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Conserved domains on  [gi|1440323440|emb|STW45815|]
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phosphatase YieH [Klebsiella variicola]

Protein Classification

6-phosphogluconate phosphatase( domain architecture ID 10793419)

6-phosphogluconate phosphatase catalyzes strongly the dephosphorylation of 6-phosphogluconate (6P-Glu) and slightly the dephosphorylation of dihydroxyacetone phosphate (DHAP) and phosphoenolpyruvate (PEP); also hydrolyzes both purines (GMP and IMP) and pyrimidines as secondary substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 1-221 0e+00

6-phosphogluconate phosphatase; Provisional


:

Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 495.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   1 MTQPEAVFFDCDGTLVDSEVICSRAYVHMFQEFGITLDLAEIFKRFKGVKLYEIIDTINVEHGVNLQKATLEPIYRAEVA 80
Cdd:PRK10563    1 MSQIEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLSLEEVFKRFKGVKLYEIIDIISKEHGVTLAKAELEPVYRAEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  81 RLFDSELEVIAGAQALLDAVSVPMCVVSNGPVSKMQHSLGRTGLLHHFADRLYSGYDIQRWKPDPALMFHAAEAMQVKAE 160
Cdd:PRK10563   81 RLFDSELEPIAGANALLESITVPMCVVSNGPVSKMQHSLGKTGMLHYFPDKLFSGYDIQRWKPDPALMFHAAEAMNVNVE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1440323440 161 NCILVDDSSAGAQSGIAAGMEVFYFCADPHNQPIDHPKVTTFTDLAELPALWQARGWDITR 221
Cdd:PRK10563  161 NCILVDDSSAGAQSGIAAGMEVFYFCADPHNKPIDHPLVTTFTDLAQLPELWKARGWDITR 221
 
Name Accession Description Interval E-value
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 1-221 0e+00

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 495.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   1 MTQPEAVFFDCDGTLVDSEVICSRAYVHMFQEFGITLDLAEIFKRFKGVKLYEIIDTINVEHGVNLQKATLEPIYRAEVA 80
Cdd:PRK10563    1 MSQIEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLSLEEVFKRFKGVKLYEIIDIISKEHGVTLAKAELEPVYRAEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  81 RLFDSELEVIAGAQALLDAVSVPMCVVSNGPVSKMQHSLGRTGLLHHFADRLYSGYDIQRWKPDPALMFHAAEAMQVKAE 160
Cdd:PRK10563   81 RLFDSELEPIAGANALLESITVPMCVVSNGPVSKMQHSLGKTGMLHYFPDKLFSGYDIQRWKPDPALMFHAAEAMNVNVE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1440323440 161 NCILVDDSSAGAQSGIAAGMEVFYFCADPHNQPIDHPKVTTFTDLAELPALWQARGWDITR 221
Cdd:PRK10563  161 NCILVDDSSAGAQSGIAAGMEVFYFCADPHNKPIDHPLVTTFTDLAQLPELWKARGWDITR 221
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 5-187 4.48e-66

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: 200.24  E-value: 4.48e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   5 EAVFFDCDGTLVDSEVICSRAYVHMFQEFGitldlaeifkrfkgvklyeiidtinvehgvnlqkatlepiyrAEVARLFD 84
Cdd:cd07526     1 DLVIFDCDGVLVDSEVIAARVLVEVLAELG------------------------------------------ARVLAAFE 38

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  85 SELEVIAGAQALLDAVSVPMCVVSNGPVSKMQHSLGRTGLLHHFADRLYSGYDIQRWKPDPALMFHAAEAMQVKAENCIL 164
Cdd:cd07526    39 AELQPIPGAAAALSALTLPFCVASNSSRERLTHSLGLAGLLAYFEGRIFSASDVGRGKPAPDLFLHAAAQMGVAPERCLV 118

                         170       180
                  ....*....|....*....|...
gi 1440323440 165 VDDSSAGAQSGIAAGMEVFYFCA 187
Cdd:cd07526   119 IEDSPTGVRAALAAGMTVFGFTG 141
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
3-208 1.75e-60

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 188.49  E-value: 1.75e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   3 QPEAVFFDCDGTLVDSEVICSRAYVHMFQEFGITLDlAEIFKRFKGVKLYEIIDTINVEHGVNLQKATLEPIYRAEVARL 82
Cdd:COG0637     1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLT-EEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYREL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  83 FDS-ELEVIAGAQALLDAVS---VPMCVVSNGPVSKMQHSLGRTGLLHHFaDRLYSGYDIQRWKPDPALMFHAAEAMQVK 158
Cdd:COG0637    80 LAEeGLPLIPGVVELLEALKeagIKIAVATSSPRENAEAVLEAAGLLDYF-DVIVTGDDVARGKPDPDIYLLAAERLGVD 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1440323440 159 AENCILVDDSSAGAQSGIAAGMEVFYFCADPHNQPIDHPKVTTFTDLAEL 208
Cdd:COG0637   159 PEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 4-183 7.08e-22

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: 88.55  E-value: 7.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   4 PEAVFFDCDGTLVDSEVICSRAYVHMFQEFGITLDlAEIFKRFKGVKLYEIIDTINVEHGVNLqkaTLEPIYR-AEVARL 82
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFD-KQYNESLKGLSREDILRAILKLRGDGL---SLEEIHQlAERKNE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  83 FDSELEVIAGAQAL---------LDAVSVPMCVVSNGPVSKMqhSLGRTGLLHHFaDRLYSGYDIQRWKPDPALMFHAAE 153
Cdd:TIGR02009  77 LYRELLRLTGVAVLpgirnllkrLKAKGIAVGLGSSSKNAPR--ILAKLGLRDYF-DAIVDASEVKNGKPHPETFLLAAE 153

                         170       180       190
                  ....*....|....*....|....*....|
gi 1440323440 154 AMQVKAENCILVDDSSAGAQSGIAAGMEVF 183
Cdd:TIGR02009 154 LLGVPPNECIVFEDALAGVQAARAAGMFAV 183
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
7-182 3.10e-21

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 86.48  E-value: 3.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   7 VFFDCDGTLVDSEVICSRAYVHMFQEFG-ITLDLAEIfKRFKGVKLYEIIDTINVEHGVNLQKATLEPIYRAEvarLFDS 85
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGyGELSEEEI-LKFIGLPLREIFRYLGVSEDEEEKIEFYLRKYNEE---LHDK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  86 ELEVIAGAQALLDAVS---VPMCVVSNGPVSKMQHSLGRTGLLHHFaDRLYSGYDIQRWKPDPALMFHAAEAMQVKAENC 162
Cdd:pfam13419  77 LVKPYPGIKELLEELKeqgYKLGIVTSKSRENVEEFLKQLGLEDYF-DVIVGGDDVEGKKPDPDPILKALEQLGLKPEEV 155

                         170       180
                  ....*....|....*....|
gi 1440323440 163 ILVDDSSAGAQSGIAAGMEV 182
Cdd:pfam13419 156 IYVGDSPRDIEAAKNAGIKV 175
 
Name Accession Description Interval E-value
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 1-221 0e+00

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 495.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   1 MTQPEAVFFDCDGTLVDSEVICSRAYVHMFQEFGITLDLAEIFKRFKGVKLYEIIDTINVEHGVNLQKATLEPIYRAEVA 80
Cdd:PRK10563    1 MSQIEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLSLEEVFKRFKGVKLYEIIDIISKEHGVTLAKAELEPVYRAEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  81 RLFDSELEVIAGAQALLDAVSVPMCVVSNGPVSKMQHSLGRTGLLHHFADRLYSGYDIQRWKPDPALMFHAAEAMQVKAE 160
Cdd:PRK10563   81 RLFDSELEPIAGANALLESITVPMCVVSNGPVSKMQHSLGKTGMLHYFPDKLFSGYDIQRWKPDPALMFHAAEAMNVNVE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1440323440 161 NCILVDDSSAGAQSGIAAGMEVFYFCADPHNQPIDHPKVTTFTDLAELPALWQARGWDITR 221
Cdd:PRK10563  161 NCILVDDSSAGAQSGIAAGMEVFYFCADPHNKPIDHPLVTTFTDLAQLPELWKARGWDITR 221
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 5-187 4.48e-66

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: 200.24  E-value: 4.48e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   5 EAVFFDCDGTLVDSEVICSRAYVHMFQEFGitldlaeifkrfkgvklyeiidtinvehgvnlqkatlepiyrAEVARLFD 84
Cdd:cd07526     1 DLVIFDCDGVLVDSEVIAARVLVEVLAELG------------------------------------------ARVLAAFE 38

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  85 SELEVIAGAQALLDAVSVPMCVVSNGPVSKMQHSLGRTGLLHHFADRLYSGYDIQRWKPDPALMFHAAEAMQVKAENCIL 164
Cdd:cd07526    39 AELQPIPGAAAALSALTLPFCVASNSSRERLTHSLGLAGLLAYFEGRIFSASDVGRGKPAPDLFLHAAAQMGVAPERCLV 118

                         170       180
                  ....*....|....*....|...
gi 1440323440 165 VDDSSAGAQSGIAAGMEVFYFCA 187
Cdd:cd07526   119 IEDSPTGVRAALAAGMTVFGFTG 141
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
3-208 1.75e-60

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 188.49  E-value: 1.75e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   3 QPEAVFFDCDGTLVDSEVICSRAYVHMFQEFGITLDlAEIFKRFKGVKLYEIIDTINVEHGVNLQKATLEPIYRAEVARL 82
Cdd:COG0637     1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGIDLT-EEEYRRLMGRSREDILRYLLEEYGLDLPEEELAARKEELYREL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  83 FDS-ELEVIAGAQALLDAVS---VPMCVVSNGPVSKMQHSLGRTGLLHHFaDRLYSGYDIQRWKPDPALMFHAAEAMQVK 158
Cdd:COG0637    80 LAEeGLPLIPGVVELLEALKeagIKIAVATSSPRENAEAVLEAAGLLDYF-DVIVTGDDVARGKPDPDIYLLAAERLGVD 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1440323440 159 AENCILVDDSSAGAQSGIAAGMEVFYFCADPHNQPIDHPKVTTFTDLAEL 208
Cdd:COG0637   159 PEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
4-211 2.52e-33

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 118.88  E-value: 2.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   4 PEAVFFDCDGTLVDSEVICSRAYVHMFQEFGITLDLAEIFKRFKGVKLYEIIDTInVEHGVNLQKATLEPIYRAEVARLF 83
Cdd:COG0546     1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRALIGLGLRELLRRL-LGEDPDEELEELLARFRELYEEEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  84 DSELEVIAGAQALLDAVS---VPMCVVSNGPVSKMQHSLGRTGLLHHFaDRLYSGYDIQRWKPDPALMFHAAEAMQVKAE 160
Cdd:COG0546    80 LDETRLFPGVRELLEALKargIKLAVVTNKPREFAERLLEALGLDDYF-DAIVGGDDVPPAKPKPEPLLEALERLGLDPE 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1440323440 161 NCILVDDSSAGAQSGIAAGMEVFYFC--ADPHNQPIDHPKVTTFTDLAELPAL 211
Cdd:COG0546   159 EVLMVGDSPHDIEAARAAGVPFIGVTwgYGSAEELEAAGADYVIDSLAELLAL 211
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 4-211 1.20e-30

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: 112.43  E-value: 1.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   4 PEAVFFDCDGTLVDSEVICSRAYVHMFQEFGITLDLAEIFKRFKGVK-------------LYEIIDTINVEHGVNLQKAT 70
Cdd:COG1011     1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAEAYRAIEyalwrryergeitFAELLRRLLEELGLDLAEEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  71 LEPIYRAevarlFDSELEVIAGAQALLDAVS---VPMCVVSNGPVSKMQHSLGRTGLLHHFaDRLYSGYDIQRWKPDPAl 147
Cdd:COG1011    81 AEAFLAA-----LPELVEPYPDALELLEALKargYRLALLTNGSAELQEAKLRRLGLDDLF-DAVVSSEEVGVRKPDPE- 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1440323440 148 MF-HAAEAMQVKAENCILVDDSS----AGAQsgiAAGMEVFYFCADPHNQPIDHPKVTTFTDLAELPAL 211
Cdd:COG1011   154 IFeLALERLGVPPEEALFVGDSPetdvAGAR---AAGMRTVWVNRSGEPAPAEPRPDYVISDLAELLEL 219
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 6-183 1.28e-22

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: 89.21  E-value: 1.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   6 AVFFDCDGTLVDSEVICSRAYvhmfqefgitldlaeifkrfkgvKLYEIIDTINVEhgvnlqkatlepiyraevaRLFDS 85
Cdd:cd07505     1 AVIFDMDGVLIDTEPLHRQAW-----------------------QLLERKNALLLE-------------------LIASE 38

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  86 ELEVIAGAQALLDAVS---VPMCVVSNGPVSKMQHSLGRTGLLHHFADRLYSGYDIQRWKPDPALMFHAAEAMQVKAENC 162
Cdd:cd07505    39 GLKLKPGVVELLDALKaagIPVAVATSSSRRNVELLLLELGLLRGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERC 118

                         170       180
                  ....*....|....*....|.
gi 1440323440 163 ILVDDSSAGAQSGIAAGMEVF 183
Cdd:cd07505   119 LVFEDSLAGIEAAKAAGMTVV 139
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 4-183 7.08e-22

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: 88.55  E-value: 7.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   4 PEAVFFDCDGTLVDSEVICSRAYVHMFQEFGITLDlAEIFKRFKGVKLYEIIDTINVEHGVNLqkaTLEPIYR-AEVARL 82
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFD-KQYNESLKGLSREDILRAILKLRGDGL---SLEEIHQlAERKNE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  83 FDSELEVIAGAQAL---------LDAVSVPMCVVSNGPVSKMqhSLGRTGLLHHFaDRLYSGYDIQRWKPDPALMFHAAE 153
Cdd:TIGR02009  77 LYRELLRLTGVAVLpgirnllkrLKAKGIAVGLGSSSKNAPR--ILAKLGLRDYF-DAIVDASEVKNGKPHPETFLLAAE 153

                         170       180       190
                  ....*....|....*....|....*....|
gi 1440323440 154 AMQVKAENCILVDDSSAGAQSGIAAGMEVF 183
Cdd:TIGR02009 154 LLGVPPNECIVFEDALAGVQAARAAGMFAV 183
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
7-182 3.10e-21

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 86.48  E-value: 3.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   7 VFFDCDGTLVDSEVICSRAYVHMFQEFG-ITLDLAEIfKRFKGVKLYEIIDTINVEHGVNLQKATLEPIYRAEvarLFDS 85
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGyGELSEEEI-LKFIGLPLREIFRYLGVSEDEEEKIEFYLRKYNEE---LHDK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  86 ELEVIAGAQALLDAVS---VPMCVVSNGPVSKMQHSLGRTGLLHHFaDRLYSGYDIQRWKPDPALMFHAAEAMQVKAENC 162
Cdd:pfam13419  77 LVKPYPGIKELLEELKeqgYKLGIVTSKSRENVEEFLKQLGLEDYF-DVIVGGDDVEGKKPDPDPILKALEQLGLKPEEV 155

                         170       180
                  ....*....|....*....|
gi 1440323440 163 ILVDDSSAGAQSGIAAGMEV 182
Cdd:pfam13419 156 IYVGDSPRDIEAAKNAGIKV 175
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 6-182 4.44e-20

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: 83.62  E-value: 4.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   6 AVFFDCDGTLVDSEVIcsrayVHMFQEFGITLDLAEIFKRFKGVKLYEIIDTINVEHGVNLQKATLEPIYRAEVARLFDS 85
Cdd:TIGR01509   1 AILFDLDGVLVDTEFA-----IAKLINREELGLVPDELGVSAVGRLELALRRFKAQYGRTISPEDAQLLYKQLFYEQIEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  86 ELEV--IAGAQALLDAVS---VPMCVVSNGPVSkMQHSLGRTGLLHHFADRLYSGyDIQRWKPDPALMFHAAEAMQVKAE 160
Cdd:TIGR01509  76 EAKLkpLPGVRALLEALRargKKLALLTNSPRA-HKLVLALLGLRDLFDVVIDSS-DVGLGKPDPDIYLQALKALGLEPS 153

                         170       180
                  ....*....|....*....|..
gi 1440323440 161 NCILVDDSSAGAQSGIAAGMEV 182
Cdd:TIGR01509 154 ECVFVDDSPAGIEAAKAAGMHT 175
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 6-205 2.02e-18

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: 78.84  E-value: 2.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   6 AVFFDCDGTLVDSEVIcsraYVHMFQEFgITLDLAEIFKRfkgvklyeiidtinvehgVNLQKATLEPiyraevarlfds 85
Cdd:cd16423     1 AVIFDFDGVIVDTEPL----WYEAWQEL-LNERRNELIKR------------------QFSEKTDLPP------------ 45

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  86 elevIAGAQALLDAV---SVPMCVVSNGPVSKMQHSLGRTGLLHHFaDRLYSGYDIQRWKPDPALMFHAAEAMQVKAENC 162
Cdd:cd16423    46 ----IEGVKELLEFLkekGIKLAVASSSPRRWIEPHLERLGLLDYF-EVIVTGDDVEKSKPDPDLYLEAAERLGVNPEEC 120

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1440323440 163 ILVDDSSAGAQSGIAAGMEVFYFcADPHNQPIDHPKVTTFTDL 205
Cdd:cd16423   121 VVIEDSRNGVLAAKAAGMKCVGV-PNPVTGSQDFSKADLVLSS 162
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 6-179 2.30e-18

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


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 79.55  E-value: 2.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   6 AVFFDCDGTLVDSEVICSRAYVHMFQEFGITLDLAEIFKR------------FKGVKLYEIIDTINVEHGVNLQKATLEP 73
Cdd:pfam00702   3 AVVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAEDlpipvedftarlLLGKRDWLEELDILRGLVETLEAEGLTV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  74 IYRAEVARLF-DSELEVIAGAQALLDAVS---VPMCVVSNGPVSKMQHSLGRTGLLHHFaDRLYSGYDIQRWKPDPALMF 149
Cdd:pfam00702  83 VLVELLGVIAlADELKLYPGAAEALKALKergIKVAILTGDNPEAAEALLRLLGLDDYF-DVVISGDDVGVGKPKPEIYL 161

                         170       180       190
                  ....*....|....*....|....*....|
gi 1440323440 150 HAAEAMQVKAENCILVDDSSAGAQSGIAAG 179
Cdd:pfam00702 162 AALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 6-182 5.57e-17

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: 75.84  E-value: 5.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   6 AVFFDCDGTLVDSEVICSRAYVHMFQEFGItlDLAEIFKRFKGVKLYEIIDTINVEHGVNLQKATLEPIYRAEVArlfdS 85
Cdd:cd07527     1 ALLFDMDGTLVDSTPAVERAWHKWAKEHGV--DPEEVLKVSHGRRAIDVIRKLAPDDADIELVLALETEEPESYP----E 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  86 ELEVIAGAQALLDAVSV---PMCVVSNGPVSKMQHSLGRTGLLHhfADRLYSGYDIQRWKPDPALMFHAAEAMQVKAENC 162
Cdd:cd07527    75 GVIAIPGAVDLLASLPAagdRWAIVTSGTRALAEARLEAAGLPH--PEVLVTADDVKNGKPDPEPYLLGAKLLGLDPSDC 152

                         170       180
                  ....*....|....*....|
gi 1440323440 163 ILVDDSSAGAQSGIAAGMEV 182
Cdd:cd07527   153 VVFEDAPAGIKAGKAAGARV 172
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
1-211 6.39e-17

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 76.39  E-value: 6.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   1 MTQPEAVFFDCDGTLVDSEVICSRAYVHMFQEFGI-TLDLAEIfKRF--KGVKlyeiidtINVEHGVNLQKATLEPIYRA 77
Cdd:PRK13222    3 FMDIRAVAFDLDGTLVDSAPDLAAAVNAALAALGLpPAGEERV-RTWvgNGAD-------VLVERALTWAGREPDEELLE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  78 EVARLFD----------SEL--EVIAGAQALlDAVSVPMCVVSNGPVSKMQHSLGRTGLLHHFADrLYSGYDIQRWKPDP 145
Cdd:PRK13222   75 KLRELFDrhyaenvaggSRLypGVKETLAAL-KAAGYPLAVVTNKPTPFVAPLLEALGIADYFSV-VIGGDSLPNKKPDP 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1440323440 146 ALMFHAAEAMQVKAENCILVDDSSAGAQSGIAAGMEVF-----YfcadPHNQPIDH--PKVtTFTDLAELPAL 211
Cdd:PRK13222  153 APLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPSVgvtygY----NYGEPIALsePDV-VIDHFAELLPL 220
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 4-180 6.69e-17

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 77.06  E-value: 6.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   4 PEAVFFDCDGTLVDSEVICSR-AYVHMFQEFGITL---------DLAEI----------FKRfKGVKLYEI--------- 54
Cdd:PLN02779   40 PEALLFDCDGVLVETERDGHRvAFNDAFKEFGLRPvewdvelydELLNIgggkermtwyFNE-NGWPTSTIekapkdeee 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  55 ----IDTIN---VEHGVNLQKATLEPIyRAEVARLFDseleviagaQALLDAVSVPMCVVSN-GPVSKMQHSLgrtgLLH 126
Cdd:PLN02779  119 rkelVDSLHdrkTELFKELIESGALPL-RPGVLRLMD---------EALAAGIKVAVCSTSNeKAVSKIVNTL----LGP 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1440323440 127 HFADRL--YSGYDIQRWKPDPALMFHAAEAMQVKAENCILVDDSSAGAQSGIAAGM 180
Cdd:PLN02779  185 ERAQGLdvFAGDDVPKKKPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAAKAAGM 240
PGP_bact TIGR01449
2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate ...
 7-211 7.57e-14

2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate salvage pathway in higher organisms (photorespiration in plants). Phosphoglycolate results from the oxidase activity of RubisCO in the Calvin cycle when concentrations of carbon dioxide are low relative to oxygen. In Ralstonia (Alcaligenes) eutropha and Rhodobacter sphaeroides, the PGP gene (CbbZ) is located on an operon along with other Calvin cycle enzymes including RubisCO. The only other pertinent experimental evidence concerns the gene from E. coli. The in vitro activity of the Ralstonia and Escherichia enzymes was determined with crude cell extracts of strains containing PGP on expression plasmids and compared to controls. In E. coli, however, there does not appear to be a functional Calvin cycle (RubisCO is absent), although the E. coli PGP gene (gph) is on the same operon (dam) with ribulose-5-phosphate-3-epimerase (rpe), a gene in the pentose-phosphate pathway (along with other, unrelated genes). The E. coli enzyme is not expressed under normal laboratory conditions; the pathway to which it belongs has not been determined. In fact, the possibility exists, although unlikely, that the E. coli enzyme and others within this equivalog have as their physiological substrate another, closely related molecule. The other seed chosen for this model, from Xylella fastidiosa has no experimental evidence, but is a plant pathogen and thus may obtain phosphoglycolate from its host. This model has been restricted to encompass only proteobacteria as no related PGP has been verified outside of this clade. Sequences from Aquifex aeolicus and Treponema pallidum fall between the trusted and noise cutoffs. Just below the noise cutoff is a gene which is part of the operon for the biosynthesis of the blue pigment, indigoidine, from Erwinia (Pectobacterium) chrysanthemi, a plant pathogen. It does not seem likely, considering the proposed biosynthetic mechanism, that the dephosphorylation of phosphoglycolate or a closely related compound is required. Possibly, this gene is fortuitously located in this operon, or has an indirect relationship to the necessity for the biosynthesis of this compound. Sequences from 11 species have been annotated as PGP or putative PGP but fall below the noise cutoff. None of these have experimental validation. This enzyme is a member of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolase enzymes (pfam00702). [Energy metabolism, Sugars]


Pssm-ID: 130516 [Multi-domain]  Cd Length: 213  Bit Score: 67.54  E-value: 7.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   7 VFFDCDGTLVDSEVICSRAYVHMFQEFG---ITLD-LAEIFKRFKGVKLYEIIDTINVEHGVNLQkATLEPIYRAEVARL 82
Cdd:TIGR01449   1 VLFDLDGTLVDSAPDIAAAVNMALAALGlppATLArVIGFIGNGVPVLMERVLAWAGQEPDAQRV-AELRKLFDRHYEEV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  83 FDSELEVIAGAQALLDAV---SVPMCVVSNGPVSKMQHSLGRTGLLHHFaDRLYSGYDIQRWKPDPALMFHAAEAMQVKA 159
Cdd:TIGR01449  80 AGELTSVFPGVEATLGALrakGLRLGLVTNKPTPLARPLLELLGLAKYF-SVLIGGDSLAQRKPHPDPLLLAAERLGVAP 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1440323440 160 ENCILVDDSSAGAQSGIAAGME--VFYFCADPHNQPIDHPKVTTFTDLAELPAL 211
Cdd:TIGR01449 159 QQMVYVGDSRVDIQAARAAGCPsvLLTYGYRYGEAIDLLPPDVLYDSLNELPPL 212
PRK11587 PRK11587
putative phosphatase; Provisional
 9-198 2.87e-13

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 66.17  E-value: 2.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   9 FDCDGTLVDSEVICSRAYVHMFQEFGITLDlaeifkrfkgvklyEIIDTInveHGVN--------LQKATLEPIyRAEVA 80
Cdd:PRK11587    8 FDLDGTLVDSLPAVERAWSNWADRHGIAPD--------------EVLNFI---HGKQaitslrhfMAGASEAEI-QAEFT 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  81 RLFDSELEVIAGAQAL---------LDAVSVPMCVVSNG--PVSKMQHSLGRTGLLHHF--ADRlysgydIQRWKPDPAL 147
Cdd:PRK11587   70 RLEQIEATDTEGITALpgaiallnhLNKLGIPWAIVTSGsvPVASARHKAAGLPAPEVFvtAER------VKRGKPEPDA 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1440323440 148 MFHAAEAMQVKAENCILVDDSSAGAQSGIAAGMEVFYFcadphNQPIDHPK 198
Cdd:PRK11587  144 YLLGAQLLGLAPQECVVVEDAPAGVLSGLAAGCHVIAV-----NAPADTPR 189
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 6-209 3.74e-13

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: 65.72  E-value: 3.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   6 AVFFDCDGTLVDSEVICSRAYVHMFQEFGITLDLAEIFKRF--KGV-KLYE--IIDTINVEHGVNLQKATLEPI---YRA 77
Cdd:cd16417     1 LVAFDLDGTLVDSAPDLAEAANAMLAALGLPPLPEETVRTWigNGAdVLVEraLTGAREAEPDEELFKEARALFdrhYAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  78 EVA---RLFDselEVIAGAQALLDAvSVPMCVVSNGPVSKMQHSLGRTGLLHHFADRLySGYDIQRWKPDPALMFHAAEA 154
Cdd:cd16417    81 TLSvhsHLYP---GVKEGLAALKAQ-GYPLACVTNKPERFVAPLLEALGISDYFSLVL-GGDSLPEKKPDPAPLLHACEK 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1440323440 155 MQVKAENCILVDDSSAGAQSGIAAGMEVF-----YfcadPHNQPIDHPK-VTTFTDLAELP 209
Cdd:cd16417   156 LGIAPAQMLMVGDSRNDILAARAAGCPSVgltygY----NYGEDIAASGpDAVIDSLAELL 212
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
5-182 4.20e-12

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 62.40  E-value: 4.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   5 EAVFFDCDGTLVDSEVICSRAYVHMFQEFGITLDLAEIFKrFKGVKLYEIIDTInvehgVNLQKATLEP-IYRAEVARLF 83
Cdd:PRK10725    6 AGLIFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVA-LNGSPTWRIAQAI-----IELNQADLDPhALAREKTEAV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  84 DSELEVIAGAQALLDAVSV-----PMCVvSNGPVSKMQHSLGRTGLLHHFADRLYSGYDIQRWKPDPALMFHAAEAMQVK 158
Cdd:PRK10725   80 KSMLLDSVEPLPLIEVVKAwhgrrPMAV-GTGSESAIAEALLAHLGLRRYFDAVVAADDVQHHKPAPDTFLRCAQLMGVQ 158

                         170       180
                  ....*....|....*....|....
gi 1440323440 159 AENCILVDDSSAGAQSGIAAGMEV 182
Cdd:PRK10725  159 PTQCVVFEDADFGIQAARAAGMDA 182
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 5-210 4.47e-12

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


Pssm-ID: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 62.67  E-value: 4.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   5 EAVFFDCDGTLVD---SEVICSRAYVH-----------MFQEFGITLDLAEIFKRFKGVkLYEIIDTINVEHGVNLQKAT 70
Cdd:cd02588     1 KALVFDVYGTLIDwhsGLAAAERAFPGrgeelsrlwrqKQLEYTWLVTLMGPYVDFDEL-TRDALRATAAELGLELDESD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  71 LEPIYRAeVARL--FDselEVIAGAQALLDAvSVPMCVVSNGPVSKMQHSLGRTGLLHHFaDRLYSGYDIQRWKPDPALM 148
Cdd:cd02588    80 LDELGDA-YLRLppFP---DVVAGLRRLREA-GYRLAILSNGSPDLIEDVVANAGLRDLF-DAVLSAEDVRAYKPAPAVY 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1440323440 149 FHAAEAMQVKAENCILVDDSS---AGAQsgiAAGMEVFyFCADPHNQP--IDHPKVTTFTDLAELPA 210
Cdd:cd02588   154 ELAAERLGVPPDEILHVASHAwdlAGAR---ALGLRTA-WINRPGEVPdpLGPAPDFVVPDLGELAD 216
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 5-179 1.08e-11

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: 61.53  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   5 EAVFFDCDGTLVDSEVICSRAYVHMFQEFGITLDLAEIFKRFKGVKLYEIIDTINVEHGVNLqkatLEpIYRAEVARLFD 84
Cdd:cd02616     2 TTILFDLDGTLIDTNELIIKSFNHTLKEYGLEGYTREEVLPFIGPPLRETFEKIDPDKLEDM----VE-EFRKYYREHND 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  85 SELEVIAGAQALLDAV---SVPMCVVSNgpvsKMQH----SLGRTGLLHHFaDRLYSGYDIQRWKPDPALMFHAAEAMQV 157
Cdd:cd02616    77 DLTKEYPGVYETLARLksqGIKLGVVTT----KLREtalkGLKLLGLDKYF-DVIVGGDDVTHHKPDPEPVLKALELLGA 151

                         170       180
                  ....*....|....*....|..
gi 1440323440 158 KAENCILVDDSSAGAQSGIAAG 179
Cdd:cd02616   152 EPEEALMVGDSPHDILAGKNAG 173
PLN02940 PLN02940
riboflavin kinase
 6-182 6.58e-11

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 61.00  E-value: 6.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   6 AVFFDCDGTLVDSEVICSRAYVHMFQEFGITLDLAEIFKRFkGVKLYEIIDTINVEHGvnLQKATLEpiYRAEVARLFDS 85
Cdd:PLN02940   13 HVILDLDGTLLNTDGIVSDVLKAFLVKYGKQWDGREAQKIV-GKTPLEAAATVVEDYG--LPCSTDE--FNSEITPLLSE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  86 E---LEVIAGAQALLDAVS---VPMCVVSNGPVSKMQHSLG-RTGLLHHFAdRLYSGYDIQRWKPDPALMFHAAEAMQVK 158
Cdd:PLN02940   88 QwcnIKALPGANRLIKHLKshgVPMALASNSPRANIEAKIScHQGWKESFS-VIVGGDEVEKGKPSPDIFLEAAKRLNVE 166

                         170       180
                  ....*....|....*....|....
gi 1440323440 159 AENCILVDDSSAGAQSGIAAGMEV 182
Cdd:PLN02940  167 PSNCLVIEDSLPGVMAGKAAGMEV 190
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 6-179 9.31e-11

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: 58.18  E-value: 9.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   6 AVFFDCDGTLVDSEVICSRAYVHMFQEFGitlDLAEIFKRFKgvKLYEIIDTINVEHGVNLQKAtlepiYRAEVARLFDS 85
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFG---LDPASFKALK--QAGGLAEEEWYRIATSALEE-----LQGRFWSEYDA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  86 ELEVIAGAQAL---LDAVSVPMCVVSNGPVSKMQHSLGRTGLLHHFADRLYSGyDIQRwKPDPALMFHAAEAMQVKAEnC 162
Cdd:TIGR01549  71 EEAYIRGAADLlarLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSD-EPGS-KPEPEIFLAALESLGVPPE-V 147

                         170
                  ....*....|....*..
gi 1440323440 163 ILVDDSSAGAQSGIAAG 179
Cdd:TIGR01549 148 LHVGDNLNDIEGARNAG 164
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 6-182 1.50e-10

subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides xylulose-1,5-bisphosphate phosphatase CbbY; This family includes Rhodobacter sphaeroides and Arabidopsis thaliana xylulose-1,5-bisphosphate phosphatase CbbY which convert xylulose-1,5-bisphosphate (a potent inhibitor of Ribulose-1,5-bisphosphate carboxylase/oxygenase, Rubisco), to the non-inhibitory compound xylulose-5-phosphate. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319830 [Multi-domain]  Cd Length: 199  Bit Score: 58.55  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   6 AVFFDCDGTLVDSEVICSRAYVHMFQEFGiTLDL---AEIFKRF----------------------KGVKLYEIIDTIN- 59
Cdd:cd07528     1 ALIFDVDGTLAETEELHRRAFNNAFFAER-GLDWywdRELYGELlrvgggkeriaayfekvgwpesAPKDLKELIADLHk 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  60 --VEHGVNLQKATLEPIyRAEVARLFDSELEviAGaqalldavsVPMCVVSNGPVSKMQHSLGRTGLLHHFA--DRLYSG 135
Cdd:cd07528    80 akTERYAELIAAGLLPL-RPGVARLIDEAKA--AG---------VRLAIATTTSPANVDALLSALLGPERRAifDAIAAG 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1440323440 136 YDIQRWKPDPALMFHAAEAMQVKAENCILVDDSSAGAQSGIAAGMEV 182
Cdd:cd07528   148 DDVAEKKPDPDIYLLALERLGVSPSDCLAIEDSAIGLQAAKAAGLPC 194
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 82-185 1.88e-10

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


Pssm-ID: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 56.01  E-value: 1.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  82 LFDSELEVIAGAQALLDAVS--VPMCVVSNGPVSKMQHSLGRTGLLHHFADRLYSGyDIQRWKPDPALMFHAAEAMQVKA 159
Cdd:cd04305     3 IFDLDDTLLPGAKELLEELKkgYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISE-EVGVQKPNPEIFDYALNQLGVKP 81

                          90       100
                  ....*....|....*....|....*..
gi 1440323440 160 ENCILVDDS-SAGAQSGIAAGMEVFYF 185
Cdd:cd04305    82 EETLMVGDSlESDILGAKNAGIKTVWF 108
YjjG/YfnB TIGR02254
noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including ...
 7-208 2.37e-10

noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including YjjG from E. coli and YfnB from B. subtilis. YjjG has been shown to act as a house-cleaning enzyme, cleaving nucleotides with non-canonical nucleotide bases. This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterized by three conserved sequence motifs. By virtue of an alpha helical domain in-between the first and second conserved motif, this family is a member of subfamily IA (TIGR01549).


Pssm-ID: 162788 [Multi-domain]  Cd Length: 224  Bit Score: 58.27  E-value: 2.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   7 VFFDCDGTLVDSEVICSRAYVHMFQEFGItlDLAEIFK-RFKGV-----KLYE----IIDTINVE--------HGVNLQK 68
Cdd:TIGR02254   4 LLFDLDDTILDFQAAEALALRLLFEDQGI--PLTEDMFaQYKEInqglwRAYEegkiTKDEVVNTrfsallkeYNTEADE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  69 ATLEPIYR---AEVARLFDSELEVIAGAQALLDavsvpMCVVSNGpVSKMQHSLGRTGLLHHFADRLYSGYDIQRWKPDP 145
Cdd:TIGR02254  82 ALLNQKYLrflEEGHQLLPGAFELMENLQQKFR-----LYIVTNG-VRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDK 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1440323440 146 ALMFHAAEAM-QVKAENCILVDDS-SAGAQSGIAAGMEVFYFCADPHNQPIDHPKVTTFTDLAEL 208
Cdd:TIGR02254 156 EIFNYALERMpKFSKEEVLMIGDSlTADIKGGQNAGLDTCWMNPDMHPNPDDIIPTYEIRSLEEL 220
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 8-185 3.07e-10

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: 57.00  E-value: 3.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   8 FFDCDGTLVDSEVICSRAYVHMFQEFGITLDLAEIFKRFKGVKLYEIIDTINVEHGVNLQKATLEPIYRAEVArLFDsel 87
Cdd:cd07523     3 IWDLDGTLLDSYPAMTKALSETLADFGIPQDLETVYKIIKESSVQFAIQYYAEVPDLEEEYKELEAEYLAKPI-LFP--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  88 eviaGAQALLDAVSVpmcvvSNGPVSKMQHS-------LGRTGLLHHFADRLYSGYDIQRwKPDPALMFHAAEAMQVKAE 160
Cdd:cd07523    79 ----GAKAVLRWIKE-----QGGKNFLMTHRdhsaltiLKKDGIASYFTEIVTSDNGFPR-KPNPEAINYLLNKYQLNPE 148

                         170       180
                  ....*....|....*....|....*
gi 1440323440 161 NCILVDDSSAGAQSGIAAGMEVFYF 185
Cdd:cd07523   149 ETVMIGDRELDIEAGHNAGISTILF 173
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 6-185 5.81e-10

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: 56.58  E-value: 5.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   6 AVFFDCDGTLVDSevicsrAYVHMFQEFGITLDLAEIFkRFKGVKLYEIID-----TINV-EHGVNLQKATLEPIYRAEV 79
Cdd:cd02603     3 AVLFDFGGVLIDP------DPAAAVARFEALTGEPSEF-VLDTEGLAGAFLelergRITEeEFWEELREELGRPLSAELF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  80 ARLFDSELEVIAGAQALLDAVS---VPMCVVSNGPVSKMQHSLGRTGLLHHFADRLYSGYDIQRWKPDPALMFHAAEAMQ 156
Cdd:cd02603    76 EELVLAAVDPNPEMLDLLEALRakgYKVYLLSNTWPDHFKFQLELLPRRGDLFDGVVESCRLGVRKPDPEIYQLALERLG 155

                         170       180
                  ....*....|....*....|....*....
gi 1440323440 157 VKAENCILVDDSSAGAQSGIAAGMEVFYF 185
Cdd:cd02603   156 VKPEEVLFIDDREENVEAARALGIHAILV 184
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 6-211 2.11e-09

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


Pssm-ID: 319815 [Multi-domain]  Cd Length: 214  Bit Score: 55.40  E-value: 2.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   6 AVFFDCDGTLVDSEVICSRAYVHMFQEFGIT-LDLAEIfKRFKGVKLYEIIDTINVEHGVNLQKATLEPI-------YRA 77
Cdd:cd07512     1 AVIFDLDGTLIDSAPDLHAALNAVLAAEGLApLSLAEV-RSFVGHGAPALIRRAFAAAGEDLDGPLHDALlarfldhYEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  78 EVA---RLFDSELEVIAGaqalLDAVSVPMCVVSNGPVSKMQHSLGRTGLLHHFADRLysGYDI--QRwKPDPALMFHAA 152
Cdd:cd07512    80 DPPgltRPYPGVIEALER----LRAAGWRLAICTNKPEAPARALLSALGLADLFAAVV--GGDTlpQR-KPDPAPLRAAI 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440 153 EAMQVKAENCILVDDSSAGAQSGIAAGMEVFYFCADPHNQPI-DHPKVTTFTDLAELPAL 211
Cdd:cd07512   153 RRLGGDVSRALMVGDSETDAATARAAGVPFVLVTFGYRHAPVaELPHDAVFSDFDALPDL 212
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 6-180 2.38e-09

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: 54.61  E-value: 2.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   6 AVFFDCDGTLVDSEVICSRAYVHMFqefgitlDLAEIFKRfKGVKLYEIIDTInvehgvnlqkaTLEPIYRAEVARLFDS 85
Cdd:cd02598     1 GVIFDLDGVITDTAEYHYRAWKKLA-------DKEELAAR-KNRIYVELIEEL-----------TPVDVLPGIASLLVDL 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  86 ELEVIAGAQAlldAVSvpmcvvSNGPvskmqHSLGRTGLLHHFaDRLYSGYDIQRWKPDPALMFHAAEAMQVKAENCILV 165
Cdd:cd02598    62 KAKGIKIALA---SAS------KNAP-----KILEKLGLAEYF-DAIVDGAVLAKGKPDPDIFLAAAEGLGLNPKDCIGV 126

                         170
                  ....*....|....*
gi 1440323440 166 DDSSAGAQSGIAAGM 180
Cdd:cd02598   127 EDAQAGIRAIKAAGF 141
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 5-182 3.12e-09

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 55.23  E-value: 3.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   5 EAVFFDCDGTLVDSEVICSRAYVHMFQEF----GITLDLAEIFKRFKGVKLYEIIDTI---NVEHGVNLQkATLEPIYRa 77
Cdd:PLN02770   23 EAVLFDVDGTLCDSDPLHYYAFREMLQEInfngGVPITEEFFVENIAGKHNEDIALGLfpdDLERGLKFT-DDKEALFR- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  78 evaRLFDSELEVIAGAQALLDAVS---VPMCVVSNGPVSKMQHSLGRTGLLHHFaDRLYSGYDIQRWKPDPALMFHAAEA 154
Cdd:PLN02770  101 ---KLASEQLKPLNGLYKLKKWIEdrgLKRAAVTNAPRENAELMISLLGLSDFF-QAVIIGSECEHAKPHPDPYLKALEV 176

                         170       180
                  ....*....|....*....|....*...
gi 1440323440 155 MQVKAENCILVDDSSAGAQSGIAAGMEV 182
Cdd:PLN02770  177 LKVSKDHTFVFEDSVSGIKAGVAAGMPV 204
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 7-180 4.09e-09

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1; This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319835 [Multi-domain]  Cd Length: 207  Bit Score: 54.33  E-value: 4.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   7 VFFDCDGTLVDSEVICSRAYVHMFQEFGITLDLAEIFKRFKGVKLYEIIDTInVEHGVNLQKATLEPIYRAEVA--RLFD 84
Cdd:cd07533     2 VIFDWDGTLADSQHNIVAAMTAAFADLGLPVPSAAEVRSIIGLSLDEAIARL-LPMATPALVAVAERYKEAFDIlrLLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  85 SELEVIAGAQALLDAVSVP--MCVVSNGPVSK-MQHSLGRTGLLHHF-----ADRLYSgydiqrwKPDPALMFHAAEAMQ 156
Cdd:cd07533    81 HAEPLFPGVREALDALAAQgvLLAVATGKSRRgLDRVLEQHGLGGYFdatrtADDTPS-------KPHPEMLREILAELG 153

                         170       180
                  ....*....|....*....|....
gi 1440323440 157 VKAENCILVDDSSAGAQSGIAAGM 180
Cdd:cd07533   154 VDPSRAVMVGDTAYDMQMAANAGA 177
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 4-182 4.22e-09

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: 54.28  E-value: 4.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   4 PEAVFFDCDGTLVDSEVICSRAYVHMFQEFGITLDLaEIFKRFKGVKLYEIIDTINVEHGVNLQKATLEPIYRAEVARLF 83
Cdd:cd07529     1 VTHCIFDMDGLLLDTERIYTETTQEILARYGKTYTW-DVKAKMMGRPASEAARIIVDELKLPMSLEEEFDEQQEALAELF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  84 DSELEVIAGAQAL---LDAVSVPMCV-VSNGPVS---KMQHSLGRTGLLHHfadrLYSGYD---IQRWKPDPALMFHAAE 153
Cdd:cd07529    80 MGTAKLMPGAERLlrhLHAHNIPIALaTSSCTRHfklKTSRHKELFSLFHH----VVTGDDpevKGRGKPAPDIFLVAAK 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1440323440 154 AMQVKAE---NCILVDDSSAGAQSGIAAGMEV 182
Cdd:cd07529   156 RFNEPPKdpsKCLVFEDSPNGVKAAKAAGMQV 187
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 6-180 6.84e-09

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 55.24  E-value: 6.84e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440    6 AVFFDCDGTLVDSEVICSRAYVHMFQEFGITLDlAEIFKRFKGVKLYEIIDTINVEHGVNlqkaTLEPIYRAEvaRLFDS 85
Cdd:PLN02919    77 AVLFDMDGVLCNSEEPSRRAAVDVFAEMGVEVT-VEDFVPFMGTGEANFLGGVASVKGVK----GFDPDAAKK--RFFEI 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   86 ELEVIA------GAQALLDAVS------VPMCVVSNGPVSKMQHSLGRTGLLHHFADRLYSGYDIQRWKPDPALMFHAAE 153
Cdd:PLN02919   150 YLEKYAkpnsgiGFPGALELITqcknkgLKVAVASSADRIKVDANLAAAGLPLSMFDAIVSADAFENLKPAPDIFLAAAK 229

                          170       180
                   ....*....|....*....|....*..
gi 1440323440  154 AMQVKAENCILVDDSSAGAQSGIAAGM 180
Cdd:PLN02919   230 ILGVPTSECVVIEDALAGVQAARAAGM 256
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 4-193 2.20e-06

2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Belongs to the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases (pfam00702), class (subfamily) I. Note that the Type I HAD enzymes have not yet been fully characterized, but clearly utilize a substantially different catalytic mechanism and are thus unlikely to be related.


Pssm-ID: 130495 [Multi-domain]  Cd Length: 198  Bit Score: 46.56  E-value: 2.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   4 PEAVFFDCDGTLVDSEVICSRA-------YVHMFQ-------EFGITLDLAEIFKRFKGVkLYEIIDTINVEHGVNLQKA 69
Cdd:TIGR01428   1 IKALVFDVYGTLFDVHSVAERAaelyggrGEALSQlwrqkqlEYSWLRTLMGPYKDFWDL-TREALRYLLGRLGLEDDES 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  70 TLEPIYRAeVARLfDSELEVIAGAQALLDAvSVPMCVVSNGPVSKMQHSLGRTGLLHHFaDRLYSGYDIQRWKPDPALMF 149
Cdd:TIGR01428  80 AADRLAEA-YLRL-PPHPDVPAGLRALKER-GYRLAILSNGSPAMLKSLVKHAGLDDPF-DAVLSADAVRAYKPAPQVYQ 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1440323440 150 HAAEAMQVKAENCILV-----DDSSAGaqsgiAAGMEVFYFcADPHNQP 193
Cdd:TIGR01428 156 LALEALGVPPDEVLFVasnpwDLGGAK-----KFGFKTAWI-NRPGEPP 198
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 97-185 3.72e-06

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


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 44.31  E-value: 3.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  97 LDAVSVPMCVVSNGPVSKMQHSLGRTGLLHHFaDRLYSGYDIQRWKPDPALMFHAAEAMQVKAENCILVDDSSAGAQSGI 176
Cdd:cd01427    19 LRAAGIKLAIVTNRSREALRALLEKLGLGDLF-DGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSENDIEAAR 97


                  ....*....
gi 1440323440 177 AAGMEVFYF 185
Cdd:cd01427    98 AAGGRTVAV 106
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 7-181 4.77e-06

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 46.18  E-value: 4.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   7 VFFDCDGTLVDSEV-ICSRAYVHMFQEFGITLDLAEIFKRFKGVKLYEIIDTI-----NVEHGVNLQKATlEPIYRAEVA 80
Cdd:PLN03243   27 VVLEWEGVIVEDDSeLERKAWRALAEEEGKRPPPAFLLKRAEGMKNEQAISEVlcwsrDFLQMKRLAIRK-EDLYEYMQG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  81 RLFdselEVIAGAQALLDAV---SVPMCVVSNGPVSKMQHSLGRTGLlHHFADRLYSGYDIQRWKPDPALMFHAAEAMQV 157
Cdd:PLN03243  106 GLY----RLRPGSREFVQALkkhEIPIAVASTRPRRYLERAIEAVGM-EGFFSVVLAAEDVYRGKPDPEMFMYAAERLGF 180

                         170       180
                  ....*....|....*....|....
gi 1440323440 158 KAENCILVDDSSAGAQSGIAAGME 181
Cdd:PLN03243  181 IPERCIVFGNSNSSVEAAHDGCMK 204
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 6-179 1.58e-05

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 44.25  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   6 AVFFDCDGTLVDS-EVICSrAYVHMFQEFgitldLAEIFKR-----FKGVKLYEIIDTINVEHGVNLQKAtlepiYRAEV 79
Cdd:PRK13288    5 TVLFDLDGTLINTnELIIS-SFLHTLKTY-----YPNQYKRedvlpFIGPSLHDTFSKIDESKVEEMITT-----YREFN 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  80 ARLFDSELE----VIAGAQALLDAvSVPMCVVSngpvSKMQHSLGRtGL----LHHFADRLYSGYDIQRWKPDPALMFHA 151
Cdd:PRK13288   74 HEHHDELVTeyetVYETLKTLKKQ-GYKLGIVT----TKMRDTVEM-GLkltgLDEFFDVVITLDDVEHAKPDPEPVLKA 147

                         170       180
                  ....*....|....*....|....*...
gi 1440323440 152 AEAMQVKAENCILVDDSSAGAQSGIAAG 179
Cdd:PRK13288  148 LELLGAKPEEALMVGDNHHDILAGKNAG 175
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 7-181 2.43e-05

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 44.47  E-value: 2.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   7 VFFDCDGTLV-DSEVICSRAYVHMFQEFGITLDLAEIFKRFKGVKLYEIIDTINV--EHGVNLQKATL--EPIYRA---E 78
Cdd:PLN02575  134 AIFEWEGVIIeDNPDLENQAWLTLAQEEGKSPPPAFILRRVEGMKNEQAISEVLCwsRDPAELRRMATrkEEIYQAlqgG 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  79 VARLFDSELEVIAgaqaLLDAVSVPMCVVSNGPVSKMQHSLGRTGLLHHFaDRLYSGYDIQRWKPDPALMFHAAEAMQVK 158
Cdd:PLN02575  214 IYRLRTGSQEFVN----VLMNYKIPMALVSTRPRKTLENAIGSIGIRGFF-SVIVAAEDVYRGKPDPEMFIYAAQLLNFI 288

                         170       180
                  ....*....|....*....|...
gi 1440323440 159 AENCILVDDSSAGAQSGIAAGME 181
Cdd:PLN02575  289 PERCIVFGNSNQTVEAAHDARMK 311
PRK09449 PRK09449
dUMP phosphatase; Provisional
 92-208 2.54e-05

dUMP phosphatase; Provisional


Pssm-ID: 181865 [Multi-domain]  Cd Length: 224  Bit Score: 43.74  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  92 GAQALLDAVS--VPMCVVSNGPVSKMQHSLGRTGLLHHFaDRLYSGYDIQRWKPDPALMFHAAEAMQVKAENCILV--DD 167
Cdd:PRK09449   99 GAVELLNALRgkVKMGIITNGFTELQQVRLERTGLRDYF-DLLVISEQVGVAKPDVAIFDYALEQMGNPDRSRVLMvgDN 177

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1440323440 168 SSAGAQSGIAAGMEVFYFCADPHNQPID---HPKVTTFTDLAEL 208
Cdd:PRK09449  178 LHSDILGGINAGIDTCWLNAHGREQPEGiapTYQVSSLSELEQL 221
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 6-167 2.71e-05

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; 5'-nucleotidases dephosphorylate nucleoside 5'-monophosphates to nucleosides and inorganic phosphate. Purified Pseudomonas aeruginosa PA0065 displayed high activity toward 5'-UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low activity against 5'-CMP. 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: 319798 [Multi-domain]  Cd Length: 209  Bit Score: 43.35  E-value: 2.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   6 AVFFDCDGTLVDSEVICSRAYVHMFQEFGI-TLDLAEIfKRFKGVKLYEIIDTINVEHGVNLQKATLepIYRAEVAR--L 82
Cdd:cd04302     1 TILFDLDGTLTDSAEGITASVQYALEELGIpVPDESEL-RRFIGPPLEDSFRELLPFDEEEAQRAVD--AYREYYKEkgL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  83 FDSEL-EVIAGAQALLDAVSVPMCVVSNGPVSKMQHSLGRTGLLHHFADRLYSGYDIQR-WKPDpaLMFHAAEAMQVKAE 160
Cdd:cd04302    78 FENEVyPGIPELLEKLKAAGYRLYVATSKPEVFARRILEHFGLDEYFDGIAGASLDGSRvHKAD--VIRYALDTLGIAPE 155


                  ....*..
gi 1440323440 161 NCILVDD 167
Cdd:cd04302   156 QAVMIGD 162
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 97-182 4.67e-05

Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGPase; 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: 319857 [Multi-domain]  Cd Length: 105  Bit Score: 41.29  E-value: 4.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  97 LDAVSVPMCVVSNGP---VSKMQHSLGRTgllhHFADRLYSGYDIQRwKPDPALMFHAAEAMQVKAENCILVDDSSAGAQ 173
Cdd:cd16421    19 LRQKGIKLAVLSNKPneaVQVLVEELFPG----SFDFVLGEKEGIRR-KPDPT*ALECAKVLGVPPDEVLYVGDSGVDMQ 93


                  ....*....
gi 1440323440 174 SGIAAGMEV 182
Cdd:cd16421    94 TARNAGMDE 102
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 6-129 3.85e-04

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: 40.03  E-value: 3.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   6 AVFFDCDGTLVDSEVICSRAYVHMFQEFGI-TLDLAEIfKRFKGVKLYEIIDtinvEHGVNLQKAtlePIYRAEVARLF- 83
Cdd:cd04303     1 LIIFDFDGTLADSFPWFLSILNQLAARHGFkTVDEEEI-EQLRQLSSREILK----QLGVPLWKL---PLIAKDFRRLMa 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1440323440  84 --DSELEVIAGAQALLDAV---SVPMCVVSNGPVSKMQHSLGRTGLLHHFA 129
Cdd:cd04303    73 eaAPELALFPGVEDMLRALharGVRLAVVSSNSEENIRRVLGPEELISLFA 123
PRK13226 PRK13226
phosphoglycolate phosphatase; Provisional
 4-180 4.25e-04

phosphoglycolate phosphatase; Provisional


Pssm-ID: 237311 [Multi-domain]  Cd Length: 229  Bit Score: 40.22  E-value: 4.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440   4 PEAVFFDCDGTLVDSEVICSRAYVHMFQEFGIT-LDLAEIfkrfkgvklyEIIDTINVEHGVNLQKATLEPIYRAEVARL 82
Cdd:PRK13226   12 PRAVLFDLDGTLLDSAPDMLATVNAMLAARGRApITLAQL----------RPVVSKGARAMLAVAFPELDAAARDALIPE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440323440  83 FDSELEVIAGAQA-LLDAVSVPMCVVSN-----GPVSKMQHSLGRTGL-LHHFADR---LYSGYDIQRWKPDPALMFHAA 152
Cdd:PRK13226   82 FLQRYEALIGTQSqLFDGVEGMLQRLECagcvwGIVTNKPEYLARLILpQLGWEQRcavLIGGDTLAERKPHPLPLLVAA 161

                         170       180
                  ....*....|....*....|....*...
gi 1440323440 153 EAMQVKAENCILVDDSSAGAQSGIAAGM 180
Cdd:PRK13226  162 ERIGVAPTDCVYVGDDERDILAARAAGM 189
 
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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