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Conserved domains on  [gi|47226791|emb|CAG06633|]
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unnamed protein product, partial [Tetraodon nigroviridis]

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 ...
 3-198 2.93e-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: 319.68  E-value: 2.93e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   3 VTHVIFDMDGLLLDTERLYTVAFQEICDRFEKQYTWAVKSSVMGRNALDACQIIRDTLDLPMTAEELLIESRQILKRIFP 82
Cdd:cd07529   1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLEEEFDEQQEALAELFM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791  83 S-AKLLPGVEKLVIHLQQHNIPIAVATSSEGVTFSLKTSQHKDFFGRFHHIVLGDDPDVK-NNKPLPDSFLVCASRFNPP 160
Cdd:cd07529  81 GtAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEVKgRGKPAPDIFLVAAKRFNEP 160

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 47226791 161 AApendwgNDTRCLVFEDAPNGVTAALAAGMQVVMIPD 198
Cdd:cd07529 161 PK------DPSKCLVFEDSPNGVKAAKAAGMQVVMVPD 192
 
Name Accession Description Interval E-value
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 3-198 2.93e-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: 319.68  E-value: 2.93e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   3 VTHVIFDMDGLLLDTERLYTVAFQEICDRFEKQYTWAVKSSVMGRNALDACQIIRDTLDLPMTAEELLIESRQILKRIFP 82
Cdd:cd07529   1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLEEEFDEQQEALAELFM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791  83 S-AKLLPGVEKLVIHLQQHNIPIAVATSSEGVTFSLKTSQHKDFFGRFHHIVLGDDPDVK-NNKPLPDSFLVCASRFNPP 160
Cdd:cd07529  81 GtAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEVKgRGKPAPDIFLVAAKRFNEP 160

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 47226791 161 AApendwgNDTRCLVFEDAPNGVTAALAAGMQVVMIPD 198
Cdd:cd07529 161 PK------DPSKCLVFEDSPNGVKAAKAAGMQVVMVPD 192
PLN02811 PLN02811
hydrolase
 10-230 1.99e-88

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 260.08  E-value: 1.99e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   10 MDGLLLDTERLYTVAFQEICDRFEKQYTWAVKSSVMGRNALDACQIIRDTLDLP--MTAEELLIESRQILKRIFPSAKLL 87
Cdd:PLN02811   1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSdsLSPEDFLVEREAMLQDLFPTSDLM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   88 PGVEKLVIHLQQHNIPIAVATSSEGVTFSLKTSQHKDFFGRFHHIVLGDDPDVKNNKPLPDSFLVCASRF-NPPAAPENd 166
Cdd:PLN02811  81 PGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVTGDDPEVKQGKPAPDIFLAAARRFeDGPVDPGK- 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47226791  167 wgndtrCLVFEDAPNGVTAALAAGMQVVMIPDDNMDPALTREATLQLRSMEEFEPRLFSLPPFS 230
Cdd:PLN02811 160 ------VLVFEDAPSGVEAAKNAGMSVVMVPDPRLDKSYCKGADQVLSSLLDFKPEEWGLPPFP 217
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
6-219 2.54e-55

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 175.78  E-value: 2.54e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   6 VIFDMDGLLLDTERLYTVAFQEICDRFEKQYTWAVKSSVMGRNALDACQIIRDTLDLPMTAEELLIESRQILKRIF--PS 83
Cdd:COG0637   5 VIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYRELLaeEG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791  84 AKLLPGVEKLVIHLQQHNIPIAVATSSEG--VTFSLKTSqhkDFFGRFHHIVLGDdpDVKNNKPLPDSFLVCASRFNppA 161
Cdd:COG0637  85 LPLIPGVVELLEALKEAGIKIAVATSSPRenAEAVLEAA---GLLDYFDVIVTGD--DVARGKPDPDIYLLAAERLG--V 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 47226791 162 APEndwgndtRCLVFEDAPNGVTAALAAGMQVVMIPDDNMDPALTREATLQLRSMEEF 219
Cdd:COG0637 158 DPE-------ECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 6-196 2.62e-32

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: 115.90  E-value: 2.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791     6 VIFDMDGLLLDTERLYTVAFQEICDRFEKQYTWAVKSSVMGRNALDACQIIRDTLDLPM---TAEELLIESRQILKRIFP 82
Cdd:TIGR02009   4 VIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDGLsleEIHQLAERKNELYRELLR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791    83 --SAKLLPGVEKLVIHLQQHNIPIAVATSSEGVTFSLKTSQHKDFFgrfHHIVLGDDpdVKNNKPLPDSFLVCASRFNPP 160
Cdd:TIGR02009  84 ltGVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRDYF---DAIVDASE--VKNGKPHPETFLLAAELLGVP 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 47226791   161 AapendwgndTRCLVFEDAPNGVTAALAAGMQVVMI 196
Cdd:TIGR02009 159 P---------NECIVFEDALAGVQAARAAGMFAVAV 185
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
6-196 8.90e-22

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 88.41  E-value: 8.90e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791     6 VIFDMDGLLLDTERLYTVAFQEICDRFE-KQYTWAVKSSVMGRNALDACQIIRDTLDLPMTAEELLIESRQILKRIFPsa 84
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGyGELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFYLRKYNEELHDKLV-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791    85 KLLPGVEKLVIHLQQHNIPIAVATS--SEGVTFSLKTSQHKDFfgrFHHIVLGDdpDVKNNKPLPDSFLVCASRFNppAA 162
Cdd:pfam13419  79 KPYPGIKELLEELKEQGYKLGIVTSksRENVEEFLKQLGLEDY---FDVIVGGD--DVEGKKPDPDPILKALEQLG--LK 151

                         170       180       190
                  ....*....|....*....|....*....|....
gi 47226791   163 PEndwgndtRCLVFEDAPNGVTAALAAGMQVVMI 196
Cdd:pfam13419 152 PE-------EVIYVGDSPRDIEAAKNAGIKVIAV 178
 
Name Accession Description Interval E-value
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 3-198 2.93e-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: 319.68  E-value: 2.93e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   3 VTHVIFDMDGLLLDTERLYTVAFQEICDRFEKQYTWAVKSSVMGRNALDACQIIRDTLDLPMTAEELLIESRQILKRIFP 82
Cdd:cd07529   1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLEEEFDEQQEALAELFM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791  83 S-AKLLPGVEKLVIHLQQHNIPIAVATSSEGVTFSLKTSQHKDFFGRFHHIVLGDDPDVK-NNKPLPDSFLVCASRFNPP 160
Cdd:cd07529  81 GtAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEVKgRGKPAPDIFLVAAKRFNEP 160

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 47226791 161 AApendwgNDTRCLVFEDAPNGVTAALAAGMQVVMIPD 198
Cdd:cd07529 161 PK------DPSKCLVFEDSPNGVKAAKAAGMQVVMVPD 192
PLN02811 PLN02811
hydrolase
 10-230 1.99e-88

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 260.08  E-value: 1.99e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   10 MDGLLLDTERLYTVAFQEICDRFEKQYTWAVKSSVMGRNALDACQIIRDTLDLP--MTAEELLIESRQILKRIFPSAKLL 87
Cdd:PLN02811   1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSdsLSPEDFLVEREAMLQDLFPTSDLM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   88 PGVEKLVIHLQQHNIPIAVATSSEGVTFSLKTSQHKDFFGRFHHIVLGDDPDVKNNKPLPDSFLVCASRF-NPPAAPENd 166
Cdd:PLN02811  81 PGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVTGDDPEVKQGKPAPDIFLAAARRFeDGPVDPGK- 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47226791  167 wgndtrCLVFEDAPNGVTAALAAGMQVVMIPDDNMDPALTREATLQLRSMEEFEPRLFSLPPFS 230
Cdd:PLN02811 160 ------VLVFEDAPSGVEAAKNAGMSVVMVPDPRLDKSYCKGADQVLSSLLDFKPEEWGLPPFP 217
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
6-219 2.54e-55

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 175.78  E-value: 2.54e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   6 VIFDMDGLLLDTERLYTVAFQEICDRFEKQYTWAVKSSVMGRNALDACQIIRDTLDLPMTAEELLIESRQILKRIF--PS 83
Cdd:COG0637   5 VIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYRELLaeEG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791  84 AKLLPGVEKLVIHLQQHNIPIAVATSSEG--VTFSLKTSqhkDFFGRFHHIVLGDdpDVKNNKPLPDSFLVCASRFNppA 161
Cdd:COG0637  85 LPLIPGVVELLEALKEAGIKIAVATSSPRenAEAVLEAA---GLLDYFDVIVTGD--DVARGKPDPDIYLLAAERLG--V 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 47226791 162 APEndwgndtRCLVFEDAPNGVTAALAAGMQVVMIPDDNMDPALTREATLQLRSMEEF 219
Cdd:COG0637 158 DPE-------ECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
PLN02940 PLN02940
riboflavin kinase
 1-230 3.50e-43

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 149.60  E-value: 3.50e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791    1 KPVTHVIFDMDGLLLDTERLYTVAFQEICDRFEKQYTWAVKSSVMGRNALDACQIIRDTLDLPMTAEELLIESRQILKRI 80
Cdd:PLN02940   9 KLVSHVILDLDGTLLNTDGIVSDVLKAFLVKYGKQWDGREAQKIVGKTPLEAAATVVEDYGLPCSTDEFNSEITPLLSEQ 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   81 FPSAKLLPGVEKLVIHLQQHNIPIAVATSSEGVTFSLKTSQHKDFFGRFHHIVLGDdpDVKNNKPLPDSFLVCASRFNPp 160
Cdd:PLN02940  89 WCNIKALPGANRLIKHLKSHGVPMALASNSPRANIEAKISCHQGWKESFSVIVGGD--EVEKGKPSPDIFLEAAKRLNV- 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791  161 aapendwgNDTRCLVFEDAPNGVTAALAAGMQVVMIPDDNMDPALTREATLQLRSMEEFEPRLFSLPPFS 230
Cdd:PLN02940 166 --------EPSNCLVIEDSLPGVMAGKAAGMEVIAVPSIPKQTHLYSSADEVINSLLDLQPEKWGLPPFN 227
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 6-198 2.77e-38

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: 130.04  E-value: 2.77e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   6 VIFDMDGLLLDTERLYTVAFQEIcDRFEKQYtwavkssvmgrnaldacqiirdtldlpmtaEELLIESRqilkrifpsAK 85
Cdd:cd07505   2 VIFDMDGVLIDTEPLHRQAWQLL-ERKNALL------------------------------LELIASEG---------LK 41

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791  86 LLPGVEKLVIHLQQHNIPIAVATSSEGVTFSLKTSQHKDFFGRFHHIVLGDDpdVKNNKPLPDSFLVCASRFNPPAApen 165
Cdd:cd07505  42 LKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLRGYFDVIVSGDD--VERGKPAPDIYLLAAERLGVDPE--- 116

                       170       180       190
                ....*....|....*....|....*....|...
gi 47226791 166 dwgndtRCLVFEDAPNGVTAALAAGMQVVMIPD 198
Cdd:cd07505 117 ------RCLVFEDSLAGIEAAKAAGMTVVAVPD 143
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 6-196 2.62e-32

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: 115.90  E-value: 2.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791     6 VIFDMDGLLLDTERLYTVAFQEICDRFEKQYTWAVKSSVMGRNALDACQIIRDTLDLPM---TAEELLIESRQILKRIFP 82
Cdd:TIGR02009   4 VIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDGLsleEIHQLAERKNELYRELLR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791    83 --SAKLLPGVEKLVIHLQQHNIPIAVATSSEGVTFSLKTSQHKDFFgrfHHIVLGDDpdVKNNKPLPDSFLVCASRFNPP 160
Cdd:TIGR02009  84 ltGVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRDYF---DAIVDASE--VKNGKPHPETFLLAAELLGVP 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 47226791   161 AapendwgndTRCLVFEDAPNGVTAALAAGMQVVMI 196
Cdd:TIGR02009 159 P---------NECIVFEDALAGVQAARAAGMFAVAV 185
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 6-218 3.35e-32

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: 115.04  E-value: 3.35e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   6 VIFDMDGLLLDTERLYTVAFQEIcdrfekqytwavkssvmgrnaldacqiirdtldlpmtaeeLLIESRQILKRIF---P 82
Cdd:cd16423   2 VIFDFDGVIVDTEPLWYEAWQEL----------------------------------------LNERRNELIKRQFsekT 41

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791  83 SAKLLPGVEKLVIHLQQHNIPIAVATSSEG--VTFSLKTSqhkDFFGRFHHIVLGDDpdVKNNKPLPDSFLVCASRFNpp 160
Cdd:cd16423  42 DLPPIEGVKELLEFLKEKGIKLAVASSSPRrwIEPHLERL---GLLDYFEVIVTGDD--VEKSKPDPDLYLEAAERLG-- 114

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 47226791 161 AAPENdwgndtrCLVFEDAPNGVTAALAAGMQVVMIPDDNMDPALTREATLQLRSMEE 218
Cdd:cd16423 115 VNPEE-------CVVIEDSRNGVLAAKAAGMKCVGVPNPVTGSQDFSKADLVLSSFAE 165
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 5-196 7.41e-23

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: 90.94  E-value: 7.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791     5 HVIFDMDGLLLDTERLYtvAFQEICDRFEKQYTWAVKSSVmgrNALDAC----QIIRDTLDLPMTAEELL--IESRQILK 78
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAI--AKLINREELGLVPDELGVSAV---GRLELAlrrfKAQYGRTISPEDAQLLYkqLFYEQIEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791    79 RIFpsAKLLPGVEKLVIHLQQHNIPIAVATSSEGVTFSLKTSQHkdFFGRFHHIVLGDDpdVKNNKPLPDSFLVCASRFN 158
Cdd:TIGR01509  76 EAK--LKPLPGVRALLEALRARGKKLALLTNSPRAHKLVLALLG--LRDLFDVVIDSSD--VGLGKPDPDIYLQALKALG 149

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 47226791   159 PPAApendwgndtRCLVFEDAPNGVTAALAAGMQVVMI 196
Cdd:TIGR01509 150 LEPS---------ECVFVDDSPAGIEAAKAAGMHTVGV 178
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
6-196 8.90e-22

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 88.41  E-value: 8.90e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791     6 VIFDMDGLLLDTERLYTVAFQEICDRFE-KQYTWAVKSSVMGRNALDACQIIRDTLDLPMTAEELLIESRQILKRIFPsa 84
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGyGELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFYLRKYNEELHDKLV-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791    85 KLLPGVEKLVIHLQQHNIPIAVATS--SEGVTFSLKTSQHKDFfgrFHHIVLGDdpDVKNNKPLPDSFLVCASRFNppAA 162
Cdd:pfam13419  79 KPYPGIKELLEELKEQGYKLGIVTSksRENVEEFLKQLGLEDY---FDVIVGGD--DVEGKKPDPDPILKALEQLG--LK 151

                         170       180       190
                  ....*....|....*....|....*....|....
gi 47226791   163 PEndwgndtRCLVFEDAPNGVTAALAAGMQVVMI 196
Cdd:pfam13419 152 PE-------EVIYVGDSPRDIEAAKNAGIKVIAV 178
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
7-194 4.64e-21

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 86.67  E-value: 4.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791    7 IFDMDGLLLDTERLYTVAFQEICDRFEKQY------------TWAVKSSVMGRNALDacqiirdtLDlpmtAEELLIESR 74
Cdd:PRK10725   9 IFDMDGTILDTEPTHRKAWREVLGRYGLQFdeqamvalngspTWRIAQAIIELNQAD--------LD----PHALAREKT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   75 QILKRI-FPSAKLLPGVEklVIHLQQHNIPIAVATSSE-GVTFSLKtsQHKDFFGRFHHIVLGDDpdVKNNKPLPDSFLV 152
Cdd:PRK10725  77 EAVKSMlLDSVEPLPLIE--VVKAWHGRRPMAVGTGSEsAIAEALL--AHLGLRRYFDAVVAADD--VQHHKPAPDTFLR 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 47226791  153 CASRFNPPAapendwgndTRCLVFEDAPNGVTAALAAGMQVV 194
Cdd:PRK10725 151 CAQLMGVQP---------TQCVVFEDADFGIQAARAAGMDAV 183
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
3-194 2.49e-19

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 82.67  E-value: 2.49e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   3 VTHVIFDMDGLLLDTERLYTVAFQEICDRF-EKQYTWAVKSSVMGRNALDACQIIrdtldLPMTAEELLIESRQILKRIF 81
Cdd:COG0546   1 IKLVLFDLDGTLVDSAPDIAAALNEALAELgLPPLDLEELRALIGLGLRELLRRL-----LGEDPDEELEELLARFRELY 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791  82 -----PSAKLLPGVEKLVIHLQQHNIPIAVATS--SEGVTFSLKtsqHKDFFGRFHHIVLGDdpDVKNNKPLPDSFLVCA 154
Cdd:COG0546  76 eeellDETRLFPGVRELLEALKARGIKLAVVTNkpREFAERLLE---ALGLDDYFDAIVGGD--DVPPAKPKPEPLLEAL 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 47226791 155 SRFNppAAPEndwgndtRCLVFEDAPNGVTAALAAGMQVV 194
Cdd:COG0546 151 ERLG--LDPE-------EVLMVGDSPHDIEAARAAGVPFI 181
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 3-190 5.57e-17

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: 76.09  E-value: 5.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791     3 VTHVIFDMDGLLLDTERLYTVAFQEICDRF---------EKQYTWAVKS----SVMGRNALDACQIIRDTLDLPMTAEEL 69
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHplakaivaaAEDLPIPVEDftarLLLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791    70 LIESRQIL--KRIFPSAKLLPGVEKLVIHLQQHNIPIAVATSSEgVTFSLKTSQHKDFFGRFHHIVLGDDPDVKnnKPLP 147
Cdd:pfam00702  81 TVVLVELLgvIALADELKLYPGAAEALKALKERGIKVAILTGDN-PEAAEALLRLLGLDDYFDVVISGDDVGVG--KPKP 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 47226791   148 DSFLVCASRFNPPAApendwgndtRCLVFEDAPNGVTAALAAG 190
Cdd:pfam00702 158 EIYLAALERLGVKPE---------EVLMVGDGVNDIPAAKAAG 191
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 6-196 2.52e-16

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: 74.30  E-value: 2.52e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   6 VIFDMDGLLLDTerlytvafQEICDRFEKQytWA---------VKSSVMGRNALDacqIIRDTLDLPMTAEELLIESRQI 76
Cdd:cd07527   2 LLFDMDGTLVDS--------TPAVERAWHK--WAkehgvdpeeVLKVSHGRRAID---VIRKLAPDDADIELVLALETEE 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791  77 LKRIFPSAKLLPGVEKLVIHLQQHNIPIAVATSSegvTFSLKTSQHkDFFGRFH--HIVLGDDpdVKNNKPLPDSFLVCA 154
Cdd:cd07527  69 PESYPEGVIAIPGAVDLLASLPAAGDRWAIVTSG---TRALAEARL-EAAGLPHpeVLVTADD--VKNGKPDPEPYLLGA 142

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 47226791 155 SRFNPPAApendwgndtRCLVFEDAPNGVTAALAAGMQVVMI 196
Cdd:cd07527 143 KLLGLDPS---------DCVVFEDAPAGIKAGKAAGARVVAV 175
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 6-193 2.52e-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: 72.74  E-value: 2.52e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   6 VIFDMDGLLLDTERLytvafqeicdrfekqytwavkssvmgrnaldACQIIRDTLDlpmtaeelliESRQILKRIFPSA- 84
Cdd:cd07526   3 VIFDCDGVLVDSEVI-------------------------------AARVLVEVLA----------ELGARVLAAFEAEl 41

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791  85 KLLPGVEKLVIHLQqhnIPIAVATSS--EGVTFSLKTSQHKDFFGrfHHIVLGDDpdVKNNKPLPDSFLVCASRFNppAA 162
Cdd:cd07526  42 QPIPGAAAALSALT---LPFCVASNSsrERLTHSLGLAGLLAYFE--GRIFSASD--VGRGKPAPDLFLHAAAQMG--VA 112

                       170       180       190
                ....*....|....*....|....*....|.
gi 47226791 163 PEndwgndtRCLVFEDAPNGVTAALAAGMQV 193
Cdd:cd07526 113 PE-------RCLVIEDSPTGVRAALAAGMTV 136
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 3-223 3.66e-14

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: 68.90  E-value: 3.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   3 VTHVIFDMDGLLLDTERLYTVAFQEICDR---------FEKQYtWAVKSSVMG---RNALDACQIIRDTL-DLPMTAEEL 69
Cdd:COG1011   1 IKAVLFDLDGTLLDFDPVIAEALRALAERlglldeaeeLAEAY-RAIEYALWRryeRGEITFAELLRRLLeELGLDLAEE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791  70 LIEsrQILKRIFPSAKLLPGVEKLVIHLQQHNIPIAVATSSEGVTFSLKTSQHkDFFGRFHHIVLGDdpDVKNNKPLPDS 149
Cdd:COG1011  80 LAE--AFLAALPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRL-GLDDLFDAVVSSE--EVGVRKPDPEI 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47226791 150 FLVCASRFNppAAPEndwgndtRCLVFEDAPNG-VTAALAAGMQVVMIPDDNMDPALTREATLQLRSMEEFEPRL 223
Cdd:COG1011 155 FELALERLG--VPPE-------EALFVGDSPETdVAGARAAGMRTVWVNRSGEPAPAEPRPDYVISDLAELLELL 220
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 6-196 3.93e-14

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: 67.70  E-value: 3.93e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   6 VIFDMDGLLLDTERLYTVAFQEICDRFEkqytwavkssvmgrnaldacqiirdtldlpMTAEELLIeSRQILKRIFPsAK 85
Cdd:cd02598   2 VIFDLDGVITDTAEYHYRAWKKLADKEE------------------------------LAARKNRI-YVELIEELTP-VD 49

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791  86 LLPGVEKLVIHLQQHNIPIAVATSSEGVTFSLKTSQHKDFFgrfHHIVlgdDPD-VKNNKPLPDSFLVCASRFNPPAApe 164
Cdd:cd02598  50 VLPGIASLLVDLKAKGIKIALASASKNAPKILEKLGLAEYF---DAIV---DGAvLAKGKPDPDIFLAAAEGLGLNPK-- 121

                       170       180       190
                ....*....|....*....|....*....|..
gi 47226791 165 ndwgndtRCLVFEDAPNGVTAALAAGMQVVMI 196
Cdd:cd02598 122 -------DCIGVEDAQAGIRAIKAAGFLVVGV 146
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 6-197 1.11e-13

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: 67.02  E-value: 1.11e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   6 VIFDMDGLLLDTERLYTVAFQEIcdrFEKQY----TWAVK------SSVMGRNaldacQIIR----------DTLDLPMT 65
Cdd:cd07528   2 LIFDVDGTLAETEELHRRAFNNA---FFAERgldwYWDRElygellRVGGGKE-----RIAAyfekvgwpesAPKDLKEL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791  66 AEEL----------LIESRQIlkrifpsaKLLPGVEKLVIHLQQHNIPIAVATSS--EGVTFSLKTSQHKDFFGRFHHIV 133
Cdd:cd07528  74 IADLhkakteryaeLIAAGLL--------PLRPGVARLIDEAKAAGVRLAIATTTspANVDALLSALLGPERRAIFDAIA 145

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47226791 134 LGDDpdVKNNKPLPDSFLVCASRFNPPaaPENdwgndtrCLVFEDAPNGVTAALAAGMQVVMIP 197
Cdd:cd07528 146 AGDD--VAEKKPDPDIYLLALERLGVS--PSD-------CLAIEDSAIGLQAAKAAGLPCIVTP 198
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 7-197 5.42e-13

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 66.66  E-value: 5.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791    7 IFDMDGLLLDTER-LYTVAFQEICDRFE-KQYTWAV-------------------------KSSVMG--------RNAL- 50
Cdd:PLN02779  44 LFDCDGVLVETERdGHRVAFNDAFKEFGlRPVEWDVelydellnigggkermtwyfnengwPTSTIEkapkdeeeRKELv 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   51 DACQIiRDTlDLPMTaeelLIESRQIlkrifpsaKLLPGVEKLVIHLQQHNIPIAVATSS--EGVTFSLKTSQHKDFFGR 128
Cdd:PLN02779 124 DSLHD-RKT-ELFKE----LIESGAL--------PLRPGVLRLMDEALAAGIKVAVCSTSneKAVSKIVNTLLGPERAQG 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47226791  129 FHhIVLGDDpdVKNNKPLPDSFLVCASRFNPPAApendwgndtRCLVFEDAPNGVTAALAAGMQVVMIP 197
Cdd:PLN02779 190 LD-VFAGDD--VPKKKPDPDIYNLAAETLGVDPS---------RCVVVEDSVIGLQAAKAAGMRCIVTK 246
PRK10826 PRK10826
hexitol phosphatase HxpB;
2-224 2.46e-12

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 63.81  E-value: 2.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791    2 PVTHVIFDMDGLLLDTERLYtvafqeicDRFEKQytwavkssVMGRNALDACQI--IRDTLDL-------------PMTA 66
Cdd:PRK10826   6 QILAAIFDMDGLLIDSEPLW--------DRAELD--------VMASLGVDISRReeLPDTLGLridqvvdlwyarqPWNG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   67 EELLIESRQILKR----IFPSAKLLPGVEKLVIHLQQHNIPIAVATSS-----EGV--TFSLKTsqhkdffgRFHHIVLG 135
Cdd:PRK10826  70 PSRQEVVQRIIARvislIEETRPLLPGVREALALCKAQGLKIGLASASplhmlEAVltMFDLRD--------YFDALASA 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791  136 DDpdVKNNKPLPDSFLVCASRFNppAAPENdwgndtrCLVFEDAPNGVTAALAAGMQVVMIPddnmDPALTRE-----AT 210
Cdd:PRK10826 142 EK--LPYSKPHPEVYLNCAAKLG--VDPLT-------CVALEDSFNGMIAAKAARMRSIVVP----APEQQNDprwalAD 206

                        250
                 ....*....|....
gi 47226791  211 LQLRSMEEFEPRLF 224
Cdd:PRK10826 207 VKLESLTELTAADL 220
PRK11587 PRK11587
putative phosphatase; Provisional
 87-220 2.16e-10

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 58.47  E-value: 2.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   87 LPGVEKLVIHLQQHNIPIAVATSSegvTFSLKTSQHKdffgrfhhivLGDDPD---------VKNNKPLPDSFLVCASRF 157
Cdd:PRK11587  85 LPGAIALLNHLNKLGIPWAIVTSG---SVPVASARHK----------AAGLPApevfvtaerVKRGKPEPDAYLLGAQLL 151

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47226791  158 NppAAPENdwgndtrCLVFEDAPNGVTAALAAGMQVVMI--PDDNmdPALTrEATLQLRSMEEFE 220
Cdd:PRK11587 152 G--LAPQE-------CVVVEDAPAGVLSGLAAGCHVIAVnaPADT--PRLD-EVDLVLHSLEQLT 204
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 5-190 4.46e-08

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: 50.86  E-value: 4.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791     5 HVIFDMDGLLLDTERLYTVAFQEIcdrFEkQYTWAVKSSvmgrNALDACQIIRDTLDLPMTAEELLIESRQILKRIFPSA 84
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQT---FE-EFGLDPASF----KALKQAGGLAEEEWYRIATSALEELQGRFWSEYDAEE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791    85 KLLPGVEKLVIHLQQHNIPIAVATSSeGVTFSLKTSQHKDFFGRFHHIVLGDDPDVKNNkplPDSFLVCAsrfnppaape 164
Cdd:TIGR01549  73 AYIRGAADLLARLKSAGIKLGIISNG-SLRAQKLLLRLFGLGDYFELILVSDEPGSKPE---PEIFLAAL---------- 138

                         170       180
                  ....*....|....*....|....*.
gi 47226791   165 NDWGNDTRCLVFEDAPNGVTAALAAG 190
Cdd:TIGR01549 139 ESLGVPPEVLHVGDNLNDIEGARNAG 164
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 2-196 1.55e-07

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 51.39  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791     2 PVTHVIFDMDGLLLDTERLYTVAfqeICDRF-EKQYTWAVKSSV--MGR---NALDACQIIRDTLDL-PMTAEELLIESr 74
Cdd:PLN02919   74 KVSAVLFDMDGVLCNSEEPSRRA---AVDVFaEMGVEVTVEDFVpfMGTgeaNFLGGVASVKGVKGFdPDAAKKRFFEI- 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791    75 QILKRIFPSAKL-LPGVEKLVIHLQQHNIPIAVATSSEGVTFSLKTSQHKDFFGRFHHIVLGDDpdVKNNKPLPDSFLVC 153
Cdd:PLN02919  150 YLEKYAKPNSGIgFPGALELITQCKNKGLKVAVASSADRIKVDANLAAAGLPLSMFDAIVSADA--FENLKPAPDIFLAA 227

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 47226791   154 ASRFNPPAapendwgndTRCLVFEDAPNGVTAALAAGMQVVMI 196
Cdd:PLN02919  228 AKILGVPT---------SECVVIEDALAGVQAARAAGMRCIAV 261
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 3-194 2.54e-07

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 49.59  E-value: 2.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   3 VTHVIFDMDGLLLDTERLYTVAFQEICDRF--EKQYTWAVKSSVmGRNALDACQIIrdtldLPMTAEELLIESRQiLKRI 80
Cdd:cd02616   1 ITTILFDLDGTLIDTNELIIKSFNHTLKEYglEGYTREEVLPFI-GPPLRETFEKI-----DPDKLEDMVEEFRK-YYRE 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791  81 FPSA--KLLPGVEKLVIHLQQHNIPIAVATS--SEGVTFSLKTSQHKDFFgrfhHIVLGDDpDVKNNKPLPDSFLVCASR 156
Cdd:cd02616  74 HNDDltKEYPGVYETLARLKSQGIKLGVVTTklRETALKGLKLLGLDKYF----DVIVGGD-DVTHHKPDPEPVLKALEL 148

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 47226791 157 FNppAAPEndwgndtRCLVFEDAPNGVTAALAAGMQVV 194
Cdd:cd02616 149 LG--AEPE-------EALMVGDSPHDILAGKNAGVKTV 177
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 85-196 1.61e-06

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 47.72  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   85 KLLPGVEKLVIHLQQHNIPIAVAtSSEGVTFSLKTSQHKDFFGRFHHIVLGDdpDVKNNKPLPDSFLVCASRFNppAAPE 164
Cdd:PLN03243 109 RLRPGSREFVQALKKHEIPIAVA-STRPRRYLERAIEAVGMEGFFSVVLAAE--DVYRGKPDPEMFMYAAERLG--FIPE 183

                         90       100       110
                 ....*....|....*....|....*....|..
gi 47226791  165 ndwgndtRCLVFEDAPNGVTAALAAGMQVVMI 196
Cdd:PLN03243 184 -------RCIVFGNSNSSVEAAHDGCMKCVAV 208
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 2-225 6.52e-06

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 45.60  E-value: 6.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791    2 PVTHVIFDMDGLLLDTERLYTVAFQEICDrfEKQYTWAVK-------SSVMGRNALD-ACQIIRDTLDLPMTaeelLIES 73
Cdd:PLN02770  21 PLEAVLFDVDGTLCDSDPLHYYAFREMLQ--EINFNGGVPiteeffvENIAGKHNEDiALGLFPDDLERGLK----FTDD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   74 RQILKRIFPSAKLLP--GVEKLVIHLQQHNIPIAVATSSEGVTFSLKTSQH--KDFFgrfHHIVLGDDPDvkNNKPLPDS 149
Cdd:PLN02770  95 KEALFRKLASEQLKPlnGLYKLKKWIEDRGLKRAAVTNAPRENAELMISLLglSDFF---QAVIIGSECE--HAKPHPDP 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47226791  150 FLVCASRFNPpaapendwgNDTRCLVFEDAPNGVTAALAAGMQVVMIPDDNMDPALTR-EATLQLRSMEefEPRLFS 225
Cdd:PLN02770 170 YLKALEVLKV---------SKDHTFVFEDSVSGIKAGVAAGMPVVGLTTRNPESLLMEaKPTFLIKDYE--DPKLWA 235
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 6-193 1.55e-05

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 44.30  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791    6 VIFDMDGLLLDTE----RLYTVAFQ---------EICDRFEKQYTWAVKSSVMGRNALDACQiirdtldlpmtaEELLIE 72
Cdd:PRK10563   7 VFFDCDGTLVDSEvicsRAYVTMFAefgitlsleEVFKRFKGVKLYEIIDIISKEHGVTLAK------------AELEPV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   73 SRQILKRIFPSA-KLLPGVEKLvihLQQHNIPIAVAtsSEG----VTFSLKTSQHKDFFGrfHHIVLGddPDVKNNKPLP 147
Cdd:PRK10563  75 YRAEVARLFDSElEPIAGANAL---LESITVPMCVV--SNGpvskMQHSLGKTGMLHYFP--DKLFSG--YDIQRWKPDP 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 47226791  148 DSFLVCASRFNPPAApendwgndtRCLVFEDAPNGVTAALAAGMQV 193
Cdd:PRK10563 146 ALMFHAAEAMNVNVE---------NCILVDDSSAGAQSGIAAGMEV 182
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 3-198 2.05e-04

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: 40.79  E-value: 2.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   3 VTHVIFDMDGLLLDTerlytvAFQEICDRFEKQytwavkssvMGRNALDACQIIRDTLDLP------MTAEELLIESRQI 76
Cdd:cd02603   1 IRAVLFDFGGVLIDP------DPAAAVARFEAL---------TGEPSEFVLDTEGLAGAFLelergrITEEEFWEELREE 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791  77 LKR----------IFPSAKLLPGVEKLVIHLQQHNIPIAVATSSEGVTFSLKTSQHKDFFGRFHHIVLGDdpDVKNNKPL 146
Cdd:cd02603  66 LGRplsaelfeelVLAAVDPNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLPRRGDLFDGVVESC--RLGVRKPD 143

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 47226791 147 PDSFLVCASRFNppAAPEndwgndtRCLVFEDAPNGVTAALAAGMQVVMIPD 198
Cdd:cd02603 144 PEIYQLALERLG--VKPE-------EVLFIDDREENVEAARALGIHAILVTD 186
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 90-194 5.16e-03

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: 35.45  E-value: 5.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791  90 VEKLVIHLQQHNIPIAVATSSEGvTFSLKTSQHKDFFGRFHHIVLGDDpdVKNNKPLPDSFLVCASRFNPPAApendwgn 169
Cdd:cd01427  12 AVELLKRLRAAGIKLAIVTNRSR-EALRALLEKLGLGDLFDGIIGSDG--GGTPKPKPKPLLLLLLKLGVDPE------- 81

                        90       100
                ....*....|....*....|....*
gi 47226791 170 dtRCLVFEDAPNGVTAALAAGMQVV 194
Cdd:cd01427  82 --EVLFVGDSENDIEAARAAGGRTV 104
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 6-109 5.97e-03

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


Pssm-ID: 319799 [Multi-domain]  Cd Length: 201  Bit Score: 36.57  E-value: 5.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791   6 VIFDMDGLLLDTERLYTVAFQEICDRFekQYTWAVKSSVMGRNALDACQIIRDtLDLPM-TAEELLIESRQILKRIFPSA 84
Cdd:cd04303   2 IIFDFDGTLADSFPWFLSILNQLAARH--GFKTVDEEEIEQLRQLSSREILKQ-LGVPLwKLPLIAKDFRRLMAEAAPEL 78

                        90       100
                ....*....|....*....|....*
gi 47226791  85 KLLPGVEKLVIHLQQHNIPIAVATS 109
Cdd:cd04303  79 ALFPGVEDMLRALHARGVRLAVVSS 103
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-148 8.14e-03

haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes.


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 36.45  E-value: 8.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47226791     6 VIFDMDGLLLDTERLYTVAFQEICDRF-EKQYTWAVKSsvmGRNALDACQIIRDT-LDLPMTAE---ELLIESRQIL-KR 79
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLkEKGIKFVIAT---GRPYRAILPVIKELgLDDPVICYngaLIYDENGKILySN 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47226791    80 IFPSAKllpgVEKLVIHLQQHNIPIAVatSSEGVTFSLKTSQHKDFFGRFHHiVLGDDPDVKNNKPLPD 148
Cdd:pfam08282  78 PISKEA----VKEIIEYLKENNLEILL--YTDDGVYILNDNELEKILKELNY-TKSFVPEIDDFELLED 139
 
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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