Haloacid dehalogenase-like hydrolase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595957    4 ILFDKDGTLIEFDKSWEKIgirlVDSLLEEY---PVADKEVAHrqlgvldnaivpdsVMGSgSLDEMIKAFN--NVVGKD 78
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKS----FNYLLEEFgygELSEEEILK--------------FIGL-PLREIFRYLGvsEDEEEK 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595957   79 VSTWTRNTSQELVDTRVPEnnwIDGVYDMIQSLKKDGYKIGIVTSDSRKGVLQFLEDTNSKDAFDLVISTESHAAEKPNP 158
Cdd:pfam13419  62 IEFYLRKYNEELHDKLVKP---YPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDP 138

                         170       180       190
                  ....*....|....*....|....*....|...
gi 499595957  159 AVLNPLFDSYDVEPEDVVIVGDTNNDMKTKVNA 191
Cdd:pfam13419 139 DPILKALEQLGLKPEEVIYVGDSPRDIEAAKNA 171

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 499595957    3 WILFDKDGTLIEFDKSWEkigiRLVDSLLEEYPVADKEV-AHRQLGVLDNAIVPDsvMGSGSLDEMIKAFnnvvgkdvst 81
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIR----RAFPQTFEEFGLDPASFkALKQAGGLAEEEWYR--IATSALEELQGRF---------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595957   82 WTRNTSQELvdtrvpennWIDGVYDMIQSLKKDGYKIGIVTSDSRKGVLQFLEDTNSKDAFDLvISTESHAAEKPNPAVL 161
Cdd:TIGR01549  65 WSEYDAEEA---------YIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFEL-ILVSDEPGSKPEPEIF 134

                         170       180
                  ....*....|....*....|....*.
gi 499595957  162 NPLFDSYDVEPEdVVIVGDTNNDMKT 187
Cdd:TIGR01549 135 LAALESLGVPPE-VLHVGDNLNDIEG 159

Haloacid dehalogenase-like hydrolase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595957    4 ILFDKDGTLIEFDKSWEKIgirlVDSLLEEY---PVADKEVAHrqlgvldnaivpdsVMGSgSLDEMIKAFN--NVVGKD 78
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKS----FNYLLEEFgygELSEEEILK--------------FIGL-PLREIFRYLGvsEDEEEK 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595957   79 VSTWTRNTSQELVDTRVPEnnwIDGVYDMIQSLKKDGYKIGIVTSDSRKGVLQFLEDTNSKDAFDLVISTESHAAEKPNP 158
Cdd:pfam13419  62 IEFYLRKYNEELHDKLVKP---YPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDP 138

                         170       180       190
                  ....*....|....*....|....*....|...
gi 499595957  159 AVLNPLFDSYDVEPEDVVIVGDTNNDMKTKVNA 191
Cdd:pfam13419 139 DPILKALEQLGLKPEEVIYVGDSPRDIEAAKNA 171

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 499595957   4 ILFDKDGTLIEfdkSWEKIgirlVDSLLEEY-----PVADKEVAHRQLGV-LDNAIVPDSVMGSGSLDEMIKAFnnvvgK 77
Cdd:cd07533    2 VIFDWDGTLAD---SQHNI----VAAMTAAFadlglPVPSAAEVRSIIGLsLDEAIARLLPMATPALVAVAERY-----K 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595957  78 DVSTWTRNTSQelvdtrvPENNWIDGVYDMIQSLKKDGYKIGIVTSDSRKGVLQFLEDTNSKDAFDlVISTESHAAEKPN 157
Cdd:cd07533   70 EAFDILRLLPE-------HAEPLFPGVREALDALAAQGVLLAVATGKSRRGLDRVLEQHGLGGYFD-ATRTADDTPSKPH 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499595957 158 PAVLNPLFDSYDVEPEDVVIVGDTNNDMKTKVNAELGlAIGVLTGIAKKEELVD--ADVIIE 217
Cdd:cd07533  142 PEMLREILAELGVDPSRAVMVGDTAYDMQMAANAGAH-AVGVAWGYHSLEDLRSagADAVVD 202

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 499595957    4 ILFDKDGTLIEFDKSWEKIgirlVDSLLEEYPVADKEVAH-RQLGVLDNAIVPDSVMGSGSLDEMIKAFNNVVGKDVSTW 82
Cdd:pfam00702   4 VVFDLDGTLTDGEPVVTEA----IAELASEHPLAKAIVAAaEDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595957   83 TRNTSQELVDTRVPENNWI--DGVYDMIQSLKKDGYKIGIVTSDSRKGVLQFLEDTNSKDAFDLVISTESHAAEKPNPAV 160
Cdd:pfam00702  80 LTVVLVELLGVIALADELKlyPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEI 159

                         170       180
                  ....*....|....*....|....*.
gi 499595957  161 LNPLFDSYDVEPEDVVIVGDTNNDMK 186
Cdd:pfam00702 160 YLAALERLGVKPEEVLMVGDGVNDIP 185

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 499595957    3 WILFDKDGTLIEFDKSWEkigiRLVDSLLEEYPVADKEV-AHRQLGVLDNAIVPDsvMGSGSLDEMIKAFnnvvgkdvst 81
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIR----RAFPQTFEEFGLDPASFkALKQAGGLAEEEWYR--IATSALEELQGRF---------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595957   82 WTRNTSQELvdtrvpennWIDGVYDMIQSLKKDGYKIGIVTSDSRKGVLQFLEDTNSKDAFDLvISTESHAAEKPNPAVL 161
Cdd:TIGR01549  65 WSEYDAEEA---------YIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFEL-ILVSDEPGSKPEPEIF 134

                         170       180
                  ....*....|....*....|....*.
gi 499595957  162 NPLFDSYDVEPEdVVIVGDTNNDMKT 187
Cdd:TIGR01549 135 LAALESLGVPPE-VLHVGDNLNDIEG 159

pyrophosphatase PpaX; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595957   4 ILFDKDGTLIEFDkswEKIGIRLVDSLLEEYP--VADKEVAH---RQLGVLDNAIVPDSVmgsgslDEMIKAFnnvvgkd 78
Cdd:PRK13288   6 VLFDLDGTLINTN---ELIISSFLHTLKTYYPnqYKREDVLPfigPSLHDTFSKIDESKV------EEMITTY------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595957  79 vstwtRNTSQELVDTRVPEnnwIDGVYDMIQSLKKDGYKIGIVTSDSRKGVLQFLEDTNSKDAFDLVISTESHAAEKPNP 158
Cdd:PRK13288  70 -----REFNHEHHDELVTE---YETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPDP 141

                        170       180       190
                 ....*....|....*....|....*....|...
gi 499595957 159 AVLNPLFDSYDVEPEDVVIVGDTNNDMKTKVNA 191
Cdd:PRK13288 142 EPVLKALELLGAKPEEALMVGDNHHDILAGKNA 174

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 499595957 101 IDGVYDMIQSLKKdGYKIGIVTSDSRKGVLQFLEDTNSKDAFDLVISTESHAAEKPNPAVLNPLFDSYDVEPEDVVIVGD 180
Cdd:cd04305   11 LPGAKELLEELKK-GYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLMVGD 89

                         90
                 ....*....|..
gi 499595957 181 T-NNDMKTKVNA 191
Cdd:cd04305   90 SlESDILGAKNA 101

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 499595957 102 DGVYDMIQSLKKDGYKIGIVTSDSRKGVLQFLEDTNSKDAFDLVISTESHAAEKPNPAVLNPLFDSYDVEPEDVVIVGDT 181
Cdd:cd07512   89 PGVIEALERLRAAGWRLAICTNKPEAPARALLSALGLADLFAAVVGGDTLPQRKPDPAPLRAAIRRLGGDVSRALMVGDS 168

                         90
                 ....*....|
gi 499595957 182 NNDMKTKVNA 191
Cdd:cd07512  169 ETDAATARAA 178

N-acetylmuramic acid 6-phosphate phosphatase MupP;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595957 102 DGVYDMIQSLKKDGYKIGIVTSDSRKGVLQFLEDTNSKDAFDLVISTESHAAEKPNPAVLNPLFDSYDVEPEDVVIVGDT 181
Cdd:PRK13222  96 PGVKETLAALKAAGYPLAVVTNKPTPFVAPLLEALGIADYFSVVIGGDSLPNKKPDPAPLLLACEKLGLDPEEMLFVGDS 175

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 499595957 182 NNDMKTKVNAelGLA-IGVLTGIAKKE--ELVDADVIIETAVSVPEVLKQ 228
Cdd:PRK13222 176 RNDIQAARAA--GCPsVGVTYGYNYGEpiALSEPDVVIDHFAELLPLLGL 223

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 499595957    4 ILFDKDGTLIEFDKSWEKIGIRlvdsllEEYPVADKEVAHrqlGVLDNAIVPDSVMGSGSLDEMIKA-FNNVVGKDVSTW 82
Cdd:TIGR01509   2 ILFDLDGVLVDTEFAIAKLINR------EELGLVPDELGV---SAVGRLELALRRFKAQYGRTISPEdAQLLYKQLFYEQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595957   83 TRNTSQELVDtrvpennwiDGVYDMIQSLKKDGYKIGIVTSdSRKGVLQFLEDTNSKDAFDLVISTESHAAEKPNPAVLN 162
Cdd:TIGR01509  73 IEEEAKLKPL---------PGVRALLEALRARGKKLALLTN-SPRAHKLVLALLGLRDLFDVVIDSSDVGLGKPDPDIYL 142

                         170
                  ....*....|....*....
gi 499595957  163 PLFDSYDVEPEDVVIVGDT 181
Cdd:TIGR01509 143 QALKALGLEPSECVFVDDS 161

REG-2-like, HAD superfamily (subfamily IA) hydrolase; This family of proteins includes uncharacterized sequences from eukaryotes, cyanobacteria and Leptospira as well as the DREG-2 protein from Drosophila melanogaster which has been identified as a rhythmically (diurnally) regulated gene. This family is a member 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. This family is a member of subfamily 1A in which the cap domain consists of a predicted alpha helical bundle found in between the first and second catalytic motifs. A distinctive feature of this family is a conserved tandem pair of tryptophan residues in the cap domain. The most divergent sequences included within the scope of this model are from plants and have "FW" at this position instead. Most likely, these sequences, like the vast majority of HAD sequences, represent phosphatase enzymes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595957  102 DGVYDMIQSLKKDGYKIGIVTS-DSR-KGVLQfleDTNSKDAFDLVISTESHAAEKPNPAVLNPLFDSYDVEPEDVVIVG 179
Cdd:TIGR02252 108 PDAIKLLKDLRERGLILGVISNfDSRlRGLLE---ALGLLEYFDFVVTSYEVGAEKPDPKIFQEALERAGISPEEALHIG 184

                  .
gi 499595957  180 D 180
Cdd:TIGR02252 185 D 185

HAD-hyrolase-like;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499595957  155 KPNPAVLNPLFDSYDVEPEDVVIVGDT-NNDMKTKVNAelGL-AIGVLTGIAKKEELVDAD 213
Cdd:pfam13242   4 KPNPGMLERALARLGLDPERTVMIGDRlDTDILGAREA--GArTILVLTGVTRPADLEKAP 62

uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid dehalogenase-like superfamily; This uncharacterized subfamily belongs to the UmpH/NagD phosphatase family and 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 499595957 148 TESHAAEKPNPAVLNPLFDSYDVEPEDVVIVGD-TNNDMKTKVNAELgLAIGVLTGIAKKEELVDAD 213
Cdd:cd16422  170 RPDLVIGKPNPIILDPVLEKFDYSKEETVMVGDrLYTDIVLGINAGV-DSILVLSGETTREDLEDLE 235

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 499595957 103 GVYDMIQSLKKDGYKIGIVTSDSRKGVLQFLEDTNSKDA---FDLVISTESHAAEKPNPAVLNPLFDSYDVEPEDVVIVG 179
Cdd:cd07528   99 GVARLIDEAKAAGVRLAIATTTSPANVDALLSALLGPERraiFDAIAAGDDVAEKKPDPDIYLLALERLGVSPSDCLAIE 178

                 ....
gi 499595957 180 DTNN 183
Cdd:cd07528  179 DSAI 182

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499595957  106 DMIQSLKKdgykIGIVTSDSRKGVLQFLEDTNSKDAFDLVISTESHAAEKPNPAVLNPLFDSYDVEPEDVVIV 178
Cdd:TIGR01493  94 DSAAALAR----VAILSNASHWAFDQFAQQAGLPWYFDRAFSVDTVRAYKPDPVVYELVFDTVGLPPDRVLMV 162

phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase PGP/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 499595957  88 QELVDTRVPENNWIDGVYDMIQSLKKDGYKIGIVTSDSRKGVLQFLEDTNskdafdlVISTESHAAEKP---NPAVLNPL 164
Cdd:cd04303   68 RRLMAEAAPELALFPGVEDMLRALHARGVRLAVVSSNSEENIRRVLGPEE-------LISLFAVIEGSSlfgKAKKIRRV 140

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499595957 165 FDSYDVEPEDVVIVGDTNNDmktkVNA--ELGLAIGVLT-GIAKKEELVDA--DVIIET 218
Cdd:cd04303  141 LRRTKITAAQVIYVGDETRD----IEAarKVGLAFAAVSwGYAKPEVLKALapDHMLED 195

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499595957 108 IQSLKKDGYKIGIVTSDSRKGVLQFLEDTNSKDAFDLVISTESHAAEKPNPAVLNPLFDSYDVEPEDVVIV 178
Cdd:cd02588  100 LRRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAEDVRAYKPAPAVYELAAERLGVPPDEILHV 170

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 499595957   1 MEWILFDKDGTLIEFD--KSWEKIGIRLVDSLLEEYPVADKEVAHRQLGVldnaivpdsvmGSGSLDEMIKAFNNVVGkd 78
Cdd:cd02603    1 IRAVLFDFGGVLIDPDpaAAVARFEALTGEPSEFVLDTEGLAGAFLELER-----------GRITEEEFWEELREELG-- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595957  79 vstwtRNTSQELVDTRVPENNWID-GVYDMIQSLKKDGYKIGIVTSDSRK-GVLQFLEDTNSKDAFDLVI--STESHAae 154
Cdd:cd02603   68 -----RPLSAELFEELVLAAVDPNpEMLDLLEALRAKGYKVYLLSNTWPDhFKFQLELLPRRGDLFDGVVesCRLGVR-- 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499595957 155 KPNPAVLNPLFDSYDVEPEDVVIVgDtnnDMKTKVNA--ELGL-AIGVLTGIAKKEEL 209
Cdd:cd02603  141 KPDPEIYQLALERLGVKPEEVLFI-D---DREENVEAarALGIhAILVTDAEDALREL 194

phosphoglycolate phosphatase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595957  95 VPENNWIDGVYDMIQSLKKDGYKIGIVTSDSRKGVLQFLEDTNSKDAFDLVISTESHAAEKpnpAVLNPLFDSYDVEPED 174
Cdd:PRK13225 138 LPALQLFPGVADLLAQLRSRSLCLGILSSNSRQNIEAFLQRQGLRSLFSVVQAGTPILSKR---RALSQLVAREGWQPAA 214

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499595957 175 VVIVGDTNNDMKTKVNAELgLAIGVLTGIAKKEELVDA--DVIIETAVSVPEVLKQYI 230
Cdd:PRK13225 215 VMYVGDETRDVEAARQVGL-IAVAVTWGFNDRQSLVAAcpDWLLETPSDLLQAVTQLM 271

phosphoglycolate phosphatase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595957 103 GVYDMIQSLKKDGYKIGIVTSDSRKGVLQFLEDTNSKDAFDLVISTESHAAEKPNPAVLNPLFDSYDVEPEDVVIVGDTN 182
Cdd:PRK13223 105 GVRDTLKWLKKQGVEMALITNKPERFVAPLLDQMKIGRYFRWIIGGDTLPQKKPDPAALLFVMKMAGVPPSQSLFVGDSR 184

                 ...
gi 499595957 183 NDM 185
Cdd:PRK13223 185 SDV 187

P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily of the heavy metal-transporting ATPases (Type IB ATPases) which transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595957   4 ILFDKDGTLIEFDKSW--------EKIGIRLVDSLLE--EYPVAD---KEVAHRQLGVLDNA----IVPDSVMG--SGSL 64
Cdd:cd07553  321 IVFDKTGTLTRGKSSFvmvnpegiDRLALRAISAIEAhsRHPISRairEHLMAKGLIKAGASelveIVGKGVSGnsSGSL 400

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595957  65 DEMIKA-FNNVVGKDVSTWTRNTSQELVdtRVPENNWIDGVYDMIQSLKKDGYKIGIVTSDsRKGVLQFLEDTNSKDAFD 143
Cdd:cd07553  401 WKLGSApDACGIQESGVVIARDGRQLLD--LSFNDLLRPDSNREIEELKKGGLSIAILSGD-NEEKVRLVGDSLGLDPRQ 477

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499595957 144 LV--ISTESHAaekpnpAVLNplfdsyDVEPEDVVIVGDTNNDMKTKVNAELGLAI 197
Cdd:cd07553  478 LFgnLSPEEKL------AWIE------SHSPENTLMVGDGANDALALASAFVGIAV 521

HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme. [Unknown function, Enzymes of unknown specificity]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595957  100 WIDGVYDMIQSLKKDGYKIGIVTSDSRKGVLQFLEDTNSKDA---------FDLVISTEShaAEKPNPAVLNPLFDSY-D 169
Cdd:TIGR01662  26 LYPEVPDALAELKEAGYKVVIVTNQSGIGRGYFSRSFSGRVArrleelgvpIDILYACPG--CRKPKPGMFLEALKRFnE 103

                          90
                  ....*....|....*...
gi 499595957  170 VEPEDVVIVGDT-NNDMK 186
Cdd:TIGR01662 104 IDPEESVYVGDQdLTDLQ 121

hexitol phosphatase HxpB;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595957 103 GVYDMIQSLKKDGYKIGIVTSDSRKGVLQFLEDTNSKDAFDLVISTESHAAEKPNPAV-LNPLfDSYDVEPEDVVIVGDT 181
Cdd:PRK10826  96 GVREALALCKAQGLKIGLASASPLHMLEAVLTMFDLRDYFDALASAEKLPYSKPHPEVyLNCA-AKLGVDPLTCVALEDS 174