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Conserved domains on  [gi|18423981|ref|NP_568858|]
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Haloacid dehalogenase-like hydrolase (HAD) superfamily protein [Arabidopsis thaliana]

Protein Classification

HAD family hydrolase( domain architecture ID 10791471)

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
PLN02811 PLN02811
hydrolase
 21-240 5.24e-167

hydrolase


:

Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 459.61  E-value: 5.24e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981   21 MDGLLLDTEKFYTEVQEIILARFNKKFDWSLKAKMMGRKAIEAARIFVEESGISDSLSAEDFLVERESMLQDLFPTSELM 100
Cdd:PLN02811   1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSDSLSPEDFLVEREAMLQDLFPTSDLM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  101 PGASRLIKHLHVKNIPICIATGTHTRHYDLKTQRHRELFSLMHHVVRGDDPEVKQGKPAPDGFLAAARRFKDGPVDSQKV 180
Cdd:PLN02811  81 PGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVTGDDPEVKQGKPAPDIFLAAARRFEDGPVDPGKV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  181 LVFEDAPSGVLAAKNAGMNVVMVPDPRLDISHQDVADQIITSLVDFKPEEWGLPPFEDSN 240
Cdd:PLN02811 161 LVFEDAPSGVEAAKNAGMSVVMVPDPRLDKSYCKGADQVLSSLLDFKPEEWGLPPFPDSS 220
 
Name Accession Description Interval E-value
PLN02811 PLN02811
hydrolase
 21-240 5.24e-167

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 459.61  E-value: 5.24e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981   21 MDGLLLDTEKFYTEVQEIILARFNKKFDWSLKAKMMGRKAIEAARIFVEESGISDSLSAEDFLVERESMLQDLFPTSELM 100
Cdd:PLN02811   1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSDSLSPEDFLVEREAMLQDLFPTSDLM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  101 PGASRLIKHLHVKNIPICIATGTHTRHYDLKTQRHRELFSLMHHVVRGDDPEVKQGKPAPDGFLAAARRFKDGPVDSQKV 180
Cdd:PLN02811  81 PGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVTGDDPEVKQGKPAPDIFLAAARRFEDGPVDPGKV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  181 LVFEDAPSGVLAAKNAGMNVVMVPDPRLDISHQDVADQIITSLVDFKPEEWGLPPFEDSN 240
Cdd:PLN02811 161 LVFEDAPSGVEAAKNAGMSVVMVPDPRLDKSYCKGADQVLSSLLDFKPEEWGLPPFPDSS 220
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 14-205 8.31e-116

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: 328.92  E-value: 8.31e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  14 ITHVIFDMDGLLLDTEKFYTEVQEIILARFNKKFDWSLKAKMMGRKAIEAARIFVEESGISDSLSaEDFLVERESMLQDL 93
Cdd:cd07529   1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLE-EEFDEQQEALAELF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  94 FPTSELMPGASRLIKHLHVKNIPICIATGTHTRHYDLKTQRHRELFSLMHHVVRGDDPEVKQ-GKPAPDGFLAAARRFKD 172
Cdd:cd07529  80 MGTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEVKGrGKPAPDIFLVAAKRFNE 159

                       170       180       190
                ....*....|....*....|....*....|...
gi 18423981 173 GPVDSQKVLVFEDAPSGVLAAKNAGMNVVMVPD 205
Cdd:cd07529 160 PPKDPSKCLVFEDSPNGVKAAKAAGMQVVMVPD 192
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
14-226 2.36e-56

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 178.48  E-value: 2.36e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  14 ITHVIFDMDGLLLDTEKFYTEVQEIILARFNKKFDWSLKAKMMGRKAIEAARIFVEESGIsdSLSAEDFLVERESMLQDL 93
Cdd:COG0637   2 IKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGL--DLPEEELAARKEELYREL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  94 FPTSE--LMPGASRLIKHLHVKNIPICIATGTHTRHYDLKTQRHrELFSLMHHVVRGDDpeVKQGKPAPDGFLAAARRFK 171
Cdd:COG0637  80 LAEEGlpLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAA-GLLDYFDVIVTGDD--VARGKPDPDIYLLAAERLG 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18423981 172 dgpVDSQKVLVFEDAPSGVLAAKNAGMNVVMVPDPRLDISHQDVADQIITSLVDF 226
Cdd:COG0637 157 ---VDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 14-203 4.00e-27

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: 102.81  E-value: 4.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981    14 ITHVIFDMDGLLLDTEKFYTEVQEIILARFNKKFDWSLKAKMMGRKAIEAARIFVEESGISDSLSAEDFLVERES-MLQD 92
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDGLSLEEIHQLAERKNeLYRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981    93 LFPT--SELMPGASRLIKHLHVKNIPICIATGTHTRHYDLKTQRHRELFSlmhhvVRGDDPEVKQGKPAPDGFLAAARRF 170
Cdd:TIGR02009  81 LLRLtgVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRDYFD-----AIVDASEVKNGKPHPETFLLAAELL 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 18423981   171 KdgpVDSQKVLVFEDAPSGVLAAKNAGMNVVMV 203
Cdd:TIGR02009 156 G---VPPNECIVFEDALAGVQAARAAGMFAVAV 185
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
17-203 1.32e-21

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 88.03  E-value: 1.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981    17 VIFDMDGLLLDTEKFYTEVQEIILARFNKKfDWSLK--AKMMGRKAIEAARIFVEESGISDSLsaeDFLVER--ESMLQD 92
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYG-ELSEEeiLKFIGLPLREIFRYLGVSEDEEEKI---EFYLRKynEELHDK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981    93 LFptsELMPGASRLIKHLHVKNIPICIATgthTRHYDLKTQRHRELF--SLMHHVVRGDDpeVKQGKPAPDGFLAAARRF 170
Cdd:pfam13419  77 LV---KPYPGIKELLEELKEQGYKLGIVT---SKSRENVEEFLKQLGleDYFDVIVGGDD--VEGKKPDPDPILKALEQL 148

                         170       180       190
                  ....*....|....*....|....*....|...
gi 18423981   171 KdgpVDSQKVLVFEDAPSGVLAAKNAGMNVVMV 203
Cdd:pfam13419 149 G---LKPEEVIYVGDSPRDIEAAKNAGIKVIAV 178
 
Name Accession Description Interval E-value
PLN02811 PLN02811
hydrolase
 21-240 5.24e-167

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 459.61  E-value: 5.24e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981   21 MDGLLLDTEKFYTEVQEIILARFNKKFDWSLKAKMMGRKAIEAARIFVEESGISDSLSAEDFLVERESMLQDLFPTSELM 100
Cdd:PLN02811   1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIFVEESGLSDSLSPEDFLVEREAMLQDLFPTSDLM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  101 PGASRLIKHLHVKNIPICIATGTHTRHYDLKTQRHRELFSLMHHVVRGDDPEVKQGKPAPDGFLAAARRFKDGPVDSQKV 180
Cdd:PLN02811  81 PGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQRHGELFSLMHHVVTGDDPEVKQGKPAPDIFLAAARRFEDGPVDPGKV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  181 LVFEDAPSGVLAAKNAGMNVVMVPDPRLDISHQDVADQIITSLVDFKPEEWGLPPFEDSN 240
Cdd:PLN02811 161 LVFEDAPSGVEAAKNAGMSVVMVPDPRLDKSYCKGADQVLSSLLDFKPEEWGLPPFPDSS 220
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 14-205 8.31e-116

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: 328.92  E-value: 8.31e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  14 ITHVIFDMDGLLLDTEKFYTEVQEIILARFNKKFDWSLKAKMMGRKAIEAARIFVEESGISDSLSaEDFLVERESMLQDL 93
Cdd:cd07529   1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVDELKLPMSLE-EEFDEQQEALAELF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  94 FPTSELMPGASRLIKHLHVKNIPICIATGTHTRHYDLKTQRHRELFSLMHHVVRGDDPEVKQ-GKPAPDGFLAAARRFKD 172
Cdd:cd07529  80 MGTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELFSLFHHVVTGDDPEVKGrGKPAPDIFLVAAKRFNE 159

                       170       180       190
                ....*....|....*....|....*....|...
gi 18423981 173 GPVDSQKVLVFEDAPSGVLAAKNAGMNVVMVPD 205
Cdd:cd07529 160 PPKDPSKCLVFEDSPNGVKAAKAAGMQVVMVPD 192
PLN02940 PLN02940
riboflavin kinase
 14-238 5.98e-57

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 185.81  E-value: 5.98e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981   14 ITHVIFDMDGLLLDTEKFYTEVQEIILARFNKKFDWSLKAKMMGRKAIEAARIFVEESGIsdSLSAEDFLVERESMLQDL 93
Cdd:PLN02940  11 VSHVILDLDGTLLNTDGIVSDVLKAFLVKYGKQWDGREAQKIVGKTPLEAAATVVEDYGL--PCSTDEFNSEITPLLSEQ 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981   94 FPTSELMPGASRLIKHLHVKNIPICIATGTHTRHYDLKTQRH---RELFSLmhhVVRGDdpEVKQGKPAPDGFLAAARRF 170
Cdd:PLN02940  89 WCNIKALPGANRLIKHLKSHGVPMALASNSPRANIEAKISCHqgwKESFSV---IVGGD--EVEKGKPSPDIFLEAAKRL 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18423981  171 KDGPVdsqKVLVFEDAPSGVLAAKNAGMNVVMVPD-PRLDISHQDvADQIITSLVDFKPEEWGLPPFED 238
Cdd:PLN02940 164 NVEPS---NCLVIEDSLPGVMAGKAAGMEVIAVPSiPKQTHLYSS-ADEVINSLLDLQPEKWGLPPFND 228
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
14-226 2.36e-56

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 178.48  E-value: 2.36e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  14 ITHVIFDMDGLLLDTEKFYTEVQEIILARFNKKFDWSLKAKMMGRKAIEAARIFVEESGIsdSLSAEDFLVERESMLQDL 93
Cdd:COG0637   2 IKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLLEEYGL--DLPEEELAARKEELYREL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  94 FPTSE--LMPGASRLIKHLHVKNIPICIATGTHTRHYDLKTQRHrELFSLMHHVVRGDDpeVKQGKPAPDGFLAAARRFK 171
Cdd:COG0637  80 LAEEGlpLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAA-GLLDYFDVIVTGDD--VARGKPDPDIYLLAAERLG 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18423981 172 dgpVDSQKVLVFEDAPSGVLAAKNAGMNVVMVPDPRLDISHQDVADQIITSLVDF 226
Cdd:COG0637 157 ---VDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 17-205 2.46e-34

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: 120.03  E-value: 2.46e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  17 VIFDMDGLLLDTEKFYTEVqeiilarfnkkfdWSLKAKmmgRKAIEAARIFVEESgisdslsaedflveresmlqdlfpt 96
Cdd:cd07505   2 VIFDMDGVLIDTEPLHRQA-------------WQLLER---KNALLLELIASEGL------------------------- 40

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  97 sELMPGASRLIKHLHVKNIPICIATGTHTRHYDLKTQRHRELFSLMHHVVRGDDpeVKQGKPAPDGFLAAARRFKdgpVD 176
Cdd:cd07505  41 -KLKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLRGYFDVIVSGDD--VERGKPAPDIYLLAAERLG---VD 114

                       170       180
                ....*....|....*....|....*....
gi 18423981 177 SQKVLVFEDAPSGVLAAKNAGMNVVMVPD 205
Cdd:cd07505 115 PERCLVFEDSLAGIEAAKAAGMTVVAVPD 143
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 14-203 4.00e-27

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: 102.81  E-value: 4.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981    14 ITHVIFDMDGLLLDTEKFYTEVQEIILARFNKKFDWSLKAKMMGRKAIEAARIFVEESGISDSLSAEDFLVERES-MLQD 92
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDGLSLEEIHQLAERKNeLYRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981    93 LFPT--SELMPGASRLIKHLHVKNIPICIATGTHTRHYDLKTQRHRELFSlmhhvVRGDDPEVKQGKPAPDGFLAAARRF 170
Cdd:TIGR02009  81 LLRLtgVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRDYFD-----AIVDASEVKNGKPHPETFLLAAELL 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 18423981   171 KdgpVDSQKVLVFEDAPSGVLAAKNAGMNVVMV 203
Cdd:TIGR02009 156 G---VPPNECIVFEDALAGVQAARAAGMFAVAV 185
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 17-225 9.77e-27

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: 101.18  E-value: 9.77e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  17 VIFDMDGLLLDTEK-FYTEVQEIILARFNKKFdwslkakmmgrkaieaARIFVEESGIsdslsaedflveresmlqdlfp 95
Cdd:cd16423   2 VIFDFDGVIVDTEPlWYEAWQELLNERRNELI----------------KRQFSEKTDL---------------------- 43

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  96 tsELMPGASRLIKHLHVKNIPICIATGThTRHYDLKTQRHRELFSLMHHVVRGDDpeVKQGKPAPDGFLAAARRFKdgpV 175
Cdd:cd16423  44 --PPIEGVKELLEFLKEKGIKLAVASSS-PRRWIEPHLERLGLLDYFEVIVTGDD--VEKSKPDPDLYLEAAERLG---V 115

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 18423981 176 DSQKVLVFEDAPSGVLAAKNAGMNVVMVPDPRLDISHQDVADQIITSLVD 225
Cdd:cd16423 116 NPEECVVIEDSRNGVLAAKAAGMKCVGVPNPVTGSQDFSKADLVLSSFAE 165
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 16-203 9.60e-26

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: 99.03  E-value: 9.60e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981    16 HVIFDMDGLLLDTEKFYTEVQEIILARFnkkFDWSLKAKMMGRkAIEAARIFVEESGisDSLSAEDF-LVERESMLQDLF 94
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAIAKLINREELGL---VPDELGVSAVGR-LELALRRFKAQYG--RTISPEDAqLLYKQLFYEQIE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981    95 PTSEL--MPGASRLIKHLHVKNIPICIATGTHTRHydLKTQRHRELFSLMHHVVRGDDpeVKQGKPAPDGFLAAARRFKd 172
Cdd:TIGR01509  75 EEAKLkpLPGVRALLEALRARGKKLALLTNSPRAH--KLVLALLGLRDLFDVVIDSSD--VGLGKPDPDIYLQALKALG- 149

                         170       180       190
                  ....*....|....*....|....*....|.
gi 18423981   173 gpVDSQKVLVFEDAPSGVLAAKNAGMNVVMV 203
Cdd:TIGR01509 150 --LEPSECVFVDDSPAGIEAAKAAGMHTVGV 178
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
14-203 1.65e-22

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 91.53  E-value: 1.65e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  14 ITHVIFDMDGLLLDTEKFYTEVQEIILARFN-KKFDWSLKAKMMGRKAIEAARIFVeesGISDSLSAEDFLVE-RESMLQ 91
Cdd:COG0546   1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGlPPLDLEELRALIGLGLRELLRRLL---GEDPDEELEELLARfRELYEE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  92 DLFPTSELMPGASRLIKHLHVKNIPICIATGTHTRHYDLKTQRHrELFSLMHHVVRGDDpeVKQGKPAPDGFLAAARRFK 171
Cdd:COG0546  78 ELLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEAL-GLDDYFDAIVGGDD--VPPAKPKPEPLLEALERLG 154

                       170       180       190
                ....*....|....*....|....*....|..
gi 18423981 172 dgpVDSQKVLVFEDAPSGVLAAKNAGMNVVMV 203
Cdd:COG0546 155 ---LDPEEVLMVGDSPHDIEAARAAGVPFIGV 183
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 17-225 3.40e-22

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: 90.48  E-value: 3.40e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  17 VIFDMDGLLLDTekfyTEVQEIILARFNKKFDWSLKAKMM---GRKAIEAARIFVEESGISDSLSA-EDFLVEresmlqD 92
Cdd:cd07527   2 LLFDMDGTLVDS----TPAVERAWHKWAKEHGVDPEEVLKvshGRRAIDVIRKLAPDDADIELVLAlETEEPE------S 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  93 LFPTSELMPGASRLIKHLHVKNIPICIAT-GTHtrhyDLKTQRHrELFSLMH--HVVRGDDpeVKQGKPAPDGFLAAARR 169
Cdd:cd07527  72 YPEGVIAIPGAVDLLASLPAAGDRWAIVTsGTR----ALAEARL-EAAGLPHpeVLVTADD--VKNGKPDPEPYLLGAKL 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18423981 170 fkdGPVDSQKVLVFEDAPSGVLAAKNAGMNVVMV-PDPRLDISHQDVADQIITSLVD 225
Cdd:cd07527 145 ---LGLDPSDCVVFEDAPAGIKAGKAAGARVVAVnTSHDLEQLEAAGADLVVEDLSD 198
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
17-203 1.32e-21

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 88.03  E-value: 1.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981    17 VIFDMDGLLLDTEKFYTEVQEIILARFNKKfDWSLK--AKMMGRKAIEAARIFVEESGISDSLsaeDFLVER--ESMLQD 92
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYG-ELSEEeiLKFIGLPLREIFRYLGVSEDEEEKI---EFYLRKynEELHDK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981    93 LFptsELMPGASRLIKHLHVKNIPICIATgthTRHYDLKTQRHRELF--SLMHHVVRGDDpeVKQGKPAPDGFLAAARRF 170
Cdd:pfam13419  77 LV---KPYPGIKELLEELKEQGYKLGIVT---SKSRENVEEFLKQLGleDYFDVIVGGDD--VEGKKPDPDPILKALEQL 148

                         170       180       190
                  ....*....|....*....|....*....|...
gi 18423981   171 KdgpVDSQKVLVFEDAPSGVLAAKNAGMNVVMV 203
Cdd:pfam13419 149 G---LKPEEVIYVGDSPRDIEAAKNAGIKVIAV 178
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 14-197 5.19e-21

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: 86.87  E-value: 5.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981    14 ITHVIFDMDGLLLDTEKFYTEV----------QEIILARFNKKF----DWSLKAKMMGRKAIEAARIFVEESGISDSLSA 79
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAiaelasehplAKAIVAAAEDLPipveDFTARLLLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981    80 EDFLVERESMLQdLFPTSELMPGASRLIKHLHVKNIPICIATGTHTRHYDlKTQRHRELFSLMHHVVRGDDpeVKQGKPA 159
Cdd:pfam00702  81 TVVLVELLGVIA-LADELKLYPGAAEALKALKERGIKVAILTGDNPEAAE-ALLRLLGLDDYFDVVISGDD--VGVGKPK 156

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 18423981   160 PDGFLAAARRFKdgpVDSQKVLVFEDAPSGVLAAKNAG 197
Cdd:pfam00702 157 PEIYLAALERLG---VKPEEVLMVGDGVNDIPAAKAAG 191
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 17-223 6.78e-18

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: 78.10  E-value: 6.78e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  17 VIFDMDGLLLDTEKFYtevqeiiLARFNKKFDwslKAKMMGRKAieaaRIFVEesgisdslsaedflveresMLQDLFPT 96
Cdd:cd02598   2 VIFDLDGVITDTAEYH-------YRAWKKLAD---KEELAARKN----RIYVE-------------------LIEELTPV 48

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  97 SELmPGASRLIKHLHVKNIPICIATgtHTRHYDlKTQRHRELFSLMHHVVRGDdpEVKQGKPAPDGFLAAARRFKdgpVD 176
Cdd:cd02598  49 DVL-PGIASLLVDLKAKGIKIALAS--ASKNAP-KILEKLGLAEYFDAIVDGA--VLAKGKPDPDIFLAAAEGLG---LN 119

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 18423981 177 SQKVLVFEDAPSGVLAAKNAGMNVVMVPDPRLDIShqdvADQIITSL 223
Cdd:cd02598 120 PKDCIGVEDAQAGIRAIKAAGFLVVGVGREEDLLG----ADIVVPDT 162
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 14-227 7.02e-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: 73.91  E-value: 7.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  14 ITHVIFDMDGLLLDTEKFYTEVQEIILARFNKKFD--------WSLKAKMMGRKAI------EAARIFVEESGISDSLSA 79
Cdd:COG1011   1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEaeelaeayRAIEYALWRRYERgeitfaELLRRLLEELGLDLAEEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  80 EDFLVERESMLQDLFPtselmpGASRLIKHLHVKNIPICIATGTHTRHYDLKTQRHrELFSLMHHVVRGDdpEVKQGKPA 159
Cdd:COG1011  81 AEAFLAALPELVEPYP------DALELLEALKARGYRLALLTNGSAELQEAKLRRL-GLDDLFDAVVSSE--EVGVRKPD 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18423981 160 PDGFLAAARRFKdgpVDSQKVLVFEDAPSG-VLAAKNAGMNVVMVPDPRLDISHQDVADQIITSLVDFK 227
Cdd:COG1011 152 PEIFELALERLG---VPPEEALFVGDSPETdVAGARAAGMRTVWVNRSGEPAPAEPRPDYVISDLAELL 217
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
18-203 1.98e-15

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 72.03  E-value: 1.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981   18 IFDMDGLLLDTEKFYTEVQEIILARFNKKFDwslKAKMMGRKAIEAARI--FVEESGISD----SLSAEDfLVERESMLQ 91
Cdd:PRK10725   9 IFDMDGTILDTEPTHRKAWREVLGRYGLQFD---EQAMVALNGSPTWRIaqAIIELNQADldphALAREK-TEAVKSMLL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981   92 DlfpTSELMPGASrLIKHLHVKNiPICIATGTHTRHYDlKTQRHRELFSLMHHVVRGDDpeVKQGKPAPDGFLAAARRFK 171
Cdd:PRK10725  85 D---SVEPLPLIE-VVKAWHGRR-PMAVGTGSESAIAE-ALLAHLGLRRYFDAVVAADD--VQHHKPAPDTFLRCAQLMG 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 18423981  172 dgpVDSQKVLVFEDAPSGVLAAKNAGMNVVMV 203
Cdd:PRK10725 157 ---VQPTQCVVFEDADFGIQAARAAGMDAVDV 185
PRK11587 PRK11587
putative phosphatase; Provisional
 100-223 6.12e-14

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 68.48  E-value: 6.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  100 MPGASRLIKHLHVKNIPICIAT-GT----HTRHydlktqrhrelfslmhHVVRGDDPE-------VKQGKPAPDGFLAAA 167
Cdd:PRK11587  85 LPGAIALLNHLNKLGIPWAIVTsGSvpvaSARH----------------KAAGLPAPEvfvtaerVKRGKPEPDAYLLGA 148

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18423981  168 RRFKDGPvdsQKVLVFEDAPSGVLAAKNAGMNVVMVPDPrLDISHQDVADQIITSL 223
Cdd:PRK11587 149 QLLGLAP---QECVVVEDAPAGVLSGLAAGCHVIAVNAP-ADTPRLDEVDLVLHSL 200
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 17-204 1.16e-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: 67.40  E-value: 1.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  17 VIFDMDGLLLDTEK-----------------------FYTEVQEII-----LARFNKKFDWSLKAKMMGRKAIEA----- 63
Cdd:cd07528   2 LIFDVDGTLAETEElhrrafnnaffaergldwywdreLYGELLRVGggkerIAAYFEKVGWPESAPKDLKELIADlhkak 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  64 ARIFVEesgisdslsaedfLVERESMlqdlfptsELMPGASRLIKHLHVKNIPICIATGTHTRHYDLKTQR-----HREL 138
Cdd:cd07528  82 TERYAE-------------LIAAGLL--------PLRPGVARLIDEAKAAGVRLAIATTTSPANVDALLSAllgpeRRAI 140

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18423981 139 FSLmhhVVRGDDpeVKQGKPAPDGFLAAARRFKdgpVDSQKVLVFEDAPSGVLAAKNAGMNVVMVP 204
Cdd:cd07528 141 FDA---IAAGDD--VAEKKPDPDIYLLALERLG---VSPSDCLAIEDSAIGLQAAKAAGLPCIVTP 198
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 17-200 3.10e-13

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: 64.65  E-value: 3.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  17 VIFDMDGLLLDTEkfytevqeiilarfnkkfdwslkakmmgrkaIEAARIFVEESGISDSLSAEDFLVEresmlqdlfpt 96
Cdd:cd07526   3 VIFDCDGVLVDSE-------------------------------VIAARVLVEVLAELGARVLAAFEAE----------- 40

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  97 SELMPGASRLIKHLhvkNIPICIATGTHTRHYDLKTQRHRELFSLMHHVVRGDDpeVKQGKPAPDGFLAAARRFKdgpVD 176
Cdd:cd07526  41 LQPIPGAAAALSAL---TLPFCVASNSSRERLTHSLGLAGLLAYFEGRIFSASD--VGRGKPAPDLFLHAAAQMG---VA 112

                       170       180
                ....*....|....*....|....
gi 18423981 177 SQKVLVFEDAPSGVLAAKNAGMNV 200
Cdd:cd07526 113 PERCLVIEDSPTGVRAALAAGMTV 136
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 16-197 3.65e-12

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 62.41  E-value: 3.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981    16 HVIFDMDGLLLDtekfYTEVQEIILARFNKKFDWSLKAKmmgrKAIEAARIFVEEsgISDSLSAEDFLVERESMLQDLFP 95
Cdd:TIGR01549   1 AILFDIDGTLVD----IKFAIRRAFPQTFEEFGLDPASF----KALKQAGGLAEE--EWYRIATSALEELQGRFWSEYDA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981    96 TSELMPGASRLIKHLHVKNIPICIATGTHTRHYDLKTqRHRELFSLMHHVVRGDDPevkQGKPAPDGFLAAARRFKDGPv 175
Cdd:TIGR01549  71 EEAYIRGAADLLARLKSAGIKLGIISNGSLRAQKLLL-RLFGLGDYFELILVSDEP---GSKPEPEIFLAALESLGVPP- 145

                         170       180
                  ....*....|....*....|..
gi 18423981   176 dsqKVLVFEDAPSGVLAAKNAG 197
Cdd:TIGR01549 146 ---EVLHVGDNLNDIEGARNAG 164
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 14-206 1.34e-09

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: 55.81  E-value: 1.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  14 ITHVIFDMDGLLLD------TEKFYTEVQEIILARFNKKFDWSLKAKMM-GRK-AIEAARIFVEESGISDSlsaEDFLVE 85
Cdd:cd02603   1 IRAVLFDFGGVLIDpdpaaaVARFEALTGEPSEFVLDTEGLAGAFLELErGRItEEEFWEELREELGRPLS---AELFEE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  86 RESMLQDLFptselmPGASRLIKHLHVKNIPICIATGTHTRHYDLKTQRHRELFSLMHHVVRGDDpeVKQGKPAPDGFLA 165
Cdd:cd02603  78 LVLAAVDPN------PEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLPRRGDLFDGVVESCR--LGVRKPDPEIYQL 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 18423981 166 AARRFKdgpVDSQKVLVFEDAPSGVLAAKNAGMNVVMVPDP 206
Cdd:cd02603 150 ALERLG---VKPEEVLFIDDREENVEAARALGIHAILVTDA 187
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 18-206 5.07e-08

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 52.40  E-value: 5.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981   18 IFDMDGLLLDTEKFytevqeiiLAR--FNKKF--------DWSL------------KAKM------MGRKAIEAARIFVE 69
Cdd:PLN02779  44 LFDCDGVLVETERD--------GHRvaFNDAFkefglrpvEWDVelydellnigggKERMtwyfneNGWPTSTIEKAPKD 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981   70 ESGIS---DSLSA---EDF--LVERESMlqdlfptsELMPGASRLIKHLHVKNIP--ICIATGTHTRHYDLKTQRHRELF 139
Cdd:PLN02779 116 EEERKelvDSLHDrktELFkeLIESGAL--------PLRPGVLRLMDEALAAGIKvaVCSTSNEKAVSKIVNTLLGPERA 187

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18423981  140 SLMHhVVRGDDpeVKQGKPAPDGFLAAARRFKdgpVDSQKVLVFEDAPSGVLAAKNAGMNVVMVPDP 206
Cdd:PLN02779 188 QGLD-VFAGDD--VPKKKPDPDIYNLAAETLG---VDPSRCVVVEDSVIGLQAAKAAGMRCIVTKSS 248
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 70-227 2.11e-07

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 50.42  E-value: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981   70 ESGISDSLS-AEDFL-VERESML-QDLFP-----TSELMPGASRLIKHLHVKNIPICIATgTHTRHYDLKTQRHRELFSL 141
Cdd:PLN03243  73 EQAISEVLCwSRDFLqMKRLAIRkEDLYEymqggLYRLRPGSREFVQALKKHEIPIAVAS-TRPRRYLERAIEAVGMEGF 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  142 MHHVVRGDDpeVKQGKPAPDGFLAAARRFKDGPvdsQKVLVFEDAPSGVLAAKNAGMNVVMVP--DPRLDISHQDVADQI 219
Cdd:PLN03243 152 FSVVLAAED--VYRGKPDPEMFMYAAERLGFIP---ERCIVFGNSNSSVEAAHDGCMKCVAVAgkHPVYELSAGDLVVRR 226

                        170
                 ....*....|
gi 18423981  220 IT--SLVDFK 227
Cdd:PLN03243 227 LDdlSVVDLK 236
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 17-225 1.44e-06

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: 47.61  E-value: 1.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  17 VIFDMDGLLLDTEKFYTEVQEIILARFNKK-FDWSLKAKMMGRkaieAARIFVEESgISDSLSAED----FLVERESML- 90
Cdd:cd16417   2 VAFDLDGTLVDSAPDLAEAANAMLAALGLPpLPEETVRTWIGN----GADVLVERA-LTGAREAEPdeelFKEARALFDr 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  91 ---QDLFPTSELMPGASRLIKHLHVKNIPICIATGTHTRH-YDLKTQRH-RELFSLmhhVVRGDDpeVKQGKPAPDGFLA 165
Cdd:cd16417  77 hyaETLSVHSHLYPGVKEGLAALKAQGYPLACVTNKPERFvAPLLEALGiSDYFSL---VLGGDS--LPEKKPDPAPLLH 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18423981 166 AARRFKdgpVDSQKVLVFEDAPSGVLAAKNAGMNVVMVP----DPRlDISHQDvADQIITSLVD 225
Cdd:cd16417 152 ACEKLG---IAPAQMLMVGDSRNDILAARAAGCPSVGLTygynYGE-DIAASG-PDAVIDSLAE 210
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 14-203 2.88e-06

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: 46.50  E-value: 2.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  14 ITHVIFDMDGLLLDTekfytevQEIILARFNKKFD------WSLKA--KMMGRKAIEAARIFVEESGISdslSAEDFLVE 85
Cdd:cd02616   1 ITTILFDLDGTLIDT-------NELIIKSFNHTLKeyglegYTREEvlPFIGPPLRETFEKIDPDKLED---MVEEFRKY 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  86 RESMLQDLfptSELMPGASRLIKHLHVKNIPICIATgthTRHYDL--KTQRHRELFSLMHHVVRGDDpeVKQGKPAPDGF 163
Cdd:cd02616  71 YREHNDDL---TKEYPGVYETLARLKSQGIKLGVVT---TKLRETalKGLKLLGLDKYFDVIVGGDD--VTHHKPDPEPV 142

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 18423981 164 LAAARRFKDGPvdsQKVLVFEDAPSGVLAAKNAGMNVVMV 203
Cdd:cd02616 143 LKALELLGAEP---EEALMVGDSPHDILAGKNAGVKTVGV 179
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 103-203 1.08e-05

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: 1.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981 103 ASRLIKHLHVKNIPICIATGTHTRHYDlKTQRHRELFSLMHHVVRGDDpeVKQGKPAPDGFLAAARRFKdgpVDSQKVLV 182
Cdd:cd01427  12 AVELLKRLRAAGIKLAIVTNRSREALR-ALLEKLGLGDLFDGIIGSDG--GGTPKPKPKPLLLLLLKLG---VDPEEVLF 85

                        90       100
                ....*....|....*....|.
gi 18423981 183 FEDAPSGVLAAKNAGMNVVMV 203
Cdd:cd01427  86 VGDSENDIEAARAAGGRTVAV 106
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 18-202 1.49e-05

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the uncharacterized Lactococcus lactis YsbA; The specific function of Lactococcus lactis YsbA is unknown. 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, 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: 319825 [Multi-domain]  Cd Length: 173  Bit Score: 43.91  E-value: 1.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  18 IFDMDGLLLDTEKFYTEVQEIILARFNKKFDWSLKAKMMGRKAIEAARIFVEESgisdslsaEDFLVERESMLQDLFPTS 97
Cdd:cd07523   3 IWDLDGTLLDSYPAMTKALSETLADFGIPQDLETVYKIIKESSVQFAIQYYAEV--------PDLEEEYKELEAEYLAKP 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  98 ELMPGASRLIKHLHVKNIPICIAtgTHTRHYDLKTQRHRELFSLMHHVVRGDDPEVKqgKPAPDGFLAAARRFKdgpVDS 177
Cdd:cd07523  75 ILFPGAKAVLRWIKEQGGKNFLM--THRDHSALTILKKDGIASYFTEIVTSDNGFPR--KPNPEAINYLLNKYQ---LNP 147

                       170       180
                ....*....|....*....|....*
gi 18423981 178 QKVLVFEDAPSGVLAAKNAGMNVVM 202
Cdd:cd07523 148 EETVMIGDRELDIEAGHNAGISTIL 172
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 157-203 3.71e-05

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 44.46  E-value: 3.71e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 18423981   157 KPAPDGFLAAARRFKdgpVDSQKVLVFEDAPSGVLAAKNAGMNVVMV 203
Cdd:PLN02919  218 KPAPDIFLAAAKILG---VPTSECVVIEDALAGVQAARAAGMRCIAV 261
PRK10826 PRK10826
hexitol phosphatase HxpB;
13-229 7.25e-05

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 42.63  E-value: 7.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981   13 SITHVIFDMDGLLLDTEKFYTEVQEIILARFN-------------------------KKFDWS--LKAKMMGR---KAIE 62
Cdd:PRK10826   6 QILAAIFDMDGLLIDSEPLWDRAELDVMASLGvdisrreelpdtlglridqvvdlwyARQPWNgpSRQEVVQRiiaRVIS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981   63 aariFVEESGisdslsaedflveresmlqdlfptsELMPGASRLIKHLHVKNIPICIATG--THTRHYDLKTQRHRELFS 140
Cdd:PRK10826  86 ----LIEETR-------------------------PLLPGVREALALCKAQGLKIGLASAspLHMLEAVLTMFDLRDYFD 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  141 LMH---HVVRGddpevkqgKPAPDGFLAAARRFKdgpVDSQKVLVFEDAPSGVLAAKNAGMNVVMVPDPrldiSHQD--- 214
Cdd:PRK10826 137 ALAsaeKLPYS--------KPHPEVYLNCAAKLG---VDPLTCVALEDSFNGMIAAKAARMRSIVVPAP----EQQNdpr 201

                        250
                 ....*....|....*..
gi 18423981  215 --VADQIITSLVDFKPE 229
Cdd:PRK10826 202 waLADVKLESLTELTAA 218
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
17-229 1.89e-04

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 41.33  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981   17 VIFDMDGLLLDTekfyteVQEIILArfnkkFDWSLKAkmMGRKAIEA----------ARIFVEE--SGISDSLSAEDFLV 84
Cdd:PRK13222   9 VAFDLDGTLVDS------APDLAAA-----VNAALAA--LGLPPAGEervrtwvgngADVLVERalTWAGREPDEELLEK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981   85 ERESML----QDLFPTSELMPGASRLIKHLHVKNIPICIATGTHTR-------HYDLktqrhRELFSLmhhVVRGDDpeV 153
Cdd:PRK13222  76 LRELFDrhyaENVAGGSRLYPGVKETLAALKAAGYPLAVVTNKPTPfvaplleALGI-----ADYFSV---VIGGDS--L 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981  154 KQGKPAPDGFLAAARRFkdgPVDSQKVLVFEDAPSGVLAAKNAGMNVVMVP----DPRlDISHQDvADQIITSLVDFKPE 229
Cdd:PRK13222 146 PNKKPDPAPLLLACEKL---GLDPEEMLFVGDSRNDIQAARAAGCPSVGVTygynYGE-PIALSE-PDVVIDHFAELLPL 220
Hydrolase_like pfam13242
HAD-hyrolase-like;
156-225 2.20e-04

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 38.75  E-value: 2.20e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18423981   156 GKPAPDGFLAAARRFKdgpVDSQKVLVFEDAP-SGVLAAKNAGMNVVMV------PDPRLDISHQdvADQIITSLVD 225
Cdd:pfam13242   3 GKPNPGMLERALARLG---LDPERTVMIGDRLdTDILGAREAGARTILVltgvtrPADLEKAPIR--PDYVVDDLAE 74
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 13-200 7.53e-04

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 39.68  E-value: 7.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981   13 SITHVIFDMDGLLLDTEKFYTEVQEIILARFNKKFDWS-LKAKMMGRKAIEAARIFVEESGIsdSLSAEDF-LVERESML 90
Cdd:PRK10563   3 QIEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLSLEeVFKRFKGVKLYEIIDIISKEHGV--TLAKAELePVYRAEVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981   91 QdLFPTS-ELMPGASRLIKHLHVkniPICIAT-GTHTrhydlKTQRHRELFSLMHH----VVRGDDpeVKQGKPAPDGFL 164
Cdd:PRK10563  81 R-LFDSElEPIAGANALLESITV---PMCVVSnGPVS-----KMQHSLGKTGMLHYfpdkLFSGYD--IQRWKPDPALMF 149

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 18423981  165 AAARRFKdgpVDSQKVLVFEDAPSGVLAAKNAGMNV 200
Cdd:PRK10563 150 HAAEAMN---VNVENCILVDDSSAGAQSGIAAGMEV 182
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 156-203 1.61e-03

inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP); LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. 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, 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: 319812 [Multi-domain]  Cd Length: 248  Bit Score: 38.80  E-value: 1.61e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 18423981 156 GKPAPDGFLAAARRFKDGPvdSQKVLVFEDAPSGVLAAKNAGMNVVMV 203
Cdd:cd07509 171 GKPSPEFFLSALRSLGVDP--EEAVMIGDDLRDDVGGAQACGMRGILV 216
HAD pfam12710
haloacid dehalogenase-like hydrolase;
17-157 2.51e-03

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 37.90  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18423981    17 VIFDMDGLLLDTE------KFYTEVQEIILARFNKKFDWSLKAKMMGRKAIEAARIFVEESgisDSLSAEDFLVERESML 90
Cdd:pfam12710   1 ALFDLDGTLLDGDslflliRALLRRGGPDLWRALLVLLLLALLRLLGRLSRAGARELLRAL---LAGLPEEDAAELERFV 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18423981    91 QDLFpTSELMPGASRLIKHLHVKNIPICIATGTHTRHYDLKTQRhrelfsLMHHVVRGDDPEVKQGK 157
Cdd:pfam12710  78 AEVA-LPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAE------LGFDEVLATELEVDDGR 137
 
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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