NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1731153586|ref|WP_148411690|]
View 

HAD family phosphatase [Enterococcus sp. T0168A.B-11]

Protein Classification

HAD family hydrolase( domain architecture ID 11428160)

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
1-218 1.82e-48

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


:

Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 158.06  E-value: 1.82e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   1 MKGIIFDFNGTMFLDSHLHEAAWLHMIHDHtkdGLS-DEDILKNIHGRTNTEILKHFISEHLTASEIAVLSEEKESYYR- 78
Cdd:COG0637     2 IKAVIFDMDGTLVDSEPLHARAWREAFAEL---GIDlTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYRe 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  79 MFclqNENELQLTKGLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLARWFDwdKIVYDDGSFPGKPQPDIFLKAAD 158
Cdd:COG0637    79 LL---AEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFD--VIVTGDDVARGKPDPDIYLLAAE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586 159 KLSLAPADCLVIEDAYSGLLAAKRAGIGTiIAIDPFGKNKTVFEQAqlnkDGTIKDFTGF 218
Cdd:COG0637   154 RLGVDPEECVVFEDSPAGIRAAKAAGMRV-VGVPDGGTAEEELAGA----DLVVDDLAEL 208
 
Name Accession Description Interval E-value
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
1-218 1.82e-48

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 158.06  E-value: 1.82e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   1 MKGIIFDFNGTMFLDSHLHEAAWLHMIHDHtkdGLS-DEDILKNIHGRTNTEILKHFISEHLTASEIAVLSEEKESYYR- 78
Cdd:COG0637     2 IKAVIFDMDGTLVDSEPLHARAWREAFAEL---GIDlTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYRe 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  79 MFclqNENELQLTKGLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLARWFDwdKIVYDDGSFPGKPQPDIFLKAAD 158
Cdd:COG0637    79 LL---AEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFD--VIVTGDDVARGKPDPDIYLLAAE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586 159 KLSLAPADCLVIEDAYSGLLAAKRAGIGTiIAIDPFGKNKTVFEQAqlnkDGTIKDFTGF 218
Cdd:COG0637   154 RLGVDPEECVVFEDSPAGIRAAKAAGMRV-VGVPDGGTAEEELAGA----DLVVDDLAEL 208
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 3-188 1.82e-27

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: 101.92  E-value: 1.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   3 GIIFDFNGTMFLDSHLHEAAWLHMihdhtkdglsdedilknihgRTNTEILKHFISEHLtaseiavlseekesyyrmfcl 82
Cdd:cd07505     1 AVIFDMDGVLIDTEPLHRQAWQLL--------------------ERKNALLLELIASEG--------------------- 39

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  83 qneneLQLTKGLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLARWFDwDKIVYDDGSFPGKPQPDIFLKAADKLSL 162
Cdd:cd07505    40 -----LKLKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLRGYF-DVIVSGDDVERGKPAPDIYLLAAERLGV 113

                         170       180
                  ....*....|....*....|....*.
gi 1731153586 163 APADCLVIEDAYSGLLAAKRAGIGTI 188
Cdd:cd07505   114 DPERCLVFEDSLAGIEAAKAAGMTVV 139
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 2-185 2.28e-25

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: 97.80  E-value: 2.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   2 KGIIFDFNGTMFLDSHLHEAAWLHMIHDHtkdGLS-DEDILKNIHGRTNTEILKHFISEH---LTASEIAVLSEEKESYY 77
Cdd:TIGR02009   2 KAVIFDMDGVITDTAPLHAQAWKHIAAKY---GISfDKQYNESLKGLSREDILRAILKLRgdgLSLEEIHQLAERKNELY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  78 RMfcLQNENELQLTKGLEATLDQLTDQQIPltIATATVKENVAFYFDIFDLARWFDwdKIVYDDGSFPGKPQPDIFLKAA 157
Cdd:TIGR02009  79 RE--LLRLTGVAVLPGIRNLLKRLKAKGIA--VGLGSSSKNAPRILAKLGLRDYFD--AIVDASEVKNGKPHPETFLLAA 152

                         170       180
                  ....*....|....*....|....*...
gi 1731153586 158 DKLSLAPADCLVIEDAYSGLLAAKRAGI 185
Cdd:TIGR02009 153 ELLGVPPNECIVFEDALAGVQAARAAGM 180
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
4-188 5.07e-19

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 81.09  E-value: 5.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   4 IIFDFNGTMfLDSH-LHEAAWLHMIHDHTKDGLSDEDILKNIhGRTNTEILKHFISEHLTASEIAVLSEEKESYyrmfcl 82
Cdd:pfam13419   1 IIFDFDGTL-LDTEeLIIKSFNYLLEEFGYGELSEEEILKFI-GLPLREIFRYLGVSEDEEEKIEFYLRKYNEE------ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  83 QNENELQLTKGLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLARWFDwdKIVYDDGSFPGKPQPDIFLKAADKLSL 162
Cdd:pfam13419  73 LHDKLVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFD--VIVGGDDVEGKKPDPDPILKALEQLGL 150

                         170       180
                  ....*....|....*....|....*.
gi 1731153586 163 APADCLVIEDAYSGLLAAKRAGIGTI 188
Cdd:pfam13419 151 KPEEVIYVGDSPRDIEAAKNAGIKVI 176
PRK11587 PRK11587
putative phosphatase; Provisional
 2-193 5.00e-16

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 73.88  E-value: 5.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   2 KGIIFDFNGTMfLDS-HLHEAAWLHMIHDHtkdGLSDEDILKNIHGRTNTEILKHFISEhltASEIAVLSEekesyyrmF 80
Cdd:PRK11587    4 KGFLFDLDGTL-VDSlPAVERAWSNWADRH---GIAPDEVLNFIHGKQAITSLRHFMAG---ASEAEIQAE--------F 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  81 CLQNENELQLTKGLEAT------LDQLTDQQIPLTIAT------ATVKENVAfyfDIFDLARWFDWDKIVYddgsfpGKP 148
Cdd:PRK11587   69 TRLEQIEATDTEGITALpgaialLNHLNKLGIPWAIVTsgsvpvASARHKAA---GLPAPEVFVTAERVKR------GKP 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1731153586 149 QPDIFLKAADKLSLAPADCLVIEDAYSGLLAAKRAGIGTIIAIDP 193
Cdd:PRK11587  140 EPDAYLLGAQLLGLAPQECVVVEDAPAGVLSGLAAGCHVIAVNAP 184
 
Name Accession Description Interval E-value
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
1-218 1.82e-48

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 158.06  E-value: 1.82e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   1 MKGIIFDFNGTMFLDSHLHEAAWLHMIHDHtkdGLS-DEDILKNIHGRTNTEILKHFISEHLTASEIAVLSEEKESYYR- 78
Cdd:COG0637     2 IKAVIFDMDGTLVDSEPLHARAWREAFAEL---GIDlTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYRe 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  79 MFclqNENELQLTKGLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLARWFDwdKIVYDDGSFPGKPQPDIFLKAAD 158
Cdd:COG0637    79 LL---AEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFD--VIVTGDDVARGKPDPDIYLLAAE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586 159 KLSLAPADCLVIEDAYSGLLAAKRAGIGTiIAIDPFGKNKTVFEQAqlnkDGTIKDFTGF 218
Cdd:COG0637   154 RLGVDPEECVVFEDSPAGIRAAKAAGMRV-VGVPDGGTAEEELAGA----DLVVDDLAEL 208
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
1-188 1.43e-29

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 109.63  E-value: 1.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   1 MKGIIFDFNGTMFLDSHLHEAAWLHMIHDHTKDGLSDEDILKNIhGRTNTEILKHFISEHLTASEIAVLSEEKESYYRMF 80
Cdd:COG0546     1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRALI-GLGLRELLRRLLGEDPDEELEELLARFRELYEEEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  81 ClqneNELQLTKGLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLARWFDWdkIVYDDGSFPGKPQPDIFLKAADKL 160
Cdd:COG0546    80 L----DETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDA--IVGGDDVPPAKPKPEPLLEALERL 153

                         170       180
                  ....*....|....*....|....*...
gi 1731153586 161 SLAPADCLVIEDAYSGLLAAKRAGIGTI 188
Cdd:COG0546   154 GLDPEEVLMVGDSPHDIEAARAAGVPFI 181
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 3-188 1.82e-27

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: 101.92  E-value: 1.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   3 GIIFDFNGTMFLDSHLHEAAWLHMihdhtkdglsdedilknihgRTNTEILKHFISEHLtaseiavlseekesyyrmfcl 82
Cdd:cd07505     1 AVIFDMDGVLIDTEPLHRQAWQLL--------------------ERKNALLLELIASEG--------------------- 39

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  83 qneneLQLTKGLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLARWFDwDKIVYDDGSFPGKPQPDIFLKAADKLSL 162
Cdd:cd07505    40 -----LKLKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLRGYF-DVIVSGDDVERGKPAPDIYLLAAERLGV 113

                         170       180
                  ....*....|....*....|....*.
gi 1731153586 163 APADCLVIEDAYSGLLAAKRAGIGTI 188
Cdd:cd07505   114 DPERCLVFEDSLAGIEAAKAAGMTVV 139
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 2-185 2.28e-25

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: 97.80  E-value: 2.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   2 KGIIFDFNGTMFLDSHLHEAAWLHMIHDHtkdGLS-DEDILKNIHGRTNTEILKHFISEH---LTASEIAVLSEEKESYY 77
Cdd:TIGR02009   2 KAVIFDMDGVITDTAPLHAQAWKHIAAKY---GISfDKQYNESLKGLSREDILRAILKLRgdgLSLEEIHQLAERKNELY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  78 RMfcLQNENELQLTKGLEATLDQLTDQQIPltIATATVKENVAFYFDIFDLARWFDwdKIVYDDGSFPGKPQPDIFLKAA 157
Cdd:TIGR02009  79 RE--LLRLTGVAVLPGIRNLLKRLKAKGIA--VGLGSSSKNAPRILAKLGLRDYFD--AIVDASEVKNGKPHPETFLLAA 152

                         170       180
                  ....*....|....*....|....*...
gi 1731153586 158 DKLSLAPADCLVIEDAYSGLLAAKRAGI 185
Cdd:TIGR02009 153 ELLGVPPNECIVFEDALAGVQAARAAGM 180
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 3-185 2.09e-22

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


Pssm-ID: 213672 [Multi-domain]  Cd Length: 185  Bit Score: 90.06  E-value: 2.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   3 GIIFDFNGTMFLDSHLHEAAWLHMIhdhTKDGLS-DEDILKNIHGRTNTEILKHFISEH---LTASEIAVLSEEKESYYR 78
Cdd:TIGR01990   1 AVIFDLDGVITDTAEYHYLAWKHLA---DELGIPfDEEFNESLKGVSREESLERILDLGgkkYSEEEKEELAERKNDYYV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  79 MFcLQNENELQLTKGLEATLDQLTDQQIPLTIATATvkENVAFYFDIFDLARWFDWdkIVYDDGSFPGKPQPDIFLKAAD 158
Cdd:TIGR01990  78 EL-LKELTPADVLPGIKSLLADLKKNNIKIALASAS--KNAPTILEKLELIDYFDA--IVDPAELKKGKPDPEIFLAAAE 152

                         170       180
                  ....*....|....*....|....*..
gi 1731153586 159 KLSLAPADCLVIEDAYSGLLAAKRAGI 185
Cdd:TIGR01990 153 GLGVSPSECIGIEDAQAGIEAIKAAGM 179
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 3-228 2.73e-22

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: 90.48  E-value: 2.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   3 GIIFDFNGTMFlDSH-LHEAAWLHMIHDHtkdGLSDEDILKNIHGRTNTEILKHFISEHL-TASEIAVLSEEKESYyrmf 80
Cdd:cd07527     1 ALLFDMDGTLV-DSTpAVERAWHKWAKEH---GVDPEEVLKVSHGRRAIDVIRKLAPDDAdIELVLALETEEPESY---- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  81 clqnENELQLTKGLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLARWfdwDKIVYDDGSFPGKPQPDIFLKAADKL 160
Cdd:cd07527    73 ----PEGVIAIPGAVDLLASLPAAGDRWAIVTSGTRALAEARLEAAGLPHP---EVLVTADDVKNGKPDPEPYLLGAKLL 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1731153586 161 SLAPADCLVIEDAYSGLLAAKRAGIgTIIAIDpfgknkTVFEQAQLNKDGTIKDFtgfwtEHLSATSV 228
Cdd:cd07527   146 GLDPSDCVVFEDAPAGIKAGKAAGA-RVVAVN------TSHDLEQLEAAGADLVV-----EDLSDISV 201
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 4-188 2.86e-19

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: 81.70  E-value: 2.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   4 IIFDFNGTMFLDSHLHEAAWLHMIHdhtkdGLSDEDILKNIHGRTNTEILKHFISEHLTASEIAVLSEEKESYYRMFclQ 83
Cdd:TIGR01509   2 ILFDLDGVLVDTEFAIAKLINREEL-----GLVPDELGVSAVGRLELALRRFKAQYGRTISPEDAQLLYKQLFYEQI--E 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  84 NENELQLTKGLEATLDQLTDQQIPLTIATATVKENVAFyFDIFDLARWFDwdKIVYDDGSFPGKPQPDIFLKAADKLSLA 163
Cdd:TIGR01509  75 EEAKLKPLPGVRALLEALRARGKKLALLTNSPRAHKLV-LALLGLRDLFD--VVIDSSDVGLGKPDPDIYLQALKALGLE 151

                         170       180
                  ....*....|....*....|....*
gi 1731153586 164 PADCLVIEDAYSGLLAAKRAGIGTI 188
Cdd:TIGR01509 152 PSECVFVDDSPAGIEAAKAAGMHTV 176
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 4-192 5.06e-19

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: 80.76  E-value: 5.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   4 IIFDFNGTMfLDShlhEAAWLHMIHDHTKDglsdedilknihgRTNTEILKHFisehltaseiavlsEEKESyyrmfclq 83
Cdd:cd16423     2 VIFDFDGVI-VDT---EPLWYEAWQELLNE-------------RRNELIKRQF--------------SEKTD-------- 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  84 neneLQLTKGLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLARWFDwdKIVYDDGSFPGKPQPDIFLKAADKLSLA 163
Cdd:cd16423    43 ----LPPIEGVKELLEFLKEKGIKLAVASSSPRRWIEPHLERLGLLDYFE--VIVTGDDVEKSKPDPDLYLEAAERLGVN 116

                         170       180
                  ....*....|....*....|....*....
gi 1731153586 164 PADCLVIEDAYSGLLAAKRAGIgTIIAID 192
Cdd:cd16423   117 PEECVVIEDSRNGVLAAKAAGM-KCVGVP 144
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
4-188 5.07e-19

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 81.09  E-value: 5.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   4 IIFDFNGTMfLDSH-LHEAAWLHMIHDHTKDGLSDEDILKNIhGRTNTEILKHFISEHLTASEIAVLSEEKESYyrmfcl 82
Cdd:pfam13419   1 IIFDFDGTL-LDTEeLIIKSFNYLLEEFGYGELSEEEILKFI-GLPLREIFRYLGVSEDEEEKIEFYLRKYNEE------ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  83 QNENELQLTKGLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLARWFDwdKIVYDDGSFPGKPQPDIFLKAADKLSL 162
Cdd:pfam13419  73 LHDKLVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFD--VIVGGDDVEGKKPDPDPILKALEQLGL 150

                         170       180
                  ....*....|....*....|....*.
gi 1731153586 163 APADCLVIEDAYSGLLAAKRAGIGTI 188
Cdd:pfam13419 151 KPEEVIYVGDSPRDIEAAKNAGIKVI 176
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 1-184 1.21e-18

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 80.32  E-value: 1.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   1 MKGIIFDFNGTMFLDSHLHEAAW--LHMIHDHTKDGLSD-EDILKNIH------GRTNTEILKHFISEHLTASEIAVLSE 71
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIaeLASEHPLAKAIVAAaEDLPIPVEdftarlLLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  72 EKESYYRMFCLQNENELQLTKGLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLARWFDWDKIVYDDGsfPGKPQPD 151
Cdd:pfam00702  81 TVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVG--VGKPKPE 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1731153586 152 IFLKAADKLSLAPADCLVIEDAYSGLLAAKRAG 184
Cdd:pfam00702 159 IYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PRK11587 PRK11587
putative phosphatase; Provisional
 2-193 5.00e-16

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 73.88  E-value: 5.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   2 KGIIFDFNGTMfLDS-HLHEAAWLHMIHDHtkdGLSDEDILKNIHGRTNTEILKHFISEhltASEIAVLSEekesyyrmF 80
Cdd:PRK11587    4 KGFLFDLDGTL-VDSlPAVERAWSNWADRH---GIAPDEVLNFIHGKQAITSLRHFMAG---ASEAEIQAE--------F 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  81 CLQNENELQLTKGLEAT------LDQLTDQQIPLTIAT------ATVKENVAfyfDIFDLARWFDWDKIVYddgsfpGKP 148
Cdd:PRK11587   69 TRLEQIEATDTEGITALpgaialLNHLNKLGIPWAIVTsgsvpvASARHKAA---GLPAPEVFVTAERVKR------GKP 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1731153586 149 QPDIFLKAADKLSLAPADCLVIEDAYSGLLAAKRAGIGTIIAIDP 193
Cdd:PRK11587  140 EPDAYLLGAQLLGLAPQECVVVEDAPAGVLSGLAAGCHVIAVNAP 184
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 66-189 5.96e-16

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: 73.18  E-value: 5.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  66 IAVLSEEKESYYRMfcLQNENELQLTKGLEATLDQLTDQQIPLTIATATVKENV----AFYFDIfdlaRWFDW-DKIVYD 140
Cdd:cd07528    74 IADLHKAKTERYAE--LIAAGLLPLRPGVARLIDEAKAAGVRLAIATTTSPANVdallSALLGP----ERRAIfDAIAAG 147

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1731153586 141 DGSFPGKPQPDIFLKAADKLSLAPADCLVIEDAYSGLLAAKRAGIGTII 189
Cdd:cd07528   148 DDVAEKKPDPDIYLLALERLGVSPSDCLAIEDSAIGLQAAKAAGLPCIV 196
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 1-218 8.17e-16

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: 73.52  E-value: 8.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   1 MKGIIFDFNGTmFLDSHLHEAAWLHMIHDHTKDGLSDEDILKNIH-------------GRTNTEILKHFISEHltasEIA 67
Cdd:COG1011     1 IKAVLFDLDGT-LLDFDPVIAEALRALAERLGLLDEAEELAEAYRaieyalwrryergEITFAELLRRLLEEL----GLD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  68 VLSEEKESYYRMFclqnENELQLTKGLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLARWFDwdKIVY--DDGSFp 145
Cdd:COG1011    76 LAEELAEAFLAAL----PELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFD--AVVSseEVGVR- 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731153586 146 gKPQPDIFLKAADKLSLAPADCLVIEDAYSG-LLAAKRAGIGTIIaIDPFGKNKTVFEQAqlnkDGTIKDFTGF 218
Cdd:COG1011   149 -KPDPEIFELALERLGVPPEEALFVGDSPETdVAGARAAGMRTVW-VNRSGEPAPAEPRP----DYVISDLAEL 216
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 3-188 1.44e-15

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: 71.55  E-value: 1.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   3 GIIFDFNGTMFLDSHLHEAAWLHMihdhtkdglsdedilknihgrtnteilkhfisehltaSEIAVLSEEKESYYRMFC- 81
Cdd:cd02598     1 GVIFDLDGVITDTAEYHYRAWKKL-------------------------------------ADKEELAARKNRIYVELIe 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  82 -LQNENELqltKGLEATLDQLTDQQIPLTIATATvkENVAFYFDIFDLARWFDwdKIVYDDGSFPGKPQPDIFLKAADKL 160
Cdd:cd02598    44 eLTPVDVL---PGIASLLVDLKAKGIKIALASAS--KNAPKILEKLGLAEYFD--AIVDGAVLAKGKPDPDIFLAAAEGL 116

                         170       180
                  ....*....|....*....|....*...
gi 1731153586 161 SLAPADCLVIEDAYSGLLAAKRAGIGTI 188
Cdd:cd02598   117 GLNPKDCIGVEDAQAGIRAIKAAGFLVV 144
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 58-188 1.93e-13

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: 65.03  E-value: 1.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  58 SEHLTAS-EIAVLSEEKESYYRMFclqnENELQLTKGLEATLDQLTdqqIPLTIATATVKENVAFYFDIFDLARWFDwDK 136
Cdd:cd07526    14 SEVIAARvLVEVLAELGARVLAAF----EAELQPIPGAAAALSALT---LPFCVASNSSRERLTHSLGLAGLLAYFE-GR 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1731153586 137 I--VYDDGSfpGKPQPDIFLKAADKLSLAPADCLVIEDAYSGLLAAKRAGIGTI 188
Cdd:cd07526    86 IfsASDVGR--GKPAPDLFLHAAAQMGVAPERCLVIEDSPTGVRAALAAGMTVF 137
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 2-187 8.61e-13

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 65.05  E-value: 8.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   2 KGIIFDFNGTMFLDSHLHEAAWLHMIHDHTKDGLSDEDILKNIhGRTNTEILKHFISEHLtaseiavlsEEKESYYRMFC 81
Cdd:PRK13288    4 NTVLFDLDGTLINTNELIISSFLHTLKTYYPNQYKREDVLPFI-GPSLHDTFSKIDESKV---------EEMITTYREFN 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  82 LQNENEL-QLTKGLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLARWFDwDKIVYDDGSFPgKPQPDIFLKAADKL 160
Cdd:PRK13288   74 HEHHDELvTEYETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFD-VVITLDDVEHA-KPDPEPVLKALELL 151

                         170       180
                  ....*....|....*....|....*..
gi 1731153586 161 SLAPADCLVIEDAYSGLLAAKRAGIGT 187
Cdd:PRK13288  152 GAKPEEALMVGDNHHDILAGKNAGTKT 178
PLN02811 PLN02811
hydrolase
 57-193 1.58e-12

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 64.39  E-value: 1.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  57 ISEHLTASEIAVlseEKESYYR-MFclqneNELQLTKGLEATLDQLTDQQIPLTIATATVKENVAF----YFDIFDLARW 131
Cdd:PLN02811   53 LSDSLSPEDFLV---EREAMLQdLF-----PTSDLMPGAERLVRHLHAKGIPIAIATGSHKRHFDLktqrHGELFSLMHH 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1731153586 132 FdwdkIVYDDGSFP-GKPQPDIFLKAADKLSLAPAD---CLVIEDAYSGLLAAKRAGIGTIIAIDP 193
Cdd:PLN02811  125 V----VTGDDPEVKqGKPAPDIFLAAARRFEDGPVDpgkVLVFEDAPSGVEAAKNAGMSVVMVPDP 186
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 4-185 1.97e-12

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: 63.96  E-value: 1.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   4 IIFDFNGTMFLDSHLHEAAWLHMIHDHTKDGLSDEDIlKNIHGRTNTEILkHFISEHLTASEIAVLSEEKESYYRMFCLQ 83
Cdd:cd07533     2 VIFDWDGTLADSQHNIVAAMTAAFADLGLPVPSAAEV-RSIIGLSLDEAI-ARLLPMATPALVAVAERYKEAFDILRLLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  84 nENELQLTKGLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLARWFDWDKiVYDDGsfPGKPQPDIFLKAADKLSLA 163
Cdd:cd07533    80 -EHAEPLFPGVREALDALAAQGVLLAVATGKSRRGLDRVLEQHGLGGYFDATR-TADDT--PSKPHPEMLREILAELGVD 155

                         170       180
                  ....*....|....*....|..
gi 1731153586 164 PADCLVIEDAYSGLLAAKRAGI 185
Cdd:cd07533   156 PSRAVMVGDTAYDMQMAANAGA 177
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 2-190 8.56e-12

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: 61.91  E-value: 8.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   2 KGIIFDFNGTMFLDSHLHEAAWLHMIHDHTKDGLSDEDILKNIhGRTNTEILKHFISEHLTAseiavLSEEKESYYRMFc 81
Cdd:cd02616     2 TTILFDLDGTLIDTNELIIKSFNHTLKEYGLEGYTREEVLPFI-GPPLRETFEKIDPDKLED-----MVEEFRKYYREH- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  82 lqNENELQLTKGLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLARWFDwdKIV-YDDGSFPgKPQPDIFLKAADKL 160
Cdd:cd02616    75 --NDDLTKEYPGVYETLARLKSQGIKLGVVTTKLRETALKGLKLLGLDKYFD--VIVgGDDVTHH-KPDPEPVLKALELL 149

                         170       180       190
                  ....*....|....*....|....*....|
gi 1731153586 161 SLAPADCLVIEDAYSGLLAAKRAGIGTIIA 190
Cdd:cd02616   150 GAEPEEALMVGDSPHDILAGKNAGVKTVGV 179
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 147-189 1.95e-11

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 62.03  E-value: 1.95e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1731153586 147 KPQPDIFLKAADKLSLAPADCLVIEDAYSGLLAAKRAGIGTII 189
Cdd:PLN02779  202 KPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAAKAAGMRCIV 244
PLN02940 PLN02940
riboflavin kinase
 137-204 2.06e-11

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 62.54  E-value: 2.06e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1731153586 137 IVYDDGSFPGKPQPDIFLKAADKLSLAPADCLVIEDAYSGLLAAKRAGIgTIIAIDPFGKNKTVFEQA 204
Cdd:PLN02940  140 IVGGDEVEKGKPSPDIFLEAAKRLNVEPSNCLVIEDSLPGVMAGKAAGM-EVIAVPSIPKQTHLYSSA 206
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 46-184 2.36e-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: 60.44  E-value: 2.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  46 GRTNTEILKHFISE-HLTASEIAVLSEEKESYYRMFclqnENELQLTKGLEATLDQLTDQQIPLTIAT----ATVKENVA 120
Cdd:cd07529    44 GRPASEAARIIVDElKLPMSLEEEFDEQQEALAELF----MGTAKLMPGAERLLRHLHAHNIPIALATssctRHFKLKTS 119

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1731153586 121 FYFDIFDlarwFDWDKIVYDDGSFP--GKPQPDIFLKAADKLSLAPAD---CLVIEDAYSGLLAAKRAG 184
Cdd:cd07529   120 RHKELFS----LFHHVVTGDDPEVKgrGKPAPDIFLVAAKRFNEPPKDpskCLVFEDSPNGVKAAKAAG 184
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 3-184 2.51e-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: 2.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   3 GIIFDFNGTMFLDSHLHEAAWLHMIHDHTKDGLSDEDILKnihgrtnteilKHFISEHLTASeiaVLSEEKESYYRMFCL 82
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFGLDPASFKALKQ-----------AGGLAEEEWYR---IATSALEELQGRFWS 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  83 QNENELQLTKGLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLarwFDWDKIVYDDGSFPGKPQPDIFLKAADKLSL 162
Cdd:TIGR01549  67 EYDAEEAYIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGL---GDYFELILVSDEPGSKPEPEIFLAALESLGV 143

                         170       180
                  ....*....|....*....|..
gi 1731153586 163 APaDCLVIEDAYSGLLAAKRAG 184
Cdd:TIGR01549 144 PP-EVLHVGDNLNDIEGARNAG 164
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
3-185 2.32e-10

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 57.78  E-value: 2.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   3 GIIFDFNGTmFLDSH-LHEAAWLHMIHDHtkdGLS-DEDILKNIHGRTNTEILKHFISEHLTASEIAVLSEEKESYYRMF 80
Cdd:PRK10725    7 GLIFDMDGT-ILDTEpTHRKAWREVLGRY---GLQfDEQAMVALNGSPTWRIAQAIIELNQADLDPHALAREKTEAVKSM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  81 CLQNENELQLTKGLEATLDQLtdqqiPLTIATATVKENVAFYFDIFDLARWFDwdKIVYDDGSFPGKPQPDIFLKAADKL 160
Cdd:PRK10725   83 LLDSVEPLPLIEVVKAWHGRR-----PMAVGTGSESAIAEALLAHLGLRRYFD--AVVAADDVQHHKPAPDTFLRCAQLM 155

                         170       180
                  ....*....|....*....|....*
gi 1731153586 161 SLAPADCLVIEDAYSGLLAAKRAGI 185
Cdd:PRK10725  156 GVQPTQCVVFEDADFGIQAARAAGM 180
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 134-188 5.30e-10

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 58.71  E-value: 5.30e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1731153586  134 WDKIVYDDGSFPGKPQPDIFLKAADKLSLAPADCLVIEDAYSGLLAAKRAGIGTI 188
Cdd:PLN02919   205 FDAIVSADAFENLKPAPDIFLAAAKILGVPTSECVVIEDALAGVQAARAAGMRCI 259
PRK10826 PRK10826
hexitol phosphatase HxpB;
146-193 6.05e-10

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 57.26  E-value: 6.05e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1731153586 146 GKPQPDIFLKAADKLSLAPADCLVIEDAYSGLLAAKRAGIGTIIAIDP 193
Cdd:PRK10826  147 SKPHPEVYLNCAAKLGVDPLTCVALEDSFNGMIAAKAARMRSIVVPAP 194
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 94-189 1.02e-07

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: 48.55  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  94 LEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLARWFDWdkIVYDDGSFPGKPQPDIFLKAADKLSLAPADCLVIEDA 173
Cdd:cd01427    12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDG--IIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDS 89

                          90
                  ....*....|....*.
gi 1731153586 174 YSGLLAAKRAGIGTII 189
Cdd:cd01427    90 ENDIEAARAAGGRTVA 105
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 1-185 1.10e-07

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 50.99  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   1 MKGIIFDFNGTMFLDSHLHEAAWLHMIHDHTKDG---LSDEDILKNIHGRTNTEILKHFISEHLTASeiAVLSEEKESYY 77
Cdd:PLN02770   22 LEAVLFDVDGTLCDSDPLHYYAFREMLQEINFNGgvpITEEFFVENIAGKHNEDIALGLFPDDLERG--LKFTDDKEALF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  78 RMFClqnENELQLTKGLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLARWFDwDKIVYDDGSFPgKPQPDIFLKAA 157
Cdd:PLN02770  100 RKLA---SEQLKPLNGLYKLKKWIEDRGLKRAAVTNAPRENAELMISLLGLSDFFQ-AVIIGSECEHA-KPHPDPYLKAL 174

                         170       180
                  ....*....|....*....|....*...
gi 1731153586 158 DKLSLAPADCLVIEDAYSGLLAAKRAGI 185
Cdd:PLN02770  175 EVLKVSKDHTFVFEDSVSGIKAGVAAGM 202
Hydrolase_like pfam13242
HAD-hyrolase-like;
146-188 2.50e-07

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 46.84  E-value: 2.50e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1731153586 146 GKPQPDIFLKAADKLSLAPADCLVIED-AYSGLLAAKRAGIGTI 188
Cdd:pfam13242   3 GKPNPGMLERALARLGLDPERTVMIGDrLDTDILGAREAGARTI 46
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 93-188 4.61e-07

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: 48.77  E-value: 4.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  93 GLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLARWFDWdkIVYDDgSFPG-KPQPDIFLKAADKLSLAPADCLVIE 171
Cdd:cd16417    91 GVKEGLAALKAQGYPLACVTNKPERFVAPLLEALGISDYFSL--VLGGD-SLPEkKPDPAPLLHACEKLGIAPAQMLMVG 167

                          90
                  ....*....|....*..
gi 1731153586 172 DAYSGLLAAKRAGIGTI 188
Cdd:cd16417   168 DSRNDILAARAAGCPSV 184
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 3-183 6.13e-07

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 48.87  E-value: 6.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   3 GIIFDFNGTMFL-DSHLHEAAWLHMIHDHTKDgLSDEDILKNIHGRTNTEILKHFISEHLTASEIAVLSEEKESYYRMFc 81
Cdd:PLN03243   26 GVVLEWEGVIVEdDSELERKAWRALAEEEGKR-PPPAFLLKRAEGMKNEQAISEVLCWSRDFLQMKRLAIRKEDLYEYM- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  82 lqNENELQLTKGLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLARWFDwdKIVYDDGSFPGKPQPDIFLKAADKLS 161
Cdd:PLN03243  104 --QGGLYRLRPGSREFVQALKKHEIPIAVASTRPRRYLERAIEAVGMEGFFS--VVLAAEDVYRGKPDPEMFMYAAERLG 179

                         170       180
                  ....*....|....*....|..
gi 1731153586 162 LAPADCLVIEDAYSGLLAAKRA 183
Cdd:PLN03243  180 FIPERCIVFGNSNSSVEAAHDG 201
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
1-215 9.38e-07

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 47.88  E-value: 9.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   1 MKGIIFDFNGTMfLDSH--LHEAAwLHMIHDHTKDGLSDEDIlknihgrtnteilKHFIS---------------EHLTA 63
Cdd:PRK13222    6 IRAVAFDLDGTL-VDSApdLAAAV-NAALAALGLPPAGEERV-------------RTWVGngadvlveraltwagREPDE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  64 SEIAVLSEEKESYYRmfclqnENELQLTK---GLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLARWFDwdKIVYD 140
Cdd:PRK13222   71 ELLEKLRELFDRHYA------ENVAGGSRlypGVKETLAALKAAGYPLAVVTNKPTPFVAPLLEALGIADYFS--VVIGG 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1731153586 141 DgSFPG-KPQPDIFLKAADKLSLAPADCLVIEDAYSGLLAAKRAGIGTIIAidPFGKNKTVfEQAQLNKDGTIKDF 215
Cdd:PRK13222  143 D-SLPNkKPDPAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPSVGV--TYGYNYGE-PIALSEPDVVIDHF 214
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 3-183 2.46e-06

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 47.55  E-value: 2.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   3 GIIFDFNGTMFLDS-HLHEAAWLhmihdhtkdGLSDED--------ILKNIHGRTNTEIlkhfISEHLTAS----EIAVL 69
Cdd:PLN02575  133 GAIFEWEGVIIEDNpDLENQAWL---------TLAQEEgkspppafILRRVEGMKNEQA----ISEVLCWSrdpaELRRM 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  70 SEEKESYYRmfCLQNeNELQLTKGLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLARWFDwdKIVYDDGSFPGKPQ 149
Cdd:PLN02575  200 ATRKEEIYQ--ALQG-GIYRLRTGSQEFVNVLMNYKIPMALVSTRPRKTLENAIGSIGIRGFFS--VIVAAEDVYRGKPD 274

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1731153586 150 PDIFLKAADKLSLAPADCLVIEDAYSGLLAAKRA 183
Cdd:PLN02575  275 PEMFIYAAQLLNFIPERCIVFGNSNQTVEAAHDA 308
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 135-189 6.11e-06

histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal domain of the Escherichia coli bifunctional enzyme histidinol-phosphate phosphatase/imidazole-glycerol-phosphate dehydratase, HisB. The N-terminal histidinol-phosphate phosphatase domain catalyzes the dephosphorylation of histidinol phosphate, the eight step of L-histidine biosynthesis. This family also includes Escherichia coli GmhB phosphatase which is highly specific for D-glycero-D-manno-heptose-1,7-bisphosphate, it removes the C(7)phosphate and not the C(1)phosphate, and this is the third essential step of lipopolysaccharide heptose biosynthesis. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319806 [Multi-domain]  Cd Length: 142  Bit Score: 44.45  E-value: 6.11e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586 135 DKIVY-----DDGSFPGKPQPDIFLKAADKLSLAPADCLVIEDAYSGLLAAKRAGIGTII 189
Cdd:cd07503    82 DDIYYcphhpDDGCPCRKPKPGMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGCKGIL 141
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 4-185 2.00e-05

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 44.30  E-value: 2.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   4 IIFDFNGTMfLDSH-LHEAAWLHMIHDHTKDgLSDEDILKNIHGRTNTEILKHFISEHLTASEIAVLseekESYYR---- 78
Cdd:PRK10563    7 VFFDCDGTL-VDSEvICSRAYVTMFAEFGIT-LSLEEVFKRFKGVKLYEIIDIISKEHGVTLAKAEL----EPVYRaeva 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  79 -MFclqnENELQLTKGLEATLDQLTdqqIPLTIATATVKENVAFYFDIFDLARWFDwDKIV--YDDGSFpgKPQPDIFLK 155
Cdd:PRK10563   81 rLF----DSELEPIAGANALLESIT---VPMCVVSNGPVSKMQHSLGKTGMLHYFP-DKLFsgYDIQRW--KPDPALMFH 150

                         170       180       190
                  ....*....|....*....|....*....|
gi 1731153586 156 AADKLSLAPADCLVIEDAYSGLLAAKRAGI 185
Cdd:PRK10563  151 AAEAMNVNVENCILVDDSSAGAQSGIAAGM 180
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 147-188 2.35e-04

Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino acid transport and metabolism]; Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 440011 [Multi-domain]  Cd Length: 176  Bit Score: 40.46  E-value: 2.35e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1731153586 147 KPQPDIFLKAADKLSLAPADCLVIEDAYSGLLAAKRAGIGTI 188
Cdd:COG0241   102 KPKPGMLLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGCKGI 143
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 147-188 5.40e-04

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: 39.64  E-value: 5.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1731153586 147 KPQPDIFLKAADKLSLAPADCLVIEDAYSGLLAAKRAGIGTI 188
Cdd:cd02603   141 KPDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGIHAI 182
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 86-188 6.81e-04

Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the uncharacterized protein Bacillus subtilis YqeG; 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: 319853 [Multi-domain]  Cd Length: 108  Bit Score: 38.02  E-value: 6.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  86 NELQLTKGLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLarwfdwdkivydDGSFP-GKPQPDIFLKAADKLSLAP 164
Cdd:cd16416    14 DNPDLTPEVKAWLADLKEAGIKVVLVSNNNERRVAKVIEKLDL------------PFVARaGKPRPRAFRRALKEMDLPP 81

                          90       100
                  ....*....|....*....|....*
gi 1731153586 165 ADCLVIEDAY-SGLLAAKRAGIGTI 188
Cdd:cd16416    82 EQVAMVGDQLfTDILGGNRAGLYTI 106
PRK06769 PRK06769
HAD-IIIA family hydrolase;
132-189 7.47e-04

HAD-IIIA family hydrolase;


Pssm-ID: 180686 [Multi-domain]  Cd Length: 173  Bit Score: 38.94  E-value: 7.47e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1731153586 132 FDWDKIV-----YDDGSFPGKPQPDIFLKAADKLSLAPADCLVIEDAYSGLLAAKRAGIGTII 189
Cdd:PRK06769   73 FGFDDIYlcphkHGDGCECRKPSTGMLLQAAEKHGLDLTQCAVIGDRWTDIVAAAKVNATTIL 135
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
 93-185 8.24e-04

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 39.46  E-value: 8.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  93 GLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLARWFDWdkIVYDDGSFPGKPQPDIFLKAADKLSLAPADCLVIED 172
Cdd:PRK13223  105 GVRDTLKWLKKQGVEMALITNKPERFVAPLLDQMKIGRYFRW--IIGGDTLPQKKPDPAALLFVMKMAGVPPSQSLFVGD 182

                          90
                  ....*....|...
gi 1731153586 173 AYSGLLAAKRAGI 185
Cdd:PRK13223  183 SRSDVLAAKAAGV 195
PRK13226 PRK13226
phosphoglycolate phosphatase; Provisional
 147-191 1.04e-03

phosphoglycolate phosphatase; Provisional


Pssm-ID: 237311 [Multi-domain]  Cd Length: 229  Bit Score: 39.06  E-value: 1.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1731153586 147 KPQPDIFLKAADKLSLAPADCLVIEDAYSGLLAAKRAGIGTIIAI 191
Cdd:PRK13226  151 KPHPLPLLVAAERIGVAPTDCVYVGDDERDILAARAAGMPSVAAL 195
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 4-185 4.87e-03

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


Pssm-ID: 319799 [Multi-domain]  Cd Length: 201  Bit Score: 36.95  E-value: 4.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586   4 IIFDFNGTMFLDSHLHEAAWLHMIHDHTKDGLSDEDIlKNIHGRTNTEILKHFiseHLTASEIAVLSEEkesyYRMFCLQ 83
Cdd:cd04303     2 IIFDFDGTLADSFPWFLSILNQLAARHGFKTVDEEEI-EQLRQLSSREILKQL---GVPLWKLPLIAKD----FRRLMAE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731153586  84 NENELQLTKGLEATLDQLTDQQIPLTIATATVKENVAFYFDIFDLARWFDwdkiVYDDGSFPGKPQPdiFLKAADKLSLA 163
Cdd:cd04303    74 AAPELALFPGVEDMLRALHARGVRLAVVSSNSEENIRRVLGPEELISLFA----VIEGSSLFGKAKK--IRRVLRRTKIT 147

                         170       180
                  ....*....|....*....|..
gi 1731153586 164 PADCLVIEDAYSGLLAAKRAGI 185
Cdd:cd04303   148 AAQVIYVGDETRDIEAARKVGL 169
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 147-188 5.02e-03

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: 35.60  E-value: 5.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1731153586 147 KPQPDIFLKAADKLSLAPADCLVIEDAY-SGLLAAKRAGIGTI 188
Cdd:cd04305    64 KPNPEIFDYALNQLGVKPEETLMVGDSLeSDILGAKNAGIKTV 106
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 126-185 6.73e-03

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: 35.73  E-value: 6.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1731153586 126 FDLARWFDWDKIVYDDGSfpGKPQPDIFLKAADKLSLAPADCLVIEDAY-SGLLAAKRAGI 185
Cdd:cd16415    43 LGLDDYFDFVVFSYEVGY--EKPDPRIFQKALERLGVSPEEALHVGDDLkNDYLGARAVGW 101
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH