uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1; This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281199625  17 VLFDKNGTLEDSEDFLRSLGQKAVRLIDAQIPGIGEplsmALGISGDVLDLTgLMAVASRKETeiaaaayiaetgrgwfD 96
Cdd:cd07533    2 VIFDWDGTLADSQHNIVAAMTAAFADLGLPVPSAAE----VRSIIGLSLDEA-IARLLPMATP----------------A 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281199625  97 CLKIARQALKEAHEY--IGQNPSSLYPGVLELLELLSSRGTKLGILSAATTKGVKQFVTCYGLRDYLELEMGVDEGLGKP 174
Cdd:cd07533   61 LVAVAERYKEAFDILrlLPEHAEPLFPGVREALDALAAQGVLLAVATGKSRRGLDRVLEQHGLGGYFDATRTADDTPSKP 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281199625 175 DPRLFLQACNTLGVQPQNALMVGDSIGDMQMARDAKAGGcIGITWN-NNLAQVR--GADVVIHQLADI 239
Cdd:cd07533  141 HPEMLREILAELGVDPSRAVMVGDTAYDMQMAANAGAHA-VGVAWGyHSLEDLRsaGADAVVDHFSEL 207

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 281199625   16 AVLFDKNGTLEDSEDFLRSLGQKAVRLIDAQIPGIgEPLSMALGISGDvldLTGLMAVASRKETEiaaaayiaetGRGWf 95
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFGLDPASF-KALKQAGGLAEE---EWYRIATSALEELQ----------GRFW- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281199625   96 DCLKIARQALKEAHEYIgqnpsslypgvlellELLSSRGTKLGILSAATTKGVKQFVTCYGLRDYLELEMGVDEGLGKPD 175
Cdd:TIGR01549  66 SEYDAEEAYIRGAADLL---------------ARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEPGSKPE 130

                         170       180       190
                  ....*....|....*....|....*....|....
gi 281199625  176 PRLFLQACNTLGVQPQnALMVGDSIGDMQMARDA 209
Cdd:TIGR01549 131 PEIFLAALESLGVPPE-VLHVGDNLNDIEGARNA 163

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1; This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281199625  17 VLFDKNGTLEDSEDFLRSLGQKAVRLIDAQIPGIGEplsmALGISGDVLDLTgLMAVASRKETeiaaaayiaetgrgwfD 96
Cdd:cd07533    2 VIFDWDGTLADSQHNIVAAMTAAFADLGLPVPSAAE----VRSIIGLSLDEA-IARLLPMATP----------------A 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281199625  97 CLKIARQALKEAHEY--IGQNPSSLYPGVLELLELLSSRGTKLGILSAATTKGVKQFVTCYGLRDYLELEMGVDEGLGKP 174
Cdd:cd07533   61 LVAVAERYKEAFDILrlLPEHAEPLFPGVREALDALAAQGVLLAVATGKSRRGLDRVLEQHGLGGYFDATRTADDTPSKP 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281199625 175 DPRLFLQACNTLGVQPQNALMVGDSIGDMQMARDAKAGGcIGITWN-NNLAQVR--GADVVIHQLADI 239
Cdd:cd07533  141 HPEMLREILAELGVDPSRAVMVGDTAYDMQMAANAGAHA-VGVAWGyHSLEDLRsaGADAVVDHFSEL 207

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 281199625   16 AVLFDKNGTLEDSEDFLRSLGQKAVRLIDAQIPGIgEPLSMALGISGDvldLTGLMAVASRKETEiaaaayiaetGRGWf 95
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFGLDPASF-KALKQAGGLAEE---EWYRIATSALEELQ----------GRFW- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281199625   96 DCLKIARQALKEAHEYIgqnpsslypgvlellELLSSRGTKLGILSAATTKGVKQFVTCYGLRDYLELEMGVDEGLGKPD 175
Cdd:TIGR01549  66 SEYDAEEAYIRGAADLL---------------ARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEPGSKPE 130

                         170       180       190
                  ....*....|....*....|....*....|....
gi 281199625  176 PRLFLQACNTLGVQPQnALMVGDSIGDMQMARDA 209
Cdd:TIGR01549 131 PEIFLAALESLGVPPE-VLHVGDNLNDIEGARNA 163

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 281199625  98 LKIARQALKEAHEYIGQNPSSLYPGVLELLELLSSRGTKLGILSAATTKGVKQFVTCYGLRDYLELEMGVDE-GLGKPDP 176
Cdd:cd16417   67 FKEARALFDRHYAETLSVHSHLYPGVKEGLAALKAQGYPLACVTNKPERFVAPLLEALGISDYFSLVLGGDSlPEKKPDP 146

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281199625 177 RLFLQACNTLGVQPQNALMVGDSIGDMQMARdakAGGC--IGITWNNN----LAQVrGADVVIHQLADI 239
Cdd:cd16417  147 APLLHACEKLGIAPAQMLMVGDSRNDILAAR---AAGCpsVGLTYGYNygedIAAS-GPDAVIDSLAEL 211

Haloacid dehalogenase-like hydrolase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281199625  118 SLYPGVLELLELLSSRGTKLGILSAATTKGVKQFVTCYGLRDYLE-LEMGVDEGLGKPDPRLFLQACNTLGVQPQNALMV 196
Cdd:pfam13419  79 KPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDvIVGGDDVEGKKPDPDPILKALEQLGLKPEEVIYV 158

                          90
                  ....*....|....*.
gi 281199625  197 GDSIGDMQMARdaKAG 212
Cdd:pfam13419 159 GDSPRDIEAAK--NAG 172

N-acetylmuramic acid 6-phosphate phosphatase MupP;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281199625  11 FSDIQAVLFDKNGTLEDSedflrslgqkavrlidaqIPGIGEPLSMALGISG-------DVLDLTG-----LMAVA---S 75
Cdd:PRK13222   3 FMDIRAVAFDLDGTLVDS------------------APDLAAAVNAALAALGlppageeRVRTWVGngadvLVERAltwA 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281199625  76 RKETEIAAaayiaetgrgwfdclkiARQALKEAHEYIGQNP---SSLYPGVLELLELLSSRGTKLGILSAATTKGVKQFV 152
Cdd:PRK13222  65 GREPDEEL-----------------LEKLRELFDRHYAENVaggSRLYPGVKETLAALKAAGYPLAVVTNKPTPFVAPLL 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281199625 153 TCYGLRDYLELEMGVDE-GLGKPDPRLFLQACNTLGVQPQNALMVGDSIGDMQMARDAkagGC--IGITWNNNLAQ-VR- 227
Cdd:PRK13222 128 EALGIADYFSVVIGGDSlPNKKPDPAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAA---GCpsVGVTYGYNYGEpIAl 204

                        250
                 ....*....|...
gi 281199625 228 -GADVVIHQLADI 239
Cdd:PRK13222 205 sEPDVVIDHFAEL 217

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 281199625   16 AVLFDKNGTLEDSEDFLRSLGQKAVRLIDAQIPGIGEPLSMALGISGDVLDLTGLMAvasrketeiaaaayiaetgRGWF 95
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAIAKLINREELGLVPDELGVSAVGRLELALRRFKAQYGRTIS-------------------PEDA 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281199625   96 DCLKIARQAlkeaHEYIGQNPSSLYPGVLELLELLSSRGTKLGILSAATtKGVKQFVTCYGLRDYLELEM-GVDEGLGKP 174
Cdd:TIGR01509  62 QLLYKQLFY----EQIEEEAKLKPLPGVRALLEALRARGKKLALLTNSP-RAHKLVLALLGLRDLFDVVIdSSDVGLGKP 136

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 281199625  175 DPRLFLQACNTLGVQPQNALMVGDSIGDMQMARDA 209
Cdd:TIGR01509 137 DPDIYLQALKALGLEPSECVFVDDSPAGIEAAKAA 171

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 281199625 117 SSLYPGVLELLELLSSRGTKLGILSAATTKGVKQFVTCYGLRDYLELEMGVDE-GLGKPDPRLFLQACNTLGVQPQNALM 195
Cdd:cd07512   85 TRPYPGVIEALERLRAAGWRLAICTNKPEAPARALLSALGLADLFAAVVGGDTlPQRKPDPAPLRAAIRRLGGDVSRALM 164

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 281199625 196 VGDSIGDMQMARDAKAGGcIGITWNNNLAQVR--GADVVIHQLADIQVL 242
Cdd:cd07512  165 VGDSETDAATARAAGVPF-VLVTFGYRHAPVAelPHDAVFSDFDALPDL 212

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 281199625 121 PGVLELLELLSSRGTKLGILSAATTKGVKQFVTCYGLRDYLE-LEMGVDEGLGKPDPRLFLQACNTLGVQPQNALMVGDS 199
Cdd:cd16423   47 EGVKELLEFLKEKGIKLAVASSSPRRWIEPHLERLGLLDYFEvIVTGDDVEKSKPDPDLYLEAAERLGVNPEECVVIEDS 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 281199625 200 I-GdmqmARDAKAGG--CIGITWNNNLAQV-RGADVVIHQLADIQVL 242
Cdd:cd16423  127 RnG----VLAAKAAGmkCVGVPNPVTGSQDfSKADLVLSSFAEKEIL 169

haloacid dehalogenase-like hydrolase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281199625  96 DCLKIARQALK--EAHEYIGQNPSSLYPGVLELLELLSSRGTKLGILSAATTKGVKQFVTCYGLRDYLELEMGVDEGL-G 172
Cdd:PLN03243  85 DFLQMKRLAIRkeDLYEYMQGGLYRLRPGSREFVQALKKHEIPIAVASTRPRRYLERAIEAVGMEGFFSVVLAAEDVYrG 164

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281199625 173 KPDPRLFLQACNTLGVQPQNALMVGDSIGDMQMARDAKAgGCIGITWNNNLAQVRGADVVIHQLADIQVL 242
Cdd:PLN03243 165 KPDPEMFMYAAERLGFIPERCIVFGNSNSSVEAAHDGCM-KCVAVAGKHPVYELSAGDLVVRRLDDLSVV 233

2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Belongs to the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases (pfam00702), class (subfamily) I. Note that the Type I HAD enzymes have not yet been fully characterized, but clearly utilize a substantially different catalytic mechanism and are thus unlikely to be related.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281199625   14 IQAVLFDKNGTLEDsedfLRSLGQKAvrliDAQIPGIGEPLSMaLGiSGDVLDLTGLMAVASRketeiaaaayiaetgrg 93
Cdd:TIGR01428   1 IKALVFDVYGTLFD----VHSVAERA----AELYGGRGEALSQ-LW-RQKQLEYSWLRTLMGP----------------- 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281199625   94 WFDCLKIARQALKEAheyIGQNPSSL-----------------YPGVLELLELLSSRGTKLGILSAATTKGVKQFVTCYG 156
Cdd:TIGR01428  54 YKDFWDLTREALRYL---LGRLGLEDdesaadrlaeaylrlppHPDVPAGLRALKERGYRLAILSNGSPAMLKSLVKHAG 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281199625  157 LRDYLELEMGVDE-GLGKPDPRLFLQACNTLGVQPQNALMVGDSIGDmqmARDAKAGGCIGI 217
Cdd:TIGR01428 131 LDDPFDAVLSADAvRAYKPAPQVYQLALEALGVPPDEVLFVASNPWD---LGGAKKFGFKTA 189

hexitol phosphatase HxpB;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281199625  14 IQAVLFDKNGTLEDSEDFLRsLGQKAVrlidaqIPGIGEPLSMAlgisGDVLDLTGL---MAVASrketeiaaaayiaet 90
Cdd:PRK10826   7 ILAAIFDMDGLLIDSEPLWD-RAELDV------MASLGVDISRR----EELPDTLGLridQVVDL--------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281199625  91 grgWFDCL--------KIARQALKEAHEYIGQNpSSLYPGVLELLELLSSRGTKLGILSAATTKGVKQFVTCYGLRDYLE 162
Cdd:PRK10826  61 ---WYARQpwngpsrqEVVQRIIARVISLIEET-RPLLPGVREALALCKAQGLKIGLASASPLHMLEAVLTMFDLRDYFD 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 281199625 163 -LEMGVDEGLGKPDPRLFLQACNTLGVQPQNALMVGDSIGDMQMARDA 209
Cdd:PRK10826 137 aLASAEKLPYSKPHPEVYLNCAAKLGVDPLTCVALEDSFNGMIAAKAA 184

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 281199625  16 AVLFDKNGTLEDsedfLRSLGQKAVRLIDAQIPGIGE-------PLSMALGISGDVLDLTGLMAVASRKeteiaaaayia 88
Cdd:cd02588    2 ALVFDVYGTLID----WHSGLAAAERAFPGRGEELSRlwrqkqlEYTWLVTLMGPYVDFDELTRDALRA----------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281199625  89 etgrgwfdCLKIARQALKEAH-EYIGQNPSSL--YPGVLELLELLSSRGTKLGILSAATTKGVKQFVTCYGLRDYLELEM 165
Cdd:cd02588   67 --------TAAELGLELDESDlDELGDAYLRLppFPDVVAGLRRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFDAVL 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 281199625 166 GVDE-GLGKPDPRLFLQACNTLGVQPQNALMVGDSIGDMQMARDA 209
Cdd:cd02588  139 SAEDvRAYKPAPAVYELAAERLGVPPDEILHVASHAWDLAGARAL 183

pyrophosphatase PpaX; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281199625 120 YPGVLELLELLSSRGTKLGILsaaTTK-------GVKQFvtcyGLRDYLELEMGVDE-GLGKPDPRLFLQACNTLGVQPQ 191
Cdd:PRK13288  84 YETVYETLKTLKKQGYKLGIV---TTKmrdtvemGLKLT----GLDEFFDVVITLDDvEHAKPDPEPVLKALELLGAKPE 156

                         90       100
                 ....*....|....*....|....*...
gi 281199625 192 NALMVGDSIGDMQMARDAKAGGCiGITW 219
Cdd:PRK13288 157 EALMVGDNHHDILAGKNAGTKTA-GVAW 183

HAD-hyrolase-like;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281199625  171 LGKPDPRLFLQACNTLGVQPQNALMVGDSIG-DMQMARDAKAGGCI---GITWNNNLAQ-VRGADVVIHQLAD 238
Cdd:pfam13242   2 CGKPNPGMLERALARLGLDPERTVMIGDRLDtDILGAREAGARTILvltGVTRPADLEKaPIRPDYVVDDLAE 74

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281199625 152 VTCYGLRDYLE--LEMGVDEGLGKPDPRLFLQACNTLGVQPQNALMVGDSIGDMQMARDA 209
Cdd:cd07526   73 LGLAGLLAYFEgrIFSASDVGRGKPAPDLFLHAAAQMGVAPERCLVIEDSPTGVRAALAA 132

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 281199625 119 LYPGVLELLELLSSRGTKLGILSAATTKGVKQFVTCY-GLRDYLELEM---GVDEGLGKPDPRLFLQACNTLGVQPQNAL 194
Cdd:cd07528   96 LRPGVARLIDEAKAAGVRLAIATTTSPANVDALLSALlGPERRAIFDAiaaGDDVAEKKPDPDIYLLALERLGVSPSDCL 175

                         90
                 ....*....|....*
gi 281199625 195 MVGDSIGDMQMARDA 209
Cdd:cd07528  176 AIEDSAIGLQAAKAA 190

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281199625 133 RGTKLGILSAATTKGVKQFVTCYGLRDYlELEMGVDEGLG-KPDPRLFLQACNTLGVQPQNALMVGDSIGDMQMARDA 209
Cdd:cd16421   22 KGIKLAVLSNKPNEAVQVLVEELFPGSF-DFVLGEKEGIRrKPDPT*ALECAKVLGVPPDEVLYVGDSGVDMQTARNA 98

D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 281199625 173 KPDPRLFLQACNTLGVQPQNALMVGDSIGDMQMARDAKA 211
Cdd:PRK08942 103 KPKPGMLLSIAERLNIDLAGSPMVGDSLRDLQAAAAAGV 141

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 281199625 133 RGTKLGILSAATTKGVKQFVTCYGLR-DYLElemGV----DEGLGKPDPRLFLQACNTLGVQPQNALMVGDSIGDMQMAR 207
Cdd:cd02603   99 KGYKVYLLSNTWPDHFKFQLELLPRRgDLFD---GVvescRLGVRKPDPEIYQLALERLGVKPEEVLFIDDREENVEAAR 175

                 ..
gi 281199625 208 DA 209
Cdd:cd02603  176 AL 177

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 281199625 116 PSSLYPGVLELLELLSSRGTKLGILSAatTKGVKQFVTCYGLRDYLELEmgVDEGL---GKPDPRLFLQACNTLGVQPQN 192
Cdd:cd02598   47 PVDVLPGIASLLVDLKAKGIKIALASA--SKNAPKILEKLGLAEYFDAI--VDGAVlakGKPDPDIFLAAAEGLGLNPKD 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 281199625 193 ALMVGDSIGDMQMardAKAGGCIGITWNNNLAQVRGADVVIHQLADIQV 241
Cdd:cd02598  123 CIGVEDAQAGIRA---IKAAGFLVVGVGREEDLLGADIVVPDTTADLTI 168