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Conserved domains on  [gi|18420570|ref|NP_568077|]
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Haloacid dehalogenase-like hydrolase (HAD) superfamily protein [Arabidopsis thaliana]

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
 29-316 1.66e-160

haloacid dehalogenase-like hydrolase family protein


:

Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 448.77  E-value: 1.66e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570   29 LIGFPRFQTLRFKSRSVYSKSRVSSPVSALPLRSLEALIFDCDGVILESE-NLHRQAYNDAFSHFDVRcppssseSLDWS 107
Cdd:PLN02779   6 SARLASASRTRAGRRRRRRSRSTARVASASASALPEALLFDCDGVLVETErDGHRVAFNDAFKEFGLR-------PVEWD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  108 LEFYDKFQNlVGGGKPKMRWYFKENGWPTSTIfDSPPQNDDDRAKLIDTLQDWKTERYKEIIKSGSVEPRPGVIRLMDEA 187
Cdd:PLN02779  79 VELYDELLN-IGGGKERMTWYFNENGWPTSTI-EKAPKDEEERKELVDSLHDRKTELFKELIESGALPLRPGVLRLMDEA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  188 KAAGKKLAVCSAATKSSVILCLENLIDIERFQGLDCFlAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAA 267
Cdd:PLN02779 157 LAAGIKVAVCSTSNEKAVSKIVNTLLGPERAQGLDVF-AGDDVPKKKPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAA 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 18420570  268 TKAGMSCVITYTSSTSDQNFNDAIAVYPDLSNVKLKDLETLLQTIVTAA 316
Cdd:PLN02779 236 KAAGMRCIVTKSSYTADEDFSGADAVFDCLGDVPLEDFDLLFCESLLTK 284
 
Name Accession Description Interval E-value
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 29-316 1.66e-160

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 448.77  E-value: 1.66e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570   29 LIGFPRFQTLRFKSRSVYSKSRVSSPVSALPLRSLEALIFDCDGVILESE-NLHRQAYNDAFSHFDVRcppssseSLDWS 107
Cdd:PLN02779   6 SARLASASRTRAGRRRRRRSRSTARVASASASALPEALLFDCDGVLVETErDGHRVAFNDAFKEFGLR-------PVEWD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  108 LEFYDKFQNlVGGGKPKMRWYFKENGWPTSTIfDSPPQNDDDRAKLIDTLQDWKTERYKEIIKSGSVEPRPGVIRLMDEA 187
Cdd:PLN02779  79 VELYDELLN-IGGGKERMTWYFNENGWPTSTI-EKAPKDEEERKELVDSLHDRKTELFKELIESGALPLRPGVLRLMDEA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  188 KAAGKKLAVCSAATKSSVILCLENLIDIERFQGLDCFlAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAA 267
Cdd:PLN02779 157 LAAGIKVAVCSTSNEKAVSKIVNTLLGPERAQGLDVF-AGDDVPKKKPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAA 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 18420570  268 TKAGMSCVITYTSSTSDQNFNDAIAVYPDLSNVKLKDLETLLQTIVTAA 316
Cdd:PLN02779 236 KAAGMRCIVTKSSYTADEDFSGADAVFDCLGDVPLEDFDLLFCESLLTK 284
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 65-279 5.18e-107

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: 310.08  E-value: 5.18e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  65 ALIFDCDGVILESENLHRQAYNDAFSHFDvrcppssSESLDWSLEFYDKFQNLVGGGKPKMRWYFKEnGWPTSTIFDSPp 144
Cdd:cd07528   1 ALIFDVDGTLAETEELHRRAFNNAFFAER-------GLDWYWDRELYGELLRVGGGKERIAAYFEKV-GWPESAPKDLK- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 145 qndddraKLIDTLQDWKTERYKEIIKSGSVEPRPGVIRLMDEAKAAGKKLAVCSAATKSSVILCLENLIDIERFQGLDCF 224
Cdd:cd07528  72 -------ELIADLHKAKTERYAELIAAGLLPLRPGVARLIDEAKAAGVRLAIATTTSPANVDALLSALLGPERRAIFDAI 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18420570 225 LAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSCVITYT 279
Cdd:cd07528 145 AAGDDVAEKKPDPDIYLLALERLGVSPSDCLAIEDSAIGLQAAKAAGLPCIVTPS 199
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
63-300 3.55e-63

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 198.89  E-value: 3.55e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  63 LEALIFDCDGVILESENLHRQAYNDAFSHFDVrcppssseslDWSLEFYDKFqnlVGGGKPKM-RWYFKENGWPTStifd 141
Cdd:COG0637   2 IKAVIFDMDGTLVDSEPLHARAWREAFAELGI----------DLTEEEYRRL---MGRSREDIlRYLLEEYGLDLP---- 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 142 sppqndddraklIDTLQDWKTERYKEIIKSGSVEPRPGVIRLMDEAKAAGKKLAVCSAATKSSVILCLENLIDIERFqgl 221
Cdd:COG0637  65 ------------EEELAARKEELYRELLAEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYF--- 129

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18420570 222 DCFLAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSCVITYTSSTSDQNFNDAIAVYPDLSNV 300
Cdd:COG0637 130 DVIVTGDDVARGKPDPDIYLLAAERLGVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 63-275 1.73e-31

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: 116.29  E-value: 1.73e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570    63 LEALIFDCDGVILESENLHRQAYNDAFSHFdvrcppsssesldwSLEFyDKFQNLVGGGKPKM---RWYFKENGWPTSTi 139
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKY--------------GISF-DKQYNESLKGLSREdilRAILKLRGDGLSL- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570   140 fdsppqndddraKLIDTLQDWKTERYKEIIKSGSVEPRPGVIRLMDEAKAAGKKLAVCSAATKSSVILCLENLIDieRFq 219
Cdd:TIGR02009  65 ------------EEIHQLAERKNELYRELLRLTGVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRD--YF- 129

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 18420570   220 glDCFLAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSCV 275
Cdd:TIGR02009 130 --DAIVDASEVKNGKPHPETFLLAAELLGVPPNECIVFEDALAGVQAARAAGMFAV 183
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
66-275 4.25e-28

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 106.90  E-value: 4.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570    66 LIFDCDGVILESENLHRQAYNDAFSHFDVRcppssseslDWSLEFYDKFQNlvgggkPKMRWYFKEngwptstiFDSPPQ 145
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYG---------ELSEEEILKFIG------LPLREIFRY--------LGVSED 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570   146 NDDDRAKLIdtlqdwktERYKEIIKSGSVEPRPGVIRLMDEAKAAGKKLAVCSAATKSSVILCLENLiDIERFqgLDCFL 225
Cdd:pfam13419  58 EEEKIEFYL--------RKYNEELHDKLVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQL-GLEDY--FDVIV 126

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 18420570   226 AGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSCV 275
Cdd:pfam13419 127 GGDDVEGKKPDPDPILKALEQLGLKPEEVIYVGDSPRDIEAAKNAGIKVI 176
 
Name Accession Description Interval E-value
PLN02779 PLN02779
haloacid dehalogenase-like hydrolase family protein
 29-316 1.66e-160

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215416 [Multi-domain]  Cd Length: 286  Bit Score: 448.77  E-value: 1.66e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570   29 LIGFPRFQTLRFKSRSVYSKSRVSSPVSALPLRSLEALIFDCDGVILESE-NLHRQAYNDAFSHFDVRcppssseSLDWS 107
Cdd:PLN02779   6 SARLASASRTRAGRRRRRRSRSTARVASASASALPEALLFDCDGVLVETErDGHRVAFNDAFKEFGLR-------PVEWD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  108 LEFYDKFQNlVGGGKPKMRWYFKENGWPTSTIfDSPPQNDDDRAKLIDTLQDWKTERYKEIIKSGSVEPRPGVIRLMDEA 187
Cdd:PLN02779  79 VELYDELLN-IGGGKERMTWYFNENGWPTSTI-EKAPKDEEERKELVDSLHDRKTELFKELIESGALPLRPGVLRLMDEA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  188 KAAGKKLAVCSAATKSSVILCLENLIDIERFQGLDCFlAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAA 267
Cdd:PLN02779 157 LAAGIKVAVCSTSNEKAVSKIVNTLLGPERAQGLDVF-AGDDVPKKKPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAA 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 18420570  268 TKAGMSCVITYTSSTSDQNFNDAIAVYPDLSNVKLKDLETLLQTIVTAA 316
Cdd:PLN02779 236 KAAGMRCIVTKSSYTADEDFSGADAVFDCLGDVPLEDFDLLFCESLLTK 284
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 65-279 5.18e-107

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: 310.08  E-value: 5.18e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  65 ALIFDCDGVILESENLHRQAYNDAFSHFDvrcppssSESLDWSLEFYDKFQNLVGGGKPKMRWYFKEnGWPTSTIFDSPp 144
Cdd:cd07528   1 ALIFDVDGTLAETEELHRRAFNNAFFAER-------GLDWYWDRELYGELLRVGGGKERIAAYFEKV-GWPESAPKDLK- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 145 qndddraKLIDTLQDWKTERYKEIIKSGSVEPRPGVIRLMDEAKAAGKKLAVCSAATKSSVILCLENLIDIERFQGLDCF 224
Cdd:cd07528  72 -------ELIADLHKAKTERYAELIAAGLLPLRPGVARLIDEAKAAGVRLAIATTTSPANVDALLSALLGPERRAIFDAI 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18420570 225 LAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSCVITYT 279
Cdd:cd07528 145 AAGDDVAEKKPDPDIYLLALERLGVSPSDCLAIEDSAIGLQAAKAAGLPCIVTPS 199
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
63-300 3.55e-63

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 198.89  E-value: 3.55e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  63 LEALIFDCDGVILESENLHRQAYNDAFSHFDVrcppssseslDWSLEFYDKFqnlVGGGKPKM-RWYFKENGWPTStifd 141
Cdd:COG0637   2 IKAVIFDMDGTLVDSEPLHARAWREAFAELGI----------DLTEEEYRRL---MGRSREDIlRYLLEEYGLDLP---- 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 142 sppqndddraklIDTLQDWKTERYKEIIKSGSVEPRPGVIRLMDEAKAAGKKLAVCSAATKSSVILCLENLIDIERFqgl 221
Cdd:COG0637  65 ------------EEELAARKEELYRELLAEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYF--- 129

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18420570 222 DCFLAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSCVITYTSSTSDQNFNDAIAVYPDLSNV 300
Cdd:COG0637 130 DVIVTGDDVARGKPDPDIYLLAAERLGVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 65-275 1.07e-34

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


Pssm-ID: 319808 [Multi-domain]  Cd Length: 143  Bit Score: 123.11  E-value: 1.07e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  65 ALIFDCDGVILESENLHRQAYNdafshfdvrcppsssesldwslefydkfqnlvgggkpkmrwyfkengwptstifdspp 144
Cdd:cd07505   1 AVIFDMDGVLIDTEPLHRQAWQ---------------------------------------------------------- 22

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 145 qndddraklidtLQDWKTERYKEIIKSGSVEPRPGVIRLMDEAKAAGKKLAVCSAATKSSVILCLENLIDIERFQglDCF 224
Cdd:cd07505  23 ------------LLERKNALLLELIASEGLKLKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLRGYF--DVI 88

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 18420570 225 LAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSCV 275
Cdd:cd07505  89 VSGDDVERGKPAPDIYLLAAERLGVDPERCLVFEDSLAGIEAAKAAGMTVV 139
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 63-275 1.73e-31

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: 116.29  E-value: 1.73e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570    63 LEALIFDCDGVILESENLHRQAYNDAFSHFdvrcppsssesldwSLEFyDKFQNLVGGGKPKM---RWYFKENGWPTSTi 139
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKY--------------GISF-DKQYNESLKGLSREdilRAILKLRGDGLSL- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570   140 fdsppqndddraKLIDTLQDWKTERYKEIIKSGSVEPRPGVIRLMDEAKAAGKKLAVCSAATKSSVILCLENLIDieRFq 219
Cdd:TIGR02009  65 ------------EEIHQLAERKNELYRELLRLTGVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRILAKLGLRD--YF- 129

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 18420570   220 glDCFLAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSCV 275
Cdd:TIGR02009 130 --DAIVDASEVKNGKPHPETFLLAAELLGVPPNECIVFEDALAGVQAARAAGMFAV 183
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
65-311 2.74e-28

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 108.48  E-value: 2.74e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  65 ALIFDCDGVILESENLHRQAYNDAFSHFDVRCPPsssesldwslefYDKFQNLVGGGKPKMrwyFKEngwptstIFDSPP 144
Cdd:COG0546   3 LVLFDLDGTLVDSAPDIAAALNEALAELGLPPLD------------LEELRALIGLGLREL---LRR-------LLGEDP 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 145 qnDDDRAKLIDTLQdwktERYKEIIKSGSvEPRPGVIRLMDEAKAAGKKLAVCSAATKSSVILCLENLiDIERFqgLDCF 224
Cdd:COG0546  61 --DEELEELLARFR----ELYEEELLDET-RLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEAL-GLDDY--FDAI 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 225 LAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSCV-ITYTSSTSDQNFN-DAIAVYPDLSnvkl 302
Cdd:COG0546 131 VGGDDVPPAKPKPEPLLEALERLGLDPEEVLMVGDSPHDIEAARAAGVPFIgVTWGYGSAEELEAaGADYVIDSLA---- 206


                ....*....
gi 18420570 303 kDLETLLQT 311
Cdd:COG0546 207 -ELLALLAE 214
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
66-275 4.25e-28

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 106.90  E-value: 4.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570    66 LIFDCDGVILESENLHRQAYNDAFSHFDVRcppssseslDWSLEFYDKFQNlvgggkPKMRWYFKEngwptstiFDSPPQ 145
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYG---------ELSEEEILKFIG------LPLREIFRY--------LGVSED 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570   146 NDDDRAKLIdtlqdwktERYKEIIKSGSVEPRPGVIRLMDEAKAAGKKLAVCSAATKSSVILCLENLiDIERFqgLDCFL 225
Cdd:pfam13419  58 EEEKIEFYL--------RKYNEELHDKLVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQL-GLEDY--FDVIV 126

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 18420570   226 AGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSCV 275
Cdd:pfam13419 127 GGDDVEGKKPDPDPILKALEQLGLKPEEVIYVGDSPRDIEAAKNAGIKVI 176
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 65-290 1.51e-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: 105.41  E-value: 1.51e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  65 ALIFDCDGVILESENLHRQAYNDAFShfdvrcppsssesldwslefydkfqnlvgggkpkmrwyfkengwptstifdspp 144
Cdd:cd16423   1 AVIFDFDGVIVDTEPLWYEAWQELLN------------------------------------------------------ 26

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 145 QNDDDRAKlidtlqdwkteryKEIIKSGSVEPRPGVIRLMDEAKAAGKKLAVCSAATKSSVIlclenlIDIERFQGLDCF 224
Cdd:cd16423  27 ERRNELIK-------------RQFSEKTDLPPIEGVKELLEFLKEKGIKLAVASSSPRRWIE------PHLERLGLLDYF 87

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18420570 225 ---LAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSCVITYTSSTSDQNFNDA 290
Cdd:cd16423  88 eviVTGDDVEKSKPDPDLYLEAAERLGVNPEECVVIEDSRNGVLAAKAAGMKCVGVPNPVTGSQDFSKA 156
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 65-275 1.01e-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: 95.56  E-value: 1.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570    65 ALIFDCDGVILESENLHRQAYNdafsHFDVRCPP-----SSSESLDWSLEFydkFQNLVGGGKPKMRWY-FKENgwptst 138
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAIAKLIN----REELGLVPdelgvSAVGRLELALRR---FKAQYGRTISPEDAQlLYKQ------ 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570   139 ifdsppqndddraklidtlqdwktERYKEIIKSGSVEPRPGVIRLMDEAKAAGKKLAVCSAATKssvILCLE-NLIDIER 217
Cdd:TIGR01509  68 ------------------------LFYEQIEEEAKLKPLPGVRALLEALRARGKKLALLTNSPR---AHKLVlALLGLRD 120

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 18420570   218 FqgLDCFLAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSCV 275
Cdd:TIGR01509 121 L--FDVVIDSSDVGLGKPDPDIYLQALKALGLEPSECVFVDDSPAGIEAAKAAGMHTV 176
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 63-271 1.12e-23

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: 95.73  E-value: 1.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570    63 LEALIFDCDGVILESENLHRQAYNDAFS-HFDVRCPPSSSESLDWSLEfydKFQNLVGGGKPKmrwYFKENGwptstifd 141
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASeHPLAKAIVAAAEDLPIPVE---DFTARLLLGKRD---WLEELD-------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570   142 spPQNDDDRAKLIDTLQDWKTERYKEIIKSGSVEPRPGVIRLMDEAKAAGKKLAVCSAATKSSVILCLENLIDIERFqgl 221
Cdd:pfam00702  67 --ILRGLVETLEAEGLTVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYF--- 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 18420570   222 DCFLAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAG 271
Cdd:pfam00702 142 DVVISGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 65-300 8.56e-20

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: 85.47  E-value: 8.56e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  65 ALIFDCDGVILESENLHRQAYNdafsHFDVRCPPSSSESLDWSlefydkfqnlvgggkpkmrwyfkeNGWPTST---IFD 141
Cdd:cd07527   1 ALLFDMDGTLVDSTPAVERAWH----KWAKEHGVDPEEVLKVS------------------------HGRRAIDvirKLA 52

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 142 sppqNDDDRAKLIDtlqdwKTERYKEIIKSGSVEPRPGVIRLMDEAKAAGKKLAVCSAATKSSVILCLENLidierfqGL 221
Cdd:cd07527  53 ----PDDADIELVL-----ALETEEPESYPEGVIAIPGAVDLLASLPAAGDRWAIVTSGTRALAEARLEAA-------GL 116

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 222 ---DCFLAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSCVITYTSSTSDQNFND-AIAVYPDL 297
Cdd:cd07527 117 phpEVLVTADDVKNGKPDPEPYLLGAKLLGLDPSDCVVFEDAPAGIKAGKAAGARVVAVNTSHDLEQLEAAgADLVVEDL 196


                ...
gi 18420570 298 SNV 300
Cdd:cd07527 197 SDI 199
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 64-309 4.11e-19

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: 83.92  E-value: 4.11e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  64 EALIFDCDGVILESENLHRQAYNDAFSHFDVrcpPSSSESL--DWSLEFYDKFQNLVGGGKPK---MRWYFKENGWPTSt 138
Cdd:COG1011   2 KAVLFDLDGTLLDFDPVIAEALRALAERLGL---LDEAEELaeAYRAIEYALWRRYERGEITFaelLRRLLEELGLDLA- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 139 ifdsppqnDDDRAKLIDTLQDWkterykeiiksgsVEPRPGVIRLMDEAKAAGKKLAVCSAATKSSVILCLENLiDIERF 218
Cdd:COG1011  78 --------EELAEAFLAALPEL-------------VEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRL-GLDDL 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 219 qgLDCFLAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIG-LQAATKAGM-SCVITytsstsDQNFNDAIAVYPD 296
Cdd:COG1011 136 --FDAVVSSEEVGVRKPDPEIFELALERLGVPPEEALFVGDSPETdVAGARAAGMrTVWVN------RSGEPAPAEPRPD 207

                       250
                ....*....|...
gi 18420570 297 LSNVKLKDLETLL 309
Cdd:COG1011 208 YVISDLAELLELL 220
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 161-272 2.04e-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: 81.18  E-value: 2.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 161 KTERYKEIIKSGSVEP-RPGVIRLMDEAKAAGKKLAVCSAATKSSVILCLENLIDIerfqgLDCFLAGDDVKEKKPDPSI 239
Cdd:cd02598  34 KNRIYVELIEELTPVDvLPGIASLLVDLKAKGIKIALASASKNAPKILEKLGLAEY-----FDAIVDGAVLAKGKPDPDI 108

                        90       100       110
                ....*....|....*....|....*....|...
gi 18420570 240 YITAAEKLGVSVKDCLVVEDSVIGLQAATKAGM 272
Cdd:cd02598 109 FLAAAEGLGLNPKDCIGVEDAQAGIRAIKAAGF 141
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 44-308 4.97e-18

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 84.90  E-value: 4.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570    44 SVYSKSRVSSpVSALPLRSLEALIFDCDGVILESENLHRQAYNDAFSHFDVRCPPsssesldwslefyDKFQNLVGGGKP 123
Cdd:PLN02919   57 KVEEKSRGAE-IATEEWGKVSAVLFDMDGVLCNSEEPSRRAAVDVFAEMGVEVTV-------------EDFVPFMGTGEA 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570   124 KMRwyfkenGWPTSTifDSPPQNDDDRAKlidtlqdwktERYKEIIKSGSVEPR-----PGVIRLMDEAKAAGKKLAVCS 198
Cdd:PLN02919  123 NFL------GGVASV--KGVKGFDPDAAK----------KRFFEIYLEKYAKPNsgigfPGALELITQCKNKGLKVAVAS 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570   199 AATKSSVIlclENL----IDIERFqglDCFLAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSC 274
Cdd:PLN02919  185 SADRIKVD---ANLaaagLPLSMF---DAIVSADAFENLKPAPDIFLAAAKILGVPTSECVVIEDALAGVQAARAAGMRC 258

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 18420570   275 vITYTSSTSDQNFNDA--IAVYPDLSNVKLKDLETL 308
Cdd:PLN02919  259 -IAVTTTLSEEILKDAgpSLIRKDIGNISLSDILTG 293
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
64-275 7.16e-17

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 77.04  E-value: 7.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570   64 EALIFDCDGVILESENLHRQAYNDAFSHFDVRcppsssesldwslefYDKfQNLVGggkpkmrwyfkENGWPTSTIFDS- 142
Cdd:PRK10725   6 AGLIFDMDGTILDTEPTHRKAWREVLGRYGLQ---------------FDE-QAMVA-----------LNGSPTWRIAQAi 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  143 --PPQNDDDRAKLIDTlqdwKTERYKEIIKSgSVEPRPgvirLMDEAKA-AGKK-LAVCSAATKSSVILCLENLidierf 218
Cdd:PRK10725  59 ieLNQADLDPHALARE----KTEAVKSMLLD-SVEPLP----LIEVVKAwHGRRpMAVGTGSESAIAEALLAHL------ 123

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18420570  219 qGL-DCF---LAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSCV 275
Cdd:PRK10725 124 -GLrRYFdavVAADDVQHHKPAPDTFLRCAQLMGVQPTQCVVFEDADFGIQAARAAGMDAV 183
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 64-274 3.16e-16

subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli 6-phosphogluconate phosphatase YieH; This subfamily includes Escherichia coli YieH/HAD3 an 6-phosphogluconate phosphatase, which can hydrolyzed purines and pyrimidines as secondary substrates. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate, and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319828 [Multi-domain]  Cd Length: 141  Bit Score: 74.28  E-value: 3.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  64 EALIFDCDGVILESENLHRQAYNDAFSHFDVRcppsssesldwslefydkfqnlvgggkpkmrwyfkengwptstifdsp 143
Cdd:cd07526   1 DLVIFDCDGVLVDSEVIAARVLVEVLAELGAR------------------------------------------------ 32

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 144 pqndddRAKLIDTlqdwkterykeiiksgSVEPRPGVIRLMDeakAAGKKLAVCSAATKSSVILCLENLIDIERFQGlDC 223
Cdd:cd07526  33 ------VLAAFEA----------------ELQPIPGAAAALS---ALTLPFCVASNSSRERLTHSLGLAGLLAYFEG-RI 86

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 18420570 224 FlAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSC 274
Cdd:cd07526  87 F-SASDVGRGKPAPDLFLHAAAQMGVAPERCLVIEDSPTGVRAALAAGMTV 136
HAD_AtGPP-like cd07529
subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and ...
 64-275 1.40e-14

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: 70.84  E-value: 1.40e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  64 EALIFDCDGVILESENLHRQAYNDAFSHFDvrcppsssESLDWSLefydKFQNLVGGGKPKMRWYFKENGWPtstifDSP 143
Cdd:cd07529   2 THCIFDMDGLLLDTERIYTETTQEILARYG--------KTYTWDV----KAKMMGRPASEAARIIVDELKLP-----MSL 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 144 PQN-DDDRAKLIDtlqdwkterykeiIKSGSVEPRPGVIRLMDEAKAAGKKLAVCSAATKSSVILCLENLIDIerFQGLD 222
Cdd:cd07529  65 EEEfDEQQEALAE-------------LFMGTAKLMPGAERLLRHLHAHNIPIALATSSCTRHFKLKTSRHKEL--FSLFH 129

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18420570 223 CFLAGDDVKEK---KPDPSIYITAAEKLGVSVKD---CLVVEDSVIGLQAATKAGMSCV 275
Cdd:cd07529 130 HVVTGDDPEVKgrgKPAPDIFLVAAKRFNEPPKDpskCLVFEDSPNGVKAAKAAGMQVV 188
PRK10826 PRK10826
hexitol phosphatase HxpB;
61-308 2.34e-14

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 70.75  E-value: 2.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570   61 RSLEALIFDCDGVILESENLHRQAYNDAFShfdvrcppssseSLDWSLEFYDKFQNLVGggkpkMR-------WYFKEng 133
Cdd:PRK10826   5 RQILAAIFDMDGLLIDSEPLWDRAELDVMA------------SLGVDISRREELPDTLG-----LRidqvvdlWYARQ-- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  134 wptstifdspPQNDDDRAKLIDTLQDwkteRYKEIIKSgSVEPRPGVIRLMDEAKAAGKKLAVCSAatksSVILCLE--- 210
Cdd:PRK10826  66 ----------PWNGPSRQEVVQRIIA----RVISLIEE-TRPLLPGVREALALCKAQGLKIGLASA----SPLHMLEavl 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  211 NLIDI-ERFqglDCFLAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGM-SCVITYTSSTSDQNFn 288
Cdd:PRK10826 127 TMFDLrDYF---DALASAEKLPYSKPHPEVYLNCAAKLGVDPLTCVALEDSFNGMIAAKAARMrSIVVPAPEQQNDPRW- 202

                        250       260
                 ....*....|....*....|
gi 18420570  289 dAIAvypdlsNVKLKDLETL 308
Cdd:PRK10826 203 -ALA------DVKLESLTEL 215
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
60-278 5.83e-14

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 69.84  E-value: 5.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570   60 LRSLEALIFDCDGVILES-ENLHRqAYNDAFSHFDVrcPPSSsesldwslefYDKFQNLVGGGKPKM-----RWYFKEng 133
Cdd:PRK13222   3 FMDIRAVAFDLDGTLVDSaPDLAA-AVNAALAALGL--PPAG----------EERVRTWVGNGADVLveralTWAGRE-- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  134 wptstifDSPPQNDDDRAKLIdtlqdwktERYKEIIKSGSVePRPGVIRLMDEAKAAGKKLAVCS-AATKSSVILcLENL 212
Cdd:PRK13222  68 -------PDEELLEKLRELFD--------RHYAENVAGGSR-LYPGVKETLAALKAAGYPLAVVTnKPTPFVAPL-LEAL 130

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18420570  213 IDIERFQGLdcfLAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSCVI-TY 278
Cdd:PRK13222 131 GIADYFSVV---IGGDSLPNKKPDPAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPSVGvTY 194
PRK10563 PRK10563
6-phosphogluconate phosphatase; Provisional
 62-272 1.26e-12

6-phosphogluconate phosphatase; Provisional


Pssm-ID: 182552 [Multi-domain]  Cd Length: 221  Bit Score: 65.87  E-value: 1.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570   62 SLEALIFDCDGVILESENLHRQAYNDAFSHFDVRCPPSssesldwslEFYDKFQNlvgggkpkMRWY------FKENGWp 135
Cdd:PRK10563   3 QIEAVFFDCDGTLVDSEVICSRAYVTMFAEFGITLSLE---------EVFKRFKG--------VKLYeiidiiSKEHGV- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  136 TSTIFDSPPQNDDDRAKLIDTlqdwkterykeiiksgSVEPRPGVIRLMDEAKAAgkkLAVCSAATKSSVILCLeNLIDI 215
Cdd:PRK10563  65 TLAKAELEPVYRAEVARLFDS----------------ELEPIAGANALLESITVP---MCVVSNGPVSKMQHSL-GKTGM 124

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18420570  216 ERFQGlDCFLAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGM 272
Cdd:PRK10563 125 LHYFP-DKLFSGYDIQRWKPDPALMFHAAEAMNVNVENCILVDDSSAGAQSGIAAGM 180
PLN02940 PLN02940
riboflavin kinase
 173-301 1.36e-12

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 67.55  E-value: 1.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  173 SVEPRPGVIRLMDEAKAAGKKLAVCSAATKSSVilclenLIDIERFQGL-DCF---LAGDDVKEKKPDPSIYITAAEKLG 248
Cdd:PLN02940  91 NIKALPGANRLIKHLKSHGVPMALASNSPRANI------EAKISCHQGWkESFsviVGGDEVEKGKPSPDIFLEAAKRLN 164

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 18420570  249 VSVKDCLVVEDSVIGLQAATKAGMSCVITYTSSTSDQNFNDAIAVYPDLSNVK 301
Cdd:PLN02940 165 VEPSNCLVIEDSLPGVMAGKAAGMEVIAVPSIPKQTHLYSSADEVINSLLDLQ 217
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 65-284 2.96e-12

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: 64.29  E-value: 2.96e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  65 ALIFDCDGVILEsenlhrQAYNDAFSHF--DVRCPPSSSESLDWSLEFYDKFqnlvgggkpkmrwyfkENGWPTSTIFDs 142
Cdd:cd02603   3 AVLFDFGGVLID------PDPAAAVARFeaLTGEPSEFVLDTEGLAGAFLEL----------------ERGRITEEEFW- 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 143 ppqndddrAKLIDTLQDWKTERYKEIIKSGSVEPRPGVIRLMDEAKAAGKKLAVCSAATKSSVILCLENLIDIERFqgLD 222
Cdd:cd02603  60 --------EELREELGRPLSAELFEELVLAAVDPNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLPRRGDL--FD 129

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18420570 223 CFLAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMScVITYTSSTSD 284
Cdd:cd02603 130 GVVESCRLGVRKPDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGIH-AILVTDAEDA 190
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 180-276 1.71e-11

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: 60.10  E-value: 1.71e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 180 VIRLMDEAKAAGKKLAVCSAATKSSVILCLENLIDIERFqglDCFLAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVED 259
Cdd:cd01427  12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLF---DGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGD 88

                        90
                ....*....|....*..
gi 18420570 260 SVIGLQAATKAGMSCVI 276
Cdd:cd01427  89 SENDIEAARAAGGRTVA 105
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 65-276 6.90e-11

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: 60.79  E-value: 6.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  65 ALIFDCDGVILESE-NLHrQAYNDAFSHFDvrCPPSSsesldwslefYDKFQNLVGGGKPKM-RWYFKENGwptstifDS 142
Cdd:cd07512   1 AVIFDLDGTLIDSApDLH-AALNAVLAAEG--LAPLS----------LAEVRSFVGHGAPALiRRAFAAAG-------ED 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 143 PPqndddrAKLIDTLQDWKTERYKEIIKSGSVePRPGVIRLMDEAKAAGKKLAVCS-AATKSSVILcLENLIDIERFQGL 221
Cdd:cd07512  61 LD------GPLHDALLARFLDHYEADPPGLTR-PYPGVIEALERLRAAGWRLAICTnKPEAPARAL-LSALGLADLFAAV 132

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18420570 222 dcfLAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSCVI 276
Cdd:cd07512 133 ---VGGDTLPQRKPDPAPLRAAIRRLGGDVSRALMVGDSETDAATARAAGVPFVL 184
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 170-278 2.38e-10

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: 59.17  E-value: 2.38e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 170 KSGSVEPR--PGVIRLMDEAKAAGKKLAVCsaaTKSSVILCLENLIDIERFQGLDCFLAGDDVKEKKPDPSIYITAAEKL 247
Cdd:cd16417  80 ETLSVHSHlyPGVKEGLAALKAQGYPLACV---TNKPERFVAPLLEALGISDYFSLVLGGDSLPEKKPDPAPLLHACEKL 156

                        90       100       110
                ....*....|....*....|....*....|..
gi 18420570 248 GVSVKDCLVVEDSVIGLQAATKAGMSCV-ITY 278
Cdd:cd16417 157 GIAPAQMLMVGDSRNDILAARAAGCPSVgLTY 188
PLN02770 PLN02770
haloacid dehalogenase-like hydrolase family protein
 43-275 4.27e-09

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215413 [Multi-domain]  Cd Length: 248  Bit Score: 56.00  E-value: 4.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570   43 RSVYSKSRVSSpvsalpLRSLEALIFDCDGVILESENLHRQAYNDAFSHFDVRcppsssesldwslefydkfqnlvgGGK 122
Cdd:PLN02770   8 NSVESKSSLSG------LAPLEAVLFDVDGTLCDSDPLHYYAFREMLQEINFN------------------------GGV 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  123 PKMRWYFKENgwptstifdSPPQNDDDRAKLI--DTLQ------DWKTERYKEIIKSgSVEPRPGVIRLMDEAKAAGKKL 194
Cdd:PLN02770  58 PITEEFFVEN---------IAGKHNEDIALGLfpDDLErglkftDDKEALFRKLASE-QLKPLNGLYKLKKWIEDRGLKR 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  195 AVCSAATKSSVILCLENLIDIERFQGLdcfLAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSC 274
Cdd:PLN02770 128 AAVTNAPRENAELMISLLGLSDFFQAV---IIGSECEHAKPHPDPYLKALEVLKVSKDHTFVFEDSVSGIKAGVAAGMPV 204


                 .
gi 18420570  275 V 275
Cdd:PLN02770 205 V 205
PLN02811 PLN02811
hydrolase
 178-276 7.22e-09

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 55.15  E-value: 7.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  178 PGVIRLMDEAKAAGKKLAVCSAATKSSVILCLENliDIERFQGLDCFLAGDD--VKEKKPDPSIYITAAEKL---GVSVK 252
Cdd:PLN02811  81 PGAERLVRHLHAKGIPIAIATGSHKRHFDLKTQR--HGELFSLMHHVVTGDDpeVKQGKPAPDIFLAAARRFedgPVDPG 158

                         90       100
                 ....*....|....*....|....
gi 18420570  253 DCLVVEDSVIGLQAATKAGMSCVI 276
Cdd:PLN02811 159 KVLVFEDAPSGVEAAKNAGMSVVM 182
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 163-279 2.55e-08

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: 53.44  E-value: 2.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 163 ERYKEIIKSgSVEPRPGVIRLMDEAKAAGKKLAVCSAATKSSVILCLENLidiERFQGLDCFLAGDDVKEKKPDPSIYIT 242
Cdd:cd02616  69 KYYREHNDD-LTKEYPGVYETLARLKSQGIKLGVVTTKLRETALKGLKLL---GLDKYFDVIVGGDDVTHHKPDPEPVLK 144

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 18420570 243 AAEKLGVSVKDCLVVEDSVIGLQAATKAGM-SCVITYT 279
Cdd:cd02616 145 ALELLGAEPEEALMVGDSPHDILAGKNAGVkTVGVTWG 182
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 161-308 2.97e-08

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 53.88  E-value: 2.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  161 KTERYKEIIKSGSVEPRPGVIRLMDEAKAagKKLAVCSAATKSSVILclENLIDIERFQGL-DCFLAGDDVKEKKPDPSI 239
Cdd:PLN03243  95 RKEDLYEYMQGGLYRLRPGSREFVQALKK--HEIPIAVASTRPRRYL--ERAIEAVGMEGFfSVVLAAEDVYRGKPDPEM 170

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18420570  240 YITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSCVI------TYTSSTSDQnfndAIAVYPDLSNVKLKDLETL 308
Cdd:PLN03243 171 FMYAAERLGFIPERCIVFGNSNSSVEAAHDGCMKCVAvagkhpVYELSAGDL----VVRRLDDLSVVDLKNLSDL 241
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 65-271 2.23e-07

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: 49.70  E-value: 2.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570    65 ALIFDCDGVILESENLHRQAYNDAFSHFDVRCPpsssesldwSLEFYDKFQNLvgggKPKMRWYFKENGWptstifdspp 144
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFGLDPA---------SFKALKQAGGL----AEEEWYRIATSAL---------- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570   145 qndddrakliDTLQdwktERYKEIIKSGSVEpRPGVIRLMDEAKAAGKKLAVCSAATKSSVILCLENLIDIERFQgldcF 224
Cdd:TIGR01549  58 ----------EELQ----GRFWSEYDAEEAY-IRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFE----L 118

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 18420570   225 LAGDDVKEKKPDPSIYITAAEKLGVSvKDCLVVEDSVIGLQAATKAG 271
Cdd:TIGR01549 119 ILVSDEPGSKPEPEIFLAALESLGVP-PEVLHVGDNLNDIEGARNAG 164
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 66-275 7.27e-07

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: 48.93  E-value: 7.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  66 LIFDCDGVILESENLHRQAYNDAFSHFDVrcPPSSSESLDWslefydkfqnLVGGGKPKMrwyfkengwpTSTIFDSPPQ 145
Cdd:cd07533   2 VIFDWDGTLADSQHNIVAAMTAAFADLGL--PVPSAAEVRS----------IIGLSLDEA----------IARLLPMATP 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 146 NDDDRAklidtlqdwktERYKE-----IIKSGSVEPR-PGVIRLMDEAKAAGKKLAVcsAATKSSVilCLENLIDIERFQ 219
Cdd:cd07533  60 ALVAVA-----------ERYKEafdilRLLPEHAEPLfPGVREALDALAAQGVLLAV--ATGKSRR--GLDRVLEQHGLG 124

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18420570 220 GLdcFLA---GDDVKeKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSCV 275
Cdd:cd07533 125 GY--FDAtrtADDTP-SKPHPEMLREILAELGVDPSRAVMVGDTAYDMQMAANAGAHAV 180
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 147-279 1.13e-06

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 48.49  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  147 DDDRA-KLIDTLQDWKTERYKEIiksgsVEPRPGVIRLMDEAKAAGKKLAVCSAATKSSVILCLEnLIDIERFqgLDCFL 225
Cdd:PRK13288  58 DESKVeEMITTYREFNHEHHDEL-----VTEYETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLK-LTGLDEF--FDVVI 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18420570  226 AGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDS----VIGLQAATKagmSCVITYT 279
Cdd:PRK13288 130 TLDDVEHAKPDPEPVLKALELLGAKPEEALMVGDNhhdiLAGKNAGTK---TAGVAWT 184
PRK11587 PRK11587
putative phosphatase; Provisional
 224-271 1.83e-06

putative phosphatase; Provisional


Pssm-ID: 183215 [Multi-domain]  Cd Length: 218  Bit Score: 48.07  E-value: 1.83e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 18420570  224 FLAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAG 271
Cdd:PRK11587 128 FVTAERVKRGKPEPDAYLLGAQLLGLAPQECVVVEDAPAGVLSGLAAG 175
PRK13478 PRK13478
phosphonoacetaldehyde hydrolase; Provisional
 175-272 2.01e-06

phosphonoacetaldehyde hydrolase; Provisional


Pssm-ID: 184075 [Multi-domain]  Cd Length: 267  Bit Score: 48.32  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  175 EPRPGVIRLMDEAKAAGKKLAVCSAATKSsvilCLENLIDIERFQGL--DCFLAGDDVKEKKPDPSIYITAAEKLGV-SV 251
Cdd:PRK13478 101 TPIPGVLEVIAALRARGIKIGSTTGYTRE----MMDVVVPLAAAQGYrpDHVVTTDDVPAGRPYPWMALKNAIELGVyDV 176

                         90       100
                 ....*....|....*....|.
gi 18420570  252 KDCLVVEDSVIGLQAATKAGM 272
Cdd:PRK13478 177 AACVKVDDTVPGIEEGLNAGM 197
PRK13226 PRK13226
phosphoglycolate phosphatase; Provisional
 225-275 1.01e-05

phosphoglycolate phosphatase; Provisional


Pssm-ID: 237311 [Multi-domain]  Cd Length: 229  Bit Score: 46.00  E-value: 1.01e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18420570  225 LAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSCV 275
Cdd:PRK13226 142 IGGDTLAERKPHPLPLLVAAERIGVAPTDCVYVGDDERDILAARAAGMPSV 192
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 180-272 1.60e-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: 1.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 180 VIRLMDEAKAAGKKLAVCSAATKSSVILCLENLIDIeRFQgldcFLAG--DDVKeKKPDPSIYITAAEKLGVSVKDCLVV 257
Cdd:cd16421  12 ILELLKALRQKGIKLAVLSNKPNEAVQVLVEELFPG-SFD----FVLGekEGIR-RKPDPT*ALECAKVLGVPPDEVLYV 85

                        90
                ....*....|....*
gi 18420570 258 EDSVIGLQAATKAGM 272
Cdd:cd16421  86 GDSGVDMQTARNAGM 100
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 175-275 2.16e-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: 44.57  E-value: 2.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 175 EPRPGVIRLMDEAKAAGKKLAVCSAATKSSVILCLENLiDIERFqgLDCFLAGDDVKEKKPDPSIYITAAEKLGVSVKDC 254
Cdd:cd02588  91 PPFPDVVAGLRRLREAGYRLAILSNGSPDLIEDVVANA-GLRDL--FDAVLSAEDVRAYKPAPAVYELAAERLGVPPDEI 167

                        90       100
                ....*....|....*....|.
gi 18420570 255 LVVEDSVIGLQAATKAGMSCV 275
Cdd:cd02588 168 LHVASHAWDLAGARALGLRTA 188
PLN02575 PLN02575
haloacid dehalogenase-like hydrolase
 209-275 4.16e-05

haloacid dehalogenase-like hydrolase


Pssm-ID: 215313 [Multi-domain]  Cd Length: 381  Bit Score: 44.86  E-value: 4.16e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570  209 LENLID---IERFqgLDCFLAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSCV 275
Cdd:PLN02575 246 LENAIGsigIRGF--FSVIVAAEDVYRGKPDPEMFIYAAQLLNFIPERCIVFGNSNQTVEAAHDARMKCV 313
HAD_PHN cd02586
Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; ...
 175-272 1.40e-04

Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; Degradation of the ubiquitous natural phosphonate 2-aminoethylphosphonate (AEP) into useable forms of nitrogen, carbon, and phosphorus is a two-step metabolic pathway. The first step, catalyzed by AEP transaminase, involves the transfer of NH3 from AEP to pyruvate, yielding phosphonoacetaldehyde (P-Ald) and alanine. In the second step, phosphonatase catalyzes the hydrolytic P-C bond cleavage of P-Ald to form orthophosphate and acetaldehyde. 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: 319785 [Multi-domain]  Cd Length: 242  Bit Score: 42.67  E-value: 1.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 175 EPRPGVIRLMDEAKAAGKKLAVCSAATKSsvilCLENLIDIERFQGL--DCFLAGDDVKEKKPDPSIYITAAEKLGV-SV 251
Cdd:cd02586  98 SPIPGVLEVIAKLRARGIKIGSTTGYTRE----MMDIVLPEAAAQGYrpDSLVTPDDVPAGRPYPWMCYKNAIELGVyDV 173

                        90       100
                ....*....|....*....|.
gi 18420570 252 KDCLVVEDSVIGLQAATKAGM 272
Cdd:cd02586 174 AAVVKVGDTVPDIKEGLNAGM 194
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 222-272 4.33e-04

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: 39.06  E-value: 4.33e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18420570 222 DCFLAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDS----VIGlqaATKAGM 272
Cdd:cd04305  52 DHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLMVGDSlesdILG---AKNAGI 103
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 174-271 1.35e-03

histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal domain of the Escherichia coli bifunctional enzyme histidinol-phosphate phosphatase/imidazole-glycerol-phosphate dehydratase, HisB. The N-terminal histidinol-phosphate phosphatase domain catalyzes the dephosphorylation of histidinol phosphate, the eight step of L-histidine biosynthesis. This family also includes Escherichia coli GmhB phosphatase which is highly specific for D-glycero-D-manno-heptose-1,7-bisphosphate, it removes the C(7)phosphate and not the C(1)phosphate, and this is the third essential step of lipopolysaccharide heptose biosynthesis. 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: 319806 [Multi-domain]  Cd Length: 142  Bit Score: 38.28  E-value: 1.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420570 174 VEPRPGVIRLMDEAKAAGKKLAVCS--------AATKSSVILCLENLIDIERFQGLD------C-FLAGDDVKEKKPDPS 238
Cdd:cd07503  24 LEFLPGVIEALKKLKDAGYLVVVVTnqsgiargYFSEADFEALHDKMRELLASQGVEiddiyyCpHHPDDGCPCRKPKPG 103

                        90       100       110
                ....*....|....*....|....*....|...
gi 18420570 239 IYITAAEKLGVSVKDCLVVEDSVIGLQAATKAG 271
Cdd:cd07503 104 MLLDAAKELGIDLARSFVIGDRLSDIQAARNAG 136
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
 225-278 1.40e-03

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 39.85  E-value: 1.40e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 18420570  225 LAGDDVKEKKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSCV-ITY 278
Cdd:PRK13223 148 IGGDTLPQKKPDPAALLFVMKMAGVPPSQSLFVGDSRSDVLAAKAAGVQCVaLSY 202
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 208-276 5.17e-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: 37.23  E-value: 5.17e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18420570 208 CLENLIDIErFQGLDCflagddvkekKPDPSIYITAAEKLGVSVKDCLVVEDSVIGLQAATKAGMSCVI 276
Cdd:cd02604 122 LFDGIFDIE-YAGPDP----------KPHPAAFEKAIREAGLDPKRAAFFDDSIRNLLAAKALGMKTVL 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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