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Conserved domains on  [gi|45550911|ref|NP_722701|]
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uncharacterized protein Dmel_CG31924 [Drosophila melanogaster]

Protein Classification

HAD_AtGPP-like domain-containing protein( domain architecture ID 11576397)

HAD_AtGPP-like domain-containing protein

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 ...
 16-205 9.19e-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: 318.52  E-value: 9.19e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  16 VTHCIFELDGLLIDSERLRTETVQRILDPYGHTYSFDLKMRCMGKPDSEQAALIVNTFNLPFSMTE-FENQQELQCRGKM 94
Cdd:cd07529   1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLEEeFDEQQEALAELFM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  95 GFIRLMPGVERLLHHLKAFNIPMAIASGCCRDSFRIKTRRHSRPFDVFHHVVLSGSDEEVKRGKPAPDVFLTTASRFEES 174
Cdd:cd07529  81 GTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEVKGRGKPAPDIFLVAAKRFNEP 160

                       170       180       190
                ....*....|....*....|....*....|..
gi 45550911 175 PE-PSKCLVFESSLVGMEAALSAGMQVVLVPD 205
Cdd:cd07529 161 PKdPSKCLVFEDSPNGVKAAKAAGMQVVMVPD 192
 
Name Accession Description Interval E-value
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 16-205 9.19e-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: 318.52  E-value: 9.19e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  16 VTHCIFELDGLLIDSERLRTETVQRILDPYGHTYSFDLKMRCMGKPDSEQAALIVNTFNLPFSMTE-FENQQELQCRGKM 94
Cdd:cd07529   1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLEEeFDEQQEALAELFM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  95 GFIRLMPGVERLLHHLKAFNIPMAIASGCCRDSFRIKTRRHSRPFDVFHHVVLSGSDEEVKRGKPAPDVFLTTASRFEES 174
Cdd:cd07529  81 GTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEVKGRGKPAPDIFLVAAKRFNEP 160

                       170       180       190
                ....*....|....*....|....*....|..
gi 45550911 175 PE-PSKCLVFESSLVGMEAALSAGMQVVLVPD 205
Cdd:cd07529 161 PKdPSKCLVFEDSPNGVKAAKAAGMQVVMVPD 192
PLN02811 PLN02811
hydrolase
 23-235 1.80e-68

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 210.00  E-value: 1.80e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911   23 LDGLLIDSERLRTETVQRILDPYGHTYSFDLKMRCMGKPDSEQAALIVNTFNLPFSMT--EFENQQELQCRGKMGFIRLM 100
Cdd:PLN02811   1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSDSLSpeDFLVEREAMLQDLFPTSDLM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  101 PGVERLLHHLKAFNIPMAIASGCCRDSFRIKTRRHSRPFDVFHHVVLsGSDEEVKRGKPAPDVFLTTASRFEE-SPEPSK 179
Cdd:PLN02811  81 PGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVT-GDDPEVKQGKPAPDIFLAAARRFEDgPVDPGK 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 45550911  180 CLVFESSLVGMEAALSAGMQVVLVPDPLVSFRASAHATLRLRSLEGFKPQYFGLPP 235
Cdd:PLN02811 160 VLVFEDAPSGVEAAKNAGMSVVMVPDPRLDKSYCKGADQVLSSLLDFKPEEWGLPP 215
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
19-226 9.80e-50

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 161.53  E-value: 9.80e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  19 CIFELDGLLIDSERLRTETVQRILDPYGHTYSFDLKMRCMGKPDSEQAALIVNTFNLPFSMTEFENQ--QELQCRGKMGF 96
Cdd:COG0637   5 VIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARkeELYRELLAEEG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  97 IRLMPGVERLLHHLKAFNIPMAIASGCCRDSFRIKTRRHSRpFDVFHHVVlsgSDEEVKRGKPAPDVFLTTASRFEESPE 176
Cdd:COG0637  85 LPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGL-LDYFDVIV---TGDDVARGKPDPDIYLLAAERLGVDPE 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 45550911 177 psKCLVFESSLVGMEAALSAGMQVVLVPDPLVSFRASAHATLRLRSLEGF 226
Cdd:COG0637 161 --ECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 19-203 1.21e-25

beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509).


Pssm-ID: 213673 [Multi-domain]  Cd Length: 185  Bit Score: 98.95  E-value: 1.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911    19 CIFELDGLLIDSERLRTETVQRILDPYGHTYSFDLKMRCMGKPDSEQAALIVNTFNLPFS------MTEFENQQeLQCRG 92
Cdd:TIGR02009   4 VIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDGLSleeihqLAERKNEL-YRELL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911    93 KMGFIRLMPGVERLLHHLKAFNIPMAIASGCCRDSFRIKTRRHSRPFDVfhhvVLSGSdeEVKRGKPAPDVFLTTASRFE 172
Cdd:TIGR02009  83 RLTGVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRDYFDA----IVDAS--EVKNGKPHPETFLLAAELLG 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 45550911   173 ESPEpsKCLVFESSLVGMEAALSAGMQVVLV 203
Cdd:TIGR02009 157 VPPN--ECIVFEDALAGVQAARAAGMFAVAV 185
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
19-203 8.02e-16

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 72.62  E-value: 8.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911    19 CIFELDGLLIDSERLRTETVQRILDPYG-HTYSFDLKMRCMGkPDSEQAA--LIVNT---FNLPFSMTEFENqqelqcRG 92
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGyGELSEEEILKFIG-LPLREIFryLGVSEdeeEKIEFYLRKYNE------EL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911    93 KMGFIRLMPGVERLLHHLKAFNIPMAIASGCCRDSFRIKTRRHsrPFDVFHHVVLSGSDeeVKRGKPAPDVFLTTASRFE 172
Cdd:pfam13419  74 HDKLVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQL--GLEDYFDVIVGGDD--VEGKKPDPDPILKALEQLG 149

                         170       180       190
                  ....*....|....*....|....*....|.
gi 45550911   173 ESPEpsKCLVFESSLVGMEAALSAGMQVVLV 203
Cdd:pfam13419 150 LKPE--EVIYVGDSPRDIEAAKNAGIKVIAV 178
 
Name Accession Description Interval E-value
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 16-205 9.19e-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: 318.52  E-value: 9.19e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  16 VTHCIFELDGLLIDSERLRTETVQRILDPYGHTYSFDLKMRCMGKPDSEQAALIVNTFNLPFSMTE-FENQQELQCRGKM 94
Cdd:cd07529   1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLEEeFDEQQEALAELFM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  95 GFIRLMPGVERLLHHLKAFNIPMAIASGCCRDSFRIKTRRHSRPFDVFHHVVLSGSDEEVKRGKPAPDVFLTTASRFEES 174
Cdd:cd07529  81 GTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEVKGRGKPAPDIFLVAAKRFNEP 160

                       170       180       190
                ....*....|....*....|....*....|..
gi 45550911 175 PE-PSKCLVFESSLVGMEAALSAGMQVVLVPD 205
Cdd:cd07529 161 PKdPSKCLVFEDSPNGVKAAKAAGMQVVMVPD 192
PLN02811 PLN02811
hydrolase
 23-235 1.80e-68

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 210.00  E-value: 1.80e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911   23 LDGLLIDSERLRTETVQRILDPYGHTYSFDLKMRCMGKPDSEQAALIVNTFNLPFSMT--EFENQQELQCRGKMGFIRLM 100
Cdd:PLN02811   1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSDSLSpeDFLVEREAMLQDLFPTSDLM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  101 PGVERLLHHLKAFNIPMAIASGCCRDSFRIKTRRHSRPFDVFHHVVLsGSDEEVKRGKPAPDVFLTTASRFEE-SPEPSK 179
Cdd:PLN02811  81 PGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVT-GDDPEVKQGKPAPDIFLAAARRFEDgPVDPGK 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 45550911  180 CLVFESSLVGMEAALSAGMQVVLVPDPLVSFRASAHATLRLRSLEGFKPQYFGLPP 235
Cdd:PLN02811 160 VLVFEDAPSGVEAAKNAGMSVVMVPDPRLDKSYCKGADQVLSSLLDFKPEEWGLPP 215
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
19-226 9.80e-50

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 161.53  E-value: 9.80e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  19 CIFELDGLLIDSERLRTETVQRILDPYGHTYSFDLKMRCMGKPDSEQAALIVNTFNLPFSMTEFENQ--QELQCRGKMGF 96
Cdd:COG0637   5 VIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARkeELYRELLAEEG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  97 IRLMPGVERLLHHLKAFNIPMAIASGCCRDSFRIKTRRHSRpFDVFHHVVlsgSDEEVKRGKPAPDVFLTTASRFEESPE 176
Cdd:COG0637  85 LPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGL-LDYFDVIV---TGDDVARGKPDPDIYLLAAERLGVDPE 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 45550911 177 psKCLVFESSLVGMEAALSAGMQVVLVPDPLVSFRASAHATLRLRSLEGF 226
Cdd:COG0637 161 --ECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
PLN02940 PLN02940
riboflavin kinase
 14-236 1.33e-41

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 145.36  E-value: 1.33e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911   14 QPVTHCIFELDGLLIDSERLRTETVQRILDPYGHTYSFDLKMRCMGKPDSEQAALIVNTFNLPFSMTEFENQQELQCRGK 93
Cdd:PLN02940   9 KLVSHVILDLDGTLLNTDGIVSDVLKAFLVKYGKQWDGREAQKIVGKTPLEAAATVVEDYGLPCSTDEFNSEITPLLSEQ 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911   94 MGFIRLMPGVERLLHHLKAFNIPMAIASGCCRDSFRIKTRRHSRPFDVFHHVVlsGSDeEVKRGKPAPDVFLTTASRFee 173
Cdd:PLN02940  89 WCNIKALPGANRLIKHLKSHGVPMALASNSPRANIEAKISCHQGWKESFSVIV--GGD-EVEKGKPSPDIFLEAAKRL-- 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45550911  174 SPEPSKCLVFESSLVGMEAALSAGMQVVLVPD-PLVSFRASAhATLRLRSLEGFKPQYFGLPPL 236
Cdd:PLN02940 164 NVEPSNCLVIEDSLPGVMAGKAAGMEVIAVPSiPKQTHLYSS-ADEVINSLLDLQPEKWGLPPF 226
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 19-205 6.64e-35

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: 121.57  E-value: 6.64e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  19 CIFELDGLLIDSERLrtetvqrildpygHTYSFDLKMRcmgKPDSEQAALIVntfnlpfsmtefenqqelqcrgkmGFIR 98
Cdd:cd07505   2 VIFDMDGVLIDTEPL-------------HRQAWQLLER---KNALLLELIAS------------------------EGLK 41

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  99 LMPGVERLLHHLKAFNIPMAIASGCCRDSFRIKTRRHSRPFDVFHHVVlsgSDEEVKRGKPAPDVFLTTASRFeeSPEPS 178
Cdd:cd07505  42 LKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLRGYFDVIV---SGDDVERGKPAPDIYLLAAERL--GVDPE 116

                       170       180
                ....*....|....*....|....*..
gi 45550911 179 KCLVFESSLVGMEAALSAGMQVVLVPD 205
Cdd:cd07505 117 RCLVFEDSLAGIEAAKAAGMTVVAVPD 143
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 19-203 1.21e-25

beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509).


Pssm-ID: 213673 [Multi-domain]  Cd Length: 185  Bit Score: 98.95  E-value: 1.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911    19 CIFELDGLLIDSERLRTETVQRILDPYGHTYSFDLKMRCMGKPDSEQAALIVNTFNLPFS------MTEFENQQeLQCRG 92
Cdd:TIGR02009   4 VIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDGLSleeihqLAERKNEL-YRELL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911    93 KMGFIRLMPGVERLLHHLKAFNIPMAIASGCCRDSFRIKTRRHSRPFDVfhhvVLSGSdeEVKRGKPAPDVFLTTASRFE 172
Cdd:TIGR02009  83 RLTGVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRDYFDA----IVDAS--EVKNGKPHPETFLLAAELLG 156

                         170       180       190
                  ....*....|....*....|....*....|.
gi 45550911   173 ESPEpsKCLVFESSLVGMEAALSAGMQVVLV 203
Cdd:TIGR02009 157 VPPN--ECIVFEDALAGVQAARAAGMFAVAV 185
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 20-206 4.86e-25

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: 96.56  E-value: 4.86e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  20 IFELDGLLIDSERLRTETVQRILDPYGHTysfdlkmrcmgkpdsEQAALIVNTFNLPfsmtefenqqelqcrgkmgfirL 99
Cdd:cd16423   3 IFDFDGVIVDTEPLWYEAWQELLNERRNE---------------LIKRQFSEKTDLP----------------------P 45

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911 100 MPGVERLLHHLKAFNIPMAIASGccrdSFRIKTRRHSRPFDV---FHHVVlsgSDEEVKRGKPAPDVFLTTASRFEESPE 176
Cdd:cd16423  46 IEGVKELLEFLKEKGIKLAVASS----SPRRWIEPHLERLGLldyFEVIV---TGDDVEKSKPDPDLYLEAAERLGVNPE 118

                       170       180       190
                ....*....|....*....|....*....|
gi 45550911 177 psKCLVFESSLVGMEAALSAGMQVVLVPDP 206
Cdd:cd16423 119 --ECVVIEDSRNGVLAAKAAGMKCVGVPNP 146
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 18-203 2.25e-24

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: 95.18  E-value: 2.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911    18 HCIFELDGLLIDSERLRTETVQRildPYGHTYSFDLKMRCMGKPD--SEQAALIVNTFNLPFSMTEFENQQELQCRGKMG 95
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAIAKLINR---EELGLVPDELGVSAVGRLElaLRRFKAQYGRTISPEDAQLLYKQLFYEQIEEEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911    96 FIRLMPGVERLLHHLKAFNIPMAIASGCCRDSFRIKTRRHsrPFDVFHHVVLSgsdEEVKRGKPAPDVFLTTASRFEEsp 175
Cdd:TIGR01509  78 KLKPLPGVRALLEALRARGKKLALLTNSPRAHKLVLALLG--LRDLFDVVIDS---SDVGLGKPDPDIYLQALKALGL-- 150

                         170       180
                  ....*....|....*....|....*...
gi 45550911   176 EPSKCLVFESSLVGMEAALSAGMQVVLV 203
Cdd:TIGR01509 151 EPSECVFVDDSPAGIEAAKAAGMHTVGV 178
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
16-224 9.26e-20

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 83.82  E-value: 9.26e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  16 VTHCIFELDGLLIDSERLRTETVQRILDPYGH-TYSFDLKMRCMGKPDSEQAALIvntfnLPFSMTE-----FENQQELQ 89
Cdd:COG0546   1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLpPLDLEELRALIGLGLRELLRRL-----LGEDPDEeleelLARFRELY 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  90 CRGKMGFIRLMPGVERLLHHLKAFNIPMAIASGCCRDSFRIKTRRH--SRPFDvfhhVVLSGSDeeVKRGKPAPDVFLTT 167
Cdd:COG0546  76 EEELLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALglDDYFD----AIVGGDD--VPPAKPKPEPLLEA 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45550911 168 ASRFEESPEpsKCLVFESSLVGMEAALSAGMQVVLV------PDPLvsfrASAHATLRLRSLE 224
Cdd:COG0546 150 LERLGLDPE--EVLMVGDSPHDIEAARAAGVPFIGVtwgygsAEEL----EAAGADYVIDSLA 206
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 16-227 2.22e-16

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 75.06  E-value: 2.22e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  16 VTHCIFELDGLLIDSERLRTETVQRILDPYGHTYSFD--------LKMRCMGK------PDSEQAALIVNTFNLPFSMTE 81
Cdd:COG1011   1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEelaeayraIEYALWRRyergeiTFAELLRRLLEELGLDLAEEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  82 FEnqQELQCRGKMgfIRLMPGVERLLHHLKAFNIPMAIASGCCRDSFRIKTRRH--SRPFDvfhHVVLSgsdEEVKRGKP 159
Cdd:COG1011  81 AE--AFLAALPEL--VEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLglDDLFD---AVVSS---EEVGVRKP 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45550911 160 APDVFLTTASRFEESPEpsKCLVFESSLVG-MEAALSAGMQVVLVPDPLVSFRASAHATLRLRSLEGFK 227
Cdd:COG1011 151 DPEIFELALERLGVPPE--EALFVGDSPETdVAGARAAGMRTVWVNRSGEPAPAEPRPDYVISDLAELL 217
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 20-200 6.11e-16

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: 71.97  E-value: 6.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  20 IFELDGLLIDSERLRTETVQRILDPYGhtysfdlkmrcmgkpdseqaALIVNTFnlpfsMTEfenqqelqcrgkmgfIRL 99
Cdd:cd07526   4 IFDCDGVLVDSEVIAARVLVEVLAELG--------------------ARVLAAF-----EAE---------------LQP 43

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911 100 MPGVERLLhhlKAFNIPMAIASGCCRDSFRIKTRRHSRpFDVFHHVVLSGSDeeVKRGKPAPDVFLTTASRFEESPEpsK 179
Cdd:cd07526  44 IPGAAAAL---SALTLPFCVASNSSRERLTHSLGLAGL-LAYFEGRIFSASD--VGRGKPAPDLFLHAAAQMGVAPE--R 115

                       170       180
                ....*....|....*....|.
gi 45550911 180 CLVFESSLVGMEAALSAGMQV 200
Cdd:cd07526 116 CLVIEDSPTGVRAALAAGMTV 136
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
19-203 8.02e-16

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 72.62  E-value: 8.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911    19 CIFELDGLLIDSERLRTETVQRILDPYG-HTYSFDLKMRCMGkPDSEQAA--LIVNT---FNLPFSMTEFENqqelqcRG 92
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGyGELSEEEILKFIG-LPLREIFryLGVSEdeeEKIEFYLRKYNE------EL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911    93 KMGFIRLMPGVERLLHHLKAFNIPMAIASGCCRDSFRIKTRRHsrPFDVFHHVVLSGSDeeVKRGKPAPDVFLTTASRFE 172
Cdd:pfam13419  74 HDKLVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQL--GLEDYFDVIVGGDD--VEGKKPDPDPILKALEQLG 149

                         170       180       190
                  ....*....|....*....|....*....|.
gi 45550911   173 ESPEpsKCLVFESSLVGMEAALSAGMQVVLV 203
Cdd:pfam13419 150 LKPE--EVIYVGDSPRDIEAAKNAGIKVIAV 178
PRK11587 PRK11587
putative phosphatase; Provisional
 97-224 2.62e-15

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 71.95  E-value: 2.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911   97 IRLMPGVERLLHHLKAFNIPMAIASGCcrdSFRIKTRRHSR---PF-DVFHhvvlsgSDEEVKRGKPAPDVFLTTASRFE 172
Cdd:PRK11587  82 ITALPGAIALLNHLNKLGIPWAIVTSG---SVPVASARHKAaglPApEVFV------TAERVKRGKPEPDAYLLGAQLLG 152

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 45550911  173 ESPEpsKCLVFESSLVGMEAALSAGMQVVLVPDPLVSFRASaHATLRLRSLE 224
Cdd:PRK11587 153 LAPQ--ECVVVEDAPAGVLSGLAAGCHVIAVNAPADTPRLD-EVDLVLHSLE 201
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 95-204 2.64e-15

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: 71.64  E-value: 2.64e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  95 GFIRLMPGVERLLHHLKAFNIPMAIAS--------GCCRDSFRIKTRRhsrPFDVFhhvvlsGSDEEVKRGKPAPDVFLT 166
Cdd:cd07528  92 GLLPLRPGVARLIDEAKAAGVRLAIATttspanvdALLSALLGPERRA---IFDAI------AAGDDVAEKKPDPDIYLL 162

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 45550911 167 TASRFEESPepSKCLVFESSLVGMEAALSAGMQVVLVP 204
Cdd:cd07528 163 ALERLGVSP--SDCLAIEDSAIGLQAAKAAGLPCIVTP 198
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 19-203 4.70e-14

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: 68.52  E-value: 4.70e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  19 CIFELDGLLIDSerlrTETVQRILDPYGHTYSFDLK---MRCMGKPDSEQAALIVNTFNLPFSMTEFENQQElqcRGKMG 95
Cdd:cd07527   2 LLFDMDGTLVDS----TPAVERAWHKWAKEHGVDPEevlKVSHGRRAIDVIRKLAPDDADIELVLALETEEP---ESYPE 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  96 FIRLMPGVERLLHHLKAFNIPMAIASGCCRdsfRIKTRRhsrpfdvFHHVVLSGSD-----EEVKRGKPAPDVFLTTASR 170
Cdd:cd07527  75 GVIAIPGAVDLLASLPAAGDRWAIVTSGTR---ALAEAR-------LEAAGLPHPEvlvtaDDVKNGKPDPEPYLLGAKL 144

                       170       180       190
                ....*....|....*....|....*....|...
gi 45550911 171 FeeSPEPSKCLVFESSLVGMEAALSAGMQVVLV 203
Cdd:cd07527 145 L--GLDPSDCVVFEDAPAGIKAGKAAGARVVAV 175
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 16-197 6.24e-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: 68.00  E-value: 6.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911    16 VTHCIFELDGLLIDSERLRTETVQRILD--PYGHTYSFDLKMRCMGKPDSEQAALIVNTFNLPFSMTEFENQQELQCRGK 93
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASehPLAKAIVAAAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911    94 MGFIR-------------LMPGVERLLHHLKAFNIPMAIASGccrdSFRIKTRRHSRPFDVFHHVVLSGSDEEVKRGKPA 160
Cdd:pfam00702  81 TVVLVellgvialadelkLYPGAAEALKALKERGIKVAILTG----DNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPK 156

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 45550911   161 PDVFLTTASRFEESPEpsKCLVFESSLVGMEAALSAG 197
Cdd:pfam00702 157 PEIYLAALERLGVKPE--EVLMVGDGVNDIPAAKAAG 191
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 101-212 2.64e-13

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: 65.78  E-value: 2.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911 101 PGVERLLHHLKAFNIPMAIASgccrdsfriktrrHSR--PF--------DVFHHVVlsgSDEEVKRGKPAPDVFLTTASR 170
Cdd:cd02598  52 PGIASLLVDLKAKGIKIALAS-------------ASKnaPKileklglaEYFDAIV---DGAVLAKGKPDPDIFLAAAEG 115

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 45550911 171 FeeSPEPSKCLVFESSLVGMEAALSAGMQVVLVPDPLVSFRA 212
Cdd:cd02598 116 L--GLNPKDCIGVEDAQAGIRAIKAAGFLVVGVGREEDLLGA 155
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
20-203 3.44e-12

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 62.78  E-value: 3.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911   20 IFELDGLLIDSERLRTETVQRILDPYGHTYSFDLKMRCMGKPDSEQAALIVNTfnlpfsmtefeNQQELQ----CRGKMG 95
Cdd:PRK10725   9 IFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVALNGSPTWRIAQAIIEL-----------NQADLDphalAREKTE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911   96 FIR--LMPGVERL--LHHLKAFN--IPMAIASGccrDSFRIKTR--RHSRPFDVFHHVVlsGSDEeVKRGKPAPDVFLTT 167
Cdd:PRK10725  78 AVKsmLLDSVEPLplIEVVKAWHgrRPMAVGTG---SESAIAEAllAHLGLRRYFDAVV--AADD-VQHHKPAPDTFLRC 151

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 45550911  168 ASRFEESPEpsKCLVFESSLVGMEAALSAGMQVVLV 203
Cdd:PRK10725 152 AQLMGVQPT--QCVVFEDADFGIQAARAAGMDAVDV 185
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 85-224 4.77e-12

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 63.90  E-value: 4.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911   85 QQELQCRGKMGFIRLMPGVERLLHHLKAFNIPMAIASGCCRdsfRIKTRR-HSRPFDVFHHVVLSGsdEEVKRGKPAPDV 163
Cdd:PLN03243  96 KEDLYEYMQGGLYRLRPGSREFVQALKKHEIPIAVASTRPR---RYLERAiEAVGMEGFFSVVLAA--EDVYRGKPDPEM 170

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45550911  164 FLTTASRFEESPEpsKCLVFESSLVGMEAALSAGMQVVLVPDPLVSFRASAhATLRLRSLE 224
Cdd:PLN03243 171 FMYAAERLGFIPE--RCIVFGNSNSSVEAAHDGCMKCVAVAGKHPVYELSA-GDLVVRRLD 228
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 95-206 6.30e-12

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 63.57  E-value: 6.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911   95 GFIRLMPGVERLLHHLKAFNIPMAIASGCCRDSFR------IKTRRHSRpFDVFhhvvlSGSDeeVKRGKPAPDVFLTTA 168
Cdd:PLN02779 141 GALPLRPGVLRLMDEALAAGIKVAVCSTSNEKAVSkivntlLGPERAQG-LDVF-----AGDD--VPKKKPDPDIYNLAA 212

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 45550911  169 SRFeeSPEPSKCLVFESSLVGMEAALSAGMQVVLVPDP 206
Cdd:PLN02779 213 ETL--GVDPSRCVVVEDSVIGLQAAKAAGMRCIVTKSS 248
PRK10826 PRK10826
hexitol phosphatase HxpB;
20-224 3.32e-10

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 58.04  E-value: 3.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911   20 IFELDGLLIDSERLRTETVQRILDPYGHTYSFDLKM----------------RCMGKPDSEQAAL---IVNTfnlpfSMT 80
Cdd:PRK10826  11 IFDMDGLLIDSEPLWDRAELDVMASLGVDISRREELpdtlglridqvvdlwyARQPWNGPSRQEVvqrIIAR-----VIS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911   81 EFENQQELqcrgkmgfirlMPGVERLLHHLKAFNIPMAIASGccrDSFRIKTR-------RHSrpFDVFHhvvlsgSDEE 153
Cdd:PRK10826  86 LIEETRPL-----------LPGVREALALCKAQGLKIGLASA---SPLHMLEAvltmfdlRDY--FDALA------SAEK 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45550911  154 VKRGKPAPDVFLTTASRFEesPEPSKCLVFESSLVGMEAALSAGMQVVLVPDPlvSFRASAH---ATLRLRSLE 224
Cdd:PRK10826 144 LPYSKPHPEVYLNCAAKLG--VDPLTCVALEDSFNGMIAAKAARMRSIVVPAP--EQQNDPRwalADVKLESLT 213
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 85-203 2.44e-07

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 50.64  E-value: 2.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911   85 QQELQCRGKMGFIRLMPGVERLLHHLKAFNIPMAIASGCCRDSfrIKTRRHSRPFDVFHHVVLSGsdEEVKRGKPAPDVF 164
Cdd:PLN02575 203 KEEIYQALQGGIYRLRTGSQEFVNVLMNYKIPMALVSTRPRKT--LENAIGSIGIRGFFSVIVAA--EDVYRGKPDPEMF 278

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 45550911  165 LTTASRFEESPEpsKCLVFESSLVGMEAALSAGMQVVLV 203
Cdd:PLN02575 279 IYAAQLLNFIPE--RCIVFGNSNQTVEAAHDARMKCVAV 315
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 15-203 4.75e-07

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 50.24  E-value: 4.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911    15 PVTHCIFELDGLLIDSERLRTETVQRILDPYGHTYSFDLKMRCMGKPDSEQAALIVNTFNLPFSMTE------FEN--QQ 86
Cdd:PLN02919   74 KVSAVLFDMDGVLCNSEEPSRRAAVDVFAEMGVEVTVEDFVPFMGTGEANFLGGVASVKGVKGFDPDaakkrfFEIylEK 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911    87 ELQCRGKMGFirlmPGVERLLHHLKAFNIPMAIASGCCRDSFRIKTRRHSRPFDVFHHVVlsgSDEEVKRGKPAPDVFLT 166
Cdd:PLN02919  154 YAKPNSGIGF----PGALELITQCKNKGLKVAVASSADRIKVDANLAAAGLPLSMFDAIV---SADAFENLKPAPDIFLA 226

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 45550911   167 tASRFEESPePSKCLVFESSLVGMEAALSAGMQVVLV 203
Cdd:PLN02919  227 -AAKILGVP-TSECVVIEDALAGVQAARAAGMRCIAV 261
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 95-212 2.02e-06

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: 46.95  E-value: 2.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  95 GFIRLMPGVERLLHHLKAFNIPMAIASGCCRDSFRIKTRRHSRPFDVFHHVVLSGsdeEVKRGKPAPDVFLTTASRFEES 174
Cdd:cd02603  81 AAVDPNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLPRRGDLFDGVVESC---RLGVRKPDPEIYQLALERLGVK 157

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 45550911 175 PEpsKCLVFESSLVGMEAALSAGMQVVLVPDPLVSFRA 212
Cdd:cd02603 158 PE--EVLFIDDREENVEAARALGIHAILVTDAEDALRE 193
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 103-203 9.58e-06

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: 43.15  E-value: 9.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911 103 VERLLHHLKAFNIPMAIASGCCRDSFRiKTRRHSRPFDVFHHVVLSGSDEEVKR-GKPAPDVFLTTASrfeespEPSKCL 181
Cdd:cd01427  12 AVELLKRLRAAGIKLAIVTNRSREALR-ALLEKLGLGDLFDGIIGSDGGGTPKPkPKPLLLLLLKLGV------DPEEVL 84

                        90       100
                ....*....|....*....|..
gi 45550911 182 VFESSLVGMEAALSAGMQVVLV 203
Cdd:cd01427  85 FVGDSENDIEAARAAGGRTVAV 106
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 98-204 2.41e-05

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


Pssm-ID: 319854 [Multi-domain]  Cd Length: 212  Bit Score: 43.76  E-value: 2.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  98 RLMPGVERLLHHLKAFNIPMAIASGccrdsfriKTRRHSRP----FDVFHH--VVLSGSDEEVKrgKPAPDVFLTTASRF 171
Cdd:cd16417  87 HLYPGVKEGLAALKAQGYPLACVTN--------KPERFVAPlleaLGISDYfsLVLGGDSLPEK--KPDPAPLLHACEKL 156

                        90       100       110
                ....*....|....*....|....*....|...
gi 45550911 172 EESPEpsKCLVFESSLVGMEAALSAGMQVVLVP 204
Cdd:cd16417 157 GIAPA--QMLMVGDSRNDILAARAAGCPSVGLT 187
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
98-204 4.81e-05

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 43.26  E-value: 4.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911   98 RLMPGVERLLHHLKAFNIPMAiasgCCRDsfriKTRRHSRP----FDVFHH--VVLSGSDeeVKRGKPAPDVFLTTASRF 171
Cdd:PRK13222  93 RLYPGVKETLAALKAAGYPLA----VVTN----KPTPFVAPlleaLGIADYfsVVIGGDS--LPNKKPDPAPLLLACEKL 162

                         90       100       110
                 ....*....|....*....|....*....|...
gi 45550911  172 EESPEpsKCLVFESSLVGMEAALSAGMQVVLVP 204
Cdd:PRK13222 163 GLDPE--EMLFVGDSRNDIQAARAAGCPSVGVT 193
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 101-203 1.40e-04

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 41.48  E-value: 1.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911 101 PGVERLLHHLKAFNIPMAIASGCCRDSFRIKTRRHSRPfDVFHHVVlsgSDEEVKRGKPAPDVFLTTASRFEESPEpsKC 180
Cdd:cd02588  94 PDVVAGLRRLREAGYRLAILSNGSPDLIEDVVANAGLR-DLFDAVL---SAEDVRAYKPAPAVYELAAERLGVPPD--EI 167

                        90       100
                ....*....|....*....|...
gi 45550911 181 LVFESSLVGMEAALSAGMQVVLV 203
Cdd:cd02588 168 LHVASHAWDLAGARALGLRTAWI 190
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 99-201 1.96e-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: 36.75  E-value: 1.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550911  99 LMPGVERLLHHLKAfNIPMAIASgccrDSFRIKTR---RHSRPFDVFHHVVLSgsdEEVKRGKPAPDVFLTTASRFEESP 175
Cdd:cd04305  10 LLPGAKELLEELKK-GYKLGIIT----NGPTEVQWeklEQLGIHKYFDHIVIS---EEVGVQKPNPEIFDYALNQLGVKP 81

                        90       100       110
                ....*....|....*....|....*....|..
gi 45550911 176 EpskclvfESSLVG------MEAALSAGMQVV 201
Cdd:cd04305  82 E-------ETLMVGdslesdILGAKNAGIKTV 106
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 140-201 2.21e-03

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 38.28  E-value: 2.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45550911  140 DVFHHVVLSgsdEEVKRGKPAPDVFLTTASRFEESPEPSkcLVFESSLVGMEAALSAGMQVV 201
Cdd:PLN02770 149 DFFQAVIIG---SECEHAKPHPDPYLKALEVLKVSKDHT--FVFEDSVSGIKAGVAAGMPVV 205
Hydrolase_like pfam13242
HAD-hyrolase-like;
156-203 2.23e-03

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 35.67  E-value: 2.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 45550911   156 RGKPAPDVFLTTASRFEESPEpsKCLVfesslVG------MEAALSAGMQVVLV 203
Cdd:pfam13242   2 CGKPNPGMLERALARLGLDPE--RTVM-----IGdrldtdILGAREAGARTILV 48
 
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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