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Cof-type HAD-IIB family hydrolase [Cytobacillus firmus]

Protein Classification

Cof-type HAD-IIB family hydrolase( domain architecture ID 11576297)

Cof-type HAD-IIB family hydrolase, part of the HAD (haloacid dehalogenase) family that includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

CATH:  3.30.1240.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|15337123|33940035|37786806
SCOP:  3001890

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-270 2.75e-74

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-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, 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: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 227.86  E-value: 2.75e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031   5 MLALNIDGTLLQSNGRLHKSTKEAIEYVQQKGIYVTLITSRSFPSAKKVAKALKINSLLVTHRGAYIAASQEKPIFVKRI 84
Cdd:cd07516     1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEILERLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031  85 QEDETFEIVRLLEGFTCQIRLVHEkyslanktklntNMLAKTVFTTGDPIFYSQQFvDSLSDTILDEPVTPPKIEVYFED 164
Cdd:cd07516    81 SKEDVKELEEFLRKLGIGINIYTN------------DDWADTIYEENEDDEIIKPA-EILDDLLLPPDEDITKILFVGED 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031 165 KEDLEDAKTAIWGMFENVEVIKLNDLRMDIVPSGVSKLNGLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGLGVAMGNA 244
Cdd:cd07516   148 EELDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNA 227

                         250       260
                  ....*....|....*....|....*.
gi 1006541031 245 PAEVKKAADWLTRSNDQSGVSYMVKE 270
Cdd:cd07516   228 IDEVKEAADYVTLTNNEDGVAKAIEK 253
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-270 2.75e-74

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-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, 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: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 227.86  E-value: 2.75e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031   5 MLALNIDGTLLQSNGRLHKSTKEAIEYVQQKGIYVTLITSRSFPSAKKVAKALKINSLLVTHRGAYIAASQEKPIFVKRI 84
Cdd:cd07516     1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEILERLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031  85 QEDETFEIVRLLEGFTCQIRLVHEkyslanktklntNMLAKTVFTTGDPIFYSQQFvDSLSDTILDEPVTPPKIEVYFED 164
Cdd:cd07516    81 SKEDVKELEEFLRKLGIGINIYTN------------DDWADTIYEENEDDEIIKPA-EILDDLLLPPDEDITKILFVGED 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031 165 KEDLEDAKTAIWGMFENVEVIKLNDLRMDIVPSGVSKLNGLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGLGVAMGNA 244
Cdd:cd07516   148 EELDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNA 227

                         250       260
                  ....*....|....*....|....*.
gi 1006541031 245 PAEVKKAADWLTRSNDQSGVSYMVKE 270
Cdd:cd07516   228 IDEVKEAADYVTLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-266 1.43e-63

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 200.54  E-value: 1.43e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031   6 LALNIDGTLLQSNGRLHKSTKEAIEYVQQKGIYVTLITSRSFPSAKKVAKALKINSLLVTHRGAYIAASQEKPIFVKRIQ 85
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDENGKILYSNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031  86 EDETFEIVRLLEGFTCQIRLVHEKYSLANKTKLNTNMLAKTVFttgdpiFYSQQFVDSLSDTILDEPVTppKIeVYFEDK 165
Cdd:pfam08282  81 KEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILKELNY------TKSFVPEIDDFELLEDEDIN--KI-LILLDE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031 166 EDLEDAK---TAIWGMFENVEVIKLNDLrmDIVPSGVSKLNGLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGLGVAMG 242
Cdd:pfam08282 152 EDLDELEkelKELFGSLITITSSGPGYL--EIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMG 229

                         250       260
                  ....*....|....*....|....
gi 1006541031 243 NAPAEVKKAADWLTRSNDQSGVSY 266
Cdd:pfam08282 230 NASPEVKAAADYVTDSNNEDGVAK 253
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 3-271 1.62e-57

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 182.64  E-value: 1.62e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031   3 YRMLALNIDGTLLQSNGRLHKSTKEAIEYVQQKGIYVTLITSRSFPSAKKVAKALKINSLLVTHRGAYIAASQEKPIFVK 82
Cdd:COG0561     2 IKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGEVLYER 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031  83 RIQEDETFEIVRLLEGFTCQIRLVhekyslanktklntnmlaktvfTTGDPIFysqqfvdslsdtildepvtppkievyf 162
Cdd:COG0561    82 PLDPEDVREILELLREHGLHLQVV----------------------VRSGPGF--------------------------- 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031 163 edkedledaktaiwgmfenveviklndlrMDIVPSGVSKLNGLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGLGVAMG 242
Cdd:COG0561   113 -----------------------------LEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMG 163

                         250       260
                  ....*....|....*....|....*....
gi 1006541031 243 NAPAEVKKAADWLTRSNDQSGVSYMVKEH 271
Cdd:COG0561   164 NAPPEVKAAADYVTGSNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-265 7.74e-45

Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 152.42  E-value: 7.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031   5 MLALNIDGTLLQSNGRLHKSTKEAIEYVQQKGIYVTLITSRSFPSAKKVAKALKINSLLVTHRGAYIAASQEKPIFVKRI 84
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEILYKKPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031  85 QEDETFEIVRLLEGFTCQIRLVHEKYSLANKtklNTNMLAKTVFTTGDPIFYSQQFVDSLSDTILdepvtppKIEVYFED 164
Cdd:TIGR00099  81 DLDLVEEILNFLKKHGLDVILYGDDSIYASK---NDPEYFTIFKKFLGEPKLEVVDIQYLPDDIL-------KILLLFLD 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031 165 KEDLEDAKTAI--WGMFENVEVIKLNDLRMDIVPSGVSKLNGLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGLGVAMG 242
Cdd:TIGR00099 151 PEDLDLLIEALnkLELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMG 230

                         250       260
                  ....*....|....*....|...
gi 1006541031 243 NAPAEVKKAADWLTRSNDQSGVS 265
Cdd:TIGR00099 231 NADEELKALADYVTDSNNEDGVA 253
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 1-266 2.61e-28

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 109.40  E-value: 2.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031   1 MIYRMLALNIDGTLLQSNGRLHKSTKEAIEYVQQKGIYVTLITSRSFPSAKKVAKALKINS---LLVTHRGAYI--AASQ 75
Cdd:PRK10513    1 MAIKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQpgdYCITNNGALVqkAADG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031  76 EKPIfvkriQEDETFEIVRLLEGFTCQIRlVHekYSLANKTKL---NTNMLAKTV---FTTGDPIFYSqqfvdSLSDtiL 149
Cdd:PRK10513   81 ETVA-----QTALSYDDYLYLEKLSREVG-VH--FHALDRNTLytaNRDISYYTVhesFLTGIPLVFR-----EVEK--M 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031 150 DEPVTPPKieVYFEDKEDLEDAktAIWGM----FENVEVIKLNDLRMDIVPSGVSKLNGLLYLCEHLGISRNQMVVIGDS 225
Cdd:PRK10513  146 DPNLQFPK--VMMIDEPEILDA--AIARIpaevKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQ 221

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1006541031 226 EDDLEMIEAAGLGVAMGNAPAEVKKAADWLTRSNDQSGVSY 266
Cdd:PRK10513  222 ENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAF 262
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-270 2.75e-74

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-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, 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: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 227.86  E-value: 2.75e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031   5 MLALNIDGTLLQSNGRLHKSTKEAIEYVQQKGIYVTLITSRSFPSAKKVAKALKINSLLVTHRGAYIAASQEKPIFVKRI 84
Cdd:cd07516     1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEILERLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031  85 QEDETFEIVRLLEGFTCQIRLVHEkyslanktklntNMLAKTVFTTGDPIFYSQQFvDSLSDTILDEPVTPPKIEVYFED 164
Cdd:cd07516    81 SKEDVKELEEFLRKLGIGINIYTN------------DDWADTIYEENEDDEIIKPA-EILDDLLLPPDEDITKILFVGED 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031 165 KEDLEDAKTAIWGMFENVEVIKLNDLRMDIVPSGVSKLNGLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGLGVAMGNA 244
Cdd:cd07516   148 EELDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNA 227

                         250       260
                  ....*....|....*....|....*.
gi 1006541031 245 PAEVKKAADWLTRSNDQSGVSYMVKE 270
Cdd:cd07516   228 IDEVKEAADYVTLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-266 1.43e-63

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 200.54  E-value: 1.43e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031   6 LALNIDGTLLQSNGRLHKSTKEAIEYVQQKGIYVTLITSRSFPSAKKVAKALKINSLLVTHRGAYIAASQEKPIFVKRIQ 85
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDENGKILYSNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031  86 EDETFEIVRLLEGFTCQIRLVHEKYSLANKTKLNTNMLAKTVFttgdpiFYSQQFVDSLSDTILDEPVTppKIeVYFEDK 165
Cdd:pfam08282  81 KEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILKELNY------TKSFVPEIDDFELLEDEDIN--KI-LILLDE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031 166 EDLEDAK---TAIWGMFENVEVIKLNDLrmDIVPSGVSKLNGLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGLGVAMG 242
Cdd:pfam08282 152 EDLDELEkelKELFGSLITITSSGPGYL--EIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMG 229

                         250       260
                  ....*....|....*....|....
gi 1006541031 243 NAPAEVKKAADWLTRSNDQSGVSY 266
Cdd:pfam08282 230 NASPEVKAAADYVTDSNNEDGVAK 253
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 3-271 1.62e-57

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 182.64  E-value: 1.62e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031   3 YRMLALNIDGTLLQSNGRLHKSTKEAIEYVQQKGIYVTLITSRSFPSAKKVAKALKINSLLVTHRGAYIAASQEKPIFVK 82
Cdd:COG0561     2 IKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGEVLYER 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031  83 RIQEDETFEIVRLLEGFTCQIRLVhekyslanktklntnmlaktvfTTGDPIFysqqfvdslsdtildepvtppkievyf 162
Cdd:COG0561    82 PLDPEDVREILELLREHGLHLQVV----------------------VRSGPGF--------------------------- 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031 163 edkedledaktaiwgmfenveviklndlrMDIVPSGVSKLNGLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGLGVAMG 242
Cdd:COG0561   113 -----------------------------LEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMG 163

                         250       260
                  ....*....|....*....|....*....
gi 1006541031 243 NAPAEVKKAADWLTRSNDQSGVSYMVKEH 271
Cdd:COG0561   164 NAPPEVKAAADYVTGSNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-265 7.74e-45

Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 152.42  E-value: 7.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031   5 MLALNIDGTLLQSNGRLHKSTKEAIEYVQQKGIYVTLITSRSFPSAKKVAKALKINSLLVTHRGAYIAASQEKPIFVKRI 84
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEILYKKPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031  85 QEDETFEIVRLLEGFTCQIRLVHEKYSLANKtklNTNMLAKTVFTTGDPIFYSQQFVDSLSDTILdepvtppKIEVYFED 164
Cdd:TIGR00099  81 DLDLVEEILNFLKKHGLDVILYGDDSIYASK---NDPEYFTIFKKFLGEPKLEVVDIQYLPDDIL-------KILLLFLD 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031 165 KEDLEDAKTAI--WGMFENVEVIKLNDLRMDIVPSGVSKLNGLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGLGVAMG 242
Cdd:TIGR00099 151 PEDLDLLIEALnkLELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMG 230

                         250       260
                  ....*....|....*....|...
gi 1006541031 243 NAPAEVKKAADWLTRSNDQSGVS 265
Cdd:TIGR00099 231 NADEELKALADYVTDSNNEDGVA 253
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 4-271 3.12e-33

phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319819 [Multi-domain]  Cd Length: 213  Bit Score: 120.79  E-value: 3.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031   4 RMLALNIDGTLLQSNGRLHKSTKEAIEYVQQKGIYVTLITSRSFPSAKKVAKALKINSLlVTHRGAYIAASQEkpifVKR 83
Cdd:cd07517     1 KIVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGIDSY-VSYNGQYVFFEGE----VIY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031  84 IQEDETFEIVRLLEgftcqirLVHEKyslanktklntnmlaktvfttGDPIFYSQQFVdslsdtildepvtppkievYFE 163
Cdd:cd07517    76 KNPLPQELVERLTE-------FAKEQ---------------------GHPVSFYGQLL-------------------LFE 108

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031 164 DKEDLEDaktaIWGMFENVEVIKLNDLRMDIVPSGVSKLNGLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGLGVAMGN 243
Cdd:cd07517   109 DEEEEQK----YEELRPELRFVRWHPLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGN 184

                         250       260
                  ....*....|....*....|....*...
gi 1006541031 244 APAEVKKAADWLTRSNDQSGVSYMVKEH 271
Cdd:cd07517   185 AHEELKEIADYVTKDVDEDGILKALKHF 212
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 1-266 2.61e-28

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 109.40  E-value: 2.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031   1 MIYRMLALNIDGTLLQSNGRLHKSTKEAIEYVQQKGIYVTLITSRSFPSAKKVAKALKINS---LLVTHRGAYI--AASQ 75
Cdd:PRK10513    1 MAIKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQpgdYCITNNGALVqkAADG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031  76 EKPIfvkriQEDETFEIVRLLEGFTCQIRlVHekYSLANKTKL---NTNMLAKTV---FTTGDPIFYSqqfvdSLSDtiL 149
Cdd:PRK10513   81 ETVA-----QTALSYDDYLYLEKLSREVG-VH--FHALDRNTLytaNRDISYYTVhesFLTGIPLVFR-----EVEK--M 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031 150 DEPVTPPKieVYFEDKEDLEDAktAIWGM----FENVEVIKLNDLRMDIVPSGVSKLNGLLYLCEHLGISRNQMVVIGDS 225
Cdd:PRK10513  146 DPNLQFPK--VMMIDEPEILDA--AIARIpaevKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQ 221

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1006541031 226 EDDLEMIEAAGLGVAMGNAPAEVKKAADWLTRSNDQSGVSY 266
Cdd:PRK10513  222 ENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAF 262
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 192-264 7.65e-25

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


Pssm-ID: 319820 [Multi-domain]  Cd Length: 184  Bit Score: 98.04  E-value: 7.65e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1006541031 192 MDIVPSGVSKLNGLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGLGVAMGNAPAEVKKAADWLTRSNDQSGV 264
Cdd:cd07518   107 IDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVKAAAKYVAPSNNENGV 179
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 6-274 1.41e-24

sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP equivalog model (TIGR01485), encompassing plants and cyanobacteria, as well as those archaeal sequences which are the closest relatives (TIGR01487). It remains to be shown whether these archaeal sequences catalyze the same reaction as SPP.


Pssm-ID: 273650 [Multi-domain]  Cd Length: 225  Bit Score: 98.30  E-value: 1.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031   6 LALNIDGTLLQSNGRLHKSTKEAIEYVQQKGIYVTLITSRSFPSAKKVAKALKINSLLVTHRGAYIaasqekpiFVKRIQ 85
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESALEAIRKAESKGIPVVLVTGNSVQFARALAKLIGTPDPVIAENGGEI--------SYNEGL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031  86 EDETFEivrllegftcqirlvhekySLANKTKLNtNMLAKTVfttgdpifysqqfvdslSDTILDepVTPP--KIEVYFE 163
Cdd:TIGR01482  73 DDIFLA-------------------YLEEEWFLD-IVIAKTF-----------------PFSRLK--VQYPrrASLVKMR 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031 164 DKEDLEDAKTAIWGMFENV-EVIKLNDLrmDIVPSGVSKLNGLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGLGVAMG 242
Cdd:TIGR01482 114 YGIDVDTVREIIKELGLNLvAVDSGFDI--HILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVA 191

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1006541031 243 NAPAEVKKAADWLTRSNDQSGVSYMVKEHFRK 274
Cdd:TIGR01482 192 NAQPELKEWADYVTESPYGEGGAEAIGEILQA 223
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-264 8.45e-24

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 96.58  E-value: 8.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031   1 MIYRMLALNIDGTLLQSNGRLHKSTKEAIEYVQQKGIYVTLITSRSFPSAKKVAKALKINSLLVTHRGAYIAASQE-KPI 79
Cdd:PRK01158    1 MKIKAIAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGNVLCFARAAAKLIGTSGPVIAENGGVISVGFDgKRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031  80 FVKRIQEDET-FEIVRllegftcqirlvhEKYSLAnktklntnmlaKTVFTTGDPifysqqfvdslsdtildepvTPPKI 158
Cdd:PRK01158   81 FLGDIEECEKaYSELK-------------KRFPEA-----------STSLTKLDP--------------------DYRKT 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031 159 EVYFEDKEDLEDAKTAIWGMFENVEVIklnDLR--MDIVPSGVSKLNGLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAG 236
Cdd:PRK01158  117 EVALRRTVPVEEVRELLEELGLDLEIV---DSGfaIHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAG 193

                         250       260
                  ....*....|....*....|....*...
gi 1006541031 237 LGVAMGNAPAEVKKAADWLTRSNDQSGV 264
Cdd:PRK01158  194 FGVAVANADEELKEAADYVTEKSYGEGV 221
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 4-264 4.14e-21

phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be phosphoglycolate phosphatases, is most closely related to the sucrose-phosphate phosphatases from plants and cyanobacteria (TIGR01485). Together, these two models comprise a subfamily model (TIGR01482). TIGR01482, in turn, is a member of the IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases.


Pssm-ID: 273652 [Multi-domain]  Cd Length: 215  Bit Score: 89.03  E-value: 4.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031   4 RMLALNIDGTLLQSNGRLHKSTKEAIEYVQQKGIYVTLITSRSFPSAKKVAKALKINSLLVTHRGAYIAASQEKPIFVKr 83
Cdd:TIGR01487   2 KLVAIDIDGTLTDPNRMISERAIEAIRKAEKKGIPVSLVTGNTVPFARALAVLIGTSGPVVAENGGVIFYNKEDIFLAN- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031  84 iqEDETFEIVRLLEgftcqirlvhekyslanKTKLNtnmlaktvfttgdpifysqqfvDSLSDTIldepvtPPKIEVYFE 163
Cdd:TIGR01487  81 --MEEEWFLDEEKK-----------------KRFPR----------------------DRLSNEY------PRASLVIMR 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031 164 DKEDLEDAKTAIWGMfenveVIKLNDLRMD--IVPSGVSKLNGLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGLGVAM 241
Cdd:TIGR01487 114 EGKDVDEVREIIKER-----GLNLVASGFAihIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAV 188

                         250       260
                  ....*....|....*....|...
gi 1006541031 242 GNAPAEVKKAADWLTRSNDQSGV 264
Cdd:TIGR01487 189 ANADDQLKEIADYVTSNPYGEGV 211
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 198-264 3.13e-20

phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), and Pyrococcus horikoshii PH1421, a magnesium-dependent phosphatase; belongs to the haloacid dehalogenase-like superfamily; Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PGPase) catalyzes the magnesium-dependent dephosphorylation of phosphoglycolate. This family also includes Pyrococcus horikoshii OT3 PH1421, a magnesium-dependent phosphatase. 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: 319816 [Multi-domain]  Cd Length: 139  Bit Score: 84.56  E-value: 3.13e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1006541031 198 GVSKLNGLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGLGVAMGNAPAEVKKAADWLTRSNDQSGV 264
Cdd:cd07514    65 GVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGV 131
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 1-271 1.04e-18

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 83.53  E-value: 1.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031   1 MIYRMLALNIDGTLLQSNGRLHKSTKEAIEYVQQKGIYVTLITSRSFPSAKKVAKALKINSLLVTHRGAYIAASQEKpif 80
Cdd:PRK10530    1 MTYRVIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALALDTPAICCNGTYLYDYQAK--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031  81 vKRIQED-----ETFEIVRLLEGFtcQI-RLVHEK----YSLANKTKLNTNMLAKTVFTTGDPIFysQQfVDSLSDTIlD 150
Cdd:PRK10530   78 -KVLEADplpvqQALQVIEMLDEH--QIhGLMYVDdamlYEHPTGHVIRTLNWAQTLPPEQRPTF--TQ-VDSLAQAA-R 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031 151 EPVTPPKIEVYFEDKEDLEDAKTAI---------WGMFENVeviklndlrmDIVPSGVSKLNGLLYLCEHLGISRNQMVV 221
Cdd:PRK10530  151 QVNAIWKFALTHEDLPQLQHFAKHVehelgleceWSWHDQV----------DIARKGNSKGKRLTQWVEAQGWSMKNVVA 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1006541031 222 IGDSEDDLEMIEAAGLGVAMGNAPAEVKKAADWLTRSNDQSGVSYMVKEH 271
Cdd:PRK10530  221 FGDNFNDISMLEAAGLGVAMGNADDAVKARADLVIGDNTTPSIAEFIYSH 270
PLN02887 PLN02887
hydrolase family protein
 3-271 7.52e-18

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 83.39  E-value: 7.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031   3 YRMLALNIDGTLLQSNGRLHKSTKEAIEYVQQKGIYVTLITSRSFPSAKKVAKALKIN---------SLLVTHRGAYIAA 73
Cdd:PLN02887  308 FSYIFCDMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGKARPAVIDILKMVDLAgkdgiisesSPGVFLQGLLVYG 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031  74 SQEKPIFVKRIQEDETFEivrllegfTCQirlvhekYSLANKTKL--NTNMLAKTVFttgdpifySQQFVDSLSdTILDE 151
Cdd:PLN02887  388 RQGREIYRSNLDQEVCRE--------ACL-------YSLEHKIPLiaFSQDRCLTLF--------DHPLVDSLH-TIYHE 443

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031 152 PVTP--PKIE-----------VYFEDKEDLEDAKTAIW--GMFENVEVIKLNDLRMDIVPSGVSKLNGLLYLCEHLGISR 216
Cdd:PLN02887  444 PKAEimSSVDqllaaadiqkvIFLDTAEGVSSVLRPYWseATGDRANVVQAQPDMLEIVPPGTSKGNGVKMLLNHLGVSP 523

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1006541031 217 NQMVVIGDSEDDLEMIEAAGLGVAMGNAPAEVKKAADWLTRSNDQSGVSYMVKEH 271
Cdd:PLN02887  524 DEIMAIGDGENDIEMLQLASLGVALSNGAEKTKAVADVIGVSNDEDGVADAIYRY 578
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 5-241 4.58e-17

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 77.81  E-value: 4.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031   5 MLALNIDGTLLQSN-GRLHKSTKEAIEYVQQKGIYVTLITSRSFPSAKKVAKALKINSLLVTHRGAYIAASQEKpIFVkr 83
Cdd:TIGR01484   1 LLFFDLDGTLLDPNaHELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPLPLIAENGALIFYPGEI-LYI-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031  84 iqEDETFEIVRLLEGFTcqiRLVHEKYSLAnktklntnmlAKTVFTTGDpiFYSQQFVDSLSDTILDEPVTPpkievyfe 163
Cdd:TIGR01484  78 --EPSDVFEEILGIKFE---EIGAELKSLS----------EHYVGTFIE--DKAIAVAIHYVGAELGQELDS-------- 132

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1006541031 164 dkeDLEDAKTAIWGMFENVEVIKLNDLRMDIVPSGVSKLNGLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGLGVAM 241
Cdd:TIGR01484 133 ---KMRERLEKIGRNDLELEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 181-263 4.47e-15

sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3.1.3.24) catalyzes the dephosphorylation of sucrose-6(F)-phosphate (Suc6P)-the final step in the pathway of sucrose biosynthesis in plants and cyanobacteria. 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: 319792 [Multi-domain]  Cd Length: 245  Bit Score: 72.77  E-value: 4.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031 181 NVEVIKLNDLRM--DIVPSGVSKLNGLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGLGVAMGNAPAEVKKAADWLTRS 258
Cdd:cd02605   148 TVRIIYSSGLAYdlDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELLKWADRVTRS 227


                  ....*
gi 1006541031 259 NDQSG 263
Cdd:cd02605   228 RLAKG 232
PRK10976 PRK10976
putative hydrolase; Provisional
 2-273 6.31e-15

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 72.77  E-value: 6.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031   2 IYRMLALNIDGTLLQSNGRLHKSTKEAIEYVQQKGIYVTLITSRSFPSAKKVAKALKINSLLVTHRGAYIAASQEKPIFV 81
Cdd:PRK10976    1 MYQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDTDGNLIFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031  82 KRIQEDetfeIVRLLegftcqIRLVHekyslaNKTKLNTNMLAKTVFTTGDPIFYSQQFV-DSLSDTILDEPVTPPK--- 157
Cdd:PRK10976   81 HNLDRD----IASDL------FGVVH------DNPDIITNVYRDDEWFMNRHRPEEMRFFkEAVFKYQLYEPGLLEPdgv 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031 158 IEVYF--EDKE---DLEDAKTAIWGMFENVEVIKLNDLrmDIVPSGVSKLNGLLYLCEHLGISRNQMVVIGDSEDDLEMI 232
Cdd:PRK10976  145 SKVFFtcDSHEkllPLEQAINARWGDRVNVSFSTLTCL--EVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEML 222

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1006541031 233 EAAGLGVAMGNAPAEVKKAADWL--TRSNDQSGVSYMVKEHFR 273
Cdd:PRK10976  223 SMAGKGCIMGNAHQRLKDLLPELevIGSNADDAVPHYLRKLYL 265
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 154-261 5.66e-12

Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate phosphohydrolase proteins found in plants and cyanobacteria. Sucrose-6(F)-phosphate phosphohydrolase catalyzes the final step in the pathway of sucrose biosynthesis.


Pssm-ID: 428314 [Multi-domain]  Cd Length: 246  Bit Score: 64.21  E-value: 5.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031 154 TPPKIEvYFEDKEDLEDAKTAIWGMFE----NVEVIKLNDLRMDIVPSGVSKLNGLLYLCEHLGISRNQMVVIGDSEDDL 229
Cdd:pfam05116 115 RPHKVS-YFLDPEAAAAVLAELEQLLRkrglDVKVIYSSGRDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDE 193

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1006541031 230 EMIEAAGLGVAMGNAPAEVKKAADWLTRSNDQ 261
Cdd:pfam05116 194 ELFIGGTRGVVVGNAQPELLQWYLENARDNPR 225
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 187-259 4.88e-11

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily phosphatases [Cell wall/membrane/envelope biogenesis, General function prediction only];


Pssm-ID: 441384 [Multi-domain]  Cd Length: 170  Bit Score: 60.06  E-value: 4.88e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1006541031 187 LNDLRMDIVPSGVS-KLNGLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGLGVAMGNAPAEVKKAADWLTRSN 259
Cdd:COG1778    69 AEELGITHVYQGVKdKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKP 142
PRK15126 PRK15126
HMP-PP phosphatase;
2-244 1.95e-09

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 57.01  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031   2 IYRMLALNIDGTLLQSNGRLHKSTKEAIEYVQQKGIYVTLITSRSFPSAKKVAKALKINSLLVTHRGAYIAASQEKPIF- 80
Cdd:PRK15126    1 MARLAAFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHVLEMQHILGALSLDAYLITGNGTRVHSLEGELLHr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031  81 ----------VKRIQEDET--------------FEIVRLLE-----GFTcqirlvhekYSLANKTKLNTNMLAKTVFTtG 131
Cdd:PRK15126   81 qdlpadvaelVLHQQWDTRasmhvfnddgwftgKEIPALLQahvysGFR---------YQLIDLKRLPAHGVTKICFC-G 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031 132 DpifysqqfvdslSDTILDEPVtppKIEVYFEDKEDLedaktaiwgMFENVEViklndlrMDIVPSGVSKLNGLLYLCEH 211
Cdd:PRK15126  151 D------------HDDLTRLQI---QLNEALGERAHL---------CFSATDC-------LEVLPVGCNKGAALAVLSQH 199

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1006541031 212 LGISRNQMVVIGDSEDDLEMIEAAGLGVAMGNA 244
Cdd:PRK15126  200 LGLSLADCMAFGDAMNDREMLGSVGRGFIMGNA 232
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 201-259 7.95e-09

haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) phosphatase KdsC, and rainbow trout N-acylneuraminate cytidylyltransferase; KDO 8-P phosphatase catalyzes the hydrolysis of KDO 8-P to KDO (3-deoxy-D-manno-octulosonate) and inorganic phosphate and is the last enzyme in the KDO biosynthetic pathway. KDO is an 8-carbon sugar that links the lipid A and polysaccharide moieties of the lipopolysaccharide region in Gram-negative bacteria. An interruption in KDO biosynthesis leads to the accumulation of lipid A precursors and subsequent arrest in cell growth. The KDO biosynthesis pathway involves five sequential enzymatic reactions. This family also includes rainbow trout CMP-sialic acid synthetase which effectively converts both deaminoneuraminic acid (KDN, 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid) and N-acetylneuraminic acid (Neu5Ac) to CMP-KDN and CMP-Neu5Ac, respectively. 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: 319769 [Multi-domain]  Cd Length: 146  Bit Score: 53.29  E-value: 7.95e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1006541031 201 KLNGLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGLGVAMGNAPAEVKKAADWLTRSN 259
Cdd:cd01630    77 KLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRAR 135
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 198-253 6.94e-07

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 49.06  E-value: 6.94e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1006541031 198 GVSKLNGLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGLGVAMgNAPAEVKKAAD 253
Cdd:COG0560   153 GEGKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAV-NPDPALREAAD 207
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 200-240 1.21e-06

phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. 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: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 47.93  E-value: 1.21e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1006541031 200 SKLNGLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGLGVA 240
Cdd:cd07500   137 RKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIA 177
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
204-255 7.81e-06

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 45.69  E-value: 7.81e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1006541031 204 GLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAG---LGVAMG-NAPAEVKKA-ADWL 255
Cdd:COG0546   145 PLLEALERLGLDPEEVLMVGDSPHDIEAARAAGvpfIGVTWGyGSAEELEAAgADYV 201
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 204-241 2.13e-05

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


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 42.77  E-value: 2.13e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1006541031 204 GLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAG-LGVAM 241
Cdd:cd01427    68 PLLLLLLKLGVDPEEVLFVGDSENDIEAARAAGgRTVAV 106
serB PRK11133
phosphoserine phosphatase; Provisional
 193-240 2.85e-05

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 44.94  E-value: 2.85e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1006541031 193 DIVpSGVSKLNGLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGLGVA 240
Cdd:PRK11133  242 DIV-DAQYKADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIA 288
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
205-237 2.09e-04

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 41.72  E-value: 2.09e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1006541031 205 LLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGL 237
Cdd:PRK13222  155 LLLACEKLGLDPEEMLFVGDSRNDIQAARAAGC 187
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 193-236 2.73e-04

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: 41.03  E-value: 2.73e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1006541031 193 DIVPSGVSKLNGLLYLCEHLGISRNQMVVIGDSEDDLEMIEAAG 236
Cdd:pfam00702 148 DDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 205-241 4.26e-04

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: 40.68  E-value: 4.26e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1006541031 205 LLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGLGVAM 241
Cdd:cd16417   149 LLHACEKLGIAPAQMLMVGDSRNDILAARAAGCPSVG 185
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
208-257 5.82e-04

3-deoxy-manno-octulosonate-8-phosphatase KdsC;


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 39.92  E-value: 5.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1006541031 208 LCEHLGISRNQMVVIGDSEDDLEMIEAAGLGVAMGNAPAEVKKAADWLTR 257
Cdd:PRK09484  104 LLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTR 153
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 10-93 7.21e-04

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: 38.15  E-value: 7.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006541031  10 IDGTLLqsngrlhksTKEAIEYVQQKGIYVTLITSRSFPSAKKVAKALKINSL---LVTHRGAYIAASQEKPIFVKRIQE 86
Cdd:cd01427     6 LDGTLL---------AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLfdgIIGSDGGGTPKPKPKPLLLLLLKL 76


                  ....*..
gi 1006541031  87 DETFEIV 93
Cdd:cd01427    77 GVDPEEV 83
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 205-257 1.21e-03

Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino acid transport and metabolism]; Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 440011 [Multi-domain]  Cd Length: 176  Bit Score: 38.92  E-value: 1.21e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1006541031 205 LLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGLG---VAMGNAPAEVKK------------AADWLTR 257
Cdd:COG0241   108 LLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGCKgilVLTGKGAEELAEalpdtvaddlaeAVDYLLA 175
PGP_bact TIGR01449
2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate ...
 205-261 2.36e-03

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


Pssm-ID: 130516 [Multi-domain]  Cd Length: 213  Bit Score: 38.26  E-value: 2.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1006541031 205 LLYLCEHLGISRNQMVVIGDSEDDLEMIEAAGL-------GVAMGNAPAEVKkaADWLTRSNDQ 261
Cdd:TIGR01449 147 LLLAAERLGVAPQQMVYVGDSRVDIQAARAAGCpsvlltyGYRYGEAIDLLP--PDVLYDSLNE 208
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 205-252 2.40e-03

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: 38.53  E-value: 2.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1006541031 205 LLYLCEHLGISRNQMVVIGDSEDDLEMIEAAG---LGVAMG-NAPAEVKKAA 252
Cdd:cd07533   145 LREILAELGVDPSRAVMVGDTAYDMQMAANAGahaVGVAWGyHSLEDLRSAG 196
PLN02382 PLN02382
probable sucrose-phosphatase
 181-247 6.73e-03

probable sucrose-phosphatase


Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 37.66  E-value: 6.73e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1006541031 181 NVEVIKLNDLRMDIVPSGVSKLNGLLYLCEHL---GISRNQMVVIGDSEDDLEMIEAAGL-GVAMGNAPAE 247
Cdd:PLN02382  156 DVKIIYSGGIDLDVLPQGAGKGQALAYLLKKLkaeGKAPVNTLVCGDSGNDAELFSVPDVyGVMVSNAQEE 226
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 4-59 6.77e-03

haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) phosphatase KdsC, and rainbow trout N-acylneuraminate cytidylyltransferase; KDO 8-P phosphatase catalyzes the hydrolysis of KDO 8-P to KDO (3-deoxy-D-manno-octulosonate) and inorganic phosphate and is the last enzyme in the KDO biosynthetic pathway. KDO is an 8-carbon sugar that links the lipid A and polysaccharide moieties of the lipopolysaccharide region in Gram-negative bacteria. An interruption in KDO biosynthesis leads to the accumulation of lipid A precursors and subsequent arrest in cell growth. The KDO biosynthesis pathway involves five sequential enzymatic reactions. This family also includes rainbow trout CMP-sialic acid synthetase which effectively converts both deaminoneuraminic acid (KDN, 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid) and N-acetylneuraminic acid (Neu5Ac) to CMP-KDN and CMP-Neu5Ac, respectively. 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: 319769 [Multi-domain]  Cd Length: 146  Bit Score: 36.35  E-value: 6.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1006541031   4 RMLALNIDGTLlqSNGRLH-----KSTKE-------AIEYVQQKGIYVTLITSRSFPSAKKVAKALKI 59
Cdd:cd01630     2 KLLVLDVDGVL--TDGRIYydsngEELKSfnvrdglGIKLLQKSGIEVAIITGRQSEAVRRRAKELGI 67
 
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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