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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801   1 MDGTLVNTEPYWisaeteliesyggswthEEALQLvgsglfnsadiirakgvdlphqeiIDRLTDRVMQQLVEFGIPWRP 80
Cdd:cd07505     6 MDGVLIDTEPLH-----------------RQAWQL------------------------LERKNALLLELIASEGLKLKP 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801  81 GARELLVDLKENGVPTALVTMSISRMAHHVADHLGFVG--FDAVVAGDDVTESKPHPEPYLRGAELLGVDPAECVSIEDS 158
Cdd:cd07505    45 GVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLRgyFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERCLVFEDS 124

                         170
                  ....*....|....*...
gi 1113526801 159 EPGIRSAVAAGTVTIGVP 176
Cdd:cd07505   125 LAGIEAAKAAGMTVVAVP 142

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801   1 MDGTLVNTEPYWISAETELIESYGGSWTHEEALQLVGSGLFNSADIIRAKGVDLPHQEIIDRLTDRVMQQLVEF----GI 76
Cdd:TIGR02009   8 MDGVITDTAPLHAQAWKHIAAKYGISFDKQYNESLKGLSREDILRAILKLRGDGLSLEEIHQLAERKNELYRELlrltGV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801  77 PWRPGARELLVDLKENGVPTALVtmSISRMAHHVADHLGFVG-FDAVVAGDDVTESKPHPEPYLRGAELLGVDPAECVSI 155
Cdd:TIGR02009  88 AVLPGIRNLLKRLKAKGIAVGLG--SSSKNAPRILAKLGLRDyFDAIVDASEVKNGKPHPETFLLAAELLGVPPNECIVF 165

                         170       180
                  ....*....|....*....|
gi 1113526801 156 EDSEPGIRSAVAAGTVTIGV 175
Cdd:TIGR02009 166 EDALAGVQAARAAGMFAVAV 185

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801   1 MDGTLVNTEPYWisaeteliesyggswthEEALQLvgsglfnsadiirakgvdlphqeiIDRLTDRVMQQLVEFGIPWRP 80
Cdd:cd07505     6 MDGVLIDTEPLH-----------------RQAWQL------------------------LERKNALLLELIASEGLKLKP 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801  81 GARELLVDLKENGVPTALVTMSISRMAHHVADHLGFVG--FDAVVAGDDVTESKPHPEPYLRGAELLGVDPAECVSIEDS 158
Cdd:cd07505    45 GVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLRgyFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERCLVFEDS 124

                         170
                  ....*....|....*...
gi 1113526801 159 EPGIRSAVAAGTVTIGVP 176
Cdd:cd07505   125 LAGIEAAKAAGMTVVAVP 142

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801   1 MDGTLVNTEPYWISAETELIESYGG-SWTHEEALQLVGSGLfnsADIIRAkGVDLPHQEIIDRLTDRV---MQQLVEFGI 76
Cdd:COG0546     8 LDGTLVDSAPDIAAALNEALAELGLpPLDLEELRALIGLGL---RELLRR-LLGEDPDEELEELLARFrelYEEELLDET 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801  77 PWRPGARELLVDLKENGVPTALVTMSISRMAHHVADHLGFVG-FDAVVAGDDVTESKPHPEPYLRGAELLGVDPAECVSI 155
Cdd:COG0546    84 RLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDyFDAIVGGDDVPPAKPKPEPLLEALERLGLDPEEVLMV 163

                         170       180
                  ....*....|....*....|
gi 1113526801 156 EDSEPGIRSAVAAGTVTIGV 175
Cdd:COG0546   164 GDSPHDIEAARAAGVPFIGV 183

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801   1 MDGTLVNTEPYWISAETELIESYggswtheealqlvgsglfnsadiirakgvdlpHQEIIDRLTDRvmqqlvEFGIPWRP 80
Cdd:cd16423     6 FDGVIVDTEPLWYEAWQELLNER--------------------------------RNELIKRQFSE------KTDLPPIE 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801  81 GARELLVDLKENGVPTALVTMSISRMAHHVADHLGFVG-FDAVVAGDDVTESKPHPEPYLRGAELLGVDPAECVSIEDSE 159
Cdd:cd16423    48 GVKELLEFLKEKGIKLAVASSSPRRWIEPHLERLGLLDyFEVIVTGDDVEKSKPDPDLYLEAAERLGVNPEECVVIEDSR 127

                         170
                  ....*....|....*...
gi 1113526801 160 PGIRSAVAAGTVTIGVPF 177
Cdd:cd16423   128 NGVLAAKAAGMKCVGVPN 145

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801   1 MDGTLVNTEPYWISAETELIESYGGSWTHEEALQL---------VGSGLFNSAdiirAKGVDLPHQEIIDRLTDRVmqql 71
Cdd:TIGR01509   6 LDGVLVDTEFAIAKLINREELGLVPDELGVSAVGRlelalrrfkAQYGRTISP----EDAQLLYKQLFYEQIEEEA---- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801  72 vefGIPWRPGARELLVDLKENGVPTALVTMSiSRMAHHVADHLGFVG-FDAVVAGDDVTESKPHPEPYLRGAELLGVDPA 150
Cdd:TIGR01509  78 ---KLKPLPGVRALLEALRARGKKLALLTNS-PRAHKLVLALLGLRDlFDVVIDSSDVGLGKPDPDIYLQALKALGLEPS 153

                         170       180
                  ....*....|....*....|....*
gi 1113526801 151 ECVSIEDSEPGIRSAVAAGTVTIGV 175
Cdd:TIGR01509 154 ECVFVDDSPAGIEAAKAAGMHTVGV 178

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801  80 PGARELLVDLKENGVPTALVtmSISRMAHHVADHLGFVG-FDAVVAGDDVTESKPHPEPYLRGAELLGVDPAECVSIEDS 158
Cdd:cd02598    52 PGIASLLVDLKAKGIKIALA--SASKNAPKILEKLGLAEyFDAIVDGAVLAKGKPDPDIFLAAAEGLGLNPKDCIGVEDA 129

                          90
                  ....*....|....*..
gi 1113526801 159 EPGIRSAVAAGTVTIGV 175
Cdd:cd02598   130 QAGIRAIKAAGFLVVGV 146

riboflavin kinase

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801   1 MDGTLVNTEPYWISAETELIESYGGSWTHEEALQLVGSGLFNSAD-IIRAKGVDLPHQEIIDRLTDRVMQQLVEfgIPWR 79
Cdd:PLN02940   18 LDGTLLNTDGIVSDVLKAFLVKYGKQWDGREAQKIVGKTPLEAAAtVVEDYGLPCSTDEFNSEITPLLSEQWCN--IKAL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801  80 PGARELLVDLKENGVPTALVTMSI-SRMAHHVADHLGFVG-FDAVVAGDDVTESKPHPEPYLRGAELLGVDPAECVSIED 157
Cdd:PLN02940   96 PGANRLIKHLKSHGVPMALASNSPrANIEAKISCHQGWKEsFSVIVGGDEVEKGKPSPDIFLEAAKRLNVEPSNCLVIED 175

                         170
                  ....*....|....*....
gi 1113526801 158 SEPGIRSAVAAGTVTIGVP 176
Cdd:PLN02940  176 SLPGVMAGKAAGMEVIAVP 194

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801   2 DGTLVNTEPYWISAETEL-IESYGGSWTHEEA----LQLVGSGL------FNSADIIRAKGVDLPHQ--EIIDRLTDRVM 68
Cdd:cd07528     7 DGTLAETEELHRRAFNNAfFAERGLDWYWDRElygeLLRVGGGKeriaayFEKVGWPESAPKDLKELiaDLHKAKTERYA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801  69 QQLVEFGIPWRPGARELLVDLKENGVPTALVTMS----ISRMAHHVADHLGFVGFDAVVAGDDVTESKPHPEPYLRGAEL 144
Cdd:cd07528    87 ELIAAGLLPLRPGVARLIDEAKAAGVRLAIATTTspanVDALLSALLGPERRAIFDAIAAGDDVAEKKPDPDIYLLALER 166

                         170       180
                  ....*....|....*....|....*....
gi 1113526801 145 LGVDPAECVSIEDSEPGIRSAVAAGTVTI 173
Cdd:cd07528   167 LGVSPSDCLAIEDSAIGLQAAKAAGLPCI 195

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801   1 MDGTLVNTEPYWISAETELIESYGGSWTHEEALQLVGSGLFNSADIIR--AKGVDLPHQEIIDRltDRVMQQLVEFGIPW 78
Cdd:cd07529     8 MDGLLLDTERIYTETTQEILARYGKTYTWDVKAKMMGRPASEAARIIVdeLKLPMSLEEEFDEQ--QEALAELFMGTAKL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801  79 RPGARELLVDLKENGVPTALVTMSISRM-----AHHvADHLGFvgFDAVVAGDD---VTESKPHPEPYLRGAELLG---V 147
Cdd:cd07529    86 MPGAERLLRHLHAHNIPIALATSSCTRHfklktSRH-KELFSL--FHHVVTGDDpevKGRGKPAPDIFLVAAKRFNeppK 162

                         170       180
                  ....*....|....*....|....*....
gi 1113526801 148 DPAECVSIEDSEPGIRSAVAAGTVTIGVP 176
Cdd:cd07529   163 DPSKCLVFEDSPNGVKAAKAAGMQVVMVP 191

fructose-1-phosphate/6-phosphogluconate phosphatase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801   1 MDGTLVNTEPYWISAETELIESYGGSWTHEEALQLVGSGLFNSAD-IIRAKGVDL-PHQEIIDR-------LTDRVMQ-Q 70
Cdd:PRK10725   12 MDGTILDTEPTHRKAWREVLGRYGLQFDEQAMVALNGSPTWRIAQaIIELNQADLdPHALAREKteavksmLLDSVEPlP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801  71 LVEFGIPWRpGARellvdlkengvPTALVTMSISRMAHHVADHLGFVG-FDAVVAGDDVTESKPHPEPYLRGAELLGVDP 149
Cdd:PRK10725   92 LIEVVKAWH-GRR-----------PMAVGTGSESAIAEALLAHLGLRRyFDAVVAADDVQHHKPAPDTFLRCAQLMGVQP 159

                         170       180
                  ....*....|....*....|
gi 1113526801 150 AECVSIEDSEPGIRSAVAAG 169
Cdd:PRK10725  160 TQCVVFEDADFGIQAARAAG 179

haloacid dehalogenase-like hydrolase family protein

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801  48 RAKGVDLPHqeiiDRLTDRVMQQLVEFGIPWRPGARELLVDLKENGVPTALVTMSISRMAHHVADH-LG---FVGFDaVV 123
Cdd:PLN02779  119 RKELVDSLH----DRKTELFKELIESGALPLRPGVLRLMDEALAAGIKVAVCSTSNEKAVSKIVNTlLGperAQGLD-VF 193

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1113526801 124 AGDDVTESKPHPEPYLRGAELLGVDPAECVSIEDSEPGIRSAVAAG 169
Cdd:PLN02779  194 AGDDVPKKKPDPDIYNLAAETLGVDPSRCVVVEDSVIGLQAAKAAG 239

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801   2 DGTLVNTEPYWISAETELIESYG-GSWTHEEALQLVGSGlfnsADII--RA---KGVDLPHQEIIDR---LTDRVMQQLV 72
Cdd:cd16417     7 DGTLVDSAPDLAEAANAMLAALGlPPLPEETVRTWIGNG----ADVLveRAltgAREAEPDEELFKEaraLFDRHYAETL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801  73 EFGIPWRPGARELLVDLKENGVPTALVTMSISRMAHHVADHLGFVG-FDAVVAGDDVTESKPHPEPYLRGAELLGVDPAE 151
Cdd:cd16417    83 SVHSHLYPGVKEGLAALKAQGYPLACVTNKPERFVAPLLEALGISDyFSLVLGGDSLPEKKPDPAPLLHACEKLGIAPAQ 162

                         170       180
                  ....*....|....*....|....*.
gi 1113526801 152 CVSIEDSEPGIRSAVAAGTVTIGVPF 177
Cdd:cd16417   163 MLMVGDSRNDILAARAAGCPSVGLTY 188

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801   1 MDGTLVNTEPYWISAETELIESYGGS-WTHEEALQLVGSG---LFNSADIIRAKGVDLPHQEIIDRLTDRVMQQLVEFGI 76
Cdd:TIGR01449   5 LDGTLVDSAPDIAAAVNMALAALGLPpATLARVIGFIGNGvpvLMERVLAWAGQEPDAQRVAELRKLFDRHYEEVAGELT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801  77 PWRPGARELLVDLKENGVPTALVTMSISRMAHHVADHLGFVG-FDAVVAGDDVTESKPHPEPYLRGAELLGVDPAECVSI 155
Cdd:TIGR01449  85 SVFPGVEATLGALRAKGLRLGLVTNKPTPLARPLLELLGLAKyFSVLIGGDSLAQRKPHPDPLLLAAERLGVAPQQMVYV 164

                         170       180
                  ....*....|....*....|....
gi 1113526801 156 EDSEPGIRSAVAAgtvtiGVPFMV 179
Cdd:TIGR01449 165 GDSRVDIQAARAA-----GCPSVL 183

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801  80 PGARELLVDLkenGVPTALVTMSISRMAHHVADHLGFVGFDA--VVAGDDVTESKPHPEPYLRGAELLGVDPAECVSIED 157
Cdd:cd07526    45 PGAAAALSAL---TLPFCVASNSSRERLTHSLGLAGLLAYFEgrIFSASDVGRGKPAPDLFLHAAAQMGVAPERCLVIED 121

                          90
                  ....*....|....*..
gi 1113526801 158 SEPGIRSAVAAGTVTIG 174
Cdd:cd07526   122 SPTGVRAALAAGMTVFG 138

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801  84 ELLVDLKENGVPTALVTMSISRMAHHVADHLGFVGFDAVVAGDDVTESKPHPEPYLRGAELLGVDPAECVSIEDSEPGIR 163
Cdd:cd16421    14 ELLKALRQKGIKLAVLSNKPNEAVQVLVEELFPGSFDFVLGEKEGIRRKPDPT*ALECAKVLGVPPDEVLYVGDSGVDMQ 93

                          90
                  ....*....|..
gi 1113526801 164 SAVAAGTVTIGV 175
Cdd:cd16421    94 TARNAGMDEIGV 105

6-phosphogluconate phosphatase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801   2 DGTLVNTEPYWISAETELIESYGGSWTHEEALQ-LVGSGLFNSADIIRAK-GVDLPHQEI-------IDRLTDRVMQQLv 72
Cdd:PRK10563   12 DGTLVDSEVICSRAYVTMFAEFGITLSLEEVFKrFKGVKLYEIIDIISKEhGVTLAKAELepvyraeVARLFDSELEPI- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801  73 efgipwrPGARELLVDLKengVPTALVTMS-ISRMAHHvadhLGFVGF-----DAVVAGDDVTESKPHPEPYLRGAELLG 146
Cdd:PRK10563   91 -------AGANALLESIT---VPMCVVSNGpVSKMQHS----LGKTGMlhyfpDKLFSGYDIQRWKPDPALMFHAAEAMN 156

                         170       180
                  ....*....|....*....|...
gi 1113526801 147 VDPAECVSIEDSEPGIRSAVAAG 169
Cdd:PRK10563  157 VNVENCILVDDSSAGAQSGIAAG 179

hydrolase

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801   1 MDGTLVNTEPYWISAETELIESYGGSWTHEEALQLVGSGLFNSADI-IRAKGVD---LPHQEIIDRltdRVMQQLVEFGI 76
Cdd:PLN02811    1 MDGLLLDTEKFYTEVQEKILARYGKTFDWSLKAKMMGKKAIEAARIfVEESGLSdslSPEDFLVER---EAMLQDLFPTS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113526801  77 PWRPGARELLVDLKENGVPTALVTMSISR-MAHHVADHLG-FVGFDAVVAGDD--VTESKPHPEPYL---RGAELLGVDP 149
Cdd:PLN02811   78 DLMPGAERLVRHLHAKGIPIAIATGSHKRhFDLKTQRHGElFSLMHHVVTGDDpeVKQGKPAPDIFLaaaRRFEDGPVDP 157

                         170       180
                  ....*....|....*....|....*..
gi 1113526801 150 AECVSIEDSEPGIRSAVAAGTVTIGVP 176
Cdd:PLN02811  158 GKVLVFEDAPSGVEAAKNAGMSVVMVP 184