L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048205782   6 KAFVFDVYGTLFDVHSVKAACDEQFPGKGDQISQTWRTKQLDYFFTRHIMGRYADFSVVTRDALRYALETADVTWTTETE 85
Cdd:cd02588     1 KALVFDVYGTLIDWHSGLAAAERAFPGRGEELSRLWRQKQLEYTWLVTLMGPYVDFDELTRDALRATAAELGLELDESDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048205782  86 DALIATYADLSPYEEVADVLHQLHHK--QTIVLSNGTDAMLEALIHNAGFTDLFDELVSIDGIKQAKPSPAAYMHWFKNS 163
Cdd:cd02588    81 DELGDAYLRLPPFPDVVAGLRRLREAgyRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAEDVRAYKPAPAVYELAAERL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2048205782 164 GLKRDEVLFMSSNGWDIAGAKNFGFHTAWINRDSKPVDMPDLAPEAVYEDLSGILE 219
Cdd:cd02588   161 GVPPDEILHVASHAWDLAGARALGLRTAWINRPGEVPDPLGPAPDFVVPDLGELAD 216

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 2048205782   5 VKAFVFDVYGTLFDVHSV-----KAACDEQFPGKGDQISQTWRTKQLDYFFTRHIMGRYADF-SVVTRDALRYALETADV 78
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVvteaiAELASEHPLAKAIVAAAEDLPIPVEDFTARLLLGKRDWLeELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048205782  79 TWTTETEDALIATYADLSPYEEVADVLHQLHHK--QTIVLSNGTDAMLEALIHNAGFTDLFDELVSIDGIKQAKPSPAAY 156
Cdd:pfam00702  81 TVVLVELLGVIALADELKLYPGAAEALKALKERgiKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIY 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2048205782 157 MHWFKNSGLKRDEVLFMSSNGWDIAGAKNFG 187
Cdd:pfam00702 161 LAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048205782   6 KAFVFDVYGTLFDVHSVKAACDEQFPGKGDQISQTWRTKQLDYFFTRHIMGRYADFSVVTRDALRYALETADVTWTTETE 85
Cdd:cd02588     1 KALVFDVYGTLIDWHSGLAAAERAFPGRGEELSRLWRQKQLEYTWLVTLMGPYVDFDELTRDALRATAAELGLELDESDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048205782  86 DALIATYADLSPYEEVADVLHQLHHK--QTIVLSNGTDAMLEALIHNAGFTDLFDELVSIDGIKQAKPSPAAYMHWFKNS 163
Cdd:cd02588    81 DELGDAYLRLPPFPDVVAGLRRLREAgyRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAEDVRAYKPAPAVYELAAERL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2048205782 164 GLKRDEVLFMSSNGWDIAGAKNFGFHTAWINRDSKPVDMPDLAPEAVYEDLSGILE 219
Cdd:cd02588   161 GVPPDEILHVASHAWDLAGARALGLRTAWINRPGEVPDPLGPAPDFVVPDLGELAD 216

Haloacid dehalogenase superfamily, subfamily IA, variant 2 with 3rd motif like haloacid dehalogenase; 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 2 (this model) is distinctive of the type II haloacid dehalogenases, and nearly all of the sequences are also part of the HAD, type II equivalog model (TIGR01428). 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048205782   7 AFVFDVYGTLFDVHSVKAACDEQFPGKGDQISQTWRTKQLDYFFTRHIMGRYADFSVVTRDALRYALETADVTWTTETED 86
Cdd:TIGR01493   1 AMVFDVYGTLVDVHGGVRACLAAIAPEGGAFSDLWRAKQQEYSWRRSLMGDRRAFPEDTVRALRYIADRLGLDAEPKYGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048205782  87 ALIATYADLSPYEEVADVLhqlhhKQTIVLSNGTDAMLEALIHNAGFTDLFDELVSIDGIKQAKPSPAAYMHWFKNSGLK 166
Cdd:TIGR01493  81 RLRDAYKNLPPWPDSAAAL-----ARVAILSNASHWAFDQFAQQAGLPWYFDRAFSVDTVRAYKPDPVVYELVFDTVGLP 155

                         170       180
                  ....*....|....*....|
gi 2048205782 167 RDEVLFMSSNGWDIAGAKNF 186
Cdd:TIGR01493 156 PDRVLMVAAHQWDLIGARKF 175

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048205782   5 VKAFVFDVYGTLFD-----VHSVKAACDEQfpgkgdqisqtwRTKQLDYFFTRHIMGRYAdfsvvtRDALRYALETADVT 79
Cdd:COG0546     1 IKLVLFDLDGTLVDsapdiAAALNEALAEL------------GLPPLDLEELRALIGLGL------RELLRRLLGEDPDE 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048205782  80 WTTETEDALIATYAD-----LSPYEEVADVLHQLHHK--QTIVLSNGTDAMLEALIHNAGFTDLFDELVSIDGIKQAKPS 152
Cdd:COG0546    63 ELEELLARFRELYEEelldeTRLFPGVRELLEALKARgiKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPK 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2048205782 153 PAAYMHWFKNSGLKRDEVLFMssnG---WDIAGAKNFGFHTAWINRD-SKPVDMPDLAPEAVYEDLSGILEWV 221
Cdd:COG0546   143 PEPLLEALERLGLDPEEVLMV---GdspHDIEAARAAGVPFIGVTWGyGSAEELEAAGADYVIDSLAELLALL 212

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048205782  98 YEEVADVLHQLHHKQTI-VLSNGTDAMLEALIHNAGFTDLFDELVSIDGIKQAKPSPAAYMHWFKNSGLKRDEVLfMSSN 176
Cdd:cd04305    11 LPGAKELLEELKKGYKLgIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETL-MVGD 89

                          90       100
                  ....*....|....*....|
gi 2048205782 177 GW--DIAGAKNFGFHTAWIN 194
Cdd:cd04305    90 SLesDILGAKNAGIKTVWFN 109

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048205782 101 VADVLHQL--HHKQTIVLSNGTDAMLEALIHNAGFTDLFDELVSIDGIKQAKPSPAAYMHWFKNSGLKRDEVLFMSSNGW 178
Cdd:cd01427    12 AVELLKRLraAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSEN 91

                          90
                  ....*....|....*
gi 2048205782 179 DIAGAKNFGFHTAWI 193
Cdd:cd01427    92 DIEAARAAGGRTVAV 106

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048205782   5 VKAFVFDVYGTLFDVHSVKAAcdEQFPGKGDQISQTWRTKQLDY-FFTRHIMGRY--ADFsvvtRDALRYALETADvtwT 81
Cdd:cd02603     1 IRAVLFDFGGVLIDPDPAAAV--ARFEALTGEPSEFVLDTEGLAgAFLELERGRIteEEF----WEELREELGRPL---S 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048205782  82 TETEDALIatYADLSPYEEVADVLHQLHHKQ--TIVLSN-GTDAMLEALIHNAGFTDLFDELVSIDGIKQAKPSPAAYMH 158
Cdd:cd02603    72 AELFEELV--LAAVDPNPEMLDLLEALRAKGykVYLLSNtWPDHFKFQLELLPRRGDLFDGVVESCRLGVRKPDPEIYQL 149

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2048205782 159 WFKNSGLKRDEVLFMSSNGWDIAGAKNFGFHT 190
Cdd:cd02603   150 ALERLGVKPEEVLFIDDREENVEAARALGIHA 181

N-acetylmuramic acid 6-phosphate phosphatase MupP;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048205782   1 MKPHVKAFVFDVYGTLfdVHSVK---AACDEQFPGKGdqisqtwrTKQLDYFFTRHIMGRYADfsVVTRDALRYALETAD 77
Cdd:PRK13222    2 KFMDIRAVAFDLDGTL--VDSAPdlaAAVNAALAALG--------LPPAGEERVRTWVGNGAD--VLVERALTWAGREPD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048205782  78 VTWTTETEDALIATYAD----LS-PYEEVADVLHQLHHKQTI--VLSNGTDAMLEALIHNAGFTDLFDELVSIDGIKQAK 150
Cdd:PRK13222   70 EELLEKLRELFDRHYAEnvagGSrLYPGVKETLAALKAAGYPlaVVTNKPTPFVAPLLEALGIADYFSVVIGGDSLPNKK 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2048205782 151 PSPAAYMHWFKNSGLKRDEVLFM--SSNgwDIAGAKNFGFHTAWI----NRdskPVDMPDLAPEAVYEDLSGILEWVT 222
Cdd:PRK13222  150 PDPAPLLLACEKLGLDPEEMLFVgdSRN--DIQAARAAGCPSVGVtygyNY---GEPIALSEPDVVIDHFAELLPLLG 222

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 2048205782   7 AFVFDVYGTLFDVHSVKAACDEQ-FPGKGDQISQTWRTKQlDYFFTRHIMGRYAdfsvvtRDALRYALETADVTWttETE 85
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQtFEEFGLDPASFKALKQ-AGGLAEEEWYRIA------TSALEELQGRFWSEY--DAE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048205782  86 DALIATYADlspyeeVADVLHQLHHKQTIVLSNGTDAMLEALIHNAGFTDLFDELVSIDGIkqAKPSPAAYMHWFKNSGL 165
Cdd:TIGR01549  72 EAYIRGAAD------LLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEPG--SKPEPEIFLAALESLGV 143

                         170       180
                  ....*....|....*....|..
gi 2048205782 166 KrDEVLFMSSNGWDIAGAKNFG 187
Cdd:TIGR01549 144 P-PEVLHVGDNLNDIEGARNAG 164

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 2048205782   7 AFVFDVYGTLfdVHSVK--AACdeqfpgkGDQISQTWRTKQLDYFFTRHIMGRYADfsVVTRDALRYALETADVTWTTET 84
Cdd:cd16417     1 LVAFDLDGTL--VDSAPdlAEA-------ANAMLAALGLPPLPEETVRTWIGNGAD--VLVERALTGAREAEPDEELFKE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048205782  85 EDAL-IATYADL-----SPYEEVADVLHQLHHKQTI--VLSNGTDAMLEALIHNAGFTDLFDELVSIDGIKQAKPSPAAY 156
Cdd:cd16417    70 ARALfDRHYAETlsvhsHLYPGVKEGLAALKAQGYPlaCVTNKPERFVAPLLEALGISDYFSLVLGGDSLPEKKPDPAPL 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2048205782 157 MHWFKNSGLKRDEVLFM--SSNgwDIAGAKNFGFHTAWI----NRdskPVDMPDLAPEAVYEDLSGIL 218
Cdd:cd16417   150 LHACEKLGIAPAQMLMVgdSRN--DILAARAAGCPSVGLtygyNY---GEDIAASGPDAVIDSLAELL 212

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p; This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and CMP. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048205782  92 YADLSPYEEVADVLHQLHHKqTIVLSNGTDAMLEALIHNAGFTDLFDELVSIDGI-KQAKPSPAAYMHWFKNSGLKRDEV 170
Cdd:cd02604    79 YDHLKPDPKLRNLLLALPGR-KIIFTNASKNHAIRVLKRLGLADLFDGIFDIEYAgPDPKPHPAAFEKAIREAGLDPKRA 157

                          90       100
                  ....*....|....*....|...
gi 2048205782 171 LFMSSNGWDIAGAKNFGFHTAWI 193
Cdd:cd02604   158 AFFDDSIRNLLAAKALGMKTVLV 180

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 2048205782  86 DALIATYADLSPYEEVADVLHQLHHK--QTIVLSNGTDAMLEALIHNAGFTDLFDELVSIDGIKQAKPSPAAYMHWFKNS 163
Cdd:cd16423    34 KRQFSEKTDLPPIEGVKELLEFLKEKgiKLAVASSSPRRWIEPHLERLGLLDYFEVIVTGDDVEKSKPDPDLYLEAAERL 113

                          90       100
                  ....*....|....*....|....*.
gi 2048205782 164 GLKRDEVLFM--SSNGwdIAGAKNFG 187
Cdd:cd16423   114 GVNPEECVVIedSRNG--VLAAKAAG 137

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048205782  97 PYEEVADVLHQLHhKQTI---VLSNGTDAMLEALIHNAGFTDLFDELVSIDGIKQAKPSPAAYMHWFKNSGLKRDEVLFM 173
Cdd:cd02616    81 EYPGVYETLARLK-SQGIklgVVTTKLRETALKGLKLLGLDKYFDVIVGGDDVTHHKPDPEPVLKALELLGAEPEEALMV 159

                          90
                  ....*....|....*...
gi 2048205782 174 SSNGWDIAGAKNFGFHTA 191
Cdd:cd02616   160 GDSPHDILAGKNAGVKTV 177