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Conserved domains on  [gi|1622970827|ref|XP_028698083|]
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pseudouridine-5'-phosphatase isoform X3 [Macaca mulatta]

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 ...
 9-168 5.27e-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: 267.29  E-value: 5.27e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827   9 VTHLIFDMDGLLLDTERLYSVVFQEICDRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTKLKEMFP 88
Cdd:cd07529     1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLEEEFDEQQEALAELFM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  89 -TAALMPGAEKLIVHLRKHGIPFALATSSGSVSFEMKTSRHKEFFSLFSHIVLGDDPEV-QHGKPDPDIFLACAKRFSPP 166
Cdd:cd07529    81 gTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEVkGRGKPAPDIFLVAAKRFNEP 160


                  ..
gi 1622970827 167 PA 168
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 ...
 9-168 5.27e-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: 267.29  E-value: 5.27e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827   9 VTHLIFDMDGLLLDTERLYSVVFQEICDRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTKLKEMFP 88
Cdd:cd07529     1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLEEEFDEQQEALAELFM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  89 -TAALMPGAEKLIVHLRKHGIPFALATSSGSVSFEMKTSRHKEFFSLFSHIVLGDDPEV-QHGKPDPDIFLACAKRFSPP 166
Cdd:cd07529    81 gTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEVkGRGKPAPDIFLVAAKRFNEP 160


                  ..
gi 1622970827 167 PA 168
Cdd:cd07529   161 PK 162
PLN02811 PLN02811
hydrolase
 16-167 1.06e-67

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 206.53  E-value: 1.06e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  16 MDGLLLDTERLYSVVFQEICDRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLP--MSKEELVEESQTKLKEMFPTAALM 93
Cdd:PLN02811    1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSdsLSPEDFLVEREAMLQDLFPTSDLM 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622970827  94 PGAEKLIVHLRKHGIPFALATSSGSVSFEMKTSRHKEFFSLFSHIVLGDDPEVQHGKPDPDIFLACAKRFSPPP 167
Cdd:PLN02811   81 PGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVTGDDPEVKQGKPAPDIFLAAARRFEDGP 154
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
12-168 4.78e-39

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 133.03  E-value: 4.78e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  12 LIFDMDGLLLDTERLYSVVFQEICDRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTKLKEMFPT-- 89
Cdd:COG0637     5 VIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYRELLAEeg 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622970827  90 AALMPGAEKLIVHLRKHGIPFALATSSGSVSFEMKTSRHkEFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPA 168
Cdd:COG0637    85 LPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAA-GLLDYFDVIVTGDD--VARGKPDPDIYLLAAERLGVDPE 160
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 12-168 1.42e-23

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: 92.41  E-value: 1.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  12 LIFDMDGLLLDTERLYSVVFQEICDRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTK---LKEMFP 88
Cdd:TIGR02009   4 VIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDGLSLEEIHQLAERKnelYRELLR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  89 T--AALMPGAEKLIVHLRKHGIPFALATSSGSVSFEMKTSrhkEFFSLFSHIVLGDdpEVQHGKPDPDIFLACAKRFSPP 166
Cdd:TIGR02009  84 LtgVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKL---GLRDYFDAIVDAS--EVKNGKPHPETFLLAAELLGVP 158


                  ..
gi 1622970827 167 PA 168
Cdd:TIGR02009 159 PN 160
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
12-163 2.42e-16

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 73.39  E-value: 2.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  12 LIFDMDGLLLDTERLYSVVFQEICDRYD-KKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTKLKEMFPTa 90
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGyGELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFYLRKYNEELHDKLVK- 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622970827  91 aLMPGAEKLIVHLRKHGIPFALATSSGSVSFEMKTSRHKeFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRF 163
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 ...
 9-168 5.27e-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: 267.29  E-value: 5.27e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827   9 VTHLIFDMDGLLLDTERLYSVVFQEICDRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTKLKEMFP 88
Cdd:cd07529     1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLEEEFDEQQEALAELFM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  89 -TAALMPGAEKLIVHLRKHGIPFALATSSGSVSFEMKTSRHKEFFSLFSHIVLGDDPEV-QHGKPDPDIFLACAKRFSPP 166
Cdd:cd07529    81 gTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEVkGRGKPAPDIFLVAAKRFNEP 160


                  ..
gi 1622970827 167 PA 168
Cdd:cd07529   161 PK 162
PLN02811 PLN02811
hydrolase
 16-167 1.06e-67

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 206.53  E-value: 1.06e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  16 MDGLLLDTERLYSVVFQEICDRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLP--MSKEELVEESQTKLKEMFPTAALM 93
Cdd:PLN02811    1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSdsLSPEDFLVEREAMLQDLFPTSDLM 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622970827  94 PGAEKLIVHLRKHGIPFALATSSGSVSFEMKTSRHKEFFSLFSHIVLGDDPEVQHGKPDPDIFLACAKRFSPPP 167
Cdd:PLN02811   81 PGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVTGDDPEVKQGKPAPDIFLAAARRFEDGP 154
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
12-168 4.78e-39

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 133.03  E-value: 4.78e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  12 LIFDMDGLLLDTERLYSVVFQEICDRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTKLKEMFPT-- 89
Cdd:COG0637     5 VIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYRELLAEeg 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622970827  90 AALMPGAEKLIVHLRKHGIPFALATSSGSVSFEMKTSRHkEFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPA 168
Cdd:COG0637    85 LPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAA-GLLDYFDVIVTGDD--VARGKPDPDIYLLAAERLGVDPE 160
PLN02940 PLN02940
riboflavin kinase
 1-168 5.28e-37

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 132.27  E-value: 5.28e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827   1 MAAPPP--QPVTHLIFDMDGLLLDTERLYSVVFQEICDRYDKKysWDVKSL--VMGKKALEAAQIIIDVLQLPMSKEELV 76
Cdd:PLN02940    1 MSAAKPlkKLVSHVILDLDGTLLNTDGIVSDVLKAFLVKYGKQ--WDGREAqkIVGKTPLEAAATVVEDYGLPCSTDEFN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  77 EESQTKLKEMFPTAALMPGAEKLIVHLRKHGIPFALATSSGSVSFEMKTSRHKEFFSLFSHIVLGDdpEVQHGKPDPDIF 156
Cdd:PLN02940   79 SEITPLLSEQWCNIKALPGANRLIKHLKSHGVPMALASNSPRANIEAKISCHQGWKESFSVIVGGD--EVEKGKPSPDIF 156

                         170
                  ....*....|..
gi 1622970827 157 LACAKRFSPPPA 168
Cdd:PLN02940  157 LEAAKRLNVEPS 168
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 12-168 2.07e-28

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: 103.85  E-value: 2.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  12 LIFDMDGLLLDTERLYSVVFQEIcDRYDKKYswdvkslvmgkkaleaaqiiidvlqlpmskEELVEESQTKLkemfptaa 91
Cdd:cd07505     2 VIFDMDGVLIDTEPLHRQAWQLL-ERKNALL------------------------------LELIASEGLKL-------- 42

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622970827  92 lMPGAEKLIVHLRKHGIPFALATSSGSVSFEMKTSRHKEFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPA 168
Cdd:cd07505    43 -KPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLRGYFDVIVSGDD--VERGKPAPDIYLLAAERLGVDPE 116
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 12-168 1.42e-23

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: 92.41  E-value: 1.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  12 LIFDMDGLLLDTERLYSVVFQEICDRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTK---LKEMFP 88
Cdd:TIGR02009   4 VIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDGLSLEEIHQLAERKnelYRELLR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  89 T--AALMPGAEKLIVHLRKHGIPFALATSSGSVSFEMKTSrhkEFFSLFSHIVLGDdpEVQHGKPDPDIFLACAKRFSPP 166
Cdd:TIGR02009  84 LtgVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKL---GLRDYFDAIVDAS--EVKNGKPHPETFLLAAELLGVP 158


                  ..
gi 1622970827 167 PA 168
Cdd:TIGR02009 159 PN 160
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 13-168 2.40e-20

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: 83.90  E-value: 2.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  13 IFDMDGLLLDTERLYSVVFQEICDRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTK-------LKE 85
Cdd:TIGR01990   3 IFDLDGVITDTAEYHYLAWKHLADELGIPFDEEFNESLKGVSREESLERILDLGGKKYSEEEKEELAERKndyyvelLKE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  86 MFPTAALmPGAEKLIVHLRKHGIPFALATSSGSVSFEMKTSRHKEFFSLfshIVlgDDPEVQHGKPDPDIFLACAKRFSP 165
Cdd:TIGR01990  83 LTPADVL-PGIKSLLADLKKNNIKIALASASKNAPTILEKLELIDYFDA---IV--DPAELKKGKPDPEIFLAAAEGLGV 156


                  ...
gi 1622970827 166 PPA 168
Cdd:TIGR01990 157 SPS 159
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
12-168 1.22e-17

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 77.04  E-value: 1.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  12 LIFDMDGLLLDTERLYSVVFQEICDRYDKKYswDVKSLVM--GKKALEAAQIIIDVLQLPMSKEELVEESQTKLKEM-FP 88
Cdd:PRK10725    8 LIFDMDGTILDTEPTHRKAWREVLGRYGLQF--DEQAMVAlnGSPTWRIAQAIIELNQADLDPHALAREKTEAVKSMlLD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  89 TAALMPGAEkliVHLRKHG-IPFALATSSGSVSFEMkTSRHKEFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPP 167
Cdd:PRK10725   86 SVEPLPLIE---VVKAWHGrRPMAVGTGSESAIAEA-LLAHLGLRRYFDAVVAADD--VQHHKPAPDTFLRCAQLMGVQP 159


                  .
gi 1622970827 168 A 168
Cdd:PRK10725  160 T 160
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 11-168 2.88e-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: 75.53  E-value: 2.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  11 HLIFDMDGLLLDTERLYsvvFQEIcDRYDKKYS--WDVKSLVmgKKALEAAQIIIDVLQLPMSKE---ELVEESQTKLKE 85
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAI---AKLI-NREELGLVpdELGVSAV--GRLELALRRFKAQYGRTISPEdaqLLYKQLFYEQIE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  86 MFPTAALMPGAEKLIVHLRKHGIPFALATSSGSVSFemKTSRHKEFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSP 165
Cdd:TIGR01509  75 EEAKLKPLPGVRALLEALRARGKKLALLTNSPRAHK--LVLALLGLRDLFDVVIDSSD--VGLGKPDPDIYLQALKALGL 150


                  ...
gi 1622970827 166 PPA 168
Cdd:TIGR01509 151 EPS 153
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
9-168 9.34e-17

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 74.97  E-value: 9.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827   9 VTHLIFDMDGLLLDTERLYSVVFQEICDRYDKKY--SWDVKSLVmGKKALEAAQIIidvlqLPMSKEELVEESQTKLKE- 85
Cdd:COG0546     1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPldLEELRALI-GLGLRELLRRL-----LGEDPDEELEELLARFREl 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  86 ----MFPTAALMPGAEKLIVHLRKHGIPFALATSSGSVSFEMKTSRHkEFFSLFSHIVLGDDpeVQHGKPDPDIFLACAK 161
Cdd:COG0546    75 yeeeLLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEAL-GLDDYFDAIVGGDD--VPPAKPKPEPLLEALE 151


                  ....*..
gi 1622970827 162 RFSPPPA 168
Cdd:COG0546   152 RLGLDPE 158
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 12-172 1.30e-16

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: 73.83  E-value: 1.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  12 LIFDMDGLLLDTERLYSVVFQEICdrydKKYSWDVKslvmgkkaleaaqiiidvlqlpmsKEELVEESQTKLKemfptaa 91
Cdd:cd16423     2 VIFDFDGVIVDTEPLWYEAWQELL----NERRNELI------------------------KRQFSEKTDLPPI------- 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  92 lmPGAEKLIVHLRKHGIPFALATSSGSVSFEMKTSRHKeFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPP---- 167
Cdd:cd16423    47 --EGVKELLEFLKEKGIKLAVASSSPRRWIEPHLERLG-LLDYFEVIVTGDD--VEKSKPDPDLYLEAAERLGVNPeecv 121


                  ....*
gi 1622970827 168 AMEKS 172
Cdd:cd16423   122 VIEDS 126
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
12-163 2.42e-16

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 73.39  E-value: 2.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  12 LIFDMDGLLLDTERLYSVVFQEICDRYD-KKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSKEELVEESQTKLKEMFPTa 90
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGyGELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFYLRKYNEELHDKLVK- 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622970827  91 aLMPGAEKLIVHLRKHGIPFALATSSGSVSFEMKTSRHKeFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRF 163
Cdd:pfam13419  80 -PYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLG-LEDYFDVIVGGDD--VEGKKPDPDPILKALEQL 148
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 9-168 1.31e-14

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: 68.77  E-value: 1.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827   9 VTHLIFDMDGLLLDTERLYSVVFQEICDRYD---------KKYSWDVKS----LVMGKKALEAAQIIIDVLqLPMSKEEL 75
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPlakaivaaaEDLPIPVEDftarLLLGKRDWLEELDILRGL-VETLEAEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  76 VEESQTKLKEMFP---TAALMPGAEKLIVHLRKHGIPFALATsSGSVSFEMKTSRHKEFFSLFSHIVLGDDpeVQHGKPD 152
Cdd:pfam00702  80 LTVVLVELLGVIAladELKLYPGAAEALKALKERGIKVAILT-GDNPEAAEALLRLLGLDDYFDVVISGDD--VGVGKPK 156

                         170
                  ....*....|....*.
gi 1622970827 153 PDIFLACAKRFSPPPA 168
Cdd:pfam00702 157 PEIYLAALERLGVKPE 172
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 11-167 3.68e-12

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: 61.64  E-value: 3.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  11 HLIFDMDGLLLDTERLYSVVFQEICDRYDkkysWDVKSLvmgkKALEAAQIIIDvlqlpmskEELVEESQTKLKEMFPTA 90
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFG----LDPASF----KALKQAGGLAE--------EEWYRIATSALEELQGRF 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  91 --------ALMPGAEKLIVHLRKHGIPFALAtSSGSVSFEMKTSRHKEFFSLFSHIVLGDDPevqHGKPDPDIFLACAKR 162
Cdd:TIGR01549  65 wseydaeeAYIRGAADLLARLKSAGIKLGII-SNGSLRAQKLLLRLFGLGDYFELILVSDEP---GSKPEPEIFLAALES 140


                  ....*
gi 1622970827 163 FSPPP 167
Cdd:TIGR01549 141 LGVPP 145
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 12-168 5.28e-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: 59.28  E-value: 5.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  12 LIFDMDGLLLDTERLYSVVFQEICDRYDKKYSwDVKSLVMGKKALEAAQIiidvLQLPMSKEELVEESQTKLKEMFPTAA 91
Cdd:cd07527     2 LLFDMDGTLVDSTPAVERAWHKWAKEHGVDPE-EVLKVSHGRRAIDVIRK----LAPDDADIELVLALETEEPESYPEGV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  92 -LMPGAEKLIVHLRKHGIPFALATSSgsvSFEMKTSRHkEFFSLF--SHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPA 168
Cdd:cd07527    77 iAIPGAVDLLASLPAAGDRWAIVTSG---TRALAEARL-EAAGLPhpEVLVTADD--VKNGKPDPEPYLLGAKLLGLDPS 150
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 12-168 1.22e-10

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: 57.69  E-value: 1.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  12 LIFDMDGLLLDTERLYSVVFQEICDrydkkyswdvkslvmgkkaleaaqiiidvlqlpmsKEELVEESQTKLKEMF---P 88
Cdd:cd02598     2 VIFDLDGVITDTAEYHYRAWKKLAD-----------------------------------KEELAARKNRIYVELIeelT 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  89 TAALMPGAEKLIVHLRKHGIPFALATSSGSVSfemKTSRHKEFFSLFSHIVlgDDPEVQHGKPDPDIFLACAKRFSPPPA 168
Cdd:cd02598    47 PVDVLPGIASLLVDLKAKGIKIALASASKNAP---KILEKLGLAEYFDAIV--DGAVLAKGKPDPDIFLAAAEGLGLNPK 121
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 12-174 2.42e-10

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: 57.39  E-value: 2.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  12 LIFDMDGLLLDTERLYSVVFQEICDR-YDKKYSWDVK------SLVMGKKALEAAQIIIDV-LQLPMSKEELVEE----S 79
Cdd:cd07528     2 LIFDVDGTLAETEELHRRAFNNAFFAeRGLDWYWDRElygellRVGGGKERIAAYFEKVGWpESAPKDLKELIADlhkaK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  80 QTKLKEMFPTAA--LMPGAEKLIVHLRKHGIPFALATSS--GSVSFEMKTSRHKEFFSLFSHIVLGDDpeVQHGKPDPDI 155
Cdd:cd07528    82 TERYAELIAAGLlpLRPGVARLIDEAKAAGVRLAIATTTspANVDALLSALLGPERRAIFDAIAAGDD--VAEKKPDPDI 159

                         170       180
                  ....*....|....*....|...
gi 1622970827 156 FLACAKRFSPPP----AMEKSSI 174
Cdd:cd07528   160 YLLALERLGVSPsdclAIEDSAI 182
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 9-163 3.92e-09

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: 54.26  E-value: 3.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827   9 VTHLIFDMDGLLLDTERLYSVVFQEIC-------------DRYDKKYSWDVKSLVMGKKAL-EAAQIIIDVLQLPMSkEE 74
Cdd:COG1011     1 IKAVLFDLDGTLLDFDPVIAEALRALAerlglldeaeelaEAYRAIEYALWRRYERGEITFaELLRRLLEELGLDLA-EE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  75 LVEESQTKLKEMFPtaaLMPGAEKLIVHLRKHGIPFALATSSGSVSFEMKTSRHkEFFSLFSHIVLGDdpEVQHGKPDPD 154
Cdd:COG1011    80 LAEAFLAALPELVE---PYPDALELLEALKARGYRLALLTNGSAELQEAKLRRL-GLDDLFDAVVSSE--EVGVRKPDPE 153


                  ....*....
gi 1622970827 155 IFLACAKRF 163
Cdd:COG1011   154 IFELALERL 162
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 12-168 6.25e-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: 52.32  E-value: 6.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  12 LIFDMDGLLLDTERLysvvfqeicdrydkkyswdvkslvmgkkaleAAQIIIDVLQlpmskeELVEE-SQTKLKEMFPta 90
Cdd:cd07526     3 VIFDCDGVLVDSEVI-------------------------------AARVLVEVLA------ELGARvLAAFEAELQP-- 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  91 alMPGAEKLivhLRKHGIPFALATSSGSVSFEMKTSRH--KEFFSlfSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPA 168
Cdd:cd07526    44 --IPGAAAA---LSALTLPFCVASNSSRERLTHSLGLAglLAYFE--GRIFSASD--VGRGKPAPDLFLHAAAQMGVAPE 114
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 12-168 9.47e-08

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 50.86  E-value: 9.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  12 LIFDMDGLLLDTER-LYSVVFQEICDRYD-KKYSWDVKslvmgkkaleaaqiIIDVLQ-----------------LPMSK 72
Cdd:PLN02779   43 LLFDCDGVLVETERdGHRVAFNDAFKEFGlRPVEWDVE--------------LYDELLnigggkermtwyfnengWPTST 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  73 EELV---EESQTKL------------KEMFPTAA--LMPGAEKLIVHLRKHGIPFALATSSG--SVSFEMKTSRHKEFFS 133
Cdd:PLN02779  109 IEKApkdEEERKELvdslhdrktelfKELIESGAlpLRPGVLRLMDEALAAGIKVAVCSTSNekAVSKIVNTLLGPERAQ 188

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622970827 134 LFShIVLGDDpeVQHGKPDPDIFLACAKRFSPPPA 168
Cdd:PLN02779  189 GLD-VFAGDD--VPKKKPDPDIYNLAAETLGVDPS 220
PRK11587 PRK11587
putative phosphatase; Provisional
 13-168 9.77e-08

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 50.38  E-value: 9.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  13 IFDMDGLLLDT----ERLYSvvfqEICDRYDKKYSwDVKSLVMGKKAleaaqiiIDVLQ--LPMSKEELVEESQTKLKEM 86
Cdd:PRK11587    7 LFDLDGTLVDSlpavERAWS----NWADRHGIAPD-EVLNFIHGKQA-------ITSLRhfMAGASEAEIQAEFTRLEQI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  87 FPT----AALMPGAEKLIVHLRKHGIPFALATsSGSVSfeMKTSRHKEffslfshivlGDDPE---------VQHGKPDP 153
Cdd:PRK11587   75 EATdtegITALPGAIALLNHLNKLGIPWAIVT-SGSVP--VASARHKA----------AGLPApevfvtaerVKRGKPEP 141

                         170
                  ....*....|....*
gi 1622970827 154 DIFLACAKRFSPPPA 168
Cdd:PRK11587  142 DAYLLGAQLLGLAPQ 156
PRK10826 PRK10826
hexitol phosphatase HxpB;
1-172 7.36e-07

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 48.02  E-value: 7.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827   1 MAAPPPqpVTHLIFDMDGLLLDTERLY-------------SVVFQEICD-----RYD-------KKYSWDvkslvmGKKA 55
Cdd:PRK10826    1 MSTPRQ--ILAAIFDMDGLLIDSEPLWdraeldvmaslgvDISRREELPdtlglRIDqvvdlwyARQPWN------GPSR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  56 LEAAQIIID-VLQLpmskeelVEESQTklkemfptaaLMPGAEKLIVHLRKHGIPFALATSSGSVSFE----MKTSRHKe 130
Cdd:PRK10826   73 QEVVQRIIArVISL-------IEETRP----------LLPGVREALALCKAQGLKIGLASASPLHMLEavltMFDLRDY- 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1622970827 131 FFSLFSHIVLgddpevQHGKPDPDIFLACAKRFSPPP----AMEKS 172
Cdd:PRK10826  135 FDALASAEKL------PYSKPHPEVYLNCAAKLGVDPltcvALEDS 174
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 9-163 7.73e-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: 7.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827   9 VTHLIFDMDGLLLDTERLYSV------VFQEICDRYDKKYSWDVKSLVM-GKK-ALEAAQIIIDVLQLPMSKEELVEesq 80
Cdd:cd02603     1 IRAVLFDFGGVLIDPDPAAAVarfealTGEPSEFVLDTEGLAGAFLELErGRItEEEFWEELREELGRPLSAELFEE--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  81 tkLKEMFPTaaLMPGAEKLIVHLRKHGIPFALATSSGSVSFEMKTSRHKEFFSLFSHIVLGDDpeVQHGKPDPDIFLACA 160
Cdd:cd02603    78 --LVLAAVD--PNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLPRRGDLFDGVVESCR--LGVRKPDPEIYQLAL 151


                  ...
gi 1622970827 161 KRF 163
Cdd:cd02603   152 ERL 154
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 8-168 8.46e-07

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 48.69  E-value: 8.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827    8 PVTHLIFDMDGLLLDTE---RLYSV-VFQEIcdrydkKYSWDVKSLV--MGKKALEAAQIIIDVLQLP-----MSKEELV 76
Cdd:PLN02919    74 KVSAVLFDMDGVLCNSEepsRRAAVdVFAEM------GVEVTVEDFVpfMGTGEANFLGGVASVKGVKgfdpdAAKKRFF 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827   77 EESQTKLKEmfPTAAL-MPGAEKLIVHLRKHGIPFALATSSGSVSFEMKTSRHKEFFSLFSHIVLGDDPEvqHGKPDPDI 155
Cdd:PLN02919   148 EIYLEKYAK--PNSGIgFPGALELITQCKNKGLKVAVASSADRIKVDANLAAAGLPLSMFDAIVSADAFE--NLKPAPDI 223

                          170
                   ....*....|...
gi 1622970827  156 FLACAKRFSPPPA 168
Cdd:PLN02919   224 FLAAAKILGVPTS 236
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 62-167 6.87e-06

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 45.41  E-value: 6.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  62 IIDVLQLPMSKEELVEESQTKLKEmfptaaLMPGAEKLIVHLRKHGIPFALAtssgSVSFEMKTSRHKEFFSL---FSHI 138
Cdd:PLN03243   86 FLQMKRLAIRKEDLYEYMQGGLYR------LRPGSREFVQALKKHEIPIAVA----STRPRRYLERAIEAVGMegfFSVV 155

                          90       100
                  ....*....|....*....|....*....
gi 1622970827 139 VLGDDpeVQHGKPDPDIFLACAKRFSPPP 167
Cdd:PLN03243  156 LAAED--VYRGKPDPEMFMYAAERLGFIP 182
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 9-166 4.05e-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: 42.65  E-value: 4.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827   9 VTHLIFDMDGLLLDTERLYSVVFQEICDRY--DKKYSWDVKSLVmGKKALEAAQIIidvlqLPMSKEELVEESQTKLKEM 86
Cdd:cd02616     1 ITTILFDLDGTLIDTNELIIKSFNHTLKEYglEGYTREEVLPFI-GPPLRETFEKI-----DPDKLEDMVEEFRKYYREH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  87 FPT-AALMPGAEKLIVHLRKHGIPFALATSSgSVSFEMKTSRHKEFFSLFSHIVLGDDpeVQHGKPDPD-IFLACAKRFS 164
Cdd:cd02616    75 NDDlTKEYPGVYETLARLKSQGIKLGVVTTK-LRETALKGLKLLGLDKYFDVIVGGDD--VTHHKPDPEpVLKALELLGA 151


                  ..
gi 1622970827 165 PP 166
Cdd:cd02616   152 EP 153
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 12-159 1.24e-03

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: 38.53  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  12 LIFDMDGLLLDTERLYSVVFQEICDRYDKKYS--WDVKSLVmGKKALEAAQIIidvlqLPMSKEELVEESQTKLKEMFPT 89
Cdd:cd07533     2 VIFDWDGTLADSQHNIVAAMTAAFADLGLPVPsaAEVRSII-GLSLDEAIARL-----LPMATPALVAVAERYKEAFDIL 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622970827  90 -------AALMPGAEKLIVHLRKHGIPFALATSSGSVSFEMKTSRHkEFFSLFSHIVLGDD-PevqhGKPDPDIFLAC 159
Cdd:cd07533    76 rllpehaEPLFPGVREALDALAAQGVLLAVATGKSRRGLDRVLEQH-GLGGYFDATRTADDtP----SKPHPEMLREI 148
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 12-138 1.43e-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: 38.11  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  12 LIFDMDGLLLDTERLYSVVFQEICDRYdkkyswdvkslvmGKKALEAAQI----------IIDVLQLPMSKEELV-EESQ 80
Cdd:cd04303     2 IIFDFDGTLADSFPWFLSILNQLAARH-------------GFKTVDEEEIeqlrqlssreILKQLGVPLWKLPLIaKDFR 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622970827  81 TKLKEMFPTAALMPGAEKLIVHLRKHGIPFALATSSGSVSFEMKTSRhKEFFSLFSHI 138
Cdd:cd04303    69 RLMAEAAPELALFPGVEDMLRALHARGVRLAVVSSNSEENIRRVLGP-EELISLFAVI 125
PRK13225 PRK13225
phosphoglycolate phosphatase; Provisional
 6-141 1.54e-03

phosphoglycolate phosphatase; Provisional


Pssm-ID: 106187 [Multi-domain]  Cd Length: 273  Bit Score: 38.54  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827   6 PQPVTHLIFDMDGLLLDTerLYSVVfqEICDRYDKKYSWD-VKSLVMGKKALEAAQIIIDVLQL-PMSKEELVEESQTKL 83
Cdd:PRK13225   59 PQTLQAIIFDFDGTLVDS--LPTVV--AIANAHAPDFGYDpIDERDYAQLRQWSSRTIVRRAGLsPWQQARLLQRVQRQL 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622970827  84 KEMFPTAALMPGAEKLIVHLRKHGIPFALATSSGSVSFEMKTSRhKEFFSLFSHIVLG 141
Cdd:PRK13225  135 GDCLPALQLFPGVADLLAQLRSRSLCLGILSSNSRQNIEAFLQR-QGLRSLFSVVQAG 191
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 92-163 2.95e-03

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


Pssm-ID: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 35.98  E-value: 2.95e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622970827  92 LMPGAEKLIVHLRKhGIPFALATSsGSVSFEMKTSRHKEFFSLFSHIVLGDdpEVQHGKPDPDIFLACAKRF 163
Cdd:cd04305    10 LLPGAKELLEELKK-GYKLGIITN-GPTEVQWEKLEQLGIHKYFDHIVISE--EVGVQKPNPEIFDYALNQL 77
HAD pfam12710
haloacid dehalogenase-like hydrolase;
12-157 8.95e-03

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 35.59  E-value: 8.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970827  12 LIFDMDGLLLDTERLY----SVVFQEICDRYD--KKYSWDVKSLVMGKKALEAAQIIIDVLQLPMSkEELVEESQTKLKE 85
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFllirALLRRGGPDLWRalLVLLLLALLRLLGRLSRAGARELLRALLAGLP-EEDAAELERFVAE 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622970827  86 MFpTAALMPGAEKLIVHLRKHGIPFALATSSGSVSFEMKTSRHKeffslfSHIVLGDDPEVQHGKPDPDIFL 157
Cdd:pfam12710  80 VA-LPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELG------FDEVLATELEVDDGRFTGELRL 144
 
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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