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Conserved domains on  [gi|449451423|ref|XP_004143461|]
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haloacid dehalogenase-like hydrolase domain-containing protein At4g39970 [Cucumis sativus]

Protein Classification

HAD family hydrolase( domain architecture ID 10010896)

HAD (haloacid dehalogenase) family hydrolase catalyzes a nucleophilic substitution reaction at a phosphorus or carbon center, using a conserved Asp carboxylate in covalent catalysis; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 32-308 6.44e-158

haloacid dehalogenase-like hydrolase family protein


:

Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 442.23  E-value: 6.44e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  32 SIIRFRTSRKSTTHKPFSLSVSATLQALIFDCDGVILESE-HLHRQAYNDAFVHFDVRcpnstsqPLNWSIEFYDELQNr 110
Cdd:PLN02779  16 RAGRRRRRRSRSTARVASASASALPEALLFDCDGVLVETErDGHRVAFNDAFKEFGLR-------PVEWDVELYDELLN- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 111 IGGGKPKMRWYFKENGWPSSTIfEKAPEDDEERAKLIDILQDWKTERYKEIIKSGTVSPRPGVLRLMDETKSAGRKLAVC 190
Cdd:PLN02779  88 IGGGKERMTWYFNENGWPTSTI-EKAPKDEEERKELVDSLHDRKTELFKELIESGALPLRPGVLRLMDEALAAGIKVAVC 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 191 SAATKSSVILCLENLIGIDRFQNLDCFlAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCVIT 270
Cdd:PLN02779 167 STSNEKAVSKIVNTLLGPERAQGLDVF-AGDDVPKKKPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAAKAAGMRCIVT 245

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 449451423 271 YTTSTANQDFKEAIATYPDLSDIRLKDLDSLLQNVATT 308
Cdd:PLN02779 246 KSSYTADEDFSGADAVFDCLGDVPLEDFDLLFCESLLT 283
 
Name Accession Description Interval E-value
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 32-308 6.44e-158

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 442.23  E-value: 6.44e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  32 SIIRFRTSRKSTTHKPFSLSVSATLQALIFDCDGVILESE-HLHRQAYNDAFVHFDVRcpnstsqPLNWSIEFYDELQNr 110
Cdd:PLN02779  16 RAGRRRRRRSRSTARVASASASALPEALLFDCDGVLVETErDGHRVAFNDAFKEFGLR-------PVEWDVELYDELLN- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 111 IGGGKPKMRWYFKENGWPSSTIfEKAPEDDEERAKLIDILQDWKTERYKEIIKSGTVSPRPGVLRLMDETKSAGRKLAVC 190
Cdd:PLN02779  88 IGGGKERMTWYFNENGWPTSTI-EKAPKDEEERKELVDSLHDRKTELFKELIESGALPLRPGVLRLMDEALAAGIKVAVC 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 191 SAATKSSVILCLENLIGIDRFQNLDCFlAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCVIT 270
Cdd:PLN02779 167 STSNEKAVSKIVNTLLGPERAQGLDVF-AGDDVPKKKPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAAKAAGMRCIVT 245

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 449451423 271 YTTSTANQDFKEAIATYPDLSDIRLKDLDSLLQNVATT 308
Cdd:PLN02779 246 KSSYTADEDFSGADAVFDCLGDVPLEDFDLLFCESLLT 283
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 58-272 2.98e-96

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: 282.35  E-value: 2.98e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  58 ALIFDCDGVILESEHLHRQAYNDAFVHFDvrcpnstSQPLNWSIEFYDELQNRIGGGKPKMRWYFKEnGWPSSTIFEKAp 137
Cdd:cd07528    1 ALIFDVDGTLAETEELHRRAFNNAFFAER-------GLDWYWDRELYGELLRVGGGKERIAAYFEKV-GWPESAPKDLK- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 138 eddeeraKLIDILQDWKTERYKEIIKSGTVSPRPGVLRLMDETKSAGRKLAVCSAATKSSVILCLENLIGIDRFQNLDCF 217
Cdd:cd07528   72 -------ELIADLHKAKTERYAELIAAGLLPLRPGVARLIDEAKAAGVRLAIATTTSPANVDALLSALLGPERRAIFDAI 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 449451423 218 LAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCVITYT 272
Cdd:cd07528  145 AAGDDVAEKKPDPDIYLLALERLGVSPSDCLAIEDSAIGLQAAKAAGLPCIVTPS 199
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
55-293 6.77e-61

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 192.73  E-value: 6.77e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  55 TLQALIFDCDGVILESEHLHRQAYNDAFVHFDVrcpnstsqplNWSIEFYDELqnrIGGGKPKM-RWYFKENGWPsstif 133
Cdd:COG0637    1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGI----------DLTEEEYRRL---MGRSREDIlRYLLEEYGLD----- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 134 ekapEDDEEraklidiLQDWKTERYKEIIKSGTVSPRPGVLRLMDETKSAGRKLAVCSAATKSSVILCLENLiGIDRFqn 213
Cdd:COG0637   63 ----LPEEE-------LAARKEELYRELLAEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAA-GLLDY-- 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 214 LDCFLAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCVITYTTSTANQDFKEAIATYPDLSDI 293
Cdd:COG0637  129 FDVIVTGDDVARGKPDPDIYLLAAERLGVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 56-268 6.37e-29

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: 109.35  E-value: 6.37e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423   56 LQALIFDCDGVILESEHLHRQAYNDAFVHFdvrcpnstsqplnwSIEFyDELQNRIGGGKPKMRwyfkengwPSSTIFEK 135
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKY--------------GISF-DKQYNESLKGLSRED--------ILRAILKL 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  136 APE--DDEERAKLIDIlqdwKTERYKEIIKSGTVSPRPGVLRLMDETKSAGRKLAVCSAATKSSVILcleNLIGIDRFqn 213
Cdd:TIGR02009  58 RGDglSLEEIHQLAER----KNELYRELLRLTGVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRIL---AKLGLRDY-- 128

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 449451423  214 LDCFLAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCV 268
Cdd:TIGR02009 129 FDAIVDASEVKNGKPHPETFLLAAELLGVPPNECIVFEDALAGVQAARAAGMFAV 183
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
59-268 2.13e-26

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 102.28  E-value: 2.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423   59 LIFDCDGVILESEHLHRQAYNDAFVHFDvrcPNSTSQplnwsiefyDELQNRIGggkPKMRWYFKEngwpsstiFEKAPE 138
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFG---YGELSE---------EEILKFIG---LPLREIFRY--------LGVSED 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  139 DDEERAKLIdilqdwktERYKEIIKSGTVSPRPGVLRLMDETKSAGRKLAVCSAATKSSVILCLENLiGIDRFqnLDCFL 218
Cdd:pfam13419  58 EEEKIEFYL--------RKYNEELHDKLVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQL-GLEDY--FDVIV 126

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 449451423  219 AGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCV 268
Cdd:pfam13419 127 GGDDVEGKKPDPDPILKALEQLGLKPEEVIYVGDSPRDIEAAKNAGIKVI 176
 
Name Accession Description Interval E-value
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 32-308 6.44e-158

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 442.23  E-value: 6.44e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  32 SIIRFRTSRKSTTHKPFSLSVSATLQALIFDCDGVILESE-HLHRQAYNDAFVHFDVRcpnstsqPLNWSIEFYDELQNr 110
Cdd:PLN02779  16 RAGRRRRRRSRSTARVASASASALPEALLFDCDGVLVETErDGHRVAFNDAFKEFGLR-------PVEWDVELYDELLN- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 111 IGGGKPKMRWYFKENGWPSSTIfEKAPEDDEERAKLIDILQDWKTERYKEIIKSGTVSPRPGVLRLMDETKSAGRKLAVC 190
Cdd:PLN02779  88 IGGGKERMTWYFNENGWPTSTI-EKAPKDEEERKELVDSLHDRKTELFKELIESGALPLRPGVLRLMDEALAAGIKVAVC 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 191 SAATKSSVILCLENLIGIDRFQNLDCFlAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCVIT 270
Cdd:PLN02779 167 STSNEKAVSKIVNTLLGPERAQGLDVF-AGDDVPKKKPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAAKAAGMRCIVT 245

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 449451423 271 YTTSTANQDFKEAIATYPDLSDIRLKDLDSLLQNVATT 308
Cdd:PLN02779 246 KSSYTADEDFSGADAVFDCLGDVPLEDFDLLFCESLLT 283
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 58-272 2.98e-96

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: 282.35  E-value: 2.98e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  58 ALIFDCDGVILESEHLHRQAYNDAFVHFDvrcpnstSQPLNWSIEFYDELQNRIGGGKPKMRWYFKEnGWPSSTIFEKAp 137
Cdd:cd07528    1 ALIFDVDGTLAETEELHRRAFNNAFFAER-------GLDWYWDRELYGELLRVGGGKERIAAYFEKV-GWPESAPKDLK- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 138 eddeeraKLIDILQDWKTERYKEIIKSGTVSPRPGVLRLMDETKSAGRKLAVCSAATKSSVILCLENLIGIDRFQNLDCF 217
Cdd:cd07528   72 -------ELIADLHKAKTERYAELIAAGLLPLRPGVARLIDEAKAAGVRLAIATTTSPANVDALLSALLGPERRAIFDAI 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 449451423 218 LAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCVITYT 272
Cdd:cd07528  145 AAGDDVAEKKPDPDIYLLALERLGVSPSDCLAIEDSAIGLQAAKAAGLPCIVTPS 199
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
55-293 6.77e-61

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 192.73  E-value: 6.77e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  55 TLQALIFDCDGVILESEHLHRQAYNDAFVHFDVrcpnstsqplNWSIEFYDELqnrIGGGKPKM-RWYFKENGWPsstif 133
Cdd:COG0637    1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGI----------DLTEEEYRRL---MGRSREDIlRYLLEEYGLD----- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 134 ekapEDDEEraklidiLQDWKTERYKEIIKSGTVSPRPGVLRLMDETKSAGRKLAVCSAATKSSVILCLENLiGIDRFqn 213
Cdd:COG0637   63 ----LPEEE-------LAARKEELYRELLAEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAA-GLLDY-- 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 214 LDCFLAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCVITYTTSTANQDFKEAIATYPDLSDI 293
Cdd:COG0637  129 FDVIVTGDDVARGKPDPDIYLLAAERLGVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 58-268 2.01e-33

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: 119.64  E-value: 2.01e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  58 ALIFDCDGVILESEHLHRQAYNdafvhfdvrcpnstsqplnwsiefydelqnrigggkpkmrwyfkengwpsstifekap 137
Cdd:cd07505    1 AVIFDMDGVLIDTEPLHRQAWQ---------------------------------------------------------- 22

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 138 eddeeraklidiLQDWKTERYKEIIKSGTVSPRPGVLRLMDETKSAGRKLAVCSAATKSSVILCLENLIGIDRFQnlDCF 217
Cdd:cd07505   23 ------------LLERKNALLLELIASEGLKLKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLRGYF--DVI 88

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 449451423 218 LAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCV 268
Cdd:cd07505   89 VSGDDVERGKPAPDIYLLAAERLGVDPERCLVFEDSLAGIEAAKAAGMTVV 139
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
56-293 9.47e-30

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 112.33  E-value: 9.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  56 LQALIFDCDGVILESEHLHRQAYNDAFVHFDVRCPNstsqplnwsiefYDELQNRIGggkpkmrwyfkengWPSSTIFEK 135
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLD------------LEELRALIG--------------LGLRELLRR 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 136 A-PEDDEERAKliDILQDWKtERYKEIIKSGTVsPRPGVLRLMDETKSAGRKLAVCSAATKSSVILCLENLiGIDRFqnL 214
Cdd:COG0546   55 LlGEDPDEELE--ELLARFR-ELYEEELLDETR-LFPGVRELLEALKARGIKLAVVTNKPREFAERLLEAL-GLDDY--F 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 215 DCFLAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCV-ITYTTSTAnQDFKEAIATY--PDLS 291
Cdd:COG0546  128 DAIVGGDDVPPAKPKPEPLLEALERLGLDPEEVLMVGDSPHDIEAARAAGVPFIgVTWGYGSA-EELEAAGADYviDSLA 206


                 ..
gi 449451423 292 DI 293
Cdd:COG0546  207 EL 208
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 56-268 6.37e-29

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: 109.35  E-value: 6.37e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423   56 LQALIFDCDGVILESEHLHRQAYNDAFVHFdvrcpnstsqplnwSIEFyDELQNRIGGGKPKMRwyfkengwPSSTIFEK 135
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKY--------------GISF-DKQYNESLKGLSRED--------ILRAILKL 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  136 APE--DDEERAKLIDIlqdwKTERYKEIIKSGTVSPRPGVLRLMDETKSAGRKLAVCSAATKSSVILcleNLIGIDRFqn 213
Cdd:TIGR02009  58 RGDglSLEEIHQLAER----KNELYRELLRLTGVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRIL---AKLGLRDY-- 128

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 449451423  214 LDCFLAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCV 268
Cdd:TIGR02009 129 FDAIVDASEVKNGKPHPETFLLAAELLGVPPNECIVFEDALAGVQAARAAGMFAV 183
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 148-296 9.41e-27

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


Pssm-ID: 319859 [Multi-domain]  Cd Length: 169  Bit Score: 103.10  E-value: 9.41e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 148 DILQDWKTERYKEIIKS-----GTVSPRPGVLRLMDETKSAGRKLAVCSAATKSSVILCLENLIGIDRFQNLDCflaGDD 222
Cdd:cd16423   19 EAWQELLNERRNELIKRqfsekTDLPPIEGVKELLEFLKEKGIKLAVASSSPRRWIEPHLERLGLLDYFEVIVT---GDD 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 449451423 223 VKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCVITYTTSTANQDFKEAIATYPDLSDIRLK 296
Cdd:cd16423   96 VEKSKPDPDLYLEAAERLGVNPEECVVIEDSRNGVLAAKAAGMKCVGVPNPVTGSQDFSKADLVLSSFAEKEIL 169
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
59-268 2.13e-26

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 102.28  E-value: 2.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423   59 LIFDCDGVILESEHLHRQAYNDAFVHFDvrcPNSTSQplnwsiefyDELQNRIGggkPKMRWYFKEngwpsstiFEKAPE 138
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFG---YGELSE---------EEILKFIG---LPLREIFRY--------LGVSED 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  139 DDEERAKLIdilqdwktERYKEIIKSGTVSPRPGVLRLMDETKSAGRKLAVCSAATKSSVILCLENLiGIDRFqnLDCFL 218
Cdd:pfam13419  58 EEEKIEFYL--------RKYNEELHDKLVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQL-GLEDY--FDVIV 126

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 449451423  219 AGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCV 268
Cdd:pfam13419 127 GGDDVEGKKPDPDPILKALEQLGLKPEEVIYVGDSPRDIEAAKNAGIKVI 176
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 58-268 1.19e-23

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 95.18  E-value: 1.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423   58 ALIFDCDGVILESEHLHrqayndafvHFDVRCPNSTSQPLNWSIEFYDELQNRIgggkpkMRWYFKEngwpsstifeKAP 137
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAI---------AKLINREELGLVPDELGVSAVGRLELAL------RRFKAQY----------GRT 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  138 EDDEERAKLIDILQdwkterYKEIIKSGTVSPRPGVLRLMDETKSAGRKLAVCSAA--TKSSVILCLENLigiDRFqnlD 215
Cdd:TIGR01509  56 ISPEDAQLLYKQLF------YEQIEEEAKLKPLPGVRALLEALRARGKKLALLTNSprAHKLVLALLGLR---DLF---D 123

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 449451423  216 CFLAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCV 268
Cdd:TIGR01509 124 VVIDSSDVGLGKPDPDIYLQALKALGLEPSECVFVDDSPAGIEAAKAAGMHTV 176
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 56-264 5.58e-22

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: 91.11  E-value: 5.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423   56 LQALIFDCDGVILESEHLHRQAYND-AFVHFDVRCPNSTSQPLNWSIEfydELQNRIGGGKPKmrwYFKENGwpsstIFE 134
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAElASEHPLAKAIVAAAEDLPIPVE---DFTARLLLGKRD---WLEELD-----ILR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  135 KAPEDDEERAKLIDILqdwktERYKEIIKSGTVSPRPGVLRLMDETKSAGRKLAVCSAATKSSVILCLENLiGIDRFqnL 214
Cdd:pfam00702  70 GLVETLEAEGLTVVLV-----ELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLL-GLDDY--F 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 449451423  215 DCFLAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAG 264
Cdd:pfam00702 142 DVVISGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 28-301 3.39e-20

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 91.07  E-value: 3.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423   28 SLPPSIIRFRTSRKSTTHKPFSLSVSATLQ-------------------ALIFDCDGVILESEHLHRQAYNDAFVHFDVR 88
Cdd:PLN02919   28 AFASSIRGRRSRSGVWLGKNGGARSKSCAKveeksrgaeiateewgkvsAVLFDMDGVLCNSEEPSRRAAVDVFAEMGVE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423   89 CPNSTSQPLNWSIEfydelQNRIGGGKPKmrwyfkengwpsstifEKAPEDDEERAKlidilqdwktERYKEIIKSGTVS 168
Cdd:PLN02919  108 VTVEDFVPFMGTGE-----ANFLGGVASV----------------KGVKGFDPDAAK----------KRFFEIYLEKYAK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  169 PR-----PGVLRLMDETKSAGRKLAVCSAATKSSVIlclENLIGIDRFQ-NLDCFLAGDDVKEKKPDPSIYITASKKLGV 242
Cdd:PLN02919  157 PNsgigfPGALELITQCKNKGLKVAVASSADRIKVD---ANLAAAGLPLsMFDAIVSADAFENLKPAPDIFLAAAKILGV 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 449451423  243 SEKDCLVVEDSVIGLQAATKAGMQCvITYTTSTANQDFKEAIATY--PDLSDIRLKDLDSL 301
Cdd:PLN02919  234 PTSECVVIEDALAGVQAARAAGMRC-IAVTTTLSEEILKDAGPSLirKDIGNISLSDILTG 293
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 58-296 1.76e-19

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: 84.70  E-value: 1.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  58 ALIFDCDGVILESEHLHRQAYNdafvHFDVRcpnstsqplnWSIEFyDELQNRIgggkpkmrwyfkeNGWPSSTIFEKAP 137
Cdd:cd07527    1 ALLFDMDGTLVDSTPAVERAWH----KWAKE----------HGVDP-EEVLKVS-------------HGRRAIDVIRKLA 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 138 EDDEERAKLIDILQDwKTERYKEiiksgTVSPRPGVLRLMDETKSAGRKLAVCSAATKSSVILCLENLiGIDRfqnLDCF 217
Cdd:cd07527   53 PDDADIELVLALETE-EPESYPE-----GVIAIPGAVDLLASLPAAGDRWAIVTSGTRALAEARLEAA-GLPH---PEVL 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 218 LAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCVITYTTSTANQ-DFKEAIATYPDLSDIRLK 296
Cdd:cd07527  123 VTADDVKNGKPDPEPYLLGAKLLGLDPSDCVVFEDAPAGIKAGKAAGARVVAVNTSHDLEQlEAAGADLVVEDLSDISVD 202
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 154-301 4.82e-18

beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); Lactococcus lactis beta-PGM catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate as an intermediate. In the forward G6P-forming direction, this reaction links polysaccharide phosphorolysis to glycolysis, in the reverse direction, the reaction provides G1P for the biosynthesis of exo-polysaccharides. This subfamily belongs to the beta-phosphoglucomutase-like family whose other members include Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319788 [Multi-domain]  Cd Length: 174  Bit Score: 80.03  E-value: 4.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 154 KTERYKEIIKSGTVSP-RPGVLRLMDETKSAGRKLAVCSAATKSSVILcleNLIGIDRFqnLDCFLAGDDVKEKKPDPSI 232
Cdd:cd02598   34 KNRIYVELIEELTPVDvLPGIASLLVDLKAKGIKIALASASKNAPKIL---EKLGLAEY--FDAIVDGAVLAKGKPDPDI 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 233 YITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQcVITYttsTANQDFKEAIATYPDL-SDIRLKDLDSL 301
Cdd:cd02598  109 FLAAAEGLGLNPKDCIGVEDAQAGIRAIKAAGFL-VVGV---GREEDLLGADIVVPDTtADLTIEELLEV 174
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 57-302 7.39e-17

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: 77.76  E-value: 7.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  57 QALIFDCDGVILESEHLHRQAYNDAFVHFDVrcpnstsqplnwsIEFYDELQNRIGGGKPKMRWYFKENGWPSSTIFEKA 136
Cdd:COG1011    2 KAVLFDLDGTLLDFDPVIAEALRALAERLGL-------------LDEAEELAEAYRAIEYALWRRYERGEITFAELLRRL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 137 ------PEDDEERAKLIDILQDWkterykeiiksgtVSPRPGVLRLMDETKSAGRKLAVCSAATKSSVILCLENLiGIDR 210
Cdd:COG1011   69 leelglDLAEELAEAFLAALPEL-------------VEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRL-GLDD 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 211 FqnLDCFLAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIG-LQAATKAGMQCVItYTTSTANQDFkeaiATYPD 289
Cdd:COG1011  135 L--FDAVVSSEEVGVRKPDPEIFELALERLGVPPEEALFVGDSPETdVAGARAAGMRTVW-VNRSGEPAPA----EPRPD 207

                        250
                 ....*....|...
gi 449451423 290 LSDIRLKDLDSLL 302
Cdd:COG1011  208 YVISDLAELLELL 220
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 58-268 7.73e-16

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: 74.31  E-value: 7.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  58 ALIFDCDGVILESEHLHRQAYNDAFVHFDvrcpnstSQPLnWsiefydELQNRIGG--GKPKMRWYFKENGWPSStifeK 135
Cdd:cd07529    3 HCIFDMDGLLLDTERIYTETTQEILARYG-------KTYT-W------DVKAKMMGrpASEAARIIVDELKLPMS----L 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 136 APEDDEERAKLIDilqdwkterykeiIKSGTVSPRPGVLRLMDETKSAGRKLAVCSAATKSSVILCLENLIGI-DRFQNL 214
Cdd:cd07529   65 EEEFDEQQEALAE-------------LFMGTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKELfSLFHHV 131

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 215 DCflaGDDVKEK---KPDPSIYITASKKLGVSEKD---CLVVEDSVIGLQAATKAGMQCV 268
Cdd:cd07529  132 VT---GDDPEVKgrgKPAPDIFLVAAKRFNEPPKDpskCLVFEDSPNGVKAAKAAGMQVV 188
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
57-268 5.93e-15

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 71.64  E-value: 5.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  57 QALIFDCDGVILESEHLHRQAYNDAFVHFDVRcpnstsqplnwsiefYDElQNRIGggkpkmrwyfkENGWPSSTIFEKA 136
Cdd:PRK10725   6 AGLIFDMDGTILDTEPTHRKAWREVLGRYGLQ---------------FDE-QAMVA-----------LNGSPTWRIAQAI 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 137 PEDDeeRAKLiD--ILQDWKTERYKEIIKSgTVSPRPgvlrLMDETKS-AGRK-LAVCSAATKSSVILCLENLiGIDRFq 212
Cdd:PRK10725  59 IELN--QADL-DphALAREKTEAVKSMLLD-SVEPLP----LIEVVKAwHGRRpMAVGTGSESAIAEALLAHL-GLRRY- 128

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 449451423 213 nLDCFLAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCV 268
Cdd:PRK10725 129 -FDAVVAADDVQHHKPAPDTFLRCAQLMGVQPTQCVVFEDADFGIQAARAAGMDAV 183
PLN02940 PLN02940
riboflavin kinase
 167-294 3.37e-13

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 69.48  E-value: 3.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 167 VSPRPGVLRLMDETKSAGRKLAVCSAATKSSV---ILCLENLIgidrfQNLDCFLAGDDVKEKKPDPSIYITASKKLGVS 243
Cdd:PLN02940  92 IKALPGANRLIKHLKSHGVPMALASNSPRANIeakISCHQGWK-----ESFSVIVGGDEVEKGKPSPDIFLEAAKRLNVE 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 449451423 244 EKDCLVVEDSVIGLQAATKAGMQCVITYTTSTANQDFKEAIATYPDLSDIR 294
Cdd:PLN02940 167 PSNCLVIEDSLPGVMAGKAAGMEVIAVPSIPKQTHLYSSADEVINSLLDLQ 217
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 167-267 1.76e-12

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: 63.88  E-value: 1.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 167 VSPRPGVLRLMDEtksAGRKLAVCSAATKSSVILCLENLIGIDRFQNlDCFlAGDDVKEKKPDPSIYITASKKLGVSEKD 246
Cdd:cd07526   41 LQPIPGAAAALSA---LTLPFCVASNSSRERLTHSLGLAGLLAYFEG-RIF-SASDVGRGKPAPDLFLHAAAQMGVAPER 115

                         90       100
                 ....*....|....*....|.
gi 449451423 247 CLVVEDSVIGLQAATKAGMQC 267
Cdd:cd07526  116 CLVIEDSPTGVRAALAAGMTV 136
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 58-293 3.44e-12

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: 64.22  E-value: 3.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  58 ALIFDCDGVILESEHLHRQAYNDAFVHFdvrcpnstsQPLNWSIEfydELQNRIGGGKPkmrwyfkengwpssTIFEKAP 137
Cdd:cd02616    3 TILFDLDGTLIDTNELIIKSFNHTLKEY---------GLEGYTRE---EVLPFIGPPLR--------------ETFEKID 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 138 EDDEERAKLIDIlqdwktERYKEIIKSgTVSPRPGVLRLMDETKSAGRKLAVCSAATKSSVILCLENLiGIDRFqnLDCF 217
Cdd:cd02616   57 PDKLEDMVEEFR------KYYREHNDD-LTKEYPGVYETLARLKSQGIKLGVVTTKLRETALKGLKLL-GLDKY--FDVI 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 218 LAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCVITYTTSTANQDFKEA-----IATYPDLSD 292
Cdd:cd02616  127 VGGDDVTHHKPDPEPVLKALELLGAEPEEALMVGDSPHDILAGKNAGVKTVGVTWGYKGREYLKAFnpdfiIDKMSDLLT 206


                 .
gi 449451423 293 I 293
Cdd:cd02616  207 I 207
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
139-271 3.48e-12

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 64.83  E-value: 3.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 139 DDEERAKLIDILQdwktERYKEIIKSGTVsPRPGVLRLMDETKSAGRKLAVCS-AATKSSVILcLENLiGI-DRFQNLdc 216
Cdd:PRK13222  69 DEELLEKLRELFD----RHYAENVAGGSR-LYPGVKETLAALKAAGYPLAVVTnKPTPFVAPL-LEAL-GIaDYFSVV-- 139

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 449451423 217 fLAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCVI-TY 271
Cdd:PRK13222 140 -IGGDSLPNKKPDPAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPSVGvTY 194
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 48-287 1.84e-11

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 62.94  E-value: 1.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  48 FSLSVSATLQALIFDCDGVILESEHLHRQAYNDAFvhfdvrcpnstsQPLNWSiefydelqnrigGGKPKMRWYFKEN-- 125
Cdd:PLN02770  14 SSLSGLAPLEAVLFDVDGTLCDSDPLHYYAFREML------------QEINFN------------GGVPITEEFFVENia 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 126 GWPSSTIFEKAPEDDEERAklIDILQDwKTERYKEIIKSgTVSPRPGVLRLMDETKSAGRKLAVCSAATKSSVILCLeNL 205
Cdd:PLN02770  70 GKHNEDIALGLFPDDLERG--LKFTDD-KEALFRKLASE-QLKPLNGLYKLKKWIEDRGLKRAAVTNAPRENAELMI-SL 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 206 IGIDRFqnLDCFLAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQcVITYTTSTANQDFKEAIA 285
Cdd:PLN02770 145 LGLSDF--FQAVIIGSECEHAKPHPDPYLKALEVLKVSKDHTFVFEDSVSGIKAGVAAGMP-VVGLTTRNPESLLMEAKP 221


                 ..
gi 449451423 286 TY 287
Cdd:PLN02770 222 TF 223
PRK10826 PRK10826
hexitol phosphatase HxpB;
50-301 1.95e-11

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 62.66  E-value: 1.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  50 LSVSATLQALIFDCDGVILESEHLHRQAYNDAFVHFDVrcpnstsqplnwSIEFYDELQNRIGggkpkMR-------WYf 122
Cdd:PRK10826   1 MSTPRQILAAIFDMDGLLIDSEPLWDRAELDVMASLGV------------DISRREELPDTLG-----LRidqvvdlWY- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 123 kengwpsstifEKAP---EDDEERAKLIdilqdwkTERYKEIIKSgTVSPRPGVLRLMDETKSAGRKLAVCSAatksSVI 199
Cdd:PRK10826  63 -----------ARQPwngPSRQEVVQRI-------IARVISLIEE-TRPLLPGVREALALCKAQGLKIGLASA----SPL 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 200 LCLE---NLIGI-DRFqnlDCFLAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCVITYTTST 275
Cdd:PRK10826 120 HMLEavlTMFDLrDYF---DALASAEKLPYSKPHPEVYLNCAAKLGVDPLTCVALEDSFNGMIAAKAARMRSIVVPAPEQ 196

                        250       260
                 ....*....|....*....|....*.
gi 449451423 276 ANqDFKEAIAtypdlsDIRLKDLDSL 301
Cdd:PRK10826 197 QN-DPRWALA------DVKLESLTEL 215
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 173-269 1.12e-10

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: 57.79  E-value: 1.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 173 VLRLMDETKSAGRKLAVCSAATKSSVILCLENLIGIDRFqnlDCFLAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVED 252
Cdd:cd01427   12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLF---DGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGD 88

                         90
                 ....*....|....*..
gi 449451423 253 SVIGLQAATKAGMQCVI 269
Cdd:cd01427   89 SENDIEAARAAGGRTVA 105
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 135-271 1.11e-09

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: 57.24  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 135 KAPEDDEERAKLIDILQdwktERYKEIIKSGTVsPRPGVLRLMDETKSAGRKLAVCsaaTKSSVILCLENLIGIDRFQNL 214
Cdd:cd16417   59 EAEPDEELFKEARALFD----RHYAETLSVHSH-LYPGVKEGLAALKAQGYPLACV---TNKPERFVAPLLEALGISDYF 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 449451423 215 DCFLAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCV-ITY 271
Cdd:cd16417  131 SLVLGGDSLPEKKPDPAPLLHACEKLGIAPAQMLMVGDSRNDILAARAAGCPSVgLTY 188
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 58-269 3.06e-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: 56.17  E-value: 3.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  58 ALIFDCDGVILESE-HLHrQAYNDAFVHFDVRcpnstsqPLNwsiefYDELQNRIGGGKPKM-RWYFKENGwpsstifek 135
Cdd:cd07512    1 AVIFDLDGTLIDSApDLH-AALNAVLAAEGLA-------PLS-----LAEVRSFVGHGAPALiRRAFAAAG--------- 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 136 APEDDEERAKLIDILQDwkteRYKEIIKSGTvSPRPGVLRLMDETKSAGRKLAVCS-AATKSSVILcLENLiGIDRFqnL 214
Cdd:cd07512   59 EDLDGPLHDALLARFLD----HYEADPPGLT-RPYPGVIEALERLRAAGWRLAICTnKPEAPARAL-LSAL-GLADL--F 129

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 449451423 215 DCFLAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCVI 269
Cdd:cd07512  130 AAVVGGDTLPQRKPDPAPLRAAIRRLGGDVSRALMVGDSETDAATARAAGVPFVL 184
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 55-266 8.89e-09

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 54.70  E-value: 8.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  55 TLQALIFDCDGVILESEHLHRQAYNDAFVHFDVRCPnstsqplnwsiefYDELQNRIGGgkpkMRWY------FKENGWp 128
Cdd:PRK10563   3 QIEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLS-------------LEEVFKRFKG----VKLYeiidiiSKEHGV- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 129 SSTIFEKAPEDDEERAKLIDI-LQdwkterykeiiksgtvsPRPGVLRLMDETKSAgrkLAVCSAATKSSVILCLENLIG 207
Cdd:PRK10563  65 TLAKAELEPVYRAEVARLFDSeLE-----------------PIAGANALLESITVP---MCVVSNGPVSKMQHSLGKTGM 124

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 449451423 208 IDRFQnlDCFLAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQ 266
Cdd:PRK10563 125 LHYFP--DKLFSGYDIQRWKPDPALMFHAAEAMNVNVENCILVDDSSAGAQSGIAAGME 181
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 154-301 6.64e-08

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 52.73  E-value: 6.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 154 KTERYKEIIKSGTVSPRPGVLRLMDETKSAGRKLAVCSAATKSSVILCLEnLIGIDRFqnLDCFLAGDDVKEKKPDPSIY 233
Cdd:PLN03243  95 RKEDLYEYMQGGLYRLRPGSREFVQALKKHEIPIAVASTRPRRYLERAIE-AVGMEGF--FSVVLAAEDVYRGKPDPEMF 171

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 449451423 234 ITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCVI------TYTTSTANQdfkeAIATYPDLSDIRLKDLDSL 301
Cdd:PLN03243 172 MYAAERLGFIPERCIVFGNSNSSVEAAHDGCMKCVAvagkhpVYELSAGDL----VVRRLDDLSVVDLKNLSDL 241
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 140-264 6.87e-08

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 51.95  E-value: 6.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 140 DEERA-KLIDILQDWKTERYKEIIKsgtvsPRPGVLRLMDETKSAGRKLAVCSAATKSSVILCLEnLIGIDRFqnLDCFL 218
Cdd:PRK13288  58 DESKVeEMITTYREFNHEHHDELVT-----EYETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLK-LTGLDEF--FDVVI 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 449451423 219 AGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDS----VIGLQAATKAG 264
Cdd:PRK13288 130 TLDDVEHAKPDPEPVLKALELLGAKPEEALMVGDNhhdiLAGKNAGTKTA 179
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 139-266 1.58e-07

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: 50.81  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 139 DDEERAKLIDILQDWKTERYKEIIKSGTVSPRPGVLRLMDETKSAGRKLAVCSAATKSSVILCLENLIgiDRFQNLDCFL 218
Cdd:cd02603   55 EEEFWEELREELGRPLSAELFEELVLAAVDPNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLP--RRGDLFDGVV 132

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 449451423 219 AGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQ 266
Cdd:cd02603  133 ESCRLGVRKPDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGIH 180
PLN02811 PLN02811
hydrolase
 171-269 3.94e-07

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 49.76  E-value: 3.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 171 PGVLRLMDETKSAGRKLAVCSAATKSSVILCLENliGIDRFQNLDCFLAGDD--VKEKKPDPSIYITASKKL---GVSEK 245
Cdd:PLN02811  81 PGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQR--HGELFSLMHHVVTGDDpeVKQGKPAPDIFLAAARRFedgPVDPG 158

                         90       100
                 ....*....|....*....|....
gi 449451423 246 DCLVVEDSVIGLQAATKAGMQCVI 269
Cdd:PLN02811 159 KVLVFEDAPSGVEAAKNAGMSVVM 182
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 58-264 2.11e-06

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: 47.01  E-value: 2.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423   58 ALIFDCDGVILESEHLHRQAYNDAFVHFDVRCPNstsqplnwsiefYDELqNRIGGGKPKMRWYFKENGWpsstifekap 137
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFGLDPAS------------FKAL-KQAGGLAEEEWYRIATSAL---------- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  138 edDEERAKlidILQDWKTERYKeiiksgtvspRPGVLRLMDETKSAGRKLAVCSAATKSSVILCLENLIGIDRFQnldcF 217
Cdd:TIGR01549  58 --EELQGR---FWSEYDAEEAY----------IRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFE----L 118

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 449451423  218 LAGDDVKEKKPDPSIYITASKKLGVSEkDCLVVEDSVIGLQAATKAG 264
Cdd:TIGR01549 119 ILVSDEPGSKPEPEIFLAALESLGVPP-EVLHVGDNLNDIEGARNAG 164
PRK11587 PRK11587
putative phosphatase; Provisional
 217-269 9.84e-06

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 45.76  E-value: 9.84e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 449451423 217 FLAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQcVI 269
Cdd:PRK11587 128 FVTAERVKRGKPEPDAYLLGAQLLGLAPQECVVVEDAPAGVLSGLAAGCH-VI 179
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 170-293 1.11e-05

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: 45.72  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 170 RPGVLRLmdetKSAGRKLAVCSAATKSSVILCLENLiGIDRFqnLDCFLAGDDVKEKKPDPSIYITASKKLGVSEKDCLV 249
Cdd:cd02588   97 VAGLRRL----REAGYRLAILSNGSPDLIEDVVANA-GLRDL--FDAVLSAEDVRAYKPAPAVYELAAERLGVPPDEILH 169

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 449451423 250 VEDSVIGLQAATKAGMQCV-ITYTTSTANQDFKEAIATYPDLSDI 293
Cdd:cd02588  170 VASHAWDLAGARALGLRTAwINRPGEVPDPLGPAPDFVVPDLGEL 214
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 173-265 1.49e-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: 43.21  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 173 VLRLMDETKSAGRKLAVCSAATKSSVILCLENLIGIdRFQnldcFLAG--DDVKeKKPDPSIYITASKKLGVSEKDCLVV 250
Cdd:cd16421   12 ILELLKALRQKGIKLAVLSNKPNEAVQVLVEELFPG-SFD----FVLGekEGIR-RKPDPT*ALECAKVLGVPPDEVLYV 85

                         90
                 ....*....|....*
gi 449451423 251 EDSVIGLQAATKAGM 265
Cdd:cd16421   86 GDSGVDMQTARNAGM 100
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 59-268 1.85e-05

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: 44.70  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423  59 LIFDCDGVILESEHLHRQAYNDAFVHFDVrcPNSTSQPLNWSIEFydELQNRIgggkpkmrwyfkengwpsSTIFEKAPE 138
Cdd:cd07533    2 VIFDWDGTLADSQHNIVAAMTAAFADLGL--PVPSAAEVRSIIGL--SLDEAI------------------ARLLPMATP 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 139 DDEERAklidilqdwktERYKE-----IIKSGTVSPR-PGVLRLMDETKSAGRKLAVCSAATKSSVILCLENLIGIDRFQ 212
Cdd:cd07533   60 ALVAVA-----------ERYKEafdilRLLPEHAEPLfPGVREALDALAAQGVLLAVATGKSRRGLDRVLEQHGLGGYFD 128

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 449451423 213 NLDCflAGDdvKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCV 268
Cdd:cd07533  129 ATRT--ADD--TPSKPHPEMLREILAELGVDPSRAVMVGDTAYDMQMAANAGAHAV 180
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 202-268 8.92e-05

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


Pssm-ID: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 40.99  E-value: 8.92e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 449451423 202 LENLiGIDRFqnLDCFLAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDS----VIGlqaATKAGMQCV 268
Cdd:cd04305   42 LEQL-GIHKY--FDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLMVGDSlesdILG---AKNAGIKTV 106
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
 218-271 9.28e-05

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 43.31  E-value: 9.28e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 449451423 218 LAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCV-ITY 271
Cdd:PRK13223 148 IGGDTLPQKKPDPAALLFVMKMAGVPPSQSLFVGDSRSDVLAAKAAGVQCVaLSY 202
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 206-268 1.02e-04

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 43.32  E-value: 1.02e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 449451423 206 IGIDRFqnLDCFLAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCV 268
Cdd:PLN02575 253 IGIRGF--FSVIVAAEDVYRGKPDPEMFIYAAQLLNFIPERCIVFGNSNQTVEAAHDARMKCV 313
PRK13226 PRK13226
phosphoglycolate phosphatase; Provisional
 139-268 1.38e-04

phosphoglycolate phosphatase; Provisional


Pssm-ID: 237311 [Multi-domain]  Cd Length: 229  Bit Score: 42.53  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 139 DDEERAKLI-DILQdwkteRYKEIIksGTVS-PRPGVLRLMDETKSAGRKLAVCSAATKSSVILCLENLIGIDRFQNLdc 216
Cdd:PRK13226  71 DAAARDALIpEFLQ-----RYEALI--GTQSqLFDGVEGMLQRLECAGCVWGIVTNKPEYLARLILPQLGWEQRCAVL-- 141

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 449451423 217 fLAGDDVKEKKPDPSIYITASKKLGVSEKDCLVVEDSVIGLQAATKAGMQCV 268
Cdd:PRK13226 142 -IGGDTLAERKPHPLPLLVAAERIGVAPTDCVYVGDDERDILAARAAGMPSV 192
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 184-269 8.59e-03

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p; This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and 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: 319791 [Multi-domain]  Cd Length: 182  Bit Score: 36.46  E-value: 8.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449451423 184 GRKLAVCSAAtKSSVILCLENLiGIDrfqnlDCFlagDDV-------KEKKPDPSIYITASKKLGVSEKDCLVVEDSVIG 256
Cdd:cd02604   97 GRKIIFTNAS-KNHAIRVLKRL-GLA-----DLF---DGIfdieyagPDPKPHPAAFEKAIREAGLDPKRAAFFDDSIRN 166

                         90
                 ....*....|...
gi 449451423 257 LQAATKAGMQCVI 269
Cdd:cd02604  167 LLAAKALGMKTVL 179
 
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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