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Conserved domains on  [gi|571487226|ref|XP_006590601|]
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haloacid dehalogenase-like hydrolase domain-containing protein Sgpp isoform X4 [Glycine max]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

HAD (haloacid dehalogenase) family hydrolase; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

EC:  3.6.3.-
Gene Ontology:  GO:0005524|GO:0016887|GO:0005215

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 2-233 3.39e-153

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member PLN02770:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 248  Bit Score: 425.41  E-value: 3.39e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   2 SSLTSLAPLEAVLFDVDGTLCDSDPLHYYALREMLQELGFNGGAPITEEFFVETFSGKHSDDTALVVFPGDLERGLKFVE 81
Cdd:PLN02770  14 SSLSGLAPLEAVLFDVDGTLCDSDPLHYYAFREMLQEINFNGGVPITEEFFVENIAGKHNEDIALGLFPDDLERGLKFTD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  82 DKEAMFRRLASEQLNPLKGLDKVRKWVENHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPYLKA 161
Cdd:PLN02770  94 DKEALFRKLASEQLKPLNGLYKLKKWIEDRGLKRAAVTNAPRENAELMISLLGLSDFFQAVIIGSECEHAKPHPDPYLKA 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 571487226 162 LEVLKASKDHAFVFEDSASGIKAGVAAGMPVIGLATRNPENLLMEAKPAFLIKDYEDSKLWAALEELDKAGA 233
Cdd:PLN02770 174 LEVLKVSKDHTFVFEDSVSGIKAGVAAGMPVVGLTTRNPESLLMEAKPTFLIKDYEDPKLWAALEELDQKGA 245
 
Name Accession Description Interval E-value
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 2-233 3.39e-153

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 425.41  E-value: 3.39e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   2 SSLTSLAPLEAVLFDVDGTLCDSDPLHYYALREMLQELGFNGGAPITEEFFVETFSGKHSDDTALVVFPGDLERGLKFVE 81
Cdd:PLN02770  14 SSLSGLAPLEAVLFDVDGTLCDSDPLHYYAFREMLQEINFNGGVPITEEFFVENIAGKHNEDIALGLFPDDLERGLKFTD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  82 DKEAMFRRLASEQLNPLKGLDKVRKWVENHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPYLKA 161
Cdd:PLN02770  94 DKEALFRKLASEQLKPLNGLYKLKKWIEDRGLKRAAVTNAPRENAELMISLLGLSDFFQAVIIGSECEHAKPHPDPYLKA 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 571487226 162 LEVLKASKDHAFVFEDSASGIKAGVAAGMPVIGLATRNPENLLMEAKPAFLIKDYEDSKLWAALEELDKAGA 233
Cdd:PLN02770 174 LEVLKVSKDHTFVFEDSVSGIKAGVAAGMPVVGLTTRNPESLLMEAKPTFLIKDYEDPKLWAALEELDQKGA 245
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
9-218 7.08e-57

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 179.63  E-value: 7.08e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   9 PLEAVLFDVDGTLCDSDPLHYYALREMLQELGFnggaPITEEFFvETFSGKHSDDTALVVFPgdlERGLK-----FVEDK 83
Cdd:COG0637    1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGI----DLTEEEY-RRLMGRSREDILRYLLE---EYGLDlpeeeLAARK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  84 EAMFR-RLASEQLNPLKGLDKVRKWVENHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPYLKAL 162
Cdd:COG0637   73 EELYReLLAEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAA 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 571487226 163 EVLKASKDHAFVFEDSASGIKAGVAAGMPVIGLATRNPENLLMeAKPAFLIKDYED 218
Cdd:COG0637  153 ERLGVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEEL-AGADLVVDDLAE 207
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 12-197 1.18e-38

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: 130.81  E-value: 1.18e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  12 AVLFDVDGTLCDSDPLHYYALREMlqelgfnggapiteeffvetfsgkhsddtalvvfpgdlerglkfvEDKEAMFRRLA 91
Cdd:cd07505    1 AVIFDMDGVLIDTEPLHRQAWQLL---------------------------------------------ERKNALLLELI 35

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  92 SEQLNPLK-GLDKVRKWVENHGLKRAAVTNAPRKNAELIISKLGLT-DFFDAVIIGDECEHAKPHPEPYLKALEVLKASK 169
Cdd:cd07505   36 ASEGLKLKpGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLrGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDP 115

                        170       180
                 ....*....|....*....|....*...
gi 571487226 170 DHAFVFEDSASGIKAGVAAGMPVIGLAT 197
Cdd:cd07505  116 ERCLVFEDSLAGIEAAKAAGMTVVAVPD 143
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
13-194 9.42e-37

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 127.32  E-value: 9.42e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   13 VLFDVDGTLCDSDPLHYYALREMLQELGFNggaPITEEFFVEtFSGKHSDDTALVVFPGdlergLKFVEDKEAMFRR--- 89
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYG---ELSEEEILK-FIGLPLREIFRYLGVS-----EDEEEKIEFYLRKyne 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   90 -LASEQLNPLKGLDKVRKWVENHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPYLKALEVLKAS 168
Cdd:pfam13419  72 eLHDKLVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLK 151

                         170       180
                  ....*....|....*....|....*.
gi 571487226  169 KDHAFVFEDSASGIKAGVAAGMPVIG 194
Cdd:pfam13419 152 PEEVIYVGDSPRDIEAAKNAGIKVIA 177
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 10-194 1.09e-36

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: 127.46  E-value: 1.09e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   10 LEAVLFDVDGTLCDSDPLHYYALREMLQELGFnggaPITEEFFVEtFSGKHSDDTA-----LVVFPGDLERGLKFVEDKE 84
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGI----SFDKQYNES-LKGLSREDILrailkLRGDGLSLEEIHQLAERKN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   85 AMFRRLASEQLN-PLKGLDKVRKWVENHGLKRAAVTNapRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPYLKALE 163
Cdd:TIGR02009  76 ELYRELLRLTGVaVLPGIRNLLKRLKAKGIAVGLGSS--SKNAPRILAKLGLRDYFDAIVDASEVKNGKPHPETFLLAAE 153

                         170       180       190
                  ....*....|....*....|....*....|.
gi 571487226  164 VLKASKDHAFVFEDSASGIKAGVAAGMPVIG 194
Cdd:TIGR02009 154 LLGVPPNECIVFEDALAGVQAARAAGMFAVA 184
 
Name Accession Description Interval E-value
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 2-233 3.39e-153

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 425.41  E-value: 3.39e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   2 SSLTSLAPLEAVLFDVDGTLCDSDPLHYYALREMLQELGFNGGAPITEEFFVETFSGKHSDDTALVVFPGDLERGLKFVE 81
Cdd:PLN02770  14 SSLSGLAPLEAVLFDVDGTLCDSDPLHYYAFREMLQEINFNGGVPITEEFFVENIAGKHNEDIALGLFPDDLERGLKFTD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  82 DKEAMFRRLASEQLNPLKGLDKVRKWVENHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPYLKA 161
Cdd:PLN02770  94 DKEALFRKLASEQLKPLNGLYKLKKWIEDRGLKRAAVTNAPRENAELMISLLGLSDFFQAVIIGSECEHAKPHPDPYLKA 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 571487226 162 LEVLKASKDHAFVFEDSASGIKAGVAAGMPVIGLATRNPENLLMEAKPAFLIKDYEDSKLWAALEELDKAGA 233
Cdd:PLN02770 174 LEVLKVSKDHTFVFEDSVSGIKAGVAAGMPVVGLTTRNPESLLMEAKPTFLIKDYEDPKLWAALEELDQKGA 245
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
9-218 7.08e-57

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 179.63  E-value: 7.08e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   9 PLEAVLFDVDGTLCDSDPLHYYALREMLQELGFnggaPITEEFFvETFSGKHSDDTALVVFPgdlERGLK-----FVEDK 83
Cdd:COG0637    1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGI----DLTEEEY-RRLMGRSREDILRYLLE---EYGLDlpeeeLAARK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  84 EAMFR-RLASEQLNPLKGLDKVRKWVENHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPYLKAL 162
Cdd:COG0637   73 EELYReLLAEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAA 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 571487226 163 EVLKASKDHAFVFEDSASGIKAGVAAGMPVIGLATRNPENLLMeAKPAFLIKDYED 218
Cdd:COG0637  153 ERLGVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEEL-AGADLVVDDLAE 207
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 12-197 1.18e-38

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: 130.81  E-value: 1.18e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  12 AVLFDVDGTLCDSDPLHYYALREMlqelgfnggapiteeffvetfsgkhsddtalvvfpgdlerglkfvEDKEAMFRRLA 91
Cdd:cd07505    1 AVIFDMDGVLIDTEPLHRQAWQLL---------------------------------------------ERKNALLLELI 35

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  92 SEQLNPLK-GLDKVRKWVENHGLKRAAVTNAPRKNAELIISKLGLT-DFFDAVIIGDECEHAKPHPEPYLKALEVLKASK 169
Cdd:cd07505   36 ASEGLKLKpGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLrGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDP 115

                        170       180
                 ....*....|....*....|....*...
gi 571487226 170 DHAFVFEDSASGIKAGVAAGMPVIGLAT 197
Cdd:cd07505  116 ERCLVFEDSLAGIEAAKAAGMTVVAVPD 143
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
12-227 1.73e-38

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 132.75  E-value: 1.73e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  12 AVLFDVDGTLCDSDPLHYYALREMLQELGFnggAPITEEFfVETFSGKHSDDTALVVFPGDLERGLKFVEDK-EAMFRRL 90
Cdd:COG0546    3 LVLFDLDGTLVDSAPDIAAALNEALAELGL---PPLDLEE-LRALIGLGLRELLRRLLGEDPDEELEELLARfRELYEEE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  91 ASEQLNPLKGLDKVRKWVENHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPYLKALEVLKASKD 170
Cdd:COG0546   79 LLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLDPE 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 571487226 171 HAFVFEDSASGIKAGVAAGMPVIGLAT-RNPENLLMEAKPAFLIKDYEDskLWAALEE 227
Cdd:COG0546  159 EVLMVGDSPHDIEAARAAGVPFIGVTWgYGSAEELEAAGADYVIDSLAE--LLALLAE 214
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
13-194 9.42e-37

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 127.32  E-value: 9.42e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   13 VLFDVDGTLCDSDPLHYYALREMLQELGFNggaPITEEFFVEtFSGKHSDDTALVVFPGdlergLKFVEDKEAMFRR--- 89
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYG---ELSEEEILK-FIGLPLREIFRYLGVS-----EDEEEKIEFYLRKyne 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   90 -LASEQLNPLKGLDKVRKWVENHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPYLKALEVLKAS 168
Cdd:pfam13419  72 eLHDKLVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLK 151

                         170       180
                  ....*....|....*....|....*.
gi 571487226  169 KDHAFVFEDSASGIKAGVAAGMPVIG 194
Cdd:pfam13419 152 PEEVIYVGDSPRDIEAAKNAGIKVIA 177
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 10-194 1.09e-36

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: 127.46  E-value: 1.09e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   10 LEAVLFDVDGTLCDSDPLHYYALREMLQELGFnggaPITEEFFVEtFSGKHSDDTA-----LVVFPGDLERGLKFVEDKE 84
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGI----SFDKQYNES-LKGLSREDILrailkLRGDGLSLEEIHQLAERKN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   85 AMFRRLASEQLN-PLKGLDKVRKWVENHGLKRAAVTNapRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPYLKALE 163
Cdd:TIGR02009  76 ELYRELLRLTGVaVLPGIRNLLKRLKAKGIAVGLGSS--SKNAPRILAKLGLRDYFDAIVDASEVKNGKPHPETFLLAAE 153

                         170       180       190
                  ....*....|....*....|....*....|.
gi 571487226  164 VLKASKDHAFVFEDSASGIKAGVAAGMPVIG 194
Cdd:TIGR02009 154 LLGVPPNECIVFEDALAGVQAARAAGMFAVA 184
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 12-207 6.85e-32

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


Pssm-ID: 319859 [Multi-domain]  Cd Length: 169  Bit Score: 114.27  E-value: 6.85e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  12 AVLFDVDGTLCDSDPLHYYALREMLQELgfnggapiTEEFFVETFSGKhsddtalvvfpgdlerglkfvedkeamfrrla 91
Cdd:cd16423    1 AVIFDFDGVIVDTEPLWYEAWQELLNER--------RNELIKRQFSEK-------------------------------- 40

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  92 sEQLNPLKGLDKVRKWVENHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPYLKALEVLKASKDH 171
Cdd:cd16423   41 -TDLPPIEGVKELLEFLKEKGIKLAVASSSPRRWIEPHLERLGLLDYFEVIVTGDDVEKSKPDPDLYLEAAERLGVNPEE 119

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 571487226 172 AFVFEDSASGIKAGVAAGMPVIGLATRNPENLLMEA 207
Cdd:cd16423  120 CVVIEDSRNGVLAAKAAGMKCVGVPNPVTGSQDFSK 155
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 11-218 6.15e-28

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: 105.44  E-value: 6.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  11 EAVLFDVDGTLCDSDPLHYYALREMLQELGFNGGAPitEEffVETFSGKHSDDTALVVFPGDLERGLK-FVEDKEAMFRR 89
Cdd:cd02616    2 TTILFDLDGTLIDTNELIIKSFNHTLKEYGLEGYTR--EE--VLPFIGPPLRETFEKIDPDKLEDMVEeFRKYYREHNDD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  90 LASEQLNPLKGLDKVRKwvenHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPYLKALEVLKASK 169
Cdd:cd02616   78 LTKEYPGVYETLARLKS----QGIKLGVVTTKLRETALKGLKLLGLDKYFDVIVGGDDVTHHKPDPEPVLKALELLGAEP 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 571487226 170 DHAFVFEDSASGIKAGVAAGMPVIGLA-TRNPENLLMEAKPAFLIKDYED 218
Cdd:cd02616  154 EEALMVGDSPHDILAGKNAGVKTVGVTwGYKGREYLKAFNPDFIIDKMSD 203
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 11-218 7.86e-27

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: 102.80  E-value: 7.86e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  11 EAVLFDVDGTLCDSDPLHYYALREMLQELGFNGGA--------PITEEFFVETFSGKHSDDTALVVFpgDLERGLKFVED 82
Cdd:COG1011    2 KAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAeelaeayrAIEYALWRRYERGEITFAELLRRL--LEELGLDLAEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  83 KEAMFRRLASEQLNPLKG----LDKVRKwvenHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPY 158
Cdd:COG1011   80 LAEAFLAALPELVEPYPDalelLEALKA----RGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIF 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 571487226 159 LKALEVLKASKDHAFVFEDSASG-IKAGVAAGMPVIgLATRNPENLLMEAKPAFLIKDYED 218
Cdd:COG1011  156 ELALERLGVPPEEALFVGDSPETdVAGARAAGMRTV-WVNRSGEPAPAEPRPDYVISDLAE 215
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 12-195 6.19e-25

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: 97.69  E-value: 6.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  12 AVLFDVDGTLCDSDPLHYYALREMLQELGFnggAPITEEFfVETFSGKHSD---DTALVvFPGDLERGLKFVEDKEAMFR 88
Cdd:cd16417    1 LVAFDLDGTLVDSAPDLAEAANAMLAALGL---PPLPEET-VRTWIGNGADvlvERALT-GAREAEPDEELFKEARALFD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  89 RLASEQL----NPLKGLDKVRKWVENHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPYLKALEV 164
Cdd:cd16417   76 RHYAETLsvhsHLYPGVKEGLAALKAQGYPLACVTNKPERFVAPLLEALGISDYFSLVLGGDSLPEKKPDPAPLLHACEK 155

                        170       180       190
                 ....*....|....*....|....*....|.
gi 571487226 165 LKASKDHAFVFEDSASGIKAGVAAGMPVIGL 195
Cdd:cd16417  156 LGIAPAQMLMVGDSRNDILAARAAGCPSVGL 186
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
5-195 9.36e-24

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 94.88  E-value: 9.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   5 TSLAPLEAVLFDVDGTLCDSDP-LHYyALREMLQELGFnggAPITEEFfVETFSGKHSD---DTALVVFPGDLERGLkfV 80
Cdd:PRK13222   1 MKFMDIRAVAFDLDGTLVDSAPdLAA-AVNAALAALGL---PPAGEER-VRTWVGNGADvlvERALTWAGREPDEEL--L 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  81 EDKEAMFRRLASE------QLNP--LKGLDKVRKwvenHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAK 152
Cdd:PRK13222  74 EKLRELFDRHYAEnvaggsRLYPgvKETLAALKA----AGYPLAVVTNKPTPFVAPLLEALGIADYFSVVIGGDSLPNKK 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 571487226 153 PHPEPYLKALEVLKASKDHAFVFEDSASGIKAGVAAGMPVIGL 195
Cdd:PRK13222 150 PDPAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPSVGV 192
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 10-189 3.99e-23

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: 92.26  E-value: 3.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   10 LEAVLFDVDGTLCDSDPLHYYALREMLQE--------LGFNGGAPITEEFFVETFSGKHSDDTALVVFPGD---LERGLK 78
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEhplakaivAAAEDLPIPVEDFTARLLLGKRDWLEELDILRGLvetLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   79 FVEDKEAMFRRLASEQLNPLKGLDKVRKWVENHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPY 158
Cdd:pfam00702  81 TVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIY 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 571487226  159 LKALEVLKASKDHAFVFEDSASGIKAGVAAG 189
Cdd:pfam00702 161 LAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 12-218 7.61e-23

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: 92.02  E-value: 7.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  12 AVLFDVDGTLCDSDPLHYYALREMLQELGFNggapitEEFFVETFSGKHSDDTALVVFPGDlerglkfvEDKEAMFRRLA 91
Cdd:cd07527    1 ALLFDMDGTLVDSTPAVERAWHKWAKEHGVD------PEEVLKVSHGRRAIDVIRKLAPDD--------ADIELVLALET 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  92 ------SEQLNPLKGLDKVRKWVENHGLKRAAVTNAPRKNAE--LIISKLGLTDFFdavIIGDECEHAKPHPEPYLKALE 163
Cdd:cd07527   67 eepesyPEGVIAIPGAVDLLASLPAAGDRWAIVTSGTRALAEarLEAAGLPHPEVL---VTADDVKNGKPDPEPYLLGAK 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 571487226 164 VLKASKDHAFVFEDSASGIKAGVAAGMPVIGLATRNPENLLMEAKPAFLIKDYED 218
Cdd:cd07527  144 LLGLDPSDCVVFEDAPAGIKAGKAAGARVVAVNTSHDLEQLEAAGADLVVEDLSD 198
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 12-218 1.15e-22

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 91.63  E-value: 1.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  12 AVLFDVDGTLCDSDPL----------HYYALREMLQE-LGFNGgapiteEFFVETFSGKhsddtalvvfpgDLERglkfV 80
Cdd:PRK13288   5 TVLFDLDGTLINTNELiissflhtlkTYYPNQYKREDvLPFIG------PSLHDTFSKI------------DESK----V 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  81 EDKEAMFRRLASEQLNPL----KGLDKVRKWVENHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPE 156
Cdd:PRK13288  63 EEMITTYREFNHEHHDELvteyETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPDPE 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 571487226 157 PYLKALEVLKASKDHAFVFEDSASGIKAGVAAGMPVIGLA-TRNPENLLMEAKPAFLIKDYED 218
Cdd:PRK13288 143 PVLKALELLGAKPEEALMVGDNHHDILAGKNAGTKTAGVAwTIKGREYLEQYKPDFMLDKMSD 205
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 12-195 1.72e-21

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: 87.48  E-value: 1.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   12 AVLFDVDGTLCDSDPLHYyalremlQELGFNGGAPITEEFFVEtfSGKHSDDTALVVFP--GDLERGLKFVEDKEAMFRR 89
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAIA-------KLINREELGLVPDELGVS--AVGRLELALRRFKAqyGRTISPEDAQLLYKQLFYE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   90 --LASEQLNPLKGLDKVRKWVENHGLKRAAVTNAPRkNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPYLKALEVLKA 167
Cdd:TIGR01509  72 qiEEEAKLKPLPGVRALLEALRARGKKLALLTNSPR-AHKLVLALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGL 150

                         170       180
                  ....*....|....*....|....*...
gi 571487226  168 SKDHAFVFEDSASGIKAGVAAGMPVIGL 195
Cdd:TIGR01509 151 EPSECVFVDDSPAGIEAAKAAGMHTVGV 178
PGP_bact TIGR01449
2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate ...
 13-195 4.35e-20

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


Pssm-ID: 130516 [Multi-domain]  Cd Length: 213  Bit Score: 84.87  E-value: 4.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   13 VLFDVDGTLCDSDPLHYYALREMLQELGfngGAPITEEFfVETFSGKHSDDTALVVFP-GDLERGLKFVEDKEAMFRR-- 89
Cdd:TIGR01449   1 VLFDLDGTLVDSAPDIAAAVNMALAALG---LPPATLAR-VIGFIGNGVPVLMERVLAwAGQEPDAQRVAELRKLFDRhy 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   90 --LASEQLNPLKGLDKVRKWVENHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPYLKALEVLKA 167
Cdd:TIGR01449  77 eeVAGELTSVFPGVEATLGALRAKGLRLGLVTNKPTPLARPLLELLGLAKYFSVLIGGDSLAQRKPHPDPLLLAAERLGV 156

                         170       180
                  ....*....|....*....|....*...
gi 571487226  168 SKDHAFVFEDSASGIKAGVAAGMPVIGL 195
Cdd:TIGR01449 157 APQQMVYVGDSRVDIQAARAAGCPSVLL 184
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
11-193 9.55e-20

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 83.20  E-value: 9.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  11 EAVLFDVDGTLCDSDPLHYYALREMLQELGFnggapiteeffvetfsgkHSDDTALVVFPG----------------DLE 74
Cdd:PRK10725   6 AGLIFDMDGTILDTEPTHRKAWREVLGRYGL------------------QFDEQAMVALNGsptwriaqaiielnqaDLD 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  75 rGLKFVEDKEAMFRRLASEQLNPLKGLDKVRKWvenHGLKRAAV-TNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKP 153
Cdd:PRK10725  68 -PHALAREKTEAVKSMLLDSVEPLPLIEVVKAW---HGRRPMAVgTGSESAIAEALLAHLGLRRYFDAVVAADDVQHHKP 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 571487226 154 HPEPYLKALEVLKASKDHAFVFEDSASGIKAGVAAGMPVI 193
Cdd:PRK10725 144 APDTFLRCAQLMGVQPTQCVVFEDADFGIQAARAAGMDAV 183
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 11-195 4.52e-18

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: 77.74  E-value: 4.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  11 EAVLFDVDGTLCDSDPLHYYALREMLQELGFnggapITEEFFvetfsgkhsddtalvvfpgdlERGLKFVEDKEAMFRRL 90
Cdd:cd07526    1 DLVIFDCDGVLVDSEVIAARVLVEVLAELGA-----RVLAAF---------------------EAELQPIPGAAAALSAL 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  91 aseqlnplkgldkvrkwvenhGLKRAAVTNAPRKNAELIISKLGLTDFFDAVII-GDECEHAKPHPEPYLKALEVLKASK 169
Cdd:cd07526   55 ---------------------TLPFCVASNSSRERLTHSLGLAGLLAYFEGRIFsASDVGRGKPAPDLFLHAAAQMGVAP 113

                        170       180
                 ....*....|....*....|....*.
gi 571487226 170 DHAFVFEDSASGIKAGVAAGMPVIGL 195
Cdd:cd07526  114 ERCLVIEDSPTGVRAALAAGMTVFGF 139
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 12-207 4.62e-18

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: 78.49  E-value: 4.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  12 AVLFDVDGTLCDSDPLHYYALREMLQElgfnggapiteEFFVEtfsgkhsddtalvvfpgdlERGLKFVEdkeaMFRRLA 91
Cdd:cd02598    1 GVIFDLDGVITDTAEYHYRAWKKLADK-----------EELAA-------------------RKNRIYVE----LIEELT 46

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  92 SEQLNPlkGLDKVRKWVENHGLKrAAVTNApRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPYLKALEVLKASKDH 171
Cdd:cd02598   47 PVDVLP--GIASLLVDLKAKGIK-IALASA-SKNAPKILEKLGLAEYFDAIVDGAVLAKGKPDPDIFLAAAEGLGLNPKD 122

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 571487226 172 AFVFEDSASGIKAGVAAGMPVIGLAtrNPENLLMEA 207
Cdd:cd02598  123 CIGVEDAQAGIRAIKAAGFLVVGVG--REEDLLGAD 156
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 9-215 5.21e-18

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 82.59  E-value: 5.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226    9 PLEAVLFDVDGTLCDSDPLHYYALREMLQELGFNggapITEEFFVeTFSGkhsddTALVVFPGDLE-----RGLKFVEDK 83
Cdd:PLN02919   74 KVSAVLFDMDGVLCNSEEPSRRAAVDVFAEMGVE----VTVEDFV-PFMG-----TGEANFLGGVAsvkgvKGFDPDAAK 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   84 EAMFRRLASEQLNPLKG------LDKVRKwVENHGLKRAAVTNAPRKNAELIISKLGLT-DFFDAVIIGDECEHAKPHPE 156
Cdd:PLN02919  144 KRFFEIYLEKYAKPNSGigfpgaLELITQ-CKNKGLKVAVASSADRIKVDANLAAAGLPlSMFDAIVSADAFENLKPAPD 222

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 571487226  157 PYLKALEVLKASKDHAFVFEDSASGIKAGVAAGMPVIGLATRNPENLLMEAKPAFLIKD 215
Cdd:PLN02919  223 IFLAAAKILGVPTSECVVIEDALAGVQAARAAGMRCIAVTTTLSEEILKDAGPSLIRKD 281
PLN02940 PLN02940
riboflavin kinase
 1-193 8.53e-18

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 81.03  E-value: 8.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   1 MSSLTSLAPL-EAVLFDVDGTLCDSDPLHYYALREMLQELGFNGGAPITEEFFvetfsGKHSDDTALVVFpGDLERGLKf 79
Cdd:PLN02940   1 MSAAKPLKKLvSHVILDLDGTLLNTDGIVSDVLKAFLVKYGKQWDGREAQKIV-----GKTPLEAAATVV-EDYGLPCS- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  80 VEDKEAMFRRLASEQ---LNPLKGLDKVRKWVENHGLKRAAVTNAPRKNAELIIS-KLGLTDFFDAVIIGDECEHAKPHP 155
Cdd:PLN02940  74 TDEFNSEITPLLSEQwcnIKALPGANRLIKHLKSHGVPMALASNSPRANIEAKIScHQGWKESFSVIVGGDEVEKGKPSP 153

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 571487226 156 EPYLKALEVLKASKDHAFVFEDSASGIKAGVAAGMPVI 193
Cdd:PLN02940 154 DIFLEAAKRLNVEPSNCLVIEDSLPGVMAGKAAGMEVI 191
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 10-192 4.08e-17

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 77.04  E-value: 4.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  10 LEAVLFDVDGTLCDSDPLHYYALREMLQELGFNggAPITEEFfvETFSG-KHSDDTALVvfpgDLERGLKF-VEDKEAMF 87
Cdd:PRK10563   4 IEAVFFDCDGTLVDSEVICSRAYVTMFAEFGIT--LSLEEVF--KRFKGvKLYEIIDII----SKEHGVTLaKAELEPVY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  88 R----RLASEQLNPLKGldkVRKWVENHGLKRAAVTNAPRKNAELIISKLGLTDFF-DAVIIGDECEHAKPHPEPYLKAL 162
Cdd:PRK10563  76 RaevaRLFDSELEPIAG---ANALLESITVPMCVVSNGPVSKMQHSLGKTGMLHYFpDKLFSGYDIQRWKPDPALMFHAA 152

                        170       180       190
                 ....*....|....*....|....*....|
gi 571487226 163 EVLKASKDHAFVFEDSASGIKAGVAAGMPV 192
Cdd:PRK10563 153 EAMNVNVENCILVDDSSAGAQSGIAAGMEV 182
CTE7 TIGR02253
HAD superfamily (subfamily IA) hydrolase, TIGR02253; This family of sequences from archaea and ...
 12-190 1.31e-16

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: 75.52  E-value: 1.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   12 AVLFDVDGTLCDSDPLHYYALREML-------QELGFNGGAPITEEFFVETFS--GKHSDDTALVVfpgDLERGLKFVED 82
Cdd:TIGR02253   4 AIFFDLDDTLIDTSGLAEKARRNAIevlieagLNVDFEEAYEELLKLIKEYGSnyPTHFDYLIRRL---WEEYNPKLVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   83 KEAMFRRLASEQLNPLKGLDKVRKWVENHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPYLKAL 162
Cdd:TIGR02253  81 FVYAYHKLKFAYLRVYPGVRDTLMELRESGYRLGIITDGLPVKQWEKLERLGVRDFFDAVITSEEEGVEKPHPKIFYAAL 160

                         170       180
                  ....*....|....*....|....*....
gi 571487226  163 EVLKASKDHAFVFEDS-ASGIKAGVAAGM 190
Cdd:TIGR02253 161 KRLGVKPEEAVMVGDRlDKDIKGAKNAGM 189
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 12-195 8.71e-16

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: 73.12  E-value: 8.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  12 AVLFDVDGTLCDSDPLHYYALREMLQELGfngGAPITEeffvetfsgkhsDDTALVVFPGD---LERGL------KFVED 82
Cdd:cd07512    1 AVIFDLDGTLIDSAPDLHAALNAVLAAEG---LAPLSL------------AEVRSFVGHGApalIRRAFaaagedLDGPL 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  83 KEAMFRRLASEQLNPLKGLDKVRKWVEN-------HGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKPHP 155
Cdd:cd07512   66 HDALLARFLDHYEADPPGLTRPYPGVIEalerlraAGWRLAICTNKPEAPARALLSALGLADLFAAVVGGDTLPQRKPDP 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 571487226 156 EPYLKALEVLKASKDHAFVFEDSASGIKAGVAAGMPVIGL 195
Cdd:cd07512  146 APLRAAIRRLGGDVSRALMVGDSETDAATARAAGVPFVLV 185
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 12-193 6.01e-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: 70.87  E-value: 6.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  12 AVLFDVDGTLCDSDPLHYYAL-------------------REMLQELGfnGGAPITEEFFVEtfsGKH-SDDTALVVFPG 71
Cdd:cd07528    1 ALIFDVDGTLAETEELHRRAFnnaffaergldwywdrelyGELLRVGG--GKERIAAYFEKV---GWPeSAPKDLKELIA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  72 DLERglkfveDKEAMFRRL-ASEQLNPLKGLDKVRKWVENHGLKRAAVTNAPRKNAELIISKL---GLTDFFDAVIIGDE 147
Cdd:cd07528   76 DLHK------AKTERYAELiAAGLLPLRPGVARLIDEAKAAGVRLAIATTTSPANVDALLSALlgpERRAIFDAIAAGDD 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 571487226 148 CEHAKPHPEPYLKALEVLKASKDHAFVFEDSASGIKAGVAAGMPVI 193
Cdd:cd07528  150 VAEKKPDPDIYLLALERLGVSPSDCLAIEDSAIGLQAAKAAGLPCI 195
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 106-195 1.38e-14

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: 67.42  E-value: 1.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226 106 KWVENHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPYLKALEVLKASKDHAFVFEDSASGIKAG 185
Cdd:cd01427   17 KRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSENDIEAA 96

                         90
                 ....*....|
gi 571487226 186 VAAGMPVIGL 195
Cdd:cd01427   97 RAAGGRTVAV 106
PRK10826 PRK10826
hexitol phosphatase HxpB;
1-190 1.15e-13

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 67.67  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   1 MSSLtslaPLEAVLFDVDGTLCDSDPLHYYALREMLQELGFnggaPITEEFFVETFSGKHSDdtaLVV------FPGDle 74
Cdd:PRK10826   2 STPR----QILAAIFDMDGLLIDSEPLWDRAELDVMASLGV----DISRREELPDTLGLRID---QVVdlwyarQPWN-- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  75 rGLKFVEDKEAMFRRLASEQLN---PLKGLDKVRKWVENHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHA 151
Cdd:PRK10826  69 -GPSRQEVVQRIIARVISLIEEtrpLLPGVREALALCKAQGLKIGLASASPLHMLEAVLTMFDLRDYFDALASAEKLPYS 147

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 571487226 152 KPHPEPYLKALEVLKASKDHAFVFEDSASGIKAGVAAGM 190
Cdd:PRK10826 148 KPHPEVYLNCAAKLGVDPLTCVALEDSFNGMIAAKAARM 186
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 11-215 1.93e-13

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: 66.91  E-value: 1.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  11 EAVLFDVDGTLCDSDPLhyyaLREMLQELGFNGGApITEEFFVETFSgkHSDDTAL----VVFPGDLERGLKFV------ 80
Cdd:cd02588    1 KALVFDVYGTLIDWHSG----LAAAERAFPGRGEE-LSRLWRQKQLE--YTWLVTLmgpyVDFDELTRDALRATaaelgl 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  81 EDKEAMFRRLASEQLNpLK-------GLDKVRKwvenHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKP 153
Cdd:cd02588   74 ELDESDLDELGDAYLR-LPpfpdvvaGLRRLRE----AGYRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAEDVRAYKP 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 571487226 154 HPEPYLKALEVLKASKDHAFVFEDSASGIKAGVAAGMPVIGLATRNPENLLMEAKPAFLIKD 215
Cdd:cd02588  149 APAVYELAAERLGVPPDEILHVASHAWDLAGARALGLRTAWINRPGEVPDPLGPAPDFVVPD 210
PRK13226 PRK13226
phosphoglycolate phosphatase; Provisional
 1-191 4.59e-13

phosphoglycolate phosphatase; Provisional


Pssm-ID: 237311 [Multi-domain]  Cd Length: 229  Bit Score: 66.03  E-value: 4.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   1 MSSLTSLAPLEAVLFDVDGTLCDSDPLHYYALREMLQElgfNGGAPITEEFFVETFSgKHSDDTALVVFPgDLERGLK-- 78
Cdd:PRK13226   3 LTEVAAVRFPRAVLFDLDGTLLDSAPDMLATVNAMLAA---RGRAPITLAQLRPVVS-KGARAMLAVAFP-ELDAAARda 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  79 ----FVEDKEAmfrrLASEQLNPLKGLDKVRKWVENHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKPH 154
Cdd:PRK13226  78 lipeFLQRYEA----LIGTQSQLFDGVEGMLQRLECAGCVWGIVTNKPEYLARLILPQLGWEQRCAVLIGGDTLAERKPH 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 571487226 155 PEPYLKALEVLKASKDHAFVFEDSASGIKAGVAAGMP 191
Cdd:PRK13226 154 PLPLLVAAERIGVAPTDCVYVGDDERDILAARAAGMP 190
YjjG/YfnB TIGR02254
noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including ...
 13-228 4.21e-12

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


Pssm-ID: 162788 [Multi-domain]  Cd Length: 224  Bit Score: 63.28  E-value: 4.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   13 VLFDVDGTLCDSDPLHYYALREMLQELGFnggaPITEEFF-----------VETFSGKHSDDTALVVFPGDLERGLKFVE 81
Cdd:TIGR02254   4 LLFDLDDTILDFQAAEALALRLLFEDQGI----PLTEDMFaqykeinqglwRAYEEGKITKDEVVNTRFSALLKEYNTEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   82 DKEAM---FRRLASEQLNPLKGLDKVRKWVENHgLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPY 158
Cdd:TIGR02254  80 DEALLnqkYLRFLEEGHQLLPGAFELMENLQQK-FRLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDKEIF 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 571487226  159 LKALE-VLKASKDHAFVFEDS-ASGIKAGVAAGMPVIGLatrNPEnllMEAKPAFLIKDYEDSKLWAALEEL 228
Cdd:TIGR02254 159 NYALErMPKFSKEEVLMIGDSlTADIKGGQNAGLDTCWM---NPD---MHPNPDDIIPTYEIRSLEELYEIL 224
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 11-193 1.23e-11

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: 61.59  E-value: 1.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  11 EAVLFDVDGTLCDSDPLHYYALREMLQELGfnggapiteeffvETFS--------GKHSDDTALVV-----FPGDLERgl 77
Cdd:cd07529    2 THCIFDMDGLLLDTERIYTETTQEILARYG-------------KTYTwdvkakmmGRPASEAARIIvdelkLPMSLEE-- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  78 KFVEDKEAMFRRLASeQLNPLKGLDKVRKWVENHGLKRAAVTNAPRKNAELIISKLG-LTDFFDAVIIGDECE---HAKP 153
Cdd:cd07529   67 EFDEQQEALAELFMG-TAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKeLFSLFHHVVTGDDPEvkgRGKP 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 571487226 154 HPEPYLKALEVLK---ASKDHAFVFEDSASGIKAGVAAGMPVI 193
Cdd:cd07529  146 APDIFLVAAKRFNeppKDPSKCLVFEDSPNGVKAAKAAGMQVV 188
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 12-189 2.53e-11

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 60.10  E-value: 2.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   12 AVLFDVDGTLCDSDPLHYYALREMLQELGFNG--------GAPITEEFFVETFSGkhSDDTALVVFPGDLERGLKFVEDK 83
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFGLDPasfkalkqAGGLAEEEWYRIATS--ALEELQGRFWSEYDAEEAYIRGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   84 EAMFRRLASEqlnplkgldkvrkwvenhGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECeHAKPHPEPYLKALE 163
Cdd:TIGR01549  79 ADLLARLKSA------------------GIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEP-GSKPEPEIFLAALE 139

                         170       180
                  ....*....|....*....|....*.
gi 571487226  164 VLKASkDHAFVFEDSASGIKAGVAAG 189
Cdd:TIGR01549 140 SLGVP-PEVLHVGDNLNDIEGARNAG 164
Pyr-5-nucltdase TIGR01993
pyrimidine 5'-nucleotidase; This family of proteins includes the SDT1/SSM1 gene from yeast ...
 77-190 1.47e-10

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


Pssm-ID: 273917 [Multi-domain]  Cd Length: 183  Bit Score: 58.52  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   77 LKFVEDKEAMFRRLASEQL-NPLKGLdKVRKWVenhglkraaVTNAPRKNAELIISKLGLTDFFDAVIigdECEHA---- 151
Cdd:TIGR01993  71 LRYVHGRLPYDKLKPDPELrNLLLRL-PGRKII---------FTNGDRAHARRALRRLGIEDCFDGIF---CFDTAnpdl 137

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 571487226  152 --KPHPEPYLKALEVLKASKDHAFVFEDSASGIKAGVAAGM 190
Cdd:TIGR01993 138 lpKPSPQAYEKALREAGVDPERAIFFDDSARNIAAGKALGM 178
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 2-193 1.75e-10

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 59.34  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   2 SSLTSLAPLEAVLFDVDGTLCDSDP-LHYYA------------------LREMLQELGfnGGAPITEEFFVETFSGKHSD 62
Cdd:PLN02779  32 ASASASALPEALLFDCDGVLVETERdGHRVAfndafkefglrpvewdveLYDELLNIG--GGKERMTWYFNENGWPTSTI 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  63 DTAlvvfPGDLERGLKFVED----KEAMFRRLASEQLNPLK-GLDKVRKWVENHGLKRAAVTNAPRKNAELIISKLGLTD 137
Cdd:PLN02779 110 EKA----PKDEEERKELVDSlhdrKTELFKELIESGALPLRpGVLRLMDEALAAGIKVAVCSTSNEKAVSKIVNTLLGPE 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 571487226 138 FFDA--VIIGDECEHAKPHPEPYLKALEVLKASKDHAFVFEDSASGIKAGVAAGMPVI 193
Cdd:PLN02779 186 RAQGldVFAGDDVPKKKPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAAKAAGMRCI 243
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 12-190 2.76e-10

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 57.74  E-value: 2.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  12 AVLFDVDGTLCDSDPLHyyalreMLQELGFNGGAPITEEFFVETFSGKHSDdtalvvfpgdLERGLKFVEDKEAMFRR-- 89
Cdd:cd02603    3 AVLFDFGGVLIDPDPAA------AVARFEALTGEPSEFVLDTEGLAGAFLE----------LERGRITEEEFWEELREel 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  90 -------------LASEQLNP--LKGLDKVRKwvenHGLKRAAVTNAPRKNAELIISKL-GLTDFFDAVIIGDECEHAKP 153
Cdd:cd02603   67 grplsaelfeelvLAAVDPNPemLDLLEALRA----KGYKVYLLSNTWPDHFKFQLELLpRRGDLFDGVVESCRLGVRKP 142

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 571487226 154 HPEPYLKALEVLKASKDHAFVFEDSASGIKAGVAAGM 190
Cdd:cd02603  143 DPEIYQLALERLGVKPEEVLFIDDREENVEAARALGI 179
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 13-197 3.18e-10

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: 57.79  E-value: 3.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  13 VLFDVDGTLCDSDPLHYYALREMLQELGFngGAPITEEffVETFSGKHSDDTALVVFP---GDLERGLKFvEDKEAMFRR 89
Cdd:cd07533    2 VIFDWDGTLADSQHNIVAAMTAAFADLGL--PVPSAAE--VRSIIGLSLDEAIARLLPmatPALVAVAER-YKEAFDILR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  90 LASEQLNPLkgLDKVRKWVE---NHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEhAKPHPEPYLKALEVLK 166
Cdd:cd07533   77 LLPEHAEPL--FPGVREALDalaAQGVLLAVATGKSRRGLDRVLEQHGLGGYFDATRTADDTP-SKPHPEMLREILAELG 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 571487226 167 ASKDHAFVFEDSASGIKAGVAAGMPVIGLAT 197
Cdd:cd07533  154 VDPSRAVMVGDTAYDMQMAANAGAHAVGVAW 184
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 10-193 4.33e-10

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: 57.35  E-value: 4.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   10 LEAVLFDVDGTLcdsdpLHYYALREMLQELGFNGGAPITEEFFvetfsGKHSDDTALVVFPGD-------LERGLKF--- 79
Cdd:TIGR01428   1 IKALVFDVYGTL-----FDVHSVAERAAELYGGRGEALSQLWR-----QKQLEYSWLRTLMGPykdfwdlTREALRYllg 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   80 ---VEDKEAMFRRLASE--QLNP----LKGLDKVRKwvenHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEH 150
Cdd:TIGR01428  71 rlgLEDDESAADRLAEAylRLPPhpdvPAGLRALKE----RGYRLAILSNGSPAMLKSLVKHAGLDDPFDAVLSADAVRA 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 571487226  151 AKPHPEPYLKALEVLKASKDHAFVFEDSASGIKAGVAAGMPVI 193
Cdd:TIGR01428 147 YKPAPQVYQLALEALGVPPDEVLFVASNPWDLGGAKKFGFKTA 189
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
 13-215 2.10e-09

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 56.41  E-value: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  13 VLFDVDGTLCDSDPLHYYALREMLQELGfnggAPITEEFFVETFSGKHSDDTALVVFPGDLERglKFVEDKEA-----MF 87
Cdd:PRK13223  16 VMFDLDGTLVDSVPDLAAAVDRMLLELG----RPPAGLEAVRHWVGNGAPVLVRRALAGSIDH--DGVDDELAeqalaLF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  88 RRlASEQLNPLK----GLDKVRKWVENHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPYLKALE 163
Cdd:PRK13223  90 ME-AYADSHELTvvypGVRDTLKWLKKQGVEMALITNKPERFVAPLLDQMKIGRYFRWIIGGDTLPQKKPDPAALLFVMK 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 571487226 164 VLKASKDHAFVFEDSASGIKAGVAAGMPVIGLA-TRNPENLLMEAKPAFLIKD 215
Cdd:PRK13223 169 MAGVPPSQSLFVGDSRSDVLAAKAAGVQCVALSyGYNHGRPIAEESPALVIDD 221
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 111-193 3.70e-09

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: 52.93  E-value: 3.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226 111 HGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPYLKALEVLKASKDHAFVFEDS-ASGIKAGVAAG 189
Cdd:cd04305   23 KGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLMVGDSlESDILGAKNAG 102


                 ....
gi 571487226 190 MPVI 193
Cdd:cd04305  103 IKTV 106
PLN02811 PLN02811
hydrolase
 79-193 2.47e-08

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 52.45  E-value: 2.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  79 FVEDKEAMFRRL-ASEQLNPlkGLDKVRKWVENHGLKRAAVTNAPRKNAELIISKLG-LTDFFDAVIIGDECE--HAKPH 154
Cdd:PLN02811  62 FLVEREAMLQDLfPTSDLMP--GAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGeLFSLMHHVVTGDDPEvkQGKPA 139

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 571487226 155 PEPYLKALEVLKASK---DHAFVFEDSASGIKAGVAAGMPVI 193
Cdd:PLN02811 140 PDIFLAAARRFEDGPvdpGKVLVFEDAPSGVEAAKNAGMSVV 181
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 110-200 3.12e-08

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 53.33  E-value: 3.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226 110 NHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPYLKALEVLKASKDHAFVFEDSASGIKAGVAAG 189
Cdd:PLN02575 230 NYKIPMALVSTRPRKTLENAIGSIGIRGFFSVIVAAEDVYRGKPDPEMFIYAAQLLNFIPERCIVFGNSNQTVEAAHDAR 309

                         90
                 ....*....|.
gi 571487226 190 MPVIGLATRNP 200
Cdd:PLN02575 310 MKCVAVASKHP 320
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 93-190 4.00e-08

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p; This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and CMP. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319791 [Multi-domain]  Cd Length: 182  Bit Score: 51.48  E-value: 4.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  93 EQLNPLKGldkvRKWVenhglkraaVTNAPRKNAELIISKLGLTDFFDAVIigdECEHA----KPHPEPYLKALEVLKAS 168
Cdd:cd02604   90 NLLLALPG----RKII---------FTNASKNHAIRVLKRLGLADLFDGIF---DIEYAgpdpKPHPAAFEKAIREAGLD 153

                         90       100
                 ....*....|....*....|..
gi 571487226 169 KDHAFVFEDSASGIKAGVAAGM 190
Cdd:cd02604  154 PKRAAFFDDSIRNLLAAKALGM 175
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 72-200 7.02e-08

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 51.57  E-value: 7.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  72 DLERGLKFVEDKEAMFRRLASEQLNPLKGLDKVRKWVENHGLKRAAVTNAPRKNAELIISKLGLTDFFDAVIIGDECEHA 151
Cdd:PLN03243  85 DFLQMKRLAIRKEDLYEYMQGGLYRLRPGSREFVQALKKHEIPIAVASTRPRRYLERAIEAVGMEGFFSVVLAAEDVYRG 164

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 571487226 152 KPHPEPYLKALEVLKASKDHAFVFEDSASGIKAGVAAGMPVIGLATRNP 200
Cdd:PLN03243 165 KPDPEMFMYAAERLGFIPERCIVFGNSNSSVEAAHDGCMKCVAVAGKHP 213
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 106-221 1.12e-07

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


Pssm-ID: 319852 [Multi-domain]  Cd Length: 128  Bit Score: 49.21  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226 106 KWVENHGLKRAAVTNAPRKnAELIISKLGLTDFFDAVIIGDECEHAKPHPEPYLKALEVLKASKDHAF-VFEDSASGIKA 184
Cdd:cd16415   17 KDLKEKGLKLAVVSNFDRR-LRELLEALGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPEEALhVGDDLKNDYLG 95

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 571487226 185 GVAAGMPVIglatrnpenLLMEAKPAFLIKDYEDSKL 221
Cdd:cd16415   96 ARAVGWHAL---------LVDREGALHELPSLANLLE 123
PRK11587 PRK11587
putative phosphatase; Provisional
 141-193 9.53e-07

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 48.07  E-value: 9.53e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 571487226 141 AVIIGDEC-EHAKPHPEPYLKALEVLKASKDHAFVFEDSASGIKAGVAAGMPVI 193
Cdd:PRK11587 126 EVFVTAERvKRGKPEPDAYLLGAQLLGLAPQECVVVEDAPAGVLSGLAAGCHVI 179
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 14-193 6.84e-06

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: 45.06  E-value: 6.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  14 LFDVDGTLCDSDPLHYYALREMLQELGfnggapitEEFFVET---FSGKHSDDTALVVFpgdlerglKFVEDKEAMFRRL 90
Cdd:cd07523    3 IWDLDGTLLDSYPAMTKALSETLADFG--------IPQDLETvykIIKESSVQFAIQYY--------AEVPDLEEEYKEL 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226  91 A---SEQLNPLKGLDKVRKWVENHGLKRAAVTNApRKNAELIISKLGLTDFFDAVIIGDECEHAKPHPEPYLKALEVLKA 167
Cdd:cd07523   67 EaeyLAKPILFPGAKAVLRWIKEQGGKNFLMTHR-DHSALTILKKDGIASYFTEIVTSDNGFPRKPNPEAINYLLNKYQL 145

                        170       180
                 ....*....|....*....|....*.
gi 571487226 168 SKDHAFVFEDSASGIKAGVAAGMPVI 193
Cdd:cd07523  146 NPEETVMIGDRELDIEAGHNAGISTI 171
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 112-194 4.10e-05

Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGPase; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319857 [Multi-domain]  Cd Length: 105  Bit Score: 41.67  E-value: 4.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226 112 GLKRAAVTNAPRKNAELIISKLGLTDFfDAVIIGDECEHAKPHPEPYLKALEVLKASKDHAFVFEDSASGIKAGVAAGMP 191
Cdd:cd16421   23 GIKLAVLSNKPNEAVQVLVEELFPGSF-DFVLGEKEGIRRKPDPT*ALECAKVLGVPPDEVLYVGDSGVDMQTARNAGMD 101


                 ...
gi 571487226 192 VIG 194
Cdd:cd16421  102 EIG 104
HAD pfam12710
haloacid dehalogenase-like hydrolase;
13-143 4.82e-04

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 39.82  E-value: 4.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571487226   13 VLFDVDGTLCDSDPLHYYAlREMLQELGFNGGAPITEEFFVETF-SGKHSDDTALVVFPGDLERGLK--FVEDKEAMFRR 89
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLI-RALLRRGGPDLWRALLVLLLLALLrLLGRLSRAGARELLRALLAGLPeeDAAELERFVAE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 571487226   90 LASEQLNPlKGLDKVRKWVENHGlkRAA-VTNAPRKNAELIISKLGltdfFDAVI 143
Cdd:pfam12710  80 VALPRLHP-GALELLAAHRAAGD--RVVvVTGGLRPLVEPVLAELG----FDEVL 127
 
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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