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 15833906   5 EAVFFDCDGTLVDSEVICSRAYVTMFREFGihvdlkeiftrfkgvklyeiidiiskeqgvtmvqadaehvyrAEVARLFD 84
Cdd:cd07526   1 DLVIFDCDGVLVDSEVIAARVLVEVLAELG------------------------------------------ARVLAAFE 38

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906  85 TELEDIAGANELLASINVPMCVVSNGPVSKMQHSLGKLNMLHYFPEKLFSGYDIQRWKPDPALMFHAAKAMNVNVENCIL 164
Cdd:cd07526  39 AELQPIPGAAAALSALTLPFCVASNSSRERLTHSLGLAGLLAYFEGRIFSASDVGRGKPAPDLFLHAAAQMGVAPERCLV 118

                       170       180
                ....*....|....*....|...
gi 15833906 165 VDDSSAGAQSGIDAGMEVFYFCA 187
Cdd:cd07526 119 IEDSPTGVRAALAAGMTVFGFTG 141

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906     4 IEAVFFDCDGTLVDSEVICSRAYVTMFREF-----------GIHVDLKEIFTRFKGVKLYEIIDIISKEQGVTMVQADAE 72
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHplakaivaaaeDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906    73 HVYRAEVARLF--DTELEDIAGANELLASI---NVPMCVVSNGPVSKMQHSLGKLNMLHYFpEKLFSGYDIQRWKPDPAL 147
Cdd:pfam00702  81 TVVLVELLGVIalADELKLYPGAAEALKALkerGIKVAILTGDNPEAAEALLRLLGLDDYF-DVVISGDDVGVGKPKPEI 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 15833906   148 MFHAAKAMNVNVENCILVDDSSAGAQSGIDAG 179
Cdd:pfam00702 160 YLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191

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 15833906   5 EAVFFDCDGTLVDSEVICSRAYVTMFREFGihvdlkeiftrfkgvklyeiidiiskeqgvtmvqadaehvyrAEVARLFD 84
Cdd:cd07526   1 DLVIFDCDGVLVDSEVIAARVLVEVLAELG------------------------------------------ARVLAAFE 38

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906  85 TELEDIAGANELLASINVPMCVVSNGPVSKMQHSLGKLNMLHYFPEKLFSGYDIQRWKPDPALMFHAAKAMNVNVENCIL 164
Cdd:cd07526  39 AELQPIPGAAAALSALTLPFCVASNSSRERLTHSLGLAGLLAYFEGRIFSASDVGRGKPAPDLFLHAAAQMGVAPERCLV 118

                       170       180
                ....*....|....*....|...
gi 15833906 165 VDDSSAGAQSGIDAGMEVFYFCA 187
Cdd:cd07526 119 IEDSPTGVRAALAAGMTVFGFTG 141

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906   4 IEAVFFDCDGTLVDSEVICSRAYVTMFREFGIHVDLKEIFTRFKGVKLYEIIDIISKEQGVTMVQAdAEHVYRAEVARLF 83
Cdd:COG0546   1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRALIGLGLRELLRRLLGEDPDEELEE-LLARFRELYEEEL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906  84 DTELEDIAGANELLASI---NVPMCVVSNGPVSKMQHSLGKLNMLHYFPEkLFSGYDIQRWKPDPALMFHAAKAMNVNVE 160
Cdd:COG0546  80 LDETRLFPGVRELLEALkarGIKLAVVTNKPREFAERLLEALGLDDYFDA-IVGGDDVPPAKPKPEPLLEALERLGLDPE 158

                       170       180
                ....*....|....*....|
gi 15833906 161 NCILVDDSSAGAQSGIDAGM 180
Cdd:COG0546 159 EVLMVGDSPHDIEAARAAGV 178

subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p); This subfamily includes Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). GPP1p and GPP2p are involved in glycerol biosynthesis, GPP1 is induced in response to both anaerobic and hyperosmotic stress, GPP2 is induced in response to hyperosmotic or oxidative stress, and during diauxic shift; overexpression of DOG1 or DOG2 confers 2-deoxyglucose resistance. These belong to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906   6 AVFFDCDGTLVDSEVICSRAYVTMFREFGIhvDLKEIFTRFKGVKLYEIIDIiskeqgVTMVQADAEHVYRAEvARLFD- 84
Cdd:cd07527   1 ALLFDMDGTLVDSTPAVERAWHKWAKEHGV--DPEEVLKVSHGRRAIDVIRK------LAPDDADIELVLALE-TEEPEs 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906  85 --TELEDIAGANELLASINV---PMCVVSNGPVSKMQHSLGKLNMLHyfPEKLFSGYDIQRWKPDPALMFHAAKAMNVNV 159
Cdd:cd07527  72 ypEGVIAIPGAVDLLASLPAagdRWAIVTSGTRALAEARLEAAGLPH--PEVLVTADDVKNGKPDPEPYLLGAKLLGLDP 149

                       170       180
                ....*....|....*....|...
gi 15833906 160 ENCILVDDSSAGAQSGIDAGMEV 182
Cdd:cd07527 150 SDCVVFEDAPAGIKAGKAAGARV 172

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 15833906     4 IEAVFFDCDGTLVDSEVICSRAYVTMFREFGIHVDlKEIFTRFKGVKLYEIIDIISKEQGVTMvqaDAEHVYR-AEVARL 82
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGISFD-KQYNESLKGLSREDILRAILKLRGDGL---SLEEIHQlAERKNE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906    83 FDTELEDIAGANEL---------LASINVPMCVVSNGPVSKMqhSLGKLNMLHYFpEKLFSGYDIQRWKPDPALMFHAAK 153
Cdd:TIGR02009  77 LYRELLRLTGVAVLpgirnllkrLKAKGIAVGLGSSSKNAPR--ILAKLGLRDYF-DAIVDASEVKNGKPHPETFLLAAE 153

                         170       180       190
                  ....*....|....*....|....*....|
gi 15833906   154 AMNVNVENCILVDDSSAGAQSGIDAGMEVF 183
Cdd:TIGR02009 154 LLGVPPNECIVFEDALAGVQAARAAGMFAV 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 15833906   6 AVFFDCDGTLVDSEVIcsrayvtmfrefgihvdlkeiftrfkgvkLYEIIDIISKEQGvtmvqadaehvyRAEVARLFD- 84
Cdd:cd16423   1 AVIFDFDGVIVDTEPL-----------------------------WYEAWQELLNERR------------NELIKRQFSe 39

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906  85 -TELEDIAGANELLASI---NVPMCVVSNGPVSKMQHSLGKLNMLHYFpEKLFSGYDIQRWKPDPALMFHAAKAMNVNVE 160
Cdd:cd16423  40 kTDLPPIEGVKELLEFLkekGIKLAVASSSPRRWIEPHLERLGLLDYF-EVIVTGDDVEKSKPDPDLYLEAAERLGVNPE 118

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15833906 161 NCILVDDSSAGAQSGIDAGMEVFYFcADPHNKPIVHPKVTTFTEL 205
Cdd:cd16423 119 ECVVIEDSRNGVLAAKAAGMKCVGV-PNPVTGSQDFSKADLVLSS 162

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 15833906     6 AVFFDCDGTLVDSEVicsrayvtmFREFGIHVDLKEIFTRFKGVKLY----EIIDIISKEQGVTMVQADA-EHVYRAEVA 80
Cdd:TIGR01509   1 AILFDLDGVLVDTEF---------AIAKLINREELGLVPDELGVSAVgrleLALRRFKAQYGRTISPEDAqLLYKQLFYE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906    81 RLFDTELEDI-AGANELLASI---NVPMCVVSNGPvskmqhSLGKLNMLHYFPEKLF----SGYDIQRWKPDPALMFHAA 152
Cdd:TIGR01509  72 QIEEEAKLKPlPGVRALLEALrarGKKLALLTNSP------RAHKLVLALLGLRDLFdvviDSSDVGLGKPDPDIYLQAL 145

                         170       180       190
                  ....*....|....*....|....*....|
gi 15833906   153 KAMNVNVENCILVDDSSAGAQSGIDAGMEV 182
Cdd:TIGR01509 146 KALGLEPSECVFVDDSPAGIEAAKAAGMHT 175

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906     6 AVFFDCDGTLVDSEVICSRAYVTMFREFG-IHVDLKEI-FTRFKGVKLYEIIDIISKE--QGVTMVQADAEHVYRAEVAR 81
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFGlDPASFKALkQAGGLAEEEWYRIATSALEelQGRFWSEYDAEEAYIRGAAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906    82 LFDTelediaganelLASINVPMCVVSNGPVSKMQHSLGKLNMLHYFpeKLFSGYDIQRWKPDPALMFHAAKAMNVNvEN 161
Cdd:TIGR01549  81 LLAR-----------LKSAGIKLGIISNGSLRAQKLLLRLFGLGDYF--ELILVSDEPGSKPEPEIFLAALESLGVP-PE 146

                         170
                  ....*....|....*...
gi 15833906   162 CILVDDSSAGAQSGIDAG 179
Cdd:TIGR01549 147 VLHVGDNLNDIEGARNAG 164

N-acetylmuramic acid 6-phosphate phosphatase MupP;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906    1 MSQIEAVFFDCDGTLVDSEVICSRAYVTMFREFGI-HVDLKEIfTRF--KGVklyeiiDIISkEQGVTMVQADAEHVYRA 77
Cdd:PRK13222   3 FMDIRAVAFDLDGTLVDSAPDLAAAVNAALAALGLpPAGEERV-RTWvgNGA------DVLV-ERALTWAGREPDEELLE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906   78 EVARLFDTELEDIA--------GANELLASI---NVPMCVVSNGPVSKMQHSLGKLNMLHYFpEKLFSGYDIQRWKPDPA 146
Cdd:PRK13222  75 KLRELFDRHYAENVaggsrlypGVKETLAALkaaGYPLAVVTNKPTPFVAPLLEALGIADYF-SVVIGGDSLPNKKPDPA 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 15833906  147 LMFHAAKAMNVNVENCILVDDSSAGAQSGIDAGMEVF 183
Cdd:PRK13222 154 PLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPSV 190

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 15833906   4 IEAVFFDCDGTLVDSEVICSRAYVTMFREFGiHVDLKEIFTRFKGVKLYEIIDIISKEQGVTMVQADAEHVYRAEVARLF 83
Cdd:cd07529   1 VTHCIFDMDGLLLDTERIYTETTQEILARYG-KTYTWDVKAKMMGRPASEAARIIVDELKLPMSLEEEFDEQQEALAELF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906  84 DTELEDIAGANEL---LASINVPMCVVS-----NGPVSKMQHSLGKLNMLHyfpekLFSGYD---IQRWKPDPALMFHAA 152
Cdd:cd07529  80 MGTAKLMPGAERLlrhLHAHNIPIALATssctrHFKLKTSRHKELFSLFHH-----VVTGDDpevKGRGKPAPDIFLVAA 154

                       170       180       190
                ....*....|....*....|....*....|...
gi 15833906 153 KAMN---VNVENCILVDDSSAGAQSGIDAGMEV 182
Cdd:cd07529 155 KRFNeppKDPSKCLVFEDSPNGVKAAKAAGMQV 187

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 15833906   6 AVFFDCDGTLVDSEVICSRAYVTMFREFGI-HVDLKEIFTRF-KGV-KLYE--IIDIISKEQGVTMVQADAE---HVYRA 77
Cdd:cd16417   1 LVAFDLDGTLVDSAPDLAEAANAMLAALGLpPLPEETVRTWIgNGAdVLVEraLTGAREAEPDEELFKEARAlfdRHYAE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906  78 EVA---RLFDteleDIAGANELLASINVPMCVVSNGPVSKMQHSLGKLNMLHYFpEKLFSGYDIQRWKPDPALMFHAAKA 154
Cdd:cd16417  81 TLSvhsHLYP----GVKEGLAALKAQGYPLACVTNKPERFVAPLLEALGISDYF-SLVLGGDSLPEKKPDPAPLLHACEK 155

                       170       180
                ....*....|....*....|....*....
gi 15833906 155 MNVNVENCILVDDSSAGAQSGIDAGMEVF 183
Cdd:cd16417 156 LGIAPAQMLMVGDSRNDILAARAAGCPSV 184

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 15833906   6 AVFFDCDGTLVDSEVICSRAYV-TMFREFGIHVDL-KEIFTRFKGV--------KLYEIID------IISKEQGVTMVQA 69
Cdd:cd07528   1 ALIFDVDGTLAETEELHRRAFNnAFFAERGLDWYWdRELYGELLRVgggkeriaAYFEKVGwpesapKDLKELIADLHKA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906  70 DAEHvY-----------RAEVARLFDtelediaganELLASiNVPMCVVSNGPVSKMQHSLGKLNMLHYFP--EKLFSGY 136
Cdd:cd07528  81 KTER-YaeliaagllplRPGVARLID----------EAKAA-GVRLAIATTTSPANVDALLSALLGPERRAifDAIAAGD 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15833906 137 DIQRWKPDPALMFHAAKAMNVNVENCILVDDSSAGAQSGIDAGMEV 182
Cdd:cd07528 149 DVAEKKPDPDIYLLALERLGVSPSDCLAIEDSAIGLQAAKAAGLPC 194

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15833906 116 QHSLGKLNMLHYFpEKLFSGYDIQRWKPDPALMFHAAKAMNVNVENCILVDDSSAGAQSGIDAGM 180
Cdd:cd02598  78 PKILEKLGLAEYF-DAIVDGAVLAKGKPDPDIFLAAAEGLGLNPKDCIGVEDAQAGIRAIKAAGF 141

haloacid dehalogenase-like hydrolase family protein

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906     4 IEAVFFDCDGTLVDSEVICSRAYVTMFREFGIHVDLkEIFTRFKGVKLYEIIDIISKEQGVTMVQADAEHvyraevARLF 83
Cdd:PLN02919   75 VSAVLFDMDGVLCNSEEPSRRAAVDVFAEMGVEVTV-EDFVPFMGTGEANFLGGVASVKGVKGFDPDAAK------KRFF 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906    84 DTELEDIA---------GANELLA---SINVPMCVVSNGPVSKMQHSLGKLNmlhyFPEKLF----SGYDIQRWKPDPAL 147
Cdd:PLN02919  148 EIYLEKYAkpnsgigfpGALELITqckNKGLKVAVASSADRIKVDANLAAAG----LPLSMFdaivSADAFENLKPAPDI 223

                         170       180       190
                  ....*....|....*....|....*....|...
gi 15833906   148 MFHAAKAMNVNVENCILVDDSSAGAQSGIDAGM 180
Cdd:PLN02919  224 FLAAAKILGVPTSECVVIEDALAGVQAARAAGM 256

hexitol phosphatase HxpB;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906    2 SQIEAVFFDCDGTLVDSEVICSRAYVTMFREFGIHVDLKEIFTRFKGVKlyeiIDiiskeQGVTMVQADA--EHVYRAEV 79
Cdd:PRK10826   5 RQILAAIFDMDGLLIDSEPLWDRAELDVMASLGVDISRREELPDTLGLR----ID-----QVVDLWYARQpwNGPSRQEV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906   80 A-RLFDTELEDIAGANELLASIN--VPMC--------VVSNGPVSKMQHSLGKLNMLHYFpEKLFSGYDIQRWKPDPALM 148
Cdd:PRK10826  76 VqRIIARVISLIEETRPLLPGVReaLALCkaqglkigLASASPLHMLEAVLTMFDLRDYF-DALASAEKLPYSKPHPEVY 154

                        170       180
                 ....*....|....*....|
gi 15833906  149 FHAAKAMNVNVENCILVDDS 168
Cdd:PRK10826 155 LNCAAKLGVDPLTCVALEDS 174

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906   6 AVFFDCDGTLVDSEVICSRAYVTMFREFGIH-VDLKEIfTRFKGvklyeiidiiskeQGV-TMVQ--------ADAEHVY 75
Cdd:cd07512   1 AVIFDLDGTLIDSAPDLHAALNAVLAAEGLApLSLAEV-RSFVG-------------HGApALIRrafaaageDLDGPLH 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906  76 RAEVARLFDTELEDIAGANEL----------LASINVPMCVVSNGPVSKMQHSLGKLNMLHYFpeKLFSGYDI--QRwKP 143
Cdd:cd07512  67 DALLARFLDHYEADPPGLTRPypgviealerLRAAGWRLAICTNKPEAPARALLSALGLADLF--AAVVGGDTlpQR-KP 143

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15833906 144 DPALMFHAAKAMNVNVENCILVDDSSAGAQSGIDAGMEVFYFCADPHNKPIV----HPKVTTFTELSQL 208
Cdd:cd07512 144 DPAPLRAAIRRLGGDVSRALMVGDSETDAATARAAGVPFVLVTFGYRHAPVAelphDAVFSDFDALPDL 212

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906     4 IEAVFFDCDGTLVDSEVICSRAYVTMFREFGIhvDLKE-IFTRFKGV-----KLYEIIDIISKEQGVTMVQADAEHVY-- 75
Cdd:TIGR02254   1 YKTLLFDLDDTILDFQAAEALALRLLFEDQGI--PLTEdMFAQYKEInqglwRAYEEGKITKDEVVNTRFSALLKEYNte 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906    76 --RAEVARLFDTELEDIA----GANELLASIN--VPMCVVSNGpVSKMQHS-LGKLNMLHYFpEKLFSGYDIQRWKPDPA 146
Cdd:TIGR02254  79 adEALLNQKYLRFLEEGHqllpGAFELMENLQqkFRLYIVTNG-VRETQYKrLRKSGLFPFF-DDIFVSEDAGIQKPDKE 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15833906   147 LMFHA-AKAMNVNVENCILVDDS-SAGAQSGIDAGMEVFYFCADPHNKPIVHPKVTTFTELSQL 208
Cdd:TIGR02254 157 IFNYAlERMPKFSKEEVLMIGDSlTADIKGGQNAGLDTCWMNPDMHPNPDDIIPTYEIRSLEEL 220

haloacid dehalogenase-like hydrolase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833906   96 LLASINVPMCVVSNGPVSKMQHSLGKLNMLHYFpEKLFSGYDIQRWKPDPALMFHAAKAMNVNVENCILVDDSSAGAQSG 175
Cdd:PLN02575 227 VLMNYKIPMALVSTRPRKTLENAIGSIGIRGFF-SVIVAAEDVYRGKPDPEMFIYAAQLLNFIPERCIVFGNSNQTVEAA 305

                 ....*.
gi 15833906  176 IDAGME 181
Cdd:PLN02575 306 HDARMK 311