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Conserved domains on  [gi|149936262|gb|ABR42959|]
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putative phosphatase [Parabacteroides distasonis ATCC 8503]

Protein Classification

HAD family hydrolase( domain architecture ID 11428160)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
7-206 1.28e-68

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


:

Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 208.91  E-value: 1.28e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   7 QLKTALFDFDGVVVDTEPIYDLFWNDAAKRYGLGID-NFADIIKGTTLPYILEKYFSGY-----TEEFRQMVTKESTEYE 80
Cdd:COG0637    1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTeEEYRRLMGRSREDILRYLLEEYgldlpEEELAARKEELYRELL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  81 KTMPLPPMPGSIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHLDNLFDTLVTADRITQGKPDPMCYLLAAKDLNVSPE 160
Cdd:COG0637   81 AEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERLGVDPE 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 149936262 161 DCIVFEDSFNGIQSGKDAGMRVIGLSTTNPAESLRDKVYEVIPNFE 206
Cdd:COG0637  161 ECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLA 206
 
Name Accession Description Interval E-value
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
7-206 1.28e-68

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 208.91  E-value: 1.28e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   7 QLKTALFDFDGVVVDTEPIYDLFWNDAAKRYGLGID-NFADIIKGTTLPYILEKYFSGY-----TEEFRQMVTKESTEYE 80
Cdd:COG0637    1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTeEEYRRLMGRSREDILRYLLEEYgldlpEEELAARKEELYRELL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  81 KTMPLPPMPGSIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHLDNLFDTLVTADRITQGKPDPMCYLLAAKDLNVSPE 160
Cdd:COG0637   81 AEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERLGVDPE 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 149936262 161 DCIVFEDSFNGIQSGKDAGMRVIGLSTTNPAESLRDKVYEVIPNFE 206
Cdd:COG0637  161 ECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLA 206
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 11-185 7.17e-46

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: 148.92  E-value: 7.17e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  11 ALFDFDGVVVDTEPIYDLFWNDAAKryglgidnfadiikgttlpyilekyfsgYTEEFRQMVTKEsteyektmPLPPMPG 90
Cdd:cd07505    2 VIFDMDGVLIDTEPLHRQAWQLLER----------------------------KNALLLELIASE--------GLKLKPG 45

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  91 SIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHL-DNLFDTLVTADRITQGKPDPMCYLLAAKDLNVSPEDCIVFEDSF 169
Cdd:cd07505   46 VVELLDALKAAGIPVAVATSSSRRNVELLLLELGLlRGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERCLVFEDSL 125

                        170
                 ....*....|....*.
gi 149936262 170 NGIQSGKDAGMRVIGL 185
Cdd:cd07505  126 AGIEAAKAAGMTVVAV 141
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 12-184 8.97e-38

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: 129.38  E-value: 8.97e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   12 LFDFDGVVVDTEPIYDLFWNDAAKRYGLGID-----NFADIIKGTTLPYILEKYFSGYTEEFRQMVTKESTEYEKTM--- 83
Cdd:TIGR02009   5 IFDMDGVITDTAPLHAQAWKHIAAKYGISFDkqyneSLKGLSREDILRAILKLRGDGLSLEEIHQLAERKNELYRELlrl 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   84 -PLPPMPGSIEFIRMLKEHGVQIGLVTSSDNAKvkRAFGLLHLDNLFDTLVTADRITQGKPDPMCYLLAAKDLNVSPEDC 162
Cdd:TIGR02009  85 tGVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAP--RILAKLGLRDYFDAIVDASEVKNGKPHPETFLLAAELLGVPPNEC 162

                         170       180
                  ....*....|....*....|..
gi 149936262  163 IVFEDSFNGIQSGKDAGMRVIG 184
Cdd:TIGR02009 163 IVFEDALAGVQAARAAGMFAVA 184
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
12-184 4.46e-36

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 125.00  E-value: 4.46e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   12 LFDFDGVVVDTEPIYDLFWNDAAKRYGLGIDNFADIIK--GTTLPYILEKYF-SGYTEEFRQMVTKESTEYEKTMPLPPM 88
Cdd:pfam13419   2 IFDFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEILKfiGLPLREIFRYLGvSEDEEEKIEFYLRKYNEELHDKLVKPY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   89 PGSIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHLDNLFDTLVTADRITQGKPDPMCYLLAAKDLNVSPEDCIVFEDS 168
Cdd:pfam13419  82 PGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVIYVGDS 161

                         170
                  ....*....|....*.
gi 149936262  169 FNGIQSGKDAGMRVIG 184
Cdd:pfam13419 162 PRDIEAAKNAGIKVIA 177
PRK11587 PRK11587
putative phosphatase; Provisional
 7-211 1.19e-31

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 114.71  E-value: 1.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   7 QLKTALFDFDGVVVDTEPIYDLFWNDAAKRYGLGIDNFADIIKGTTLPYILEKYFSGYTE-----EFRQMvtkESTEYEK 81
Cdd:PRK11587   2 RCKGFLFDLDGTLVDSLPAVERAWSNWADRHGIAPDEVLNFIHGKQAITSLRHFMAGASEaeiqaEFTRL---EQIEATD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  82 TMPLPPMPGSIEFIRMLKEHGVQIGLVTSSDN--AKVKRAFGLLHLDNLFdtlVTADRITQGKPDPMCYLLAAKDLNVSP 159
Cdd:PRK11587  79 TEGITALPGAIALLNHLNKLGIPWAIVTSGSVpvASARHKAAGLPAPEVF---VTAERVKRGKPEPDAYLLGAQLLGLAP 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 149936262 160 EDCIVFEDSFNGIQSGKDAGMRVIGLSttNPAESLR-DKVYEVIPNFEKVTFE 211
Cdd:PRK11587 156 QECVVVEDAPAGVLSGLAAGCHVIAVN--APADTPRlDEVDLVLHSLEQLTVT 206
 
Name Accession Description Interval E-value
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
7-206 1.28e-68

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 208.91  E-value: 1.28e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   7 QLKTALFDFDGVVVDTEPIYDLFWNDAAKRYGLGID-NFADIIKGTTLPYILEKYFSGY-----TEEFRQMVTKESTEYE 80
Cdd:COG0637    1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTeEEYRRLMGRSREDILRYLLEEYgldlpEEELAARKEELYRELL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  81 KTMPLPPMPGSIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHLDNLFDTLVTADRITQGKPDPMCYLLAAKDLNVSPE 160
Cdd:COG0637   81 AEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERLGVDPE 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 149936262 161 DCIVFEDSFNGIQSGKDAGMRVIGLSTTNPAESLRDKVYEVIPNFE 206
Cdd:COG0637  161 ECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLA 206
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 11-185 7.17e-46

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: 148.92  E-value: 7.17e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  11 ALFDFDGVVVDTEPIYDLFWNDAAKryglgidnfadiikgttlpyilekyfsgYTEEFRQMVTKEsteyektmPLPPMPG 90
Cdd:cd07505    2 VIFDMDGVLIDTEPLHRQAWQLLER----------------------------KNALLLELIASE--------GLKLKPG 45

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  91 SIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHL-DNLFDTLVTADRITQGKPDPMCYLLAAKDLNVSPEDCIVFEDSF 169
Cdd:cd07505   46 VVELLDALKAAGIPVAVATSSSRRNVELLLLELGLlRGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERCLVFEDSL 125

                        170
                 ....*....|....*.
gi 149936262 170 NGIQSGKDAGMRVIGL 185
Cdd:cd07505  126 AGIEAAKAAGMTVVAV 141
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 11-211 7.75e-45

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: 148.26  E-value: 7.75e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  11 ALFDFDGVVVDTEPIYDLFWNDAAKRYGLGIDNFADIIKGTTLPYILEKYFSGYTEEfrQMVTKESTEYEKTMP--LPPM 88
Cdd:cd07527    2 LLFDMDGTLVDSTPAVERAWHKWAKEHGVDPEEVLKVSHGRRAIDVIRKLAPDDADI--ELVLALETEEPESYPegVIAI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  89 PGSIEFIRMLKEHGVQIGLVTSSDNAkvkRAFGLLHLDNLF--DTLVTADRITQGKPDPMCYLLAAKDLNVSPEDCIVFE 166
Cdd:cd07527   80 PGAVDLLASLPAAGDRWAIVTSGTRA---LAEARLEAAGLPhpEVLVTADDVKNGKPDPEPYLLGAKLLGLDPSDCVVFE 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 149936262 167 DSFNGIQSGKDAGMRVIGLSTTNPAESLRDKVYEVI-PNFEKVTFE 211
Cdd:cd07527  157 DAPAGIKAGKAAGARVVAVNTSHDLEQLEAAGADLVvEDLSDISVD 202
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 13-206 4.54e-42

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: 140.08  E-value: 4.54e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  13 FDFDGVVVDTEPIYDLFWNDAAKRYglgidnfadiikgttLPYILEKYFSGYTeefrqmvtkesteyektmPLPPMPGSI 92
Cdd:cd16423    4 FDFDGVIVDTEPLWYEAWQELLNER---------------RNELIKRQFSEKT------------------DLPPIEGVK 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  93 EFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHLDNLFDTLVTADRITQGKPDPMCYLLAAKDLNVSPEDCIVFEDSFNGI 172
Cdd:cd16423   51 ELLEFLKEKGIKLAVASSSPRRWIEPHLERLGLLDYFEVIVTGDDVEKSKPDPDLYLEAAERLGVNPEECVVIEDSRNGV 130

                        170       180       190
                 ....*....|....*....|....*....|....
gi 149936262 173 QSGKDAGMRVIGLSTTNPAESLRDKVYEVIPNFE 206
Cdd:cd16423  131 LAAKAAGMKCVGVPNPVTGSQDFSKADLVLSSFA 164
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
8-196 5.10e-40

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 136.21  E-value: 5.10e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   8 LKTALFDFDGVVVDTEPIYDLFWNDAAKRYGLGIDNFADIIK--GTTLPYILEKYFSGY-TEEFRQMVTKESTEYEKTM- 83
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRAliGLGLRELLRRLLGEDpDEELEELLARFRELYEEELl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  84 -PLPPMPGSIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHLDNLFDTLVTADRITQGKPDPMCYLLAAKDLNVSPEDC 162
Cdd:COG0546   81 dETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLDPEEV 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 149936262 163 IVFEDSFNGIQSGKDAGMRVIGLST-TNPAESLRD 196
Cdd:COG0546  161 LMVGDSPHDIEAARAAGVPFIGVTWgYGSAEELEA 195
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 12-184 8.97e-38

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: 129.38  E-value: 8.97e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   12 LFDFDGVVVDTEPIYDLFWNDAAKRYGLGID-----NFADIIKGTTLPYILEKYFSGYTEEFRQMVTKESTEYEKTM--- 83
Cdd:TIGR02009   5 IFDMDGVITDTAPLHAQAWKHIAAKYGISFDkqyneSLKGLSREDILRAILKLRGDGLSLEEIHQLAERKNELYRELlrl 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   84 -PLPPMPGSIEFIRMLKEHGVQIGLVTSSDNAKvkRAFGLLHLDNLFDTLVTADRITQGKPDPMCYLLAAKDLNVSPEDC 162
Cdd:TIGR02009  85 tGVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAP--RILAKLGLRDYFDAIVDASEVKNGKPHPETFLLAAELLGVPPNEC 162

                         170       180
                  ....*....|....*....|..
gi 149936262  163 IVFEDSFNGIQSGKDAGMRVIG 184
Cdd:TIGR02009 163 IVFEDALAGVQAARAAGMFAVA 184
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 10-185 1.80e-36

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: 126.00  E-value: 1.80e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   10 TALFDFDGVVVDTEPIYDlfwnDAAKRYGLGIDNFADIIK-----GTTLPYILEKYFSGYTEEFRQMVTKEST--EYEKT 82
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAIA----KLINREELGLVPDELGVSavgrlELALRRFKAQYGRTISPEDAQLLYKQLFyeQIEEE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   83 MPLPPMPGSIEFIRMLKEHGVQIGLVTSSDNAKvKRAFGLLHLDNLFDTLVTADRITQGKPDPMCYLLAAKDLNVSPEDC 162
Cdd:TIGR01509  77 AKLKPLPGVRALLEALRARGKKLALLTNSPRAH-KLVLALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLEPSEC 155

                         170       180
                  ....*....|....*....|...
gi 149936262  163 IVFEDSFNGIQSGKDAGMRVIGL 185
Cdd:TIGR01509 156 VFVDDSPAGIEAAKAAGMHTVGV 178
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
12-184 4.46e-36

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 125.00  E-value: 4.46e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   12 LFDFDGVVVDTEPIYDLFWNDAAKRYGLGIDNFADIIK--GTTLPYILEKYF-SGYTEEFRQMVTKESTEYEKTMPLPPM 88
Cdd:pfam13419   2 IFDFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEILKfiGLPLREIFRYLGvSEDEEEKIEFYLRKYNEELHDKLVKPY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   89 PGSIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHLDNLFDTLVTADRITQGKPDPMCYLLAAKDLNVSPEDCIVFEDS 168
Cdd:pfam13419  82 PGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVIYVGDS 161

                         170
                  ....*....|....*.
gi 149936262  169 FNGIQSGKDAGMRVIG 184
Cdd:pfam13419 162 PRDIEAAKNAGIKVIA 177
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 12-183 1.03e-31

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: 113.98  E-value: 1.03e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  12 LFDFDGVVVDTEPIY-------------DLFWNDAAKRYGLGIDNFAD-IIKGTTLPYILEKYFSgytEEFRQMVtkest 77
Cdd:cd07529    5 IFDMDGLLLDTERIYtettqeilarygkTYTWDVKAKMMGRPASEAARiIVDELKLPMSLEEEFD---EQQEALA----- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  78 eyEKTMP-LPPMPGSIEFIRMLKEHGVQIGLVTSSDNAKVK-RAFGLLHLDNLFDTLVTAD--RI-TQGKPDPMCYLLAA 152
Cdd:cd07529   77 --ELFMGtAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKlKTSRHKELFSLFHHVVTGDdpEVkGRGKPAPDIFLVAA 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 149936262 153 KDLN---VSPEDCIVFEDSFNGIQSGKDAGMRVI 183
Cdd:cd07529  155 KRFNeppKDPSKCLVFEDSPNGVKAAKAAGMQVV 188
PRK11587 PRK11587
putative phosphatase; Provisional
 7-211 1.19e-31

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 114.71  E-value: 1.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   7 QLKTALFDFDGVVVDTEPIYDLFWNDAAKRYGLGIDNFADIIKGTTLPYILEKYFSGYTE-----EFRQMvtkESTEYEK 81
Cdd:PRK11587   2 RCKGFLFDLDGTLVDSLPAVERAWSNWADRHGIAPDEVLNFIHGKQAITSLRHFMAGASEaeiqaEFTRL---EQIEATD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  82 TMPLPPMPGSIEFIRMLKEHGVQIGLVTSSDN--AKVKRAFGLLHLDNLFdtlVTADRITQGKPDPMCYLLAAKDLNVSP 159
Cdd:PRK11587  79 TEGITALPGAIALLNHLNKLGIPWAIVTSGSVpvASARHKAAGLPAPEVF---VTAERVKRGKPEPDAYLLGAQLLGLAP 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 149936262 160 EDCIVFEDSFNGIQSGKDAGMRVIGLSttNPAESLR-DKVYEVIPNFEKVTFE 211
Cdd:PRK11587 156 QECVVVEDAPAGVLSGLAAGCHVIAVN--APADTPRlDEVDLVLHSLEQLTVT 206
PRK10826 PRK10826
hexitol phosphatase HxpB;
7-196 4.36e-31

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 113.50  E-value: 4.36e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   7 QLKTALFDFDGVVVDTEPiydlFWNDAAKRY--GLGID-NFADIIKGTT-------LPYILEKY-FSGYTEE--FRQMVT 73
Cdd:PRK10826   6 QILAAIFDMDGLLIDSEP----LWDRAELDVmaSLGVDiSRREELPDTLglridqvVDLWYARQpWNGPSRQevVQRIIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  74 KESTEYEKTMPLppMPGSIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHLDNLFDTLVTADRITQGKPDPMCYLLAAK 153
Cdd:PRK10826  82 RVISLIEETRPL--LPGVREALALCKAQGLKIGLASASPLHMLEAVLTMFDLRDYFDALASAEKLPYSKPHPEVYLNCAA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 149936262 154 DLNVSPEDCIVFEDSFNGIQSGKDAGMRVIGLsttnPAESLRD 196
Cdd:PRK10826 160 KLGVDPLTCVALEDSFNGMIAAKAARMRSIVV----PAPEQQN 198
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 12-216 2.77e-29

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: 107.38  E-value: 2.77e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  12 LFDFDGVVVDTEPIYDLFWNDAAKRYGL---GIDNfadiikgttlpyilekyfsgYTEEFRQMVTKESteyektmplppM 88
Cdd:cd02598    3 IFDLDGVITDTAEYHYRAWKKLADKEELaarKNRI--------------------YVELIEELTPVDV-----------L 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  89 PGSIEFIRMLKEHGVQIGLVTSSDNA-KVKRAFGLLHLdnlFDTLVTADRITQGKPDPMCYLLAAKDLNVSPEDCIVFED 167
Cdd:cd02598   52 PGIASLLVDLKAKGIKIALASASKNApKILEKLGLAEY---FDAIVDGAVLAKGKPDPDIFLAAAEGLGLNPKDCIGVED 128

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 149936262 168 SFNGIQSGKDAGMRVIGLSttnPAESLRDKVYEVIPNFEKVTFEDYLRW 216
Cdd:cd02598  129 AQAGIRAIKAAGFLVVGVG---REEDLLGADIVVPDTTADLTIEELLEV 174
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 8-179 2.63e-28

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: 105.36  E-value: 2.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262    8 LKTALFDFDGVVVDTEPIYDLFWNDAAKRYGLGI--------------DNFADIIKG-----TTLPYILEKYFSGYTEEF 68
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAKaivaaaedlpipveDFTARLLLGkrdwlEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   69 RQMVTKESTEYEKTMPLPPMPGSIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHLDNLFDTLVTADRITQGKPDPMCY 148
Cdd:pfam00702  81 TVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIY 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 149936262  149 LLAAKDLNVSPEDCIVFEDSFNGIQSGKDAG 179
Cdd:pfam00702 161 LAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 12-183 2.93e-25

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: 97.45  E-value: 2.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  12 LFDFDGVVVDTEPIY-DLFWNDAAKRYGL----GIDNFADIIK-GTTLPYILEKYFSGYTEEFRQMVTKE--------ST 77
Cdd:cd07528    3 IFDVDGTLAETEELHrRAFNNAFFAERGLdwywDRELYGELLRvGGGKERIAAYFEKVGWPESAPKDLKEliadlhkaKT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  78 EYEKTMP----LPPMPGSIEFIRMLKEHGVQIGLVTSSD----NAKVKRAFGLlHLDNLFDTLVTADRITQGKPDPMCYL 149
Cdd:cd07528   83 ERYAELIaaglLPLRPGVARLIDEAKAAGVRLAIATTTSpanvDALLSALLGP-ERRAIFDAIAAGDDVAEKKPDPDIYL 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 149936262 150 LAAKDLNVSPEDCIVFEDSFNGIQSGKDAGMRVI 183
Cdd:cd07528  162 LALERLGVSPSDCLAIEDSAIGLQAAKAAGLPCI 195
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 12-186 6.05e-25

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: 95.08  E-value: 6.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  12 LFDFDGVVVDTEPIYDLFWNDAAKRYGLgidnfadiikgttlpyilekyfsgytEEFRQMVTKesteyektmpLPPMPGS 91
Cdd:cd07526    4 IFDCDGVLVDSEVIAARVLVEVLAELGA--------------------------RVLAAFEAE----------LQPIPGA 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  92 IEFIRMLkehGVQIGLVTSSDNAKVKRAFGLLHLDNLFDT-LVTADRITQGKPDPMCYLLAAKDLNVSPEDCIVFEDSFN 170
Cdd:cd07526   48 AAALSAL---TLPFCVASNSSRERLTHSLGLAGLLAYFEGrIFSASDVGRGKPAPDLFLHAAAQMGVAPERCLVIEDSPT 124

                        170
                 ....*....|....*.
gi 149936262 171 GIQSGKDAGMRVIGLS 186
Cdd:cd07526  125 GVRAALAAGMTVFGFT 140
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 9-183 1.95e-24

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: 95.87  E-value: 1.95e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   9 KTALFDFDGVVVDTEPIYDLFWNDAAKRYGLGI--DNFADIIKGTTLPYI---------LEKYFSGYTEEFRQMVTKEST 77
Cdd:COG1011    2 KAVLFDLDGTLLDFDPVIAEALRALAERLGLLDeaEELAEAYRAIEYALWrryergeitFAELLRRLLEELGLDLAEELA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  78 E-YEKTMP--LPPMPGSIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHLDNLFDTLVTADRITQGKPDPMCYLLAAKD 154
Cdd:COG1011   82 EaFLAALPelVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIFELALER 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 149936262 155 LNVSPEDCIVFEDSFNG-IQSGKDAGMRVI 183
Cdd:COG1011  162 LGVPPEEALFVGDSPETdVAGARAAGMRTV 191
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
12-183 1.97e-21

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 87.44  E-value: 1.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  12 LFDFDGVVVDTEPIYDLFWNDAAKRYGLGIDNFADI-IKGTTLPYILEKYFSGYTEEFR-QMVTKESTEYEKTM------ 83
Cdd:PRK10725   9 IFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVaLNGSPTWRIAQAIIELNQADLDpHALAREKTEAVKSMlldsve 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  84 PLPpmpgsieFIRMLKE-HG---VQIGlvTSSDNAKVKRAFGLLHLDNLFDTLVTADRITQGKPDPMCYLLAAKDLNVSP 159
Cdd:PRK10725  89 PLP-------LIEVVKAwHGrrpMAVG--TGSESAIAEALLAHLGLRRYFDAVVAADDVQHHKPAPDTFLRCAQLMGVQP 159

                        170       180
                 ....*....|....*....|....
gi 149936262 160 EDCIVFEDSFNGIQSGKDAGMRVI 183
Cdd:PRK10725 160 TQCVVFEDADFGIQAARAAGMDAV 183
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 9-186 3.38e-21

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: 86.95  E-value: 3.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   9 KTALFDFDGVVVDTEPIYDLFWNDAAKRYGLGIDNFADIIK--GTTLPYILEKYFSGYTEEFRQMVTKESTEYEKTMPLP 86
Cdd:cd02616    2 TTILFDLDGTLIDTNELIIKSFNHTLKEYGLEGYTREEVLPfiGPPLRETFEKIDPDKLEDMVEEFRKYYREHNDDLTKE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  87 pMPGSIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHLDNLFDTLVTADRITQGKPDPMCYLLAAKDLNVSPEDCIVFE 166
Cdd:cd02616   82 -YPGVYETLARLKSQGIKLGVVTTKLRETALKGLKLLGLDKYFDVIVGGDDVTHHKPDPEPVLKALELLGAEPEEALMVG 160

                        170       180
                 ....*....|....*....|
gi 149936262 167 DSFNGIQSGKDAGMRVIGLS 186
Cdd:cd02616  161 DSPHDILAGKNAGVKTVGVT 180
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 12-196 5.83e-21

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 90.68  E-value: 5.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   12 LFDFDGVVVDTEPI-----YDLFW--------NDAAKRYGLGIDNF----ADI--IKGTTLPYILEKYFSGYTEEfrqmv 72
Cdd:PLN02919   79 LFDMDGVLCNSEEPsrraaVDVFAemgvevtvEDFVPFMGTGEANFlggvASVkgVKGFDPDAAKKRFFEIYLEK----- 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   73 tkesteYEKTMPLPPMPGSIEFIRMLKEHGVQIGLVTSSDNAKVK---RAFGLLHldNLFDTLVTADRITQGKPDPMCYL 149
Cdd:PLN02919  154 ------YAKPNSGIGFPGALELITQCKNKGLKVAVASSADRIKVDanlAAAGLPL--SMFDAIVSADAFENLKPAPDIFL 225

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 149936262  150 LAAKDLNVSPEDCIVFEDSFNGIQSGKDAGMRVIGLSTTNPAESLRD 196
Cdd:PLN02919  226 AAAKILGVPTSECVVIEDALAGVQAARAAGMRCIAVTTTLSEEILKD 272
PLN02940 PLN02940
riboflavin kinase
 5-202 1.10e-20

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 88.74  E-value: 1.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   5 MKQLKTA-LFDFDGVVVDTEPIYDLFWNDAAKRYGLGIDNF-ADIIKGTTlPY-----ILEKYFSGY-TEEFRQMVTKes 76
Cdd:PLN02940   7 LKKLVSHvILDLDGTLLNTDGIVSDVLKAFLVKYGKQWDGReAQKIVGKT-PLeaaatVVEDYGLPCsTDEFNSEITP-- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  77 TEYEKTMPLPPMPGSIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLH-LDNLFDTLVTADRITQGKPDPMCYLLAAKDL 155
Cdd:PLN02940  84 LLSEQWCNIKALPGANRLIKHLKSHGVPMALASNSPRANIEAKISCHQgWKESFSVIVGGDEVEKGKPSPDIFLEAAKRL 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 149936262 156 NVSPEDCIVFEDSFNGIQSGKDAGMRVIGLSTTNPAESLRDKVYEVI 202
Cdd:PLN02940 164 NVEPSNCLVIEDSLPGVMAGKAAGMEVIAVPSIPKQTHLYSSADEVI 210
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 12-211 5.79e-19

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 82.83  E-value: 5.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  12 LFDFDGVVVDTEPiyDLF---WNDAAKRYGLG--------IDNFADIIKGTtlpyilEK---YFSGY------------T 65
Cdd:PLN02779  44 LFDCDGVLVETER--DGHrvaFNDAFKEFGLRpvewdvelYDELLNIGGGK------ERmtwYFNENgwptstiekapkD 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  66 EEFRQMVTKE----STEYEKTM----PLPPMPGSIEFIRMLKEHGVQIGlVTSSDNakvKRAFGLLhLDNL-----FDTL 132
Cdd:PLN02779 116 EEERKELVDSlhdrKTELFKELiesgALPLRPGVLRLMDEALAAGIKVA-VCSTSN---EKAVSKI-VNTLlgperAQGL 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262 133 -VTA-DRITQGKPDPMCYLLAAKDLNVSPEDCIVFEDSFNGIQSGKDAGMRVI---GLSTTNPAESLRDKVYEVIPNFEK 207
Cdd:PLN02779 191 dVFAgDDVPKKKPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAAKAAGMRCIvtkSSYTADEDFSGADAVFDCLGDVPL 270


                 ....
gi 149936262 208 VTFE 211
Cdd:PLN02779 271 EDFD 274
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 8-216 1.50e-18

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 81.04  E-value: 1.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   8 LKTALFDFDGVVVDTEPIYDLFWNDAAKRY----GLGIDN--FADIIKGTTLPYILEKYFSGYTEEFRQMVTKESTEYEK 81
Cdd:PLN02770  22 LEAVLFDVDGTLCDSDPLHYYAFREMLQEInfngGVPITEefFVENIAGKHNEDIALGLFPDDLERGLKFTDDKEALFRK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  82 TMP--LPPMPGSIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHLDNLFDTLVTADRITQGKPDPMCYLLAAKDLNVSP 159
Cdd:PLN02770 102 LASeqLKPLNGLYKLKKWIEDRGLKRAAVTNAPRENAELMISLLGLSDFFQAVIIGSECEHAKPHPDPYLKALEVLKVSK 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 149936262 160 EDCIVFEDSFNGIQSGKDAGMRVIGLSTTNPAESLrdkvYEVIPNFEKVTFEDYLRW 216
Cdd:PLN02770 182 DHTFVFEDSVSGIKAGVAAGMPVVGLTTRNPESLL----MEAKPTFLIKDYEDPKLW 234
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 88-194 2.06e-18

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 80.85  E-value: 2.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  88 MPGSIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHLDNLFDTLVTADRITQGKPDPMCYLLAAKDLNVSPEDCIVFED 167
Cdd:PLN03243 111 RPGSREFVQALKKHEIPIAVASTRPRRYLERAIEAVGMEGFFSVVLAAEDVYRGKPDPEMFMYAAERLGFIPERCIVFGN 190

                         90       100
                 ....*....|....*....|....*..
gi 149936262 168 SFNGIQSGKDAGMRVIGLSTTNPAESL 194
Cdd:PLN03243 191 SNSSVEAAHDGCMKCVAVAGKHPVYEL 217
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 8-196 2.84e-18

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: 78.93  E-value: 2.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   8 LKTALFDFDGVVVDTEPiydlfWNDAAKRYGLGIDNFADIIKGTTLPYILEKYFSG------YTEEFRQMV----TKEST 77
Cdd:cd02603    1 IRAVLFDFGGVLIDPDP-----AAAVARFEALTGEPSEFVLDTEGLAGAFLELERGriteeeFWEELREELgrplSAELF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  78 EYEKTMPLPPMPGSIEFIRMLKEHGVQIGLVtsSDNAKVKRAFGLLHLDN---LFDTLVTADRITQGKPDPMCYLLAAKD 154
Cdd:cd02603   76 EELVLAAVDPNPEMLDLLEALRAKGYKVYLL--SNTWPDHFKFQLELLPRrgdLFDGVVESCRLGVRKPDPEIYQLALER 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 149936262 155 LNVSPEDCIVFEDSFNGIQSGKDAGMRVIGLstTNPAESLRD 196
Cdd:cd02603  154 LGVKPEEVLFIDDREENVEAARALGIHAILV--TDAEDALRE 193
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 6-195 9.36e-18

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 78.15  E-value: 9.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   6 KQLKTALFDFDGVVVDT-EPIYDLFWNdAAKRYGLGIDNFADIIK--GTTLPYILEKYFSGYTEEFRQMVTK-------- 74
Cdd:PRK13288   1 MKINTVLFDLDGTLINTnELIISSFLH-TLKTYYPNQYKREDVLPfiGPSLHDTFSKIDESKVEEMITTYREfnhehhde 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  75 ESTEYEktmplppmpGSIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHLDNLFDTLVTADRITQGKPDPMCYLLAAKD 154
Cdd:PRK13288  80 LVTEYE---------TVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPDPEPVLKALEL 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 149936262 155 LNVSPEDCIVFEDSFNGIQSGKDAGMRVIGLS-TTNPAESLR 195
Cdd:PRK13288 151 LGAKPEEALMVGDNHHDILAGKNAGTKTAGVAwTIKGREYLE 192
PLN02811 PLN02811
hydrolase
 86-206 1.47e-16

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 75.18  E-value: 1.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  86 PPMPGSIEFIRMLKEHGVQIGLVTSSDnakvKRAFGLL---H--LDNLFDTLVTAD--RITQGKPDPMCYLLAA---KDL 155
Cdd:PLN02811  78 DLMPGAERLVRHLHAKGIPIAIATGSH----KRHFDLKtqrHgeLFSLMHHVVTGDdpEVKQGKPAPDIFLAAArrfEDG 153

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 149936262 156 NVSPEDCIVFEDSFNGIQSGKDAGMRVIGLSTTNPAESLRDKVYEVIPNFE 206
Cdd:PLN02811 154 PVDPGKVLVFEDAPSGVEAAKNAGMSVVMVPDPRLDKSYCKGADQVLSSLL 204
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
5-186 3.28e-16

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 74.08  E-value: 3.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   5 MKQLKTALFDFDGVVVDTEPiyDLFW--NDAAKRYGLG----------IDNFADIIKGTTL---PYILEKyfsgytEEFR 69
Cdd:PRK13222   3 FMDIRAVAFDLDGTLVDSAP--DLAAavNAALAALGLPpageervrtwVGNGADVLVERALtwaGREPDE------ELLE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  70 QMVTKESTEYEKTMPL--PPMPGSIEFIRMLKEHGVQIGLVTssdNAKVKRAFGLLH---LDNLFDTLVTADRITQGKPD 144
Cdd:PRK13222  75 KLRELFDRHYAENVAGgsRLYPGVKETLAALKAAGYPLAVVT---NKPTPFVAPLLEalgIADYFSVVIGGDSLPNKKPD 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 149936262 145 PMCYLLAAKDLNVSPEDCIVFEDSFNGIQSGKDAGMRVIGLS 186
Cdd:PRK13222 152 PAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPSVGVT 193
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 92-185 6.99e-16

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: 70.50  E-value: 6.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  92 IEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHLDNLFDTLVTADRITQGKPDPMCYLLAAKDLNVSPEDCIVFEDSFNG 171
Cdd:cd01427   13 VELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSEND 92

                         90
                 ....*....|....
gi 149936262 172 IQSGKDAGMRVIGL 185
Cdd:cd01427   93 IEAARAAGGRTVAV 106
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 11-187 5.15e-15

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: 70.51  E-value: 5.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  11 ALFDFDGVVVDTE-PIYDLFwNDAAKRYGLGIDNFADI--IKGTTLPYILEKYFSGYTEEFRQMVTKESTEYEKTM---- 83
Cdd:cd07533    2 VIFDWDGTLADSQhNIVAAM-TAAFADLGLPVPSAAEVrsIIGLSLDEAIARLLPMATPALVAVAERYKEAFDILRllpe 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  84 -PLPPMPGSIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHLDNLFDTLVTADRiTQGKPDPMCYLLAAKDLNVSPEDC 162
Cdd:cd07533   81 hAEPLFPGVREALDALAAQGVLLAVATGKSRRGLDRVLEQHGLGGYFDATRTADD-TPSKPHPEMLREILAELGVDPSRA 159

                        170       180
                 ....*....|....*....|....*
gi 149936262 163 IVFEDSFNGIQSGKDAGMRVIGLST 187
Cdd:cd07533  160 VMVGDTAYDMQMAANAGAHAVGVAW 184
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 90-201 6.29e-15

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 72.59  E-value: 6.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  90 GSIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHLDNLFDTLVTADRITQGKPDPMCYLLAAKDLNVSPEDCIVFEDSF 169
Cdd:PLN02575 220 GSQEFVNVLMNYKIPMALVSTRPRKTLENAIGSIGIRGFFSVIVAAEDVYRGKPDPEMFIYAAQLLNFIPERCIVFGNSN 299

                         90       100       110
                 ....*....|....*....|....*....|..
gi 149936262 170 NGIQSGKDAGMRVIGLSTTNPaeslrdkVYEV 201
Cdd:PLN02575 300 QTVEAAHDARMKCVAVASKHP-------IYEL 324
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 10-179 1.10e-14

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


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 68.96  E-value: 1.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   10 TALFDFDGVVVDTEPIYDLFWNDAAKRYGLGIDNFADIIKGTTL-PYILEKYFSGYTEEFRQMVTKESTEYEKTMPLPpm 88
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFGLDPASFKALKQAGGLaEEEWYRIATSALEELQGRFWSEYDAEEAYIRGA-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   89 pgsIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHLDNLFDTLVTADRITQgKPDPMCYLLAAKDLNVSPEdCIVFEDS 168
Cdd:TIGR01549  79 ---ADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEPGS-KPEPEIFLAALESLGVPPE-VLHVGDN 153

                         170
                  ....*....|.
gi 149936262  169 FNGIQSGKDAG 179
Cdd:TIGR01549 154 LNDIEGARNAG 164
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 12-186 2.27e-14

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


Pssm-ID: 319854 [Multi-domain]  Cd Length: 212  Bit Score: 68.80  E-value: 2.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  12 LFDFDGVVVDTEPiyDLFW--NDAAKRYGL--------------GIDNF-----ADIIKGTTLPYILEKYFSGYTEEFRQ 70
Cdd:cd16417    3 AFDLDGTLVDSAP--DLAEaaNAMLAALGLpplpeetvrtwignGADVLveralTGAREAEPDEELFKEARALFDRHYAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  71 MVTKESTEYektmplppmPGSIEFIRMLKEHGVQIGLVTssdNAKVKRAFGLLH---LDNLFDTLVTADRITQGKPDPMC 147
Cdd:cd16417   81 TLSVHSHLY---------PGVKEGLAALKAQGYPLACVT---NKPERFVAPLLEalgISDYFSLVLGGDSLPEKKPDPAP 148

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 149936262 148 YLLAAKDLNVSPEDCIVFEDSFNGIQSGKDAGMRVIGLS 186
Cdd:cd16417  149 LLHACEKLGIAPAQMLMVGDSRNDILAARAAGCPSVGLT 187
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 5-182 2.73e-13

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 66.26  E-value: 2.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   5 MKQLKTALFDFDGVVVDTEPIYDLFWNDAAKRYGLGIDnFADII---KGTTLPYILEKYfsgyTEEFRQMVTKESTE--Y 79
Cdd:PRK10563   1 MSQIEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLS-LEEVFkrfKGVKLYEIIDII----SKEHGVTLAKAELEpvY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  80 EKTMP------LPPMPGSIEFIRMLKehgVQIGLVTSSDNAKVKRAFGLLHLDNLF-DTLVTADRITQGKPDPMCYLLAA 152
Cdd:PRK10563  76 RAEVArlfdseLEPIAGANALLESIT---VPMCVVSNGPVSKMQHSLGKTGMLHYFpDKLFSGYDIQRWKPDPALMFHAA 152

                        170       180       190
                 ....*....|....*....|....*....|
gi 149936262 153 KDLNVSPEDCIVFEDSFNGIQSGKDAGMRV 182
Cdd:PRK10563 153 EAMNVNVENCILVDDSSAGAQSGIAAGMEV 182
HAD_PHN cd02586
Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; ...
 12-188 2.68e-11

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


Pssm-ID: 319785 [Multi-domain]  Cd Length: 242  Bit Score: 60.78  E-value: 2.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  12 LFDFDGVVVDTEPIydlfwndaakRYGLGIDNFADIIKGTTLPYILEKYFsgytEEFRQMVTKESTE--YEKTMPL---- 85
Cdd:cd02586   27 AFAQRGVQITLEEA----------RKPMGLLKIDHIRALLEMPRVAEAWR----AVFGRLPTEADVDalYEEFEPIlias 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  86 -----PPMPGSIEFIRMLKEHGVQIGLVTSSDNAK----VKRAFGL-LHLDNLfdtlVTADRITQGKPDP-MCYLlAAKD 154
Cdd:cd02586   93 laeysSPIPGVLEVIAKLRARGIKIGSTTGYTREMmdivLPEAAAQgYRPDSL----VTPDDVPAGRPYPwMCYK-NAIE 167

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 149936262 155 LNV-SPEDCIVFEDSFNGIQSGKDAGMRVIGLSTT 188
Cdd:cd02586  168 LGVyDVAAVVKVGDTVPDIKEGLNAGMWTVGVILS 202
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 10-194 1.26e-10

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: 58.87  E-value: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  10 TALFDFDGVVVDTEPiyDLF--WNDAAKRYGLGIDNFADI--IKGTTLPYILEKYFSGYTE-----EFRQMVTKESTEYE 80
Cdd:cd07512    1 AVIFDLDGTLIDSAP--DLHaaLNAVLAAEGLAPLSLAEVrsFVGHGAPALIRRAFAAAGEdldgpLHDALLARFLDHYE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  81 KTMPLP--PMPGSIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHLDNLFDTLVTADRITQGKPDPMCYLLAAKDLNVS 158
Cdd:cd07512   79 ADPPGLtrPYPGVIEALERLRAAGWRLAICTNKPEAPARALLSALGLADLFAAVVGGDTLPQRKPDPAPLRAAIRRLGGD 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 149936262 159 PEDCIVFEDSFNGIQSGKDAGMRVIGLS---TTNPAESL 194
Cdd:cd07512  159 VSRALMVGDSETDAATARAAGVPFVLVTfgyRHAPVAEL 197
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 89-183 3.63e-10

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: 55.24  E-value: 3.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  89 PGSIEFIRMLKeHGVQIGLVTSSDNAKVKRAFGLLHLDNLFDTLVTADRITQGKPDPMCYLLAAKDLNVSPEDCIVFEDS 168
Cdd:cd04305   12 PGAKELLEELK-KGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLMVGDS 90

                         90
                 ....*....|....*.
gi 149936262 169 F-NGIQSGKDAGMRVI 183
Cdd:cd04305   91 LeSDILGAKNAGIKTV 106
PRK13478 PRK13478
phosphonoacetaldehyde hydrolase; Provisional
 5-188 1.17e-09

phosphonoacetaldehyde hydrolase; Provisional


Pssm-ID: 184075 [Multi-domain]  Cd Length: 267  Bit Score: 56.41  E-value: 1.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   5 MKQLKTALFDFDGVVVD------TEPIYDLFWN--------DAAKRYGLG-IDNFADIIKgttLPYILEKYFsgytEEFR 69
Cdd:PRK13478   1 MMKIQAVIFDWAGTTVDfgsfapTQAFVEAFAQfgveitleEARGPMGLGkWDHIRALLK---MPRVAARWQ----AVFG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  70 QMVTKESTE--YEKTMPL---------PPMPGSIEFIRMLKEHGVQIGLVTSSDN------AKVKRAFGLLHldnlfDTL 132
Cdd:PRK13478  74 RLPTEADVDalYAAFEPLqiakladyaTPIPGVLEVIAALRARGIKIGSTTGYTRemmdvvVPLAAAQGYRP-----DHV 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 149936262 133 VTADRITQGKPDP-MCYlLAAKDLNVSP-EDCIVFEDSFNGIQSGKDAGMRVIGLSTT 188
Cdd:PRK13478 149 VTTDDVPAGRPYPwMAL-KNAIELGVYDvAACVKVDDTVPGIEEGLNAGMWTVGVILS 205
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 43-162 2.11e-08

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: 52.27  E-value: 2.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  43 NFADIIKGTtLPYILEKYFSGYTEEFRQMVTKESTEyektmpLPPMPGSIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGL 122
Cdd:cd02588   55 DFDELTRDA-LRATAAELGLELDESDLDELGDAYLR------LPPFPDVVAGLRRLREAGYRLAILSNGSPDLIEDVVAN 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 149936262 123 LHLDNLFDTLVTADRITQGKPDPMCYLLAAKDLNVSPEDC 162
Cdd:cd02588  128 AGLRDLFDAVLSAEDVRAYKPAPAVYELAAERLGVPPDEI 167
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 11-200 6.24e-08

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


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 50.99  E-value: 6.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  11 ALFDFDGVVVDTEPIYDLFWnDAAKRYGLGIDNFADIIKGTTLPY---------ILEKY---FSGYTEEFrqmVTKESTE 78
Cdd:COG0560    6 AVFDLDGTLIAGESIDELAR-FLGRRGLVDRREVLEEVAAITERAmageldfeeSLRFRvalLAGLPEEE---LEELAER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  79 YEKTMPlPPMPGSIEFIRMLKEHGVQIGLVTSSDN---AKVKRAFGllhLDNLF-DTLVTAD-RITqGKPD-PMCY---- 148
Cdd:COG0560   82 LFEEVP-RLYPGARELIAEHRAAGHKVAIVSGGFTffvEPIAERLG---IDHVIaNELEVEDgRLT-GEVVgPIVDgegk 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 149936262 149 ---LLA-AKDLNVSPEDCIVFEDSFNgiqsgkDAGM-RVIGLST-TNPAESLRDKVYE 200
Cdd:COG0560  157 aeaLRElAAELGIDLEQSYAYGDSAN------DLPMlEAAGLPVaVNPDPALREAADR 208
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 109-181 3.35e-07

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


Pssm-ID: 319791 [Multi-domain]  Cd Length: 182  Bit Score: 48.78  E-value: 3.35e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149936262 109 TSSDNAKVKRAFGLLHLDNLFD--TLVTADRiTQGKPDPMCYLLAAKDLNVSPEDCIVFEDSFNGIQSGKDAGMR 181
Cdd:cd02604  103 TNASKNHAIRVLKRLGLADLFDgiFDIEYAG-PDPKPHPAAFEKAIREAGLDPKRAAFFDDSIRNLLAAKALGMK 176
HAD-1A3-hyp TIGR02247
epoxide hydrolase N-terminal domain-like phosphatase; This model represents a small clade of ...
 7-183 7.86e-07

epoxide hydrolase N-terminal domain-like phosphatase; This model represents a small clade of sequences including C. elegans and mammalian sequences as well as a small number of bacteria. In eukaryotes, this domain exists as an N-terminal fusion to the soluble epoxide hydrolase enzyme and has recently been shown to be an active phosphatase, although the nature of the biological substrate is unclear. These appear to be members of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases by general homology and the conservation of all of the recognized catalytic motifs (although the first motif is unusual in the replacement of the more common aspartate with glycine...). The variable domain is found in between motifs 1 and 2, indicating membership in subfamily I and phylogeny and prediction of the alpha helical nature of the variable domain (by PSI-PRED) indicate membership in subfamily IA.


Pssm-ID: 274054 [Multi-domain]  Cd Length: 211  Bit Score: 47.90  E-value: 7.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262    7 QLKTALFDFDGVVVdTEPIYDLFW----------NDAAKRYGLGIDNF--------ADIIKGTTLPYILEKYF-----SG 63
Cdd:TIGR02247   1 AIKAVIFDFGGVLL-PSPGVMRRWeterglpglkDFIVTVNITGPDFNpwartferGELTAEAFDGLFRHEYGlrlghDV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   64 YTEEFRQMVTKESTEYEKTMplppmpgsIEFIRMLKEHGVQIGLVTSS---DNAKvKRAFGLLHLDNLFDTLVTADRITQ 140
Cdd:TIGR02247  80 RIAPVFPLLYGENTKLRPSM--------MAAIKTLRAKGFKTACITNNfptDHSA-EEALLPGDIMALFDAVVESCLEGL 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 149936262  141 GKPDPMCYLLAAKDLNVSPEDCIVFEDSFNGIQSGKDAGMRVI 183
Cdd:TIGR02247 151 RKPDPRIYQLMLERLGVAPEECVFLDDLGSNLKPAAALGITTI 193
HAD pfam12710
haloacid dehalogenase-like hydrolase;
11-168 1.78e-06

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 46.76  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   11 ALFDFDGVVVDTEPIYDLF-----------WNDAAKRYGLGIDNFADIIKGTTLPYILEKYFSGYTEEFRQMVTKEsteY 79
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIrallrrggpdlWRALLVLLLLALLRLLGRLSRAGARELLRALLAGLPEEDAAELERF---V 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   80 EKTMPLPPMPGSIEFIRMLKEHGVQIGLVTSS--DNAK-VKRAFGllhLDNLFDT--LVTADRITQG--KPDPMCY---- 148
Cdd:pfam12710  78 AEVALPRLHPGALELLAAHRAAGDRVVVVTGGlrPLVEpVLAELG---FDEVLATelEVDDGRFTGElrLIGPPCAgegk 154

                         170       180
                  ....*....|....*....|....*.
gi 149936262  149 ------LLAAKDLNVSPEDCIVFEDS 168
Cdd:pfam12710 155 vrrlraWLAARGLGLDLADSVAYGDS 180
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 91-183 4.61e-06

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


Pssm-ID: 319852 [Multi-domain]  Cd Length: 128  Bit Score: 44.59  E-value: 4.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  91 SIEFIRMLKEHGVQIGLVTSSDNA--KVKRAFGLLHLdnlFDTLVTADRITQGKPDPMCYLLAAKDLNVSPEDCIVFEDS 168
Cdd:cd16415   12 AVETLKDLKEKGLKLAVVSNFDRRlrELLEALGLDDY---FDFVVFSYEVGYEKPDPRIFQKALERLGVSPEEALHVGDD 88

                         90
                 ....*....|....*.
gi 149936262 169 F-NGIQSGKDAGMRVI 183
Cdd:cd16415   89 LkNDYLGARAVGWHAL 104
Hydrolase_like pfam13242
HAD-hyrolase-like;
141-205 4.85e-06

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 42.99  E-value: 4.85e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149936262  141 GKPDPMCYLLAAKDLNVSPEDCIVFEDSFN-GIQSGKDAGMRVIGLST--TNPAEsLRDKVYE---VIPNF 205
Cdd:pfam13242   3 GKPNPGMLERALARLGLDPERTVMIGDRLDtDILGAREAGARTILVLTgvTRPAD-LEKAPIRpdyVVDDL 72
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 10-183 8.11e-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: 44.68  E-value: 8.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  10 TALFDFDGVVVDTEPIYDLFWNDAAKRYGLGIDNFAD--IIKGTTLPYILEKYfsGYTEEFRQMVTKESTEYEKTMPLPP 87
Cdd:cd07523    1 NFIWDLDGTLLDSYPAMTKALSETLADFGIPQDLETVykIIKESSVQFAIQYY--AEVPDLEEEYKELEAEYLAKPILFP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  88 mpGSIEFIRMLKEHGVQIGLVTSSDNAkvkrAFGLL---HLDNLFDTLVTADRITQGKPDPMCYLLAAKDLNVSPEDCIV 164
Cdd:cd07523   79 --GAKAVLRWIKEQGGKNFLMTHRDHS----ALTILkkdGIASYFTEIVTSDNGFPRKPNPEAINYLLNKYQLNPEETVM 152

                        170
                 ....*....|....*....
gi 149936262 165 FEDSFNGIQSGKDAGMRVI 183
Cdd:cd07523  153 IGDRELDIEAGHNAGISTI 171
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 11-129 6.51e-05

Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273653 [Multi-domain]  Cd Length: 177  Bit Score: 41.96  E-value: 6.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   11 ALFDFDGVVVDTEPIYDLFwndaaKRYGLGIDNFADIIKGTTLPYILEKYFSGYTEEFRQMVTKESTEYE--KTMPLPPm 88
Cdd:TIGR01488   2 AIFDFDGTLTRQDSLIDLL-----AKLLGTNDEVIELTRLAPSGRISFEDALGRRLALLHRSRSEEVAKEflARQVALR- 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 149936262   89 PGSIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHLDNLF 129
Cdd:TIGR01488  76 PGARELISWLKERGIDTVIVSGGFDFFVEPVAEKLGIDDVF 116
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 89-183 9.79e-05

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: 40.33  E-value: 9.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  89 PGSIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHLDNLFDTlvtadritqGKPDPMCYLLAAKDLNVSPEDCIVFEDS 168
Cdd:cd16416   20 PEVKAWLADLKEAGIKVVLVSNNNERRVAKVIEKLDLPFVARA---------GKPRPRAFRRALKEMDLPPEQVAMVGDQ 90

                         90
                 ....*....|....*.
gi 149936262 169 -FNGIQSGKDAGMRVI 183
Cdd:cd16416   91 lFTDILGGNRAGLYTI 106
PRK13226 PRK13226
phosphoglycolate phosphatase; Provisional
 87-180 3.27e-04

phosphoglycolate phosphatase; Provisional


Pssm-ID: 237311 [Multi-domain]  Cd Length: 229  Bit Score: 40.60  E-value: 3.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  87 PMPGSIEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLHLDNLFDTLVTADRITQGKPDPMCYLLAAKDLNVSPEDCIVFE 166
Cdd:PRK13226  96 LFDGVEGMLQRLECAGCVWGIVTNKPEYLARLILPQLGWEQRCAVLIGGDTLAERKPHPLPLLVAAERIGVAPTDCVYVG 175

                         90
                 ....*....|....
gi 149936262 167 DSFNGIQSGKDAGM 180
Cdd:PRK13226 176 DDERDILAARAAGM 189
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 92-184 1.55e-03

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: 37.05  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262  92 IEFIRMLKEHGVQIGLVTSSDNAKVKRAFGLLhLDNLFDTLVTADRITQGKPDPMCYLLAAKDLNVSPEDCIVFEDSFNG 171
Cdd:cd16421   13 LELLKALRQKGIKLAVLSNKPNEAVQVLVEEL-FPGSFDFVLGEKEGIRRKPDPT*ALECAKVLGVPPDEVLYVGDSGVD 91

                         90
                 ....*....|...
gi 149936262 172 IQSGKDAGMRVIG 184
Cdd:cd16421   92 MQTARNAGMDEIG 104
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 89-183 2.13e-03

HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273742 [Multi-domain]  Cd Length: 135  Bit Score: 37.00  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   89 PGSIEFIRMLKEHGVQIGLVTS-----------SDNAKVKRAfgLLHLDNLFDTLVTADRITqgKPDPMCYLLAAKDLN- 156
Cdd:TIGR01662  28 PEVPDALAELKEAGYKVVIVTNqsgigrgyfsrSFSGRVARR--LEELGVPIDILYACPGCR--KPKPGMFLEALKRFNe 103

                          90       100
                  ....*....|....*....|....*...
gi 149936262  157 VSPEDCIVFED-SFNGIQSGKDAGMRVI 183
Cdd:TIGR01662 104 IDPEESVYVGDqDLTDLQAAKRVGLATI 131
YorC COG4502
5'(3')-deoxyribonucleotidase [Nucleotide transport and metabolism];
9-136 2.27e-03

5'(3')-deoxyribonucleotidase [Nucleotide transport and metabolism];


Pssm-ID: 443586 [Multi-domain]  Cd Length: 177  Bit Score: 37.54  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149936262   9 KTALFDFDGVVVDTEPIYDLFWNdaaKRYGLGIdnfadiikgtTLPYILEKYFSG-YTEEFRQMVTKESTEYEKTMPLPP 87
Cdd:COG4502    3 PRIAVDMDGVLADFYAAFLDIYN---KEYGTNL----------TLEDLDGWDLWElVPPEHRERIREFLNEPGFFRDLPP 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149936262  88 MPGSIEFIRMLKEHGvQIGLVTS------SDNAK---VKRAFGLLHLDNLFD----TLVTAD 136
Cdd:COG4502   70 IPGAQEVLKELSDKY-EVYIVTAamefpnSLEEKyewLDEHFPFIPWQNIIFcgdkSLVGGD 130
 
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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