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Conserved domains on  [gi|207113149|ref|NP_001129037|]
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pseudouridine-5'-phosphatase isoform a [Homo sapiens]

Protein Classification

HAD family hydrolase( domain architecture ID 11576397)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 8-219 1.57e-112

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: 321.22  E-value: 1.57e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149   8 VTHLIFDMDGLLLgytgsivaaasgessrglqsrwtDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDV 87
Cdd:cd07529    1 VTHCIFDMDGLLL-----------------------DTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDE 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  88 LQLPMSKEELVEESQTKLKEVFP-TAALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDP 166
Cdd:cd07529   58 LKLPMSLEEEFDEQQEALAELFMgTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDP 137

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 207113149 167 EV-QHGKPDPDIFLACAKRFSPPPA-MEKCLVFEDAPNGVEAALAAGMQVVMVPD 219
Cdd:cd07529  138 EVkGRGKPAPDIFLVAAKRFNEPPKdPSKCLVFEDSPNGVKAAKAAGMQVVMVPD 192
 
Name Accession Description Interval E-value
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 8-219 1.57e-112

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: 321.22  E-value: 1.57e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149   8 VTHLIFDMDGLLLgytgsivaaasgessrglqsrwtDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDV 87
Cdd:cd07529    1 VTHCIFDMDGLLL-----------------------DTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDE 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  88 LQLPMSKEELVEESQTKLKEVFP-TAALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDP 166
Cdd:cd07529   58 LKLPMSLEEEFDEQQEALAELFMgTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDP 137

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 207113149 167 EV-QHGKPDPDIFLACAKRFSPPPA-MEKCLVFEDAPNGVEAALAAGMQVVMVPD 219
Cdd:cd07529  138 EVkGRGKPAPDIFLVAAKRFNEPPKdPSKCLVFEDSPNGVKAAKAAGMQVVMVPD 192
PLN02811 PLN02811
hydrolase
 15-251 2.95e-96

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 280.88  E-value: 2.95e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  15 MDGLLLgytgsivaaasgessrglqsrwtDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLP--M 92
Cdd:PLN02811   1 MDGLLL-----------------------DTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSdsL 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  93 SKEELVEESQTKLKEVFPTAALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDPEVQHGK 172
Cdd:PLN02811  58 SPEDFLVEREAMLQDLFPTSDLMPGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVTGDDPEVKQGK 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149 173 PDPDIFLACAKRFS-PPPAMEKCLVFEDAPNGVEAALAAGMQVVMVPDGNLSRDLTTKATLVLNSLQDFQPELFGLPSYE 251
Cdd:PLN02811 138 PAPDIFLAAARRFEdGPVDPGKVLVFEDAPSGVEAAKNAGMSVVMVPDPRLDKSYCKGADQVLSSLLDFKPEEWGLPPFP 217
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
11-240 1.94e-55

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 176.55  E-value: 1.94e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  11 LIFDMDGLLlgytgsivaaasgessrglqsrwTDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQL 90
Cdd:COG0637    5 VIFDMDGTL-----------------------VDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGL 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  91 PMSKEELVEESQTKLKEVFPT--AALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHkEFFSLFSHIVLGDDpeV 168
Cdd:COG0637   62 DLPEEELAARKEELYRELLAEegLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAA-GLLDYFDVIVTGDD--V 138

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 207113149 169 QHGKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQVVMVPDGNLSRDLTTKATLVLNSLQDF 240
Cdd:COG0637  139 ARGKPDPDIYLLAAERLGVDP--EECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 11-217 3.71e-30

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: 110.90  E-value: 3.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149   11 LIFDMDGLLlgytgsivaaasgessrglqsrwTDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQL 90
Cdd:TIGR02009   4 VIFDMDGVI-----------------------TDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGD 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149   91 PMSKEELVEESQTK---LKEVFPT--AALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSrhkEFFSLFSHIVLGDd 165
Cdd:TIGR02009  61 GLSLEEIHQLAERKnelYRELLRLtgVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKL---GLRDYFDAIVDAS- 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 207113149  166 pEVQHGKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQVVMV 217
Cdd:TIGR02009 137 -EVKNGKPHPETFLLAAELLGVPP--NECIVFEDALAGVQAARAAGMFAVAV 185
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
11-217 7.11e-22

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 89.18  E-value: 7.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149   11 LIFDMDGLLLgytgsivaaasgessrglqsrwtDTERLYSVVFQEICNRYD-KKYSWDVKSLVMGKKALEAAQIIIDVLQ 89
Cdd:pfam13419   1 IIFDFDGTLL-----------------------DTEELIIKSFNYLLEEFGyGELSEEEILKFIGLPLREIFRYLGVSED 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149   90 LPMSKEELVEESQTKLKEVFPTaaLMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKeFFSLFSHIVLGDDpeVQ 169
Cdd:pfam13419  58 EEEKIEFYLRKYNEELHDKLVK--PYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLG-LEDYFDVIVGGDD--VE 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 207113149  170 HGKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQVVMV 217
Cdd:pfam13419 133 GKKPDPDPILKALEQLGLKP--EEVIYVGDSPRDIEAAKNAGIKVIAV 178
 
Name Accession Description Interval E-value
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 8-219 1.57e-112

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: 321.22  E-value: 1.57e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149   8 VTHLIFDMDGLLLgytgsivaaasgessrglqsrwtDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDV 87
Cdd:cd07529    1 VTHCIFDMDGLLL-----------------------DTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDE 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  88 LQLPMSKEELVEESQTKLKEVFP-TAALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDP 166
Cdd:cd07529   58 LKLPMSLEEEFDEQQEALAELFMgTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDP 137

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 207113149 167 EV-QHGKPDPDIFLACAKRFSPPPA-MEKCLVFEDAPNGVEAALAAGMQVVMVPD 219
Cdd:cd07529  138 EVkGRGKPAPDIFLVAAKRFNEPPKdPSKCLVFEDSPNGVKAAKAAGMQVVMVPD 192
PLN02811 PLN02811
hydrolase
 15-251 2.95e-96

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 280.88  E-value: 2.95e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  15 MDGLLLgytgsivaaasgessrglqsrwtDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLP--M 92
Cdd:PLN02811   1 MDGLLL-----------------------DTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSdsL 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  93 SKEELVEESQTKLKEVFPTAALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDPEVQHGK 172
Cdd:PLN02811  58 SPEDFLVEREAMLQDLFPTSDLMPGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVTGDDPEVKQGK 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149 173 PDPDIFLACAKRFS-PPPAMEKCLVFEDAPNGVEAALAAGMQVVMVPDGNLSRDLTTKATLVLNSLQDFQPELFGLPSYE 251
Cdd:PLN02811 138 PAPDIFLAAARRFEdGPVDPGKVLVFEDAPSGVEAAKNAGMSVVMVPDPRLDKSYCKGADQVLSSLLDFKPEEWGLPPFP 217
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
11-240 1.94e-55

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 176.55  E-value: 1.94e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  11 LIFDMDGLLlgytgsivaaasgessrglqsrwTDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQL 90
Cdd:COG0637    5 VIFDMDGTL-----------------------VDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGL 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  91 PMSKEELVEESQTKLKEVFPT--AALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHkEFFSLFSHIVLGDDpeV 168
Cdd:COG0637   62 DLPEEELAARKEELYRELLAEegLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAA-GLLDYFDVIVTGDD--V 138

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 207113149 169 QHGKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQVVMVPDGNLSRDLTTKATLVLNSLQDF 240
Cdd:COG0637  139 ARGKPDPDIYLLAAERLGVDP--EECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
PLN02940 PLN02940
riboflavin kinase
 1-251 1.94e-52

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 174.25  E-value: 1.94e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149   1 MAAP---PQPVTHLIFDMDGLLLgytgsivaaasgessrglqsrwtDTERLYSVVFQEICNRYDKKysWDVKSL--VMGK 75
Cdd:PLN02940   1 MSAAkplKKLVSHVILDLDGTLL-----------------------NTDGIVSDVLKAFLVKYGKQ--WDGREAqkIVGK 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  76 KALEAAQIIIDVLQLPMSKEELVEESQTKLKEVFPTAALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFS 155
Cdd:PLN02940  56 TPLEAAATVVEDYGLPCSTDEFNSEITPLLSEQWCNIKALPGANRLIKHLKSHGVPMALASNSPRANIEAKISCHQGWKE 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149 156 LFSHIVLGDdpEVQHGKPDPDIFLACAKRFSPPPAmeKCLVFEDAPNGVEAALAAGMQVVMVPDGNLSRDLTTKATLVLN 235
Cdd:PLN02940 136 SFSVIVGGD--EVEKGKPSPDIFLEAAKRLNVEPS--NCLVIEDSLPGVMAGKAAGMEVIAVPSIPKQTHLYSSADEVIN 211

                        250
                 ....*....|....*.
gi 207113149 236 SLQDFQPELFGLPSYE 251
Cdd:PLN02940 212 SLLDLQPEKWGLPPFN 227
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 11-219 1.71e-41

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: 138.90  E-value: 1.71e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  11 LIFDMDGLLLgytgsivaaasgessrglqsrwtDTERLYSVVFQEIcNRYDKKYswdvkslvmgkkaleaaqiiidvlql 90
Cdd:cd07505    2 VIFDMDGVLI-----------------------DTEPLHRQAWQLL-ERKNALL-------------------------- 31

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  91 pmskEELVEESQTKLkevfptaalMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDpeVQH 170
Cdd:cd07505   32 ----LELIASEGLKL---------KPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLRGYFDVIVSGDD--VER 96

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 207113149 171 GKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQVVMVPD 219
Cdd:cd07505   97 GKPAPDIYLLAAERLGVDP--ERCLVFEDSLAGIEAAKAAGMTVVAVPD 143
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 11-217 3.71e-30

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: 110.90  E-value: 3.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149   11 LIFDMDGLLlgytgsivaaasgessrglqsrwTDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQL 90
Cdd:TIGR02009   4 VIFDMDGVI-----------------------TDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGD 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149   91 PMSKEELVEESQTK---LKEVFPT--AALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSrhkEFFSLFSHIVLGDd 165
Cdd:TIGR02009  61 GLSLEEIHQLAERKnelYRELLRLtgVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKL---GLRDYFDAIVDAS- 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 207113149  166 pEVQHGKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQVVMV 217
Cdd:TIGR02009 137 -EVKNGKPHPETFLLAAELLGVPP--NECIVFEDALAGVQAARAAGMFAVAV 185
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 10-217 9.62e-29

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: 107.12  E-value: 9.62e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149   10 HLIFDMDGLLLGYTGSIVAAASGESSRGLQsrwtDTERLYSVVFQEICNRYDKKYSWDVKSlvmgkkaleaaqiiidvlq 89
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAIAKLINREELGLVP----DELGVSAVGRLELALRRFKAQYGRTIS------------------- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149   90 lPMSKEELVEESQTKLKEVFPTAALMPGAEKLIIHLRKHGIPFALATSSgsASFDMKTSRHKEFFSLFSHIVLGDDpeVQ 169
Cdd:TIGR01509  58 -PEDAQLLYKQLFYEQIEEEAKLKPLPGVRALLEALRARGKKLALLTNS--PRAHKLVLALLGLRDLFDVVIDSSD--VG 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 207113149  170 HGKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQVVMV 217
Cdd:TIGR01509 133 LGKPDPDIYLQALKALGLEP--SECVFVDDSPAGIEAAKAAGMHTVGV 178
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 11-239 5.25e-28

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: 105.03  E-value: 5.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  11 LIFDMDGLLLgytgsivaaasgessrglqsrwtDTERLYSVVFQEICNRYdkkyswdvkslvmgKKALEAAQIiidvlql 90
Cdd:cd16423    2 VIFDFDGVIV-----------------------DTEPLWYEAWQELLNER--------------RNELIKRQF------- 37

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  91 pmskeelveESQTKLKevfptaaLMPGAEKLIIHLRKHGIPFALATSSgSASFDMKTSRHKEFFSLFSHIVLGDDpeVQH 170
Cdd:cd16423   38 ---------SEKTDLP-------PIEGVKELLEFLKEKGIKLAVASSS-PRRWIEPHLERLGLLDYFEVIVTGDD--VEK 98

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 207113149 171 GKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQVVMVPDGNLSRDLTTKATLVLNSLQD 239
Cdd:cd16423   99 SKPDPDLYLEAAERLGVNP--EECVVIEDSRNGVLAAKAAGMKCVGVPNPVTGSQDFSKADLVLSSFAE 165
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 12-217 6.01e-25

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: 97.38  E-value: 6.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149   12 IFDMDGLLlgytgsivaaasgessrglqsrwTDTERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQIIIDVLQLP 91
Cdd:TIGR01990   3 IFDLDGVI-----------------------TDTAEYHYLAWKHLADELGIPFDEEFNESLKGVSREESLERILDLGGKK 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149   92 MSKEELVEESQTK-------LKEVFPTAALmPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLfshIVlgD 164
Cdd:TIGR01990  60 YSEEEKEELAERKndyyvelLKELTPADVL-PGIKSLLADLKKNNIKIALASASKNAPTILEKLELIDYFDA---IV--D 133

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 207113149  165 DPEVQHGKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQVVMV 217
Cdd:TIGR01990 134 PAELKKGKPDPEIFLAAAEGLGVSP--SECIGIEDAQAGIEAIKAAGMFAVGV 184
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
11-217 2.81e-23

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 93.22  E-value: 2.81e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  11 LIFDMDGLLLgytgsivaaasgessrglqsrwtDTERLYSVVFQEICNRYDKKYswDVKSLVM--GKKALEAAQIIIDVL 88
Cdd:PRK10725   8 LIFDMDGTIL-----------------------DTEPTHRKAWREVLGRYGLQF--DEQAMVAlnGSPTWRIAQAIIELN 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  89 QLPMSKEELVEESQTKLKEVfptaaLMPGAEKL-IIHLRK--HG-IPFALATSSGSASFDMKTsRHKEFFSLFSHIVLGD 164
Cdd:PRK10725  63 QADLDPHALAREKTEAVKSM-----LLDSVEPLpLIEVVKawHGrRPMAVGTGSESAIAEALL-AHLGLRRYFDAVVAAD 136

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 207113149 165 DpeVQHGKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQVVMV 217
Cdd:PRK10725 137 D--VQHHKPAPDTFLRCAQLMGVQP--TQCVVFEDADFGIQAARAAGMDAVDV 185
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 11-239 5.33e-23

subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p); This subfamily includes Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). GPP1p and GPP2p are involved in glycerol biosynthesis, GPP1 is induced in response to both anaerobic and hyperosmotic stress, GPP2 is induced in response to hyperosmotic or oxidative stress, and during diauxic shift; overexpression of DOG1 or DOG2 confers 2-deoxyglucose resistance. These belong to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319829 [Multi-domain]  Cd Length: 205  Bit Score: 92.79  E-value: 5.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  11 LIFDMDGLLLGYTGSIVAAasgessrglqsrWTDTERLYSVVFQEicnrydkkyswdVKSLVMGKKALEAAQIiidvLQL 90
Cdd:cd07527    2 LLFDMDGTLVDSTPAVERA------------WHKWAKEHGVDPEE------------VLKVSHGRRAIDVIRK----LAP 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  91 PMSKEELVEESQTKLKEVFPTAA-LMPGAEKLIIHLRKHGIPFALATSsgsASFDMKTSRHkEFFSLF--SHIVLGDDpe 167
Cdd:cd07527   54 DDADIELVLALETEEPESYPEGViAIPGAVDLLASLPAAGDRWAIVTS---GTRALAEARL-EAAGLPhpEVLVTADD-- 127

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 207113149 168 VQHGKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQVVMVPDGNLSRDLTTK-ATLVLNSLQD 239
Cdd:cd07527  128 VKNGKPDPEPYLLGAKLLGLDP--SDCVVFEDAPAGIKAGKAAGARVVAVNTSHDLEQLEAAgADLVVEDLSD 198
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
11-217 7.11e-22

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 89.18  E-value: 7.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149   11 LIFDMDGLLLgytgsivaaasgessrglqsrwtDTERLYSVVFQEICNRYD-KKYSWDVKSLVMGKKALEAAQIIIDVLQ 89
Cdd:pfam13419   1 IIFDFDGTLL-----------------------DTEELIIKSFNYLLEEFGyGELSEEEILKFIGLPLREIFRYLGVSED 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149   90 LPMSKEELVEESQTKLKEVFPTaaLMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKeFFSLFSHIVLGDDpeVQ 169
Cdd:pfam13419  58 EEEKIEFYLRKYNEELHDKLVK--PYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLG-LEDYFDVIVGGDD--VE 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 207113149  170 HGKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQVVMV 217
Cdd:pfam13419 133 GKKPDPDPILKALEQLGLKP--EEVIYVGDSPRDIEAAKNAGIKVIAV 178
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
8-240 1.07e-21

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 89.60  E-value: 1.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149   8 VTHLIFDMDGLLLgytgsivaaasgessrglqsrwtDTERLYSVVFQEICNRYDKKY--SWDVKSLVmGKKALEAAQIIi 85
Cdd:COG0546    1 IKLVLFDLDGTLV-----------------------DSAPDIAAALNEALAELGLPPldLEELRALI-GLGLRELLRRL- 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  86 dvlqLPMSKEELVEESQTKLKEVF-----PTAALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHkEFFSLFSHI 160
Cdd:COG0546   56 ----LGEDPDEELEELLARFRELYeeellDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEAL-GLDDYFDAI 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149 161 VLGDDpeVQHGKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQVVMVPDGNLSRD--LTTKATLVLNSLQ 238
Cdd:COG0546  131 VGGDD--VPPAKPKPEPLLEALERLGLDP--EEVLMVGDSPHDIEAARAAGVPFIGVTWGYGSAEelEAAGADYVIDSLA 206


                 ..
gi 207113149 239 DF 240
Cdd:COG0546  207 EL 208
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 94-240 3.68e-20

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: 84.27  E-value: 3.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  94 KEELVEESQTKLKEVF---PTAALMPGAEKLIIHLRKHGIPFALATSSGSASfdmKTSRHKEFFSLFSHIVlgDDPEVQH 170
Cdd:cd02598   27 KEELAARKNRIYVELIeelTPVDVLPGIASLLVDLKAKGIKIALASASKNAP---KILEKLGLAEYFDAIV--DGAVLAK 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149 171 GKPDPDIFLACAKRFSPPPAmeKCLVFEDAPNGVEAALAAGMQVVMVPDGNlsrDLTTKATLVLNSLQDF 240
Cdd:cd02598  102 GKPDPDIFLAAAEGLGLNPK--DCIGVEDAQAGIRAIKAAGFLVVGVGREE---DLLGADIVVPDTTADL 166
PRK11587 PRK11587
putative phosphatase; Provisional
 115-241 2.19e-19

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 83.51  E-value: 2.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149 115 MPGAEKLIIHLRKHGIPFALATSsgsASFDMKTSRHKEffslfshivlGDDPE---------VQHGKPDPDIFLACAKRF 185
Cdd:PRK11587  85 LPGAIALLNHLNKLGIPWAIVTS---GSVPVASARHKA----------AGLPApevfvtaerVKRGKPEPDAYLLGAQLL 151

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 207113149 186 SPPPamEKCLVFEDAPNGVEAALAAGMQVVMV--PDGNLSRDlttKATLVLNSLQDFQ 241
Cdd:PRK11587 152 GLAP--QECVVVEDAPAGVLSGLAAGCHVIAVnaPADTPRLD---EVDLVLHSLEQLT 204
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 80-214 7.18e-19

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: 80.06  E-value: 7.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  80 AAQIIIDVLQlpmskeELVEE-SQTKLKEVFPtaalMPGAEKLiihLRKHGIPFALATSSGSASFDMKTSRH--KEFFSl 156
Cdd:cd07526   18 AARVLVEVLA------ELGARvLAAFEAELQP----IPGAAAA---LSALTLPFCVASNSSRERLTHSLGLAglLAYFE- 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 207113149 157 fSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQV 214
Cdd:cd07526   84 -GRIFSASD--VGRGKPAPDLFLHAAAQMGVAP--ERCLVIEDSPTGVRAALAAGMTV 136
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 8-211 3.57e-18

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


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 79.55  E-value: 3.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149    8 VTHLIFDMDGLLL----GYTGSIVAAASgessrglqsrwtdtERLYSVVFQEICNRYDKKYSWDVKSLVMGKKALEAAQI 83
Cdd:pfam00702   1 IKAVVFDLDGTLTdgepVVTEAIAELAS--------------EHPLAKAIVAAAEDLPIPVEDFTARLLLGKRDWLEELD 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149   84 IIDVLQLPMSKEELVEESQTKL--KEVFPTAALMPGAEKLIIHLRKHGIPFALATSsGSASFDMKTSRHKEFFSLFSHIV 161
Cdd:pfam00702  67 ILRGLVETLEAEGLTVVLVELLgvIALADELKLYPGAAEALKALKERGIKVAILTG-DNPEAAEALLRLLGLDDYFDVVI 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 207113149  162 LGDDpeVQHGKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAG 211
Cdd:pfam00702 146 SGDD--VGVGKPKPEIYLAALERLGVKP--EEVLMVGDGVNDIPAAKAAG 191
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 8-244 9.19e-18

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: 79.30  E-value: 9.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149   8 VTHLIFDMDGLLLGYTGSIVAAASGESSR-GLQSRWTDTERLYSVVFQEICNRYDK-KYSWDvkslvmgkkalEAAQIII 85
Cdd:COG1011    1 IKAVLFDLDGTLLDFDPVIAEALRALAERlGLLDEAEELAEAYRAIEYALWRRYERgEITFA-----------ELLRRLL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  86 DVLQLPMSkEELVEESQTKLKEVFPtaaLMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHkEFFSLFSHIVLGDd 165
Cdd:COG1011   70 EELGLDLA-EELAEAFLAALPELVE---PYPDALELLEALKARGYRLALLTNGSAELQEAKLRRL-GLDDLFDAVVSSE- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149 166 pEVQHGKPDPDIFLACAKRFSPPPamEKCLVFEDAPNG-VEAALAAGMQVVMVPDGNLSRDLTTKATLVLNSLQDFQPEL 244
Cdd:COG1011  144 -EVGVRKPDPEIFELALERLGVPP--EEALFVGDSPETdVAGARAAGMRTVWVNRSGEPAPAEPRPDYVISDLAELLELL 220
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 113-218 1.46e-17

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: 78.19  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149 113 ALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRH--KEFFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPa 190
Cdd:cd07528   95 PLRPGVARLIDEAKAAGVRLAIATTTSPANVDALLSALlgPERRAIFDAIAAGDD--VAEKKPDPDIYLLALERLGVSP- 171

                         90       100
                 ....*....|....*....|....*...
gi 207113149 191 mEKCLVFEDAPNGVEAALAAGMQVVMVP 218
Cdd:cd07528  172 -SDCLAIEDSAIGLQAAKAAGLPCIVTP 198
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 116-244 2.19e-13

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 69.50  E-value: 2.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  116 PGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDPEvqHGKPDPDIFLACAKRFSPPPAmeKCL 195
Cdd:PLN02919  164 PGALELITQCKNKGLKVAVASSADRIKVDANLAAAGLPLSMFDAIVSADAFE--NLKPAPDIFLAAAKILGVPTS--ECV 239

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 207113149  196 VFEDAPNGVEAALAAGMQVVMVpdgnlsrdlttKATLVLNSLQDFQPEL 244
Cdd:PLN02919  240 VIEDALAGVQAARAAGMRCIAV-----------TTTLSEEILKDAGPSL 277
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 8-220 2.93e-12

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: 63.52  E-value: 2.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149   8 VTHLIFDMDGLLLGYTGSIVAAASGESsRGLQSRWTDTERLYSVVFQeicnRYDKkyswdvkslvmGKK-ALEAAQIIID 86
Cdd:cd02603    1 IRAVLFDFGGVLIDPDPAAAVARFEAL-TGEPSEFVLDTEGLAGAFL----ELER-----------GRItEEEFWEELRE 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  87 VLQLPMSKEELVEESQTKLKevfptaaLMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSRHKEFFSLFSHIVLGDDp 166
Cdd:cd02603   65 ELGRPLSAELFEELVLAAVD-------PNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLPRRGDLFDGVVESCR- 136

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 207113149 167 eVQHGKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQVVMVPDG 220
Cdd:cd02603  137 -LGVRKPDPEIYQLALERLGVKP--EEVLFIDDREENVEAARALGIHAILVTDA 187
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 84-248 4.06e-12

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 64.28  E-value: 4.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  84 IIDVLQLPMSKEELVEESQTKLKEvfptaaLMPGAEKLIIHLRKHGIPFALATSSGSASfdmkTSRHKEFFSL---FSHI 160
Cdd:PLN03243  86 FLQMKRLAIRKEDLYEYMQGGLYR------LRPGSREFVQALKKHEIPIAVASTRPRRY----LERAIEAVGMegfFSVV 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149 161 VLGDDpeVQHGKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQVVMV----PDGNLS------RDLTTKA 230
Cdd:PLN03243 156 LAAED--VYRGKPDPEMFMYAAERLGFIP--ERCIVFGNSNSSVEAAHDGCMKCVAVagkhPVYELSagdlvvRRLDDLS 231

                        170
                 ....*....|....*...
gi 207113149 231 TLVLNSLQDFQPELFGLP 248
Cdd:PLN03243 232 VVDLKNLSDLDSPEFQIP 249
PRK10826 PRK10826
hexitol phosphatase HxpB;
79-219 1.47e-11

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 61.89  E-value: 1.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  79 EAAQIIID-VLQLpmskeelVEESQTklkevfptaaLMPGAEKLIIHLRKHGIPFALATSSGS----ASFDMKTSRHKeF 153
Cdd:PRK10826  74 EVVQRIIArVISL-------IEETRP----------LLPGVREALALCKAQGLKIGLASASPLhmleAVLTMFDLRDY-F 135

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 207113149 154 FSLFSHIVLgddpevQHGKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQVVMVPD 219
Cdd:PRK10826 136 DALASAEKL------PYSKPHPEVYLNCAAKLGVDP--LTCVALEDSFNGMIAAKAARMRSIVVPA 193
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 11-247 1.63e-10

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 59.72  E-value: 1.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  11 LIFDMDGLLL-----GYTGSIVAAASGESSRGLQsrWTdtERLYSVvFQEI------CNRYDKKYSWDVKSLVMGKKALE 79
Cdd:PLN02779  43 LLFDCDGVLVeterdGHRVAFNDAFKEFGLRPVE--WD--VELYDE-LLNIgggkerMTWYFNENGWPTSTIEKAPKDEE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  80 AAQIIIDVLQLpMSKE---ELVEESQTKLKevfptaalmPGAEKLIIHLRKHGIPFALATSSGSASFDM--KTSRHKEFF 154
Cdd:PLN02779 118 ERKELVDSLHD-RKTElfkELIESGALPLR---------PGVLRLMDEALAAGIKVAVCSTSNEKAVSKivNTLLGPERA 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149 155 SLFShIVLGDDpeVQHGKPDPDIFLACAKRFSPPPAmeKCLVFEDAPNGVEAALAAGMQVVMVPDGNLSRDLTTKATLVL 234
Cdd:PLN02779 188 QGLD-VFAGDD--VPKKKPDPDIYNLAAETLGVDPS--RCVVVEDSVIGLQAAKAAGMRCIVTKSSYTADEDFSGADAVF 262

                        250
                 ....*....|...
gi 207113149 235 NSLQDFQPELFGL 247
Cdd:PLN02779 263 DCLGDVPLEDFDL 275
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 10-211 8.67e-09

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: 53.17  E-value: 8.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149   10 HLIFDMDGLLLGYTGSIvaaasgessrglqsrwtdtERLYSVVFqeicnrydKKYSWDVKSLvmgkKALEAAQIIIDvlq 89
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAI-------------------RRAFPQTF--------EEFGLDPASF----KALKQAGGLAE--- 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149   90 lpmskEELVEESQTKLKEVFPTA--------ALMPGAEKLIIHLRKHGIPFALAtSSGSASFDMKTSRHKEFFSLFSHIV 161
Cdd:TIGR01549  47 -----EEWYRIATSALEELQGRFwseydaeeAYIRGAADLLARLKSAGIKLGII-SNGSLRAQKLLLRLFGLGDYFELIL 120

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 207113149  162 LGDDPevqHGKPDPDIFLACAKRFSPPPameKCLVFEDAPNGVEAALAAG 211
Cdd:TIGR01549 121 VSDEP---GSKPEPEIFLAALESLGVPP---EVLHVGDNLNDIEGARNAG 164
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 118-217 5.11e-08

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 49.70  E-value: 5.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149 118 AEKLIIHLRKHGIPFALATSsGSASFDMKTSRHKEFFSLFSHIVLGDDPEVQHGKPDPDIFLACAKRFSPppamEKCLVF 197
Cdd:cd01427   12 AVELLKRLRAAGIKLAIVTN-RSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDP----EEVLFV 86

                         90       100
                 ....*....|....*....|
gi 207113149 198 EDAPNGVEAALAAGMQVVMV 217
Cdd:cd01427   87 GDSENDIEAARAAGGRTVAV 106
Hydrolase_like pfam13242
HAD-hyrolase-like;
171-239 1.16e-07

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 48.00  E-value: 1.16e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 207113149  171 GKPDPDIFLACAKRFSPPPamEKCLVFEDAPN-GVEAALAAGMQVVMVPDGNLSRDLTTKA----TLVLNSLQD 239
Cdd:pfam13242   3 GKPNPGMLERALARLGLDP--ERTVMIGDRLDtDILGAREAGARTILVLTGVTRPADLEKApirpDYVVDDLAE 74
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
72-244 1.70e-06

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 47.50  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  72 VMGKKALEAAQIIIDVLQLPMSKEELVE---ESQTKLKEVFPtaalmpGAEKLIIHLRKHGIPFALATSsgsasfdmKTS 148
Cdd:PRK13222  55 VLVERALTWAGREPDEELLEKLRELFDRhyaENVAGGSRLYP------GVKETLAALKAAGYPLAVVTN--------KPT 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149 149 RHKE-------FFSLFSHIVLGDDpeVQHGKPDPDIFLACAKRFSPPPamEKCLVFEDAPNGVEAALAAGMQVVMVPDG- 220
Cdd:PRK13222 121 PFVApllealgIADYFSVVIGGDS--LPNKKPDPAPLLLACEKLGLDP--EEMLFVGDSRNDIQAARAAGCPSVGVTYGy 196

                        170       180
                 ....*....|....*....|....*
gi 207113149 221 NLSRDLTT-KATLVLNSLQDFQPEL 244
Cdd:PRK13222 197 NYGEPIALsEPDVVIDHFAELLPLL 221
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 114-251 1.77e-06

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 48.33  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149 114 LMPGAEKLIIHLRKHGIPFALATSSGSASFD--MKTSRHKEFFSLfshIVLGDDpeVQHGKPDPDIFLACAKRFSPPPam 191
Cdd:PLN02575 217 LRTGSQEFVNVLMNYKIPMALVSTRPRKTLEnaIGSIGIRGFFSV---IVAAED--VYRGKPDPEMFIYAAQLLNFIP-- 289

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149 192 EKCLVFEDAPNGVEAALAAGMQVVMV----PDGNLS------RDLTTKATLVLNSLQDFQPELFGLPSYE 251
Cdd:PLN02575 290 ERCIVFGNSNQTVEAAHDARMKCVAVaskhPIYELGaadlvvRRLDELSIVDLKNLADIESPEFGPPEPE 359
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 84-214 8.60e-05

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 42.37  E-value: 8.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149  84 IIDVLQ----LPMSKEELVEESQTKLKEVFPTA-ALMPGAEKLiihLRKHGIPFALAtSSGSASfDMKTSRHK----EFF 154
Cdd:PRK10563  54 IIDIISkehgVTLAKAELEPVYRAEVARLFDSElEPIAGANAL---LESITVPMCVV-SNGPVS-KMQHSLGKtgmlHYF 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 207113149 155 S--LFShivlGDDpeVQHGKPDPDIFLACAKRFSPPpaMEKCLVFEDAPNGVEAALAAGMQV 214
Cdd:PRK10563 129 PdkLFS----GYD--IQRWKPDPALMFHAAEAMNVN--VENCILVDDSSAGAQSGIAAGMEV 182
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 114-215 9.43e-05

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: 40.60  E-value: 9.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149 114 LMPGAEKLIIHLRKhGIPFALATSsGSAsfdmKTSRHK----EFFSLFSHIVLGDdpEVQHGKPDPDIFLACAKRFSPPP 189
Cdd:cd04305   10 LLPGAKELLEELKK-GYKLGIITN-GPT----EVQWEKleqlGIHKYFDHIVISE--EVGVQKPNPEIFDYALNQLGVKP 81

                         90       100
                 ....*....|....*....|....*..
gi 207113149 190 amEKCLVFED-APNGVEAALAAGMQVV 215
Cdd:cd04305   82 --EETLMVGDsLESDILGAKNAGIKTV 106
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 157-221 2.45e-04

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 41.36  E-value: 2.45e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 207113149 157 FSHIVLGDdpEVQHGKPDPDIFLACAKRFSPppAMEKCLVFEDAPNGVEAALAAGMQVVMVPDGN 221
Cdd:PLN02770 151 FQAVIIGS--ECEHAKPHPDPYLKALEVLKV--SKDHTFVFEDSVSGIKAGVAAGMPVVGLTTRN 211
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 112-220 3.14e-03

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


Pssm-ID: 319815 [Multi-domain]  Cd Length: 214  Bit Score: 37.68  E-value: 3.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 207113149 112 AALMPGAEKLIIHLRKHGIPFALATSSGSASFDMKTSrHKEFFSLFSHIVLGDDPEVQhgKPDPDIFLACAKRFSPPpaM 191
Cdd:cd07512   85 TRPYPGVIEALERLRAAGWRLAICTNKPEAPARALLS-ALGLADLFAAVVGGDTLPQR--KPDPAPLRAAIRRLGGD--V 159

                         90       100
                 ....*....|....*....|....*....
gi 207113149 192 EKCLVFEDAPNGVEAALAAGMQVVMVPDG 220
Cdd:cd07512  160 SRALMVGDSETDAATARAAGVPFVLVTFG 188
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 153-217 9.23e-03

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


Pssm-ID: 319852 [Multi-domain]  Cd Length: 128  Bit Score: 35.34  E-value: 9.23e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 207113149 153 FFSLFSHIVLGDdpEVQHGKPDPDIFLACAKRFSPPPamEKCLVFEDAP-NGVEAALAAGMQVVMV 217
Cdd:cd16415   45 LDDYFDFVVFSY--EVGYEKPDPRIFQKALERLGVSP--EEALHVGDDLkNDYLGARAVGWHALLV 106
 
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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