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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546160123    3 YDIILFDADETLFDFKKSEKEAFKNSMIEFKFDYEENYhLEVYKNINTAIWKEFEEGLITQEKLKVERFKRLSDRLEVKF 82
Cdd:TIGR02254   1 YKTLLFDLDDTILDFQAAEALALRLLFEDQGIPLTEDM-FAQYKEINQGLWRAYEEGKITKDEVVNTRFSALLKEYNTEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546160123   83 DELEFAKAYMKHLSLGSFLYDESEEILNSLYENHRMAIITNGLRDVQNGRIKQSKVAHLFEAIIVSEEVNVSKPNPKIFE 162
Cdd:TIGR02254  80 DEALLNQKYLRFLEEGHQLLPGAFELMENLQQKFRLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDKEIFN 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 546160123  163 ITLDSLKFTDKSKVLMVGDSLTSDILGGINYGVDTCWYNPGRIKNSTSIKPTYEINSLYQLNEVL 227
Cdd:TIGR02254 160 YALERMPKFSKEEVLMIGDSLTADIKGGQNAGLDTCWMNPDMHPNPDDIIPTYEIRSLEELYEIL 224

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 546160123 101 LYDESEEILNSLYENHRMAIITNGLRDVQNGRIKQSKVAHLFEAIIVSEEVNVSKPNPKIFEITLDSLKFTdKSKVLMVG 180
Cdd:cd04305   10 LLPGAKELLEELKKGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVK-PEETLMVG 88

                         90       100
                 ....*....|....*....|.
gi 546160123 181 DSLTSDILGGINYGVDTCWYN 201
Cdd:cd04305   89 DSLESDILGAKNAGIKTVWFN 109

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546160123    3 YDIILFDADETLFDFKKSEKEAFKNSMIEFKFDYEENYhLEVYKNINTAIWKEFEEGLITQEKLKVERFKRLSDRLEVKF 82
Cdd:TIGR02254   1 YKTLLFDLDDTILDFQAAEALALRLLFEDQGIPLTEDM-FAQYKEINQGLWRAYEEGKITKDEVVNTRFSALLKEYNTEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546160123   83 DELEFAKAYMKHLSLGSFLYDESEEILNSLYENHRMAIITNGLRDVQNGRIKQSKVAHLFEAIIVSEEVNVSKPNPKIFE 162
Cdd:TIGR02254  80 DEALLNQKYLRFLEEGHQLLPGAFELMENLQQKFRLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDKEIFN 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 546160123  163 ITLDSLKFTDKSKVLMVGDSLTSDILGGINYGVDTCWYNPGRIKNSTSIKPTYEINSLYQLNEVL 227
Cdd:TIGR02254 160 YALERMPKFSKEEVLMIGDSLTADIKGGQNAGLDTCWMNPDMHPNPDDIIPTYEIRSLEELYEIL 224

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 546160123 101 LYDESEEILNSLYENHRMAIITNGLRDVQNGRIKQSKVAHLFEAIIVSEEVNVSKPNPKIFEITLDSLKFTdKSKVLMVG 180
Cdd:cd04305   10 LLPGAKELLEELKKGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVK-PEETLMVG 88

                         90       100
                 ....*....|....*....|.
gi 546160123 181 DSLTSDILGGINYGVDTCWYN 201
Cdd:cd04305   89 DSLESDILGAKNAGIKTVWFN 109

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 546160123   4 DIILFDADETLFDFKKSEKEAFKnsmiEFKFDYEENYHLEVYKNIN-------TAIWKEFEEglITQEKLKverfkRLSD 76
Cdd:cd02588    1 KALVFDVYGTLIDWHSGLAAAER----AFPGRGEELSRLWRQKQLEytwlvtlMGPYVDFDE--LTRDALR-----ATAA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546160123  77 RLEVKFDELEFAKAYMKHLSLGSFlyDESEEILNSLYEN-HRMAIITNGLRDVQNGRIKQSKVAHLFEAIIVSEEVNVSK 155
Cdd:cd02588   70 ELGLELDESDLDELGDAYLRLPPF--PDVVAGLRRLREAgYRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAEDVRAYK 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 546160123 156 PNPKIFEITLDSLKfTDKSKVLMVGDSlTSDILGGINYGVDTCWYN-PGRIKNSTSIKPTYEINSLYQLNE 225
Cdd:cd02588  148 PAPAVYELAAERLG-VPPDEILHVASH-AWDLAGARALGLRTAWINrPGEVPDPLGPAPDFVVPDLGELAD 216

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546160123   3 YDIILFDADETLFDFKKSEKEAFkNSMIEfKFDYEENYHLEVYKNINTAIWKEFEEGLitqEKLKVERFKRLSDRlevkf 82
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAAL-NEALA-ELGLPPLDLEELRALIGLGLRELLRRLL---GEDPDEELEELLAR----- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546160123  83 deleFAKAYMKHLSLGSFLYDESEEILNSLYE-NHRMAIITNGLRDVQNGRIKQSKVAHLFEAIIVSEEVNVSKPNPKIF 161
Cdd:COG0546   71 ----FRELYEEELLDETRLFPGVRELLEALKArGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPL 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 546160123 162 EITLDSLKFtDKSKVLMVGDSlTSDILGGINYGVDTCWYNPGRIKNS--TSIKPTYEINSLYQLNEVLK 228
Cdd:COG0546  147 LEALERLGL-DPEEVLMVGDS-PHDIEAARAAGVPFIGVTWGYGSAEelEAAGADYVIDSLAELLALLA 213

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 546160123    5 IILFDADETLFDFKKSEKEAFknsMIEFKFDYEENYHLEVYKnintaiwkefEEGLITQEKLK---VERFKRLSDRLEVK 81
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAF---PQTFEEFGLDPASFKALK----------QAGGLAEEEWYriaTSALEELQGRFWSE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546160123   82 FDELEfakaymkhlslgSFLYDESEEILNSLYENHRMAIITNGLRDVQNGRIKQSKVAHLFEAIIVSEEvNVSKPNPKIF 161
Cdd:TIGR01549  68 YDAEE------------AYIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDE-PGSKPEPEIF 134

                         170       180       190
                  ....*....|....*....|....*....|...
gi 546160123  162 EITLDSLKftDKSKVLMVGDSLtSDILGGINYG 194
Cdd:TIGR01549 135 LAALESLG--VPPEVLHVGDNL-NDIEGARNAG 164

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 546160123    5 IILFDADETLFDFKKSEKEAFKNSMIEFKFDYEENYHLEVYKNINTAIWKEF-----EEGLITQE---KLKVERFKRLSD 76
Cdd:TIGR02252   2 LITFDAVGTLLALKEPVGEVYCEIARKYGVEVSPDELEQAFRKAFKAMSEAFpnfgfSSGLTPQQwwqKLVRDTFGRAGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546160123   77 RLEVKFDELeFAKAYMKHLSLGS-FLYDESEEILNSLYENH-RMAIITN---GLRDVqngrIKQSKVAHLFEAIIVSEEV 151
Cdd:TIGR02252  82 PDPESFEKI-FEELYSYFATPEPwQVYPDAIKLLKDLRERGlILGVISNfdsRLRGL----LEALGLLEYFDFVVTSYEV 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 546160123  152 NVSKPNPKIFEITLDSLKFTdKSKVLMVGDSLTSDILGGINYGVDTCW 199
Cdd:TIGR02252 157 GAEKPDPKIFQEALERAGIS-PEEALHIGDSLRNDYQGARAAGWRALL 203

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 546160123 106 EEILNSLYE-NHRMAIITNGLRDVQNGRIKQSKVAHLFEAIIVSEEVNVSKPNPKIFEITLDSLKFtDKSKVLMVGDSLT 184
Cdd:cd01427   13 VELLKRLRAaGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGV-DPEEVLFVGDSEN 91

                         90
                 ....*....|....*.
gi 546160123 185 sDILGGINYGVDTCWY 200
Cdd:cd01427   92 -DIEAARAAGGRTVAV 106

HAD-hyrolase-like;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 546160123  155 KPNPKIFEITLDSLKFtDKSKVLMVGDSLTSDILGGINYGVDTCW-----YNPGRIKnSTSIKPTYEINSLYQL 223
Cdd:pfam13242   4 KPNPGMLERALARLGL-DPERTVMIGDRLDTDILGAREAGARTILvltgvTRPADLE-KAPIRPDYVVDDLAEA 75

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to uncharacterized Drosophila melanogaster rhythmically expressed gene 2 protein and human haloacid dehalogenase-like hydrolase domain-containing protein 3; The haloacid dehalogenase-like (HAD) hydrolases are 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 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. Members 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 546160123 117 RMAIITN---GLRDVqngrIKQSKVAHLFEAIIVSEEVNVSKPNPKIFEITLDSLKfTDKSKVLMVGDSLTSDILGGINY 193
Cdd:cd16415   25 KLAVVSNfdrRLREL----LEALGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLG-VSPEEALHVGDDLKNDYLGARAV 99

                 ....*....
gi 546160123 194 GVDTCWYNP 202
Cdd:cd16415  100 GWHALLVDR 108

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 546160123   6 ILFDADETLFDFKKSEK-EAFKNSMIEFKFDYEENYHLEvyknintAIWKEFEEGLITQEklkvERFKRLSDRLEvkfde 84
Cdd:cd02603    4 VLFDFGGVLIDPDPAAAvARFEALTGEPSEFVLDTEGLA-------GAFLELERGRITEE----EFWEELREELG----- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546160123  85 LEFAKAYMKHLSLGSF-LYDESEEILNSL-YENHRMAIITN-GLRDVQNGRIKQSKVAHLFEAIIVSEEVNVSKPNPKIF 161
Cdd:cd02603   68 RPLSAELFEELVLAAVdPNPEMLDLLEALrAKGYKVYLLSNtWPDHFKFQLELLPRRGDLFDGVVESCRLGVRKPDPEIY 147

                 ....*...
gi 546160123 162 EITLDSLK 169
Cdd:cd02603  148 QLALERLG 155

N-acetylmuramic acid 6-phosphate phosphatase MupP;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546160123  79 EVKFDEL--EFAKAYMKHLSLGSFLYDESEEILNSLYE-NHRMAIITN-------GLrdvqngrIKQSKVAHLFEAIIVS 148
Cdd:PRK13222  70 EELLEKLreLFDRHYAENVAGGSRLYPGVKETLAALKAaGYPLAVVTNkptpfvaPL-------LEALGIADYFSVVIGG 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546160123 149 EEVNVSKPNPKIFEITLDSLKFtDKSKVLMVGDSLtSDILGGINYGVDTCW----YNPGR-IKNStsiKPTYEINSLYQL 223
Cdd:PRK13222 143 DSLPNKKPDPAPLLLACEKLGL-DPEEMLFVGDSR-NDIQAARAAGCPSVGvtygYNYGEpIALS---EPDVVIDHFAEL 217

                 ....
gi 546160123 224 NEVL 227
Cdd:PRK13222 218 LPLL 221

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The haloacid dehalogenase-like (HAD) hydrolases are 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 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. Members 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 546160123 101 LYDESEEILNSLYENHRMAIITNG-LRDvQNGRIKQSKVAHLFEAIIVseevnVSKPNPKIFEITLDSLKfTDKSKVLMV 179
Cdd:cd07515   18 LLPGVREALAALKADYRLVLITKGdLLD-QEQKLARSGLSDYFDAVEV-----VSEKDPDTYRRVLSRYG-IGPERFVMV 90

                 ....*....
gi 546160123 180 GDSLTSDIL 188
Cdd:cd07515   91 GNSLRSDIL 99

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 546160123  68 VER-FKRLSDRLEV-KFDELE--FAKAYMKHLSLGSFLYDESEEILNSLY-ENHRMAIITNGLRDVQNGRIKQSKVAHLF 142
Cdd:cd07512   50 IRRaFAAAGEDLDGpLHDALLarFLDHYEADPPGLTRPYPGVIEALERLRaAGWRLAICTNKPEAPARALLSALGLADLF 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 546160123 143 EAIIVSEEVNVSKPNPKIFEITLDSLKfTDKSKVLMVGDSLTsDILGGINYGV 195
Cdd:cd07512  130 AAVVGGDTLPQRKPDPAPLRAAIRRLG-GDVSRALMVGDSET-DAATARAAGV 180

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The haloacid dehalogenase-like (HAD) hydrolases are 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 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. Members 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 546160123 103 DESEEILNSLYENHRMAIITNGLRDVQNG---RIKQSKVAHLFEAIIvSEEVNVSKPNPKIFEITLDSLKFTDKSKVLMV 179
Cdd:cd07525  129 EDYRKLLKAAAARGLPLICANPDLVVPRGgklIYCAGALAELYEELG-GEVIYFGKPHPPIYDLALARLGRPAKARILAV 207

                         90
                 ....*....|....*...
gi 546160123 180 GDSLTSDILGGINYGVDT 197
Cdd:cd07525  208 GDGLHTDILGANAAGLDS 225

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 546160123   99 SFLYDESEEILNSLYE-NHRMAIITN--GLRDVQNGRIKQSKVAHLFEAIIVSEEVNV-----SKPNPKIFEITLDSLKF 170
Cdd:TIGR01662  24 RILYPEVPDALAELKEaGYKVVIVTNqsGIGRGYFSRSFSGRVARRLEELGVPIDILYacpgcRKPKPGMFLEALKRFNE 103

                          90       100       110
                  ....*....|....*....|....*....|..
gi 546160123  171 TDKSKVLMVGDSLTSDILGGINYGVDTCWYNP 202
Cdd:TIGR01662 104 IDPEESVYVGDQDLTDLQAAKRVGLATILVAP 135

5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546160123   6 ILFDADETLFD----FKKSEKEAFKnsmiefkfdYEENYHlevyKNINTAIWKEFEEglITQEKLKVE----------RF 71
Cdd:PRK10748  13 LTFDLDDTLYDnrpvILRTEQEALA---------FVQNYH----PALRSFQNEDLQR--LRQALREAEpeiyhdvtrwRW 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546160123  72 KR----LSDRLEVKFDELEFAKAYMKHLSLGSFLYD---ESEEILNSLYENHRMAIITNGlrdvqNGRIKQSKVAHLFEA 144
Cdd:PRK10748  78 RAieqaMLDAGLSAEEASAGADAAMINFAKWRSRIDvpqATHDTLKQLAKKWPLVAITNG-----NAQPELFGLGDYFEF 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 546160123 145 IIVSEEVNVSKPNPKIFEITLDSLKFTDKsKVLMVGDSLTSDILGGINYGVDTCWYNP 202
Cdd:PRK10748 153 VLRAGPHGRSKPFSDMYHLAAEKLNVPIG-EILHVGDDLTTDVAGAIRCGMQACWINP 209

inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP); LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. 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, 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 546160123 152 NVSKPNPKIFEITLDSLKfTDKSKVLMVGDSLTSDILGGINYG-----VDTCWYNPGrIKNSTSIKPTYEINSLYQ 222
Cdd:cd07509  169 VVGKPSPEFFLSALRSLG-VDPEEAVMIGDDLRDDVGGAQACGmrgilVRTGKYRPS-DEKKPNVPPDLTADSFAD 242

UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar phosphatase; Bacillus subtilis AraL is a phosphatase displaying activity towards different sugar phosphate substrates; it is encoded by the arabinose metabolic operon araABDLMNPQ-abfA and may play a role in the dephosphorylation of substrates related to l-arabinose metabolism. This 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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546160123  49 NTAIWKEFEEGLItqEKLKVERFKRLSdrlevKFDELEFAKAymkhLSLGSFLYDESEEILNSLYENHRMaIITNGLRDV 128
Cdd:cd07531   82 NAKVFVTGEEGLI--EELRLAGLEIVD-----KYDEAEYVVV----GSNRKITYELLTKAFRACLRGARY-IATNPDRIF 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546160123 129 QNGRIKQSKVAHLFEAIIVSE----EVNVSKPNPKIFEITLDSLKFtDKSKVLMVGDSLTSDILGGINYGVDTCWYNPGR 204
Cdd:cd07531  150 PAEDGPIPDTAAIIGAIEWCTgrepEVVVGKPSEVMAREALDILGL-DAKDCAIVGDQIDVDIAMGKAIGMETALVLTGV 228