVEDSPV-GIASAKAANLYTIALKQ-----DLPLDQAQADIVIDDLNDII 202
Cdd:TIGR02253 160 LKRLgvKPEEAVMVGDRLDkDIKGAKNAGMKTVWINQgksskMEDDVYPYPDYEISSLRELL 221
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 3-211 3.15e-09

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 55.64  E-value: 3.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   3 LGMIFDMDGVLIDsENFYFDRRMQFFKEKNilPGSTNKLDFV-----GL-TENGIWEVLVSEKD----QRADLRKEYLaY 72
Cdd:PLN02575 132 LGAIFEWEGVIIE-DNPDLENQAWLTLAQE--EGKSPPPAFIlrrveGMkNEQAISEVLCWSRDpaelRRMATRKEEI-Y 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  73 REKHPIDFKiaLRKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNAL 152
Cdd:PLN02575 208 QALQGGIYR--LRTGSQEFVNVLMNYKIPMALVSTRPRKTLENAIGSIGIRGFFSVIVAAEDVYRGKPDPEMFIYAAQLL 285

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488238094 153 D--GRHCIAVEDSPVGIASAKAANLYTIALKQDLPL-DQAQADIVIDDLND--IIQIIETYDID 211
Cdd:PLN02575 286 NfiPERCIVFGNSNQTVEAAHDARMKCVAVASKHPIyELGAADLVVRRLDElsIVDLKNLADIE 349
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 6-178 6.35e-09

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: 53.50  E-value: 6.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   6 IFDMDGVLIDSEnfyFDRRMQFFKEKNILPgSTNKLDFVGLT------ENGIWevlvSEKDQRADLRKEYLAYREK---- 75
Cdd:cd02603    5 LFDFGGVLIDPD---PAAAVARFEALTGEP-SEFVLDTEGLAgaflelERGRI----TEEEFWEELREELGRPLSAelfe 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  76 HPIDFKIALRKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAP-YFDFVISGEKLSKSKPHPEIYQIAVNAL-- 152
Cdd:cd02603   77 ELVLAAVDPNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLPRRGdLFDGVVESCRLGVRKPDPEIYQLALERLgv 156

                        170       180
                 ....*....|....*....|....*.
gi 488238094 153 DGRHCIAVEDSPVGIASAKAANLYTI 178
Cdd:cd02603  157 KPEEVLFIDDREENVEAARALGIHAI 182
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 92-203 1.65e-07

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 49.96  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  92 LDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNALD---GRHC-IAVedSPVGI 167
Cdd:cd02588  100 LRRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAEDVRAYKPAPAVYELAAERLGvppDEILhVAS--HAWDL 177

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488238094 168 ASAKAANLYTIALK---QDLPLDQAQADIVIDDLNDIIQ 203
Cdd:cd02588  178 AGARALGLRTAWINrpgEVPDPLGPAPDFVVPDLGELAD 216
PRK13478 PRK13478
phosphonoacetaldehyde hydrolase; Provisional
 87-206 1.08e-06

phosphonoacetaldehyde hydrolase; Provisional


Pssm-ID: 184075 [Multi-domain]  Cd Length: 267  Bit Score: 47.93  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  87 GAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYF-DFVISGEKLSKSKPHPE-IYQ--IAVNALDGRHCIAVED 162
Cdd:PRK13478 105 GVLEVIAALRARGIKIGSTTGYTREMMDVVVPLAAAQGYRpDHVVTTDDVPAGRPYPWmALKnaIELGVYDVAACVKVDD 184

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488238094 163 SPVGIASAKAANLYTIALK-------------QDLP--------------LDQAQADIVIDDLNDIIQIIE 206
Cdd:PRK13478 185 TVPGIEEGLNAGMWTVGVIlsgnelglseeeyQALSaaelaarrerararLRAAGAHYVIDTIADLPAVIA 255
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 90-179 1.36e-06

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: 45.53  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  90 DILDYLKKKSIKIALASSSPQREIdKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNAL--DGRHCIAVEDSPVGI 167
Cdd:cd16421   14 ELLKALRQKGIKLAVLSNKPNEAV-QVLVEELFPGSFDFVLGEKEGIRRKPDPT*ALECAKVLgvPPDEVLYVGDSGVDM 92

                         90
                 ....*....|..
gi 488238094 168 ASAKAANLYTIA 179
Cdd:cd16421   93 QTARNAGMDEIG 104
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 92-153 2.69e-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: 46.18  E-value: 2.69e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488238094   92 LDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNALD 153
Cdd:TIGR01428 101 LRALKERGYRLAILSNGSPAMLKSLVKHAGLDDPFDAVLSADAVRAYKPAPQVYQLALEALG 162
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 88-208 4.33e-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: 44.59  E-value: 4.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  88 AEDILDYLKKKSIKIALASSSPQReIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNALDGR--HCIAVEDSPV 165
Cdd:cd16415   12 AVETLKDLKEKGLKLAVVSNFDRR-LRELLEALGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSpeEALHVGDDLK 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488238094 166 G-IASAKAANLytialkQDLPLDQAQADIVIDDLNDIIQIIETY 208
Cdd:cd16415   91 NdYLGARAVGW------HALLVDREGALHELPSLANLLERLLEL 128
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
 1-207 6.46e-06

bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 46.16  E-value: 6.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   1 MNLGMIFDMDGVLIDSENFY-------FD--RRMQFFKekNILPGSTNKlDFVGLTENGIWEVLVSekDQRADLRKEYLA 71
Cdd:PRK06698 240 MLQALIFDMDGTLFQTDKILelslddtFDhlRSLQLWD--TVTPIDKYR-EIMGVPLPKVWEALLP--DHSLEIREQTDA 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  72 YREKHPIDF----KIALRKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSkSKPHPEIYQI 147
Cdd:PRK06698 315 YFLERLIENiksgKGALYPNVKEIFTYIKENNCSIYIASNGLTEYLRAIVSYYDLDQWVTETFSIEQIN-SLNKSDLVKS 393

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488238094 148 AVNALDGRHCIAVEDSPVGIASAKAANLYTIALKQDLPLDQ--AQADIVIDDLNDIIQIIET 207
Cdd:PRK06698 394 ILNKYDIKEAAVVGDRLSDINAAKDNGLIAIGCNFDFAQEDelAQADIVIDDLLELKGILST 455
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 87-178 1.26e-05

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: 42.91  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  87 GAEDILDYLKKkSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNALD--GRHCIAVEDS- 163
Cdd:cd04305   13 GAKELLEELKK-GYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGvkPEETLMVGDSl 91

                         90
                 ....*....|....*
gi 488238094 164 PVGIASAKAANLYTI 178
Cdd:cd04305   92 ESDILGAKNAGIKTV 106
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 7-173 3.41e-05

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 43.14  E-value: 3.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   7 FDMDGVLIDSENFYFDRRMQFFKEKNIlpgsTNKLDFVGLTENGI--WEVL-VSEKDQRADLRKEYL--AYREKHPIDFK 81
Cdd:PRK10563   9 FDCDGTLVDSEVICSRAYVTMFAEFGI----TLSLEEVFKRFKGVklYEIIdIISKEHGVTLAKAELepVYRAEVARLFD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  82 IALR--KGAEDILDYLKkksIKIALASSSPQREIDKMLTQNALAPYF-DFVISGEKLSKSKPHPEIYQIAVNAL--DGRH 156
Cdd:PRK10563  85 SELEpiAGANALLESIT---VPMCVVSNGPVSKMQHSLGKTGMLHYFpDKLFSGYDIQRWKPDPALMFHAAEAMnvNVEN 161

                        170
                 ....*....|....*..
gi 488238094 157 CIAVEDSPVGIASAKAA 173
Cdd:PRK10563 162 CILVDDSSAGAQSGIAA 178
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 6-203 3.46e-05

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: 43.11  E-value: 3.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   6 IFDMDGVLIDSENFYFdrrmqffkekNILPGSTNKLDFVGLTENGIwEVL----VSEKDQRADLRKEYLA------YREK 75
Cdd:cd04303    3 IFDFDGTLADSFPWFL----------SILNQLAARHGFKTVDEEEI-EQLrqlsSREILKQLGVPLWKLPliakdfRRLM 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  76 HPIDFKIALRKGAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVNALDgr 155
Cdd:cd04303   72 AEAAPELALFPGVEDMLRALHARGVRLAVVSSNSEENIRRVLGPEELISLFAVIEGSSLFGKAKKIRRVLRRTKITAA-- 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488238094 156 HCIAVEDSPVGIASAKAANLYTIA----------LKQDLPldqaqaDIVIDDLNDIIQ 203
Cdd:cd04303  150 QVIYVGDETRDIEAARKVGLAFAAvswgyakpevLKALAP------DHMLEDPEDLIQ 201
HAD_PHN cd02586
Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; ...
 87-180 3.15e-04

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: 40.36  E-value: 3.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  87 GAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYF-DFVISGEKLSKSKPHPeiYQIAVNAL-----DGRHCIAV 160
Cdd:cd02586  102 GVLEVIAKLRARGIKIGSTTGYTREMMDIVLPEAAAQGYRpDSLVTPDDVPAGRPYP--WMCYKNAIelgvyDVAAVVKV 179

                         90       100
                 ....*....|....*....|
gi 488238094 161 EDSPVGIASAKAANLYTIAL 180
Cdd:cd02586  180 GDTVPDIKEGLNAGMWTVGV 199
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 6-178 2.55e-03

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: 37.36  E-value: 2.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094   6 IFDMDGVLIDSENFYFDRRMQFFKEKNILPGSTNKLDFVGLTENGIWEVLVSE-KDQRADlRKEYLAYREKHPIDFKial 84
Cdd:cd07523    3 IWDLDGTLLDSYPAMTKALSETLADFGIPQDLETVYKIIKESSVQFAIQYYAEvPDLEEE-YKELEAEYLAKPILFP--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  85 rkGAEDILDYLKKKSIKIALASSSPQREIDkMLTQNALAPYFDFVISGEKLSKSKPHPEIYQIAVN--ALDGRHCIAVED 162
Cdd:cd07523   79 --GAKAVLRWIKEQGGKNFLMTHRDHSALT-ILKKDGIASYFTEIVTSDNGFPRKPNPEAINYLLNkyQLNPEETVMIGD 155

                        170
                 ....*....|....*.
gi 488238094 163 SPVGIASAKAANLYTI 178
Cdd:cd07523  156 RELDIEAGHNAGISTI 171
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 87-179 3.65e-03

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: 37.19  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488238094  87 GAEDILDYLKKKSIKIALASSSPQREIDKMLTQNALAPYFDFVIsGEKLSKSKPH-PEI--YQIAVNALDGRHCIAVEDS 163
Cdd:cd04302   85 GIPELLEKLKAAGYRLYVATSKPEVFARRILEHFGLDEYFDGIA-GASLDGSRVHkADVirYALDTLGIAPEQAVMIGDR 163

                         90
                 ....*....|....*.
gi 488238094 164 PVGIASAKAANLYTIA 179
Cdd:cd04302  164 KHDIIGARANGIDSIG 179
 
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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