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Conserved domains on  [gi|296011028|ref|NP_001171606|]
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pseudouridine-5'-phosphatase isoform c [Homo sapiens]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 8-167 1.03e-92

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


The actual alignment was detected with superfamily member cd07529:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 192  Bit Score: 269.22  E-value: 1.03e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   8 VTHLIFDMDGLLLDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTKLKEVFP 87
Cdd:cd07529    1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLEEEFDEQQEALAELFM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  88 -TAALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDPEV-QHGKPDPDIFLACAKRFSPP 165
Cdd:cd07529   81 gTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEVkGRGKPAPDIFLVAAKRFNEP 160


                 ..
gi 296011028 166 PA 167
Cdd:cd07529  161 PK 162
 
Name Accession Description Interval E-value
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 8-167 1.03e-92

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: 269.22  E-value: 1.03e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   8 VTHLIFDMDGLLLDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTKLKEVFP 87
Cdd:cd07529    1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLEEEFDEQQEALAELFM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  88 -TAALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDPEV-QHGKPDPDIFLACAKRFSPP 165
Cdd:cd07529   81 gTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEVkGRGKPAPDIFLVAAKRFNEP 160


                 ..
gi 296011028 166 PA 167
Cdd:cd07529  161 PK 162
PLN02811 PLN02811
hydrolase
 15-166 1.57e-67

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 206.15  E-value: 1.57e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  15 MDGLLLDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLP--MSKEELVEESQTKLKEVFPTAALM 92
Cdd:PLN02811   1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSdsLSPEDFLVEREAMLQDLFPTSDLM 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296011028  93 PGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDPEVQHGKPDPDIFLACAKRFSPPP 166
Cdd:PLN02811  81 PGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVTGDDPEVKQGKPAPDIFLAAARRFEDGP 154
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
11-167 1.99e-38

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 131.48  E-value: 1.99e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  11 LIFDMDGLLLDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTKLKEVFPT-- 88
Cdd:COG0637    5 VIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYRELLAEeg 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296011028  89 AALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHkEFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPA 167
Cdd:COG0637   85 LPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAA-GLLDYFDVIVTGDD--VARGKPDPDIYLLAAERLGVDPE 160
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 11-167 4.21e-22

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: 88.55  E-value: 4.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   11 LIFDMDGLLLDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTK---LKEVFP 87
Cdd:TIGR02009   4 VIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDGLSLEEIHQLAERKnelYRELLR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   88 T--AALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSrhkEFFSLFSHIVLGDdpEVQHGKPDPDIFLACAKRFSPP 165
Cdd:TIGR02009  84 LtgVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKL---GLRDYFDAIVDAS--EVKNGKPHPETFLLAAELLGVP 158


                  ..
gi 296011028  166 PA 167
Cdd:TIGR02009 159 PN 160
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
11-162 8.87e-18

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 77.24  E-value: 8.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   11 LIFDMDGLLLDTERLYSVVFQEICNRYD-KKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTKLKEVFPTa 89
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGyGELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFYLRKYNEELHDKLVK- 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296011028   90 aLMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKeFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRF 162
Cdd:pfam13419  80 -PYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLG-LEDYFDVIVGGDD--VEGKKPDPDPILKALEQL 148
 
Name Accession Description Interval E-value
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 8-167 1.03e-92

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: 269.22  E-value: 1.03e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   8 VTHLIFDMDGLLLDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTKLKEVFP 87
Cdd:cd07529    1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLEEEFDEQQEALAELFM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  88 -TAALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDPEV-QHGKPDPDIFLACAKRFSPP 165
Cdd:cd07529   81 gTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEVkGRGKPAPDIFLVAAKRFNEP 160


                 ..
gi 296011028 166 PA 167
Cdd:cd07529  161 PK 162
PLN02811 PLN02811
hydrolase
 15-166 1.57e-67

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 206.15  E-value: 1.57e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  15 MDGLLLDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLP--MSKEELVEESQTKLKEVFPTAALM 92
Cdd:PLN02811   1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSdsLSPEDFLVEREAMLQDLFPTSDLM 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296011028  93 PGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDPEVQHGKPDPDIFLACAKRFSPPP 166
Cdd:PLN02811  81 PGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVTGDDPEVKQGKPAPDIFLAAARRFEDGP 154
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
11-167 1.99e-38

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 131.48  E-value: 1.99e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  11 LIFDMDGLLLDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTKLKEVFPT-- 88
Cdd:COG0637    5 VIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYRELLAEeg 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296011028  89 AALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHkEFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPA 167
Cdd:COG0637   85 LPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAA-GLLDYFDVIVTGDD--VARGKPDPDIYLLAAERLGVDPE 160
PLN02940 PLN02940
riboflavin kinase
 1-167 2.50e-36

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 130.72  E-value: 2.50e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   1 MAAP---PQPVTHLIFDMDGLLLDTERLYSVVFQEICNRYDKKysWDVKSL--VMGKKALEAAQIIIDVLQLPMSKEELV 75
Cdd:PLN02940   1 MSAAkplKKLVSHVILDLDGTLLNTDGIVSDVLKAFLVKYGKQ--WDGREAqkIVGKTPLEAAATVVEDYGLPCSTDEFN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  76 EESQTKLKEVFPTAALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDdpEVQHGKPDPDIF 155
Cdd:PLN02940  79 SEITPLLSEQWCNIKALPGANRLIKHLKSHGVPMALASNSPRANIEAKISCHQGWKESFSVIVGGD--EVEKGKPSPDIF 156

                        170
                 ....*....|..
gi 296011028 156 LACAKRFSPPPA 167
Cdd:PLN02940 157 LEAAKRLNVEPS 168
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 11-167 2.70e-29

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: 106.16  E-value: 2.70e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  11 LIFDMDGLLLDTERLYSVVFQEIcNRYDKKYswdvkslvmgkkaleaaqiiidvlqlpmskEELVEESQTKLkevfptaa 90
Cdd:cd07505    2 VIFDMDGVLIDTEPLHRQAWQLL-ERKNALL------------------------------LELIASEGLKL-------- 42

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296011028  91 lMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPA 167
Cdd:cd07505   43 -KPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLRGYFDVIVSGDD--VERGKPAPDIYLLAAERLGVDPE 116
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 11-167 4.21e-22

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: 88.55  E-value: 4.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   11 LIFDMDGLLLDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTK---LKEVFP 87
Cdd:TIGR02009   4 VIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDGLSLEEIHQLAERKnelYRELLR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   88 T--AALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSrhkEFFSLFSHIVLGDdpEVQHGKPDPDIFLACAKRFSPP 165
Cdd:TIGR02009  84 LtgVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKL---GLRDYFDAIVDAS--EVKNGKPHPETFLLAAELLGVP 158


                  ..
gi 296011028  166 PA 167
Cdd:TIGR02009 159 PN 160
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 12-167 2.37e-19

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


Pssm-ID: 213672 [Multi-domain]  Cd Length: 185  Bit Score: 81.59  E-value: 2.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   12 IFDMDGLLLDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTK-------LKE 84
Cdd:TIGR01990   3 IFDLDGVITDTAEYHYLAWKHLADELGIPFDEEFNESLKGVSREESLERILDLGGKKYSEEEKEELAERKndyyvelLKE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   85 VFPTAALmPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLfshIVlgDDPEVQHGKPDPDIFLACAKRFSP 164
Cdd:TIGR01990  83 LTPADVL-PGIKSLLADLKKNNIKIALASASKNAPTILEKLELIDYFDA---IV--DPAELKKGKPDPEIFLAAAEGLGV 156


                  ...
gi 296011028  165 PPA 167
Cdd:TIGR01990 157 SPS 159
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
11-162 8.87e-18

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 77.24  E-value: 8.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   11 LIFDMDGLLLDTERLYSVVFQEICNRYD-KKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTKLKEVFPTa 89
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGyGELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFYLRKYNEELHDKLVK- 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296011028   90 aLMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKeFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRF 162
Cdd:pfam13419  80 -PYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLG-LEDYFDVIVGGDD--VEGKKPDPDPILKALEQL 148
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 10-167 1.18e-17

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: 76.69  E-value: 1.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   10 HLIFDMDGLLLDTERLYsvvFQEIcNRYDKKYS--WDVKSLVmgKKALEAAQIIIDVLQLPMSKE---ELVEESQTKLKE 84
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAI---AKLI-NREELGLVpdELGVSAV--GRLELALRRFKAQYGRTISPEdaqLLYKQLFYEQIE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   85 VFPTAALMPGAEKLIIHLRKHGIPFALATSsgSASFDMKTSRHKEFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSP 164
Cdd:TIGR01509  75 EEAKLKPLPGVRALLEALRARGKKLALLTN--SPRAHKLVLALLGLRDLFDVVIDSSD--VGLGKPDPDIYLQALKALGL 150


                  ...
gi 296011028  165 PPA 167
Cdd:TIGR01509 151 EPS 153
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 11-171 5.60e-17

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: 74.60  E-value: 5.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  11 LIFDMDGLLLDTERLYSVVFQEICNRYdkkyswdvkslvmgKKALEAAQIiidvlqlpmskeelveESQTKLKevfptaa 90
Cdd:cd16423    2 VIFDFDGVIVDTEPLWYEAWQELLNER--------------RNELIKRQF----------------SEKTDLP------- 44

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  91 LMPGAEKLIIHLRKHGIPFALATSSgSASFDMKTSRHKEFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPP---- 166
Cdd:cd16423   45 PIEGVKELLEFLKEKGIKLAVASSS-PRRWIEPHLERLGLLDYFEVIVTGDD--VEKSKPDPDLYLEAAERLGVNPeecv 121


                 ....*
gi 296011028 167 AMEKS 171
Cdd:cd16423  122 VIEDS 126
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
8-167 1.00e-16

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 74.97  E-value: 1.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   8 VTHLIFDMDGLLLDTERLYSVVFQEICNRYDKKY--SWDVKSLVmGKKALEAAQIIidvlqLPMSKEELVEESQTKLKEV 85
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPldLEELRALI-GLGLRELLRRL-----LGEDPDEELEELLARFREL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  86 F-----PTAALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHkEFFSLFSHIVLGDDpeVQHGKPDPDIFLACAK 160
Cdd:COG0546   75 YeeellDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEAL-GLDDYFDAIVGGDD--VPPAKPKPEPLLEALE 151


                 ....*..
gi 296011028 161 RFSPPPA 167
Cdd:COG0546  152 RLGLDPE 158
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
11-167 2.00e-16

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 73.96  E-value: 2.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  11 LIFDMDGLLLDTERLYSVVFQEICNRYDKKYswDVKSLVM--GKKALEAAQIIIDVLQLPMSKEELVEESQTKLKEVfpt 88
Cdd:PRK10725   8 LIFDMDGTILDTEPTHRKAWREVLGRYGLQF--DEQAMVAlnGSPTWRIAQAIIELNQADLDPHALAREKTEAVKSM--- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  89 aaLMPGAEKL-IIHLRK--HG-IPFALATSSGSASFDMkTSRHKEFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSP 164
Cdd:PRK10725  83 --LLDSVEPLpLIEVVKawHGrRPMAVGTGSESAIAEA-LLAHLGLRRYFDAVVAADD--VQHHKPAPDTFLRCAQLMGV 157


                 ...
gi 296011028 165 PPA 167
Cdd:PRK10725 158 QPT 160
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 8-167 4.05e-15

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: 70.31  E-value: 4.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028    8 VTHLIFDMDGLLLDTERLYSVVFQEICNRYD---------KKYSWDVKS----LVMGKKALEAAQIIIDVLQLPMSKEEL 74
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPlakaivaaaEDLPIPVEDftarLLLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   75 VEESQTKL--KEVFPTAALMPGAEKLIIHLRKHGIPFALATsSGSASFDMKTSRHKEFFSLFSHIVLGDDpeVQHGKPDP 152
Cdd:pfam00702  81 TVVLVELLgvIALADELKLYPGAAEALKALKERGIKVAILT-GDNPEAAEALLRLLGLDDYFDVVISGDD--VGVGKPKP 157

                         170
                  ....*....|....*
gi 296011028  153 DIFLACAKRFSPPPA 167
Cdd:pfam00702 158 EIYLAALERLGVKPE 172
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 11-173 3.51e-11

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: 59.70  E-value: 3.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  11 LIFDMDGLLLDTERLYSVVFQEICNR-YDKKYSWDVK------SLVMGKKALEAAQIIIDV-LQLPMSKEELVEESQ--- 79
Cdd:cd07528    2 LIFDVDGTLAETEELHRRAFNNAFFAeRGLDWYWDRElygellRVGGGKERIAAYFEKVGWpESAPKDLKELIADLHkak 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  80 TKLKEVFPTA---ALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRH--KEFFSLFSHIVLGDDpeVQHGKPDPDI 154
Cdd:cd07528   82 TERYAELIAAgllPLRPGVARLIDEAKAAGVRLAIATTTSPANVDALLSALlgPERRAIFDAIAAGDD--VAEKKPDPDI 159

                        170       180
                 ....*....|....*....|...
gi 296011028 155 FLACAKRFSPPP----AMEKSSI 173
Cdd:cd07528  160 YLLALERLGVSPsdclAIEDSAI 182
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 11-167 4.00e-11

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: 59.23  E-value: 4.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  11 LIFDMDGLLLDTERLYSvvfqeicnrydkkyswdvkslvmgkkalEAAQIIIDVLQLPMSKEELVEESQTKLkevfPTAA 90
Cdd:cd02598    2 VIFDLDGVITDTAEYHY----------------------------RAWKKLADKEELAARKNRIYVELIEEL----TPVD 49

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296011028  91 LMPGAEKLIIHLRKHGIPFALATSSGSASfdmKTSRHKEFFSLFSHIVlgDDPEVQHGKPDPDIFLACAKRFSPPPA 167
Cdd:cd02598   50 VLPGIASLLVDLKAKGIKIALASASKNAP---KILEKLGLAEYFDAIV--DGAVLAKGKPDPDIFLAAAEGLGLNPK 121
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 11-167 4.03e-11

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: 59.66  E-value: 4.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  11 LIFDMDGLLLDTERLYSVVFQEICNRYDKKYSwDVKSLVMGKKALEAAQIiidvLQLPMSKEELVEESQTKLKEVFPTAA 90
Cdd:cd07527    2 LLFDMDGTLVDSTPAVERAWHKWAKEHGVDPE-EVLKVSHGRRAIDVIRK----LAPDDADIELVLALETEEPESYPEGV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  91 -LMPGAEKLIIHLRKHGIPFALATssgSASFDMKTSRHkEFFSLF--SHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPA 167
Cdd:cd07527   77 iAIPGAVDLLASLPAAGDRWAIVT---SGTRALAEARL-EAAGLPhpEVLVTADD--VKNGKPDPEPYLLGAKLLGLDPS 150
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 10-166 1.67e-10

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: 57.41  E-value: 1.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   10 HLIFDMDGLLLDTERLYSVVFQEICNRYDkkysWDVKSLvmgkKALEAAQIIIDvlqlpmskEELVEESQTKLKEVFPTA 89
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFG----LDPASF----KALKQAGGLAE--------EEWYRIATSALEELQGRF 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   90 --------ALMPGAEKLIIHLRKHGIPFALAtSSGSASFDMKTSRHKEFFSLFSHIVLGDDPevqHGKPDPDIFLACAKR 161
Cdd:TIGR01549  65 wseydaeeAYIRGAADLLARLKSAGIKLGII-SNGSLRAQKLLLRLFGLGDYFELILVSDEP---GSKPEPEIFLAALES 140


                  ....*
gi 296011028  162 FSPPP 166
Cdd:TIGR01549 141 LGVPP 145
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 11-167 2.77e-09

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: 53.48  E-value: 2.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  11 LIFDMDGLLLDTERLysvvfqeicnrydkkyswdvkslvmgkkaleAAQIIIDVLQlpmskeELVEE-SQTKLKEVFPta 89
Cdd:cd07526    3 VIFDCDGVLVDSEVI-------------------------------AARVLVEVLA------ELGARvLAAFEAELQP-- 43

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  90 alMPGAEKLiihLRKHGIPFALATSSGSASFDMKTSRH--KEFFSlfSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPA 167
Cdd:cd07526   44 --IPGAAAA---LSALTLPFCVASNSSRERLTHSLGLAglLAYFE--GRIFSASD--VGRGKPAPDLFLHAAAQMGVAPE 114
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 8-162 1.18e-08

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: 53.11  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   8 VTHLIFDMDGLLLDTERLYSVVFQEIC-------------NRYDKKYSWDVKSLVMGKKAL-EAAQIIIDVLQLPMSkEE 73
Cdd:COG1011    1 IKAVLFDLDGTLLDFDPVIAEALRALAerlglldeaeelaEAYRAIEYALWRRYERGEITFaELLRRLLEELGLDLA-EE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  74 LVEESQTKLKEVFPtaaLMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHkEFFSLFSHIVLGDdpEVQHGKPDPD 153
Cdd:COG1011   80 LAEAFLAALPELVE---PYPDALELLEALKARGYRLALLTNGSAELQEAKLRRL-GLDDLFDAVVSSE--EVGVRKPDPE 153


                 ....*....
gi 296011028 154 IFLACAKRF 162
Cdd:COG1011  154 IFELALERL 162
PRK10826 PRK10826
hexitol phosphatase HxpB;
1-171 1.14e-07

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 50.33  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   1 MAAPPqPVTHLIFDMDGLLLDTERLYS-------------VVFQEICN-----RYD-------KKYSWDvkslvmGKKAL 55
Cdd:PRK10826   1 MSTPR-QILAAIFDMDGLLIDSEPLWDraeldvmaslgvdISRREELPdtlglRIDqvvdlwyARQPWN------GPSRQ 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  56 EAAQIIID-VLQLpmskeelVEESQTklkevfptaaLMPGAEKLIIHLRKHGIPFALATSSGS----ASFDMKTSRHKeF 130
Cdd:PRK10826  74 EVVQRIIArVISL-------IEETRP----------LLPGVREALALCKAQGLKIGLASASPLhmleAVLTMFDLRDY-F 135

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 296011028 131 FSLFSHIVLgddpevQHGKPDPDIFLACAKRFSPPP----AMEKS 171
Cdd:PRK10826 136 DALASAEKL------PYSKPHPEVYLNCAAKLGVDPltcvALEDS 174
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 8-162 6.27e-07

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: 47.72  E-value: 6.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   8 VTHLIFDMDGLLLDTERLYSV------VFQEICNRYDKKYSWDVKSLVM-GKK-ALEAAQIIIDVLQLPMSKEELVEESQ 79
Cdd:cd02603    1 IRAVLFDFGGVLIDPDPAAAVarfealTGEPSEFVLDTEGLAGAFLELErGRItEEEFWEELREELGRPLSAELFEELVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  80 TKLKevfptaaLMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDpeVQHGKPDPDIFLACA 159
Cdd:cd02603   81 AAVD-------PNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLPRRGDLFDGVVESCR--LGVRKPDPEIYQLAL 151


                 ...
gi 296011028 160 KRF 162
Cdd:cd02603  152 ERL 154
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 7-167 6.44e-07

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 49.08  E-value: 6.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028    7 PVTHLIFDMDGLLLDTE---RLYSV-VFQEIcnrydkKYSWDVKSLV--MGKKALEAAQIIIDVLQLP-----MSKEELV 75
Cdd:PLN02919   74 KVSAVLFDMDGVLCNSEepsRRAAVdVFAEM------GVEVTVEDFVpfMGTGEANFLGGVASVKGVKgfdpdAAKKRFF 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   76 EESQTKLKEvfPTAAL-MPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDPEvqHGKPDPDI 154
Cdd:PLN02919  148 EIYLEKYAK--PNSGIgFPGALELITQCKNKGLKVAVASSADRIKVDANLAAAGLPLSMFDAIVSADAFE--NLKPAPDI 223

                         170
                  ....*....|...
gi 296011028  155 FLACAKRFSPPPA 167
Cdd:PLN02919  224 FLAAAKILGVPTS 236
PRK11587 PRK11587
putative phosphatase; Provisional
 12-167 6.90e-07

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 48.07  E-value: 6.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  12 IFDMDGLLLDTerlYSVVFQEICN---RYDKKYSwDVKSLVMGKKAleaaqiiIDVLQ--LPMSKEELVEESQTKLKEVF 86
Cdd:PRK11587   7 LFDLDGTLVDS---LPAVERAWSNwadRHGIAPD-EVLNFIHGKQA-------ITSLRhfMAGASEAEIQAEFTRLEQIE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  87 PT----AALMPGAEKLIIHLRKHGIPFALATssgSASFDMKTSRHKEffslfshivlGDDPE---------VQHGKPDPD 153
Cdd:PRK11587  76 ATdtegITALPGAIALLNHLNKLGIPWAIVT---SGSVPVASARHKA----------AGLPApevfvtaerVKRGKPEPD 142

                        170
                 ....*....|....
gi 296011028 154 IFLACAKRFSPPPA 167
Cdd:PRK11587 143 AYLLGAQLLGLAPQ 156
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 11-167 7.90e-07

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 48.17  E-value: 7.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  11 LIFDMDGLLLDTER-LYSVVFQEICNRYD-KKYSWDV-------------------------KSLVMGK--KALEAAQII 61
Cdd:PLN02779  43 LLFDCDGVLVETERdGHRVAFNDAFKEFGlRPVEWDVelydellnigggkermtwyfnengwPTSTIEKapKDEEERKEL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  62 IDVLQLpMSKE---ELVEESQTKLKevfptaalmPGAEKLIIHLRKHGIPFALATSSGSASFDM--KTSRHKEFFSLFSh 136
Cdd:PLN02779 123 VDSLHD-RKTElfkELIESGALPLR---------PGVLRLMDEALAAGIKVAVCSTSNEKAVSKivNTLLGPERAQGLD- 191

                        170       180       190
                 ....*....|....*....|....*....|.
gi 296011028 137 IVLGDDpeVQHGKPDPDIFLACAKRFSPPPA 167
Cdd:PLN02779 192 VFAGDD--VPKKKPDPDIYNLAAETLGVDPS 220
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 61-166 8.19e-06

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 45.41  E-value: 8.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  61 IIDVLQLPMSKEELVEESQTKLKEvfptaaLMPGAEKLIIHLRKHGIPFALATSSGSASfdmkTSRHKEFFSL---FSHI 137
Cdd:PLN03243  86 FLQMKRLAIRKEDLYEYMQGGLYR------LRPGSREFVQALKKHEIPIAVASTRPRRY----LERAIEAVGMegfFSVV 155

                         90       100
                 ....*....|....*....|....*....
gi 296011028 138 VLGDDpeVQHGKPDPDIFLACAKRFSPPP 166
Cdd:PLN03243 156 LAAED--VYRGKPDPEMFMYAAERLGFIP 182
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 8-165 7.09e-05

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: 42.27  E-value: 7.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   8 VTHLIFDMDGLLLDTERLYSVVFQEICNRY--DKKYSWDVKSLVmGKKALEAAQIIidvlqLPMSKEELVEE-------S 78
Cdd:cd02616    1 ITTILFDLDGTLIDTNELIIKSFNHTLKEYglEGYTREEVLPFI-GPPLRETFEKI-----DPDKLEDMVEEfrkyyreH 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  79 QTKLKEVFptaalmPGAEKLIIHLRKHGIPFALATSsgSASFD-MKTSRHKEFFSLFSHIVLGDDpeVQHGKPDPD-IFL 156
Cdd:cd02616   75 NDDLTKEY------PGVYETLARLKSQGIKLGVVTT--KLRETaLKGLKLLGLDKYFDVIVGGDD--VTHHKPDPEpVLK 144


                 ....*....
gi 296011028 157 ACAKRFSPP 165
Cdd:cd02616  145 ALELLGAEP 153
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 11-158 6.42e-04

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: 39.30  E-value: 6.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  11 LIFDMDGLLLDTERLYSVVFQEICNRYDKKYS--WDVKSLVmGKKALEAAQIIidvlqLPMSKEELVEESQTKLKEVFPT 88
Cdd:cd07533    2 VIFDWDGTLADSQHNIVAAMTAAFADLGLPVPsaAEVRSII-GLSLDEAIARL-----LPMATPALVAVAERYKEAFDIL 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296011028  89 -------AALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHkEFFSLFSHIVLGDDpevQHGKPDPDIFLAC 158
Cdd:cd07533   76 rllpehaEPLFPGVREALDALAAQGVLLAVATGKSRRGLDRVLEQH-GLGGYFDATRTADD---TPSKPHPEMLREI 148
PRK13225 PRK13225
phosphoglycolate phosphatase; Provisional
 5-140 8.89e-04

phosphoglycolate phosphatase; Provisional


Pssm-ID: 106187 [Multi-domain]  Cd Length: 273  Bit Score: 39.31  E-value: 8.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   5 PQPVTHLIFDMDGLLLDTerLYSVVfqEICNRYDKKYSWD-VKSLVMGKKALEAAQIIIDVLQL-PMSKEELVEESQTKL 82
Cdd:PRK13225  59 PQTLQAIIFDFDGTLVDS--LPTVV--AIANAHAPDFGYDpIDERDYAQLRQWSSRTIVRRAGLsPWQQARLLQRVQRQL 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 296011028  83 KEVFPTAALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRhKEFFSLFSHIVLG 140
Cdd:PRK13225 135 GDCLPALQLFPGVADLLAQLRSRSLCLGILSSNSRQNIEAFLQR-QGLRSLFSVVQAG 191
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 91-162 1.13e-03

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


Pssm-ID: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 37.14  E-value: 1.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296011028  91 LMPGAEKLIIHLRKhGIPFALATSsGSAsfdmKTSRHK----EFFSLFSHIVLGDdpEVQHGKPDPDIFLACAKRF 162
Cdd:cd04305   10 LLPGAKELLEELKK-GYKLGIITN-GPT----EVQWEKleqlGIHKYFDHIVISE--EVGVQKPNPEIFDYALNQL 77
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 11-137 2.57e-03

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


Pssm-ID: 319799 [Multi-domain]  Cd Length: 201  Bit Score: 37.34  E-value: 2.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028  11 LIFDMDGLLLDTERLysvvFQEICNRYDKKYSWDVKSL--VMGKKALEAAQII----IDVLQLPMskeeLVEESQTKLKE 84
Cdd:cd04303    2 IIFDFDGTLADSFPW----FLSILNQLAARHGFKTVDEeeIEQLRQLSSREILkqlgVPLWKLPL----IAKDFRRLMAE 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 296011028  85 VFPTAALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRhKEFFSLFSHI 137
Cdd:cd04303   74 AAPELALFPGVEDMLRALHARGVRLAVVSSNSEENIRRVLGP-EELISLFAVI 125
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 12-120 8.49e-03

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: 35.79  E-value: 8.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011028   12 IFDMDGLLLDTERLYSVVFQEIcnrydkKYSWDVKSL---VMGKKALEAAQIIIDVLQLPMS-KEELVEEsqtklkEVFP 87
Cdd:TIGR01488   3 IFDFDGTLTRQDSLIDLLAKLL------GTNDEVIELtrlAPSGRISFEDALGRRLALLHRSrSEEVAKE------FLAR 70

                          90       100       110
                  ....*....|....*....|....*....|...
gi 296011028   88 TAALMPGAEKLIIHLRKHGIPFALAtsSGSASF 120
Cdd:TIGR01488  71 QVALRPGARELISWLKERGIDTVIV--SGGFDF 101
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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