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 495777498    4 DWIFFDADETLFTFDSFGG--LQRMFLDYSVTFTAEDFQDYQAVNKPLWVDYQNGAITALQLQHQRFDVWAERLKVS--P 79
Cdd:TIGR02254   2 KTLLFDLDDTILDFQAAEAlaLRLLFEDQGIPLTEDMFAQYKEINQGLWRAYEEGKITKDEVVNTRFSALLKEYNTEadE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777498   80 GTLNEAFLNAMADICAPLPGAVSLLNALKGKVKLGIITNGFTALQQIRLERTGLRDHFDALVISEEVGVPKPDPRIFDYA 159
Cdd:TIGR02254  82 ALLNQKYLRFLEEGHQLLPGAFELMENLQQKFRLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDKEIFNYA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495777498  160 LAQAGNPDRDRVLMVGDTAESDILGGMKAGLSTVWLNAHGRVKPEGIEPTWTVTSLNELEQLL 222
Cdd:TIGR02254 162 LERMPKFSKEEVLMIGDSLTADIKGGQNAGLDTCWMNPDMHPNPDDIIPTYEIRSLEELYEIL 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 495777498  97 LPGAVSLLNALKGKVKLGIITNGFTALQQIRLERTGLRDHFDALVISEEVGVPKPDPRIFDYALAQAGNPdRDRVLMVGD 176
Cdd:cd04305   11 LPGAKELLEELKKGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVK-PEETLMVGD 89

                         90       100
                 ....*....|....*....|
gi 495777498 177 TAESDILGGMKAGLSTVWLN 196
Cdd:cd04305   90 SLESDILGAKNAGIKTVWFN 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 495777498    4 DWIFFDADETLFTFDSFGG--LQRMFLDYSVTFTAEDFQDYQAVNKPLWVDYQNGAITALQLQHQRFDVWAERLKVS--P 79
Cdd:TIGR02254   2 KTLLFDLDDTILDFQAAEAlaLRLLFEDQGIPLTEDMFAQYKEINQGLWRAYEEGKITKDEVVNTRFSALLKEYNTEadE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777498   80 GTLNEAFLNAMADICAPLPGAVSLLNALKGKVKLGIITNGFTALQQIRLERTGLRDHFDALVISEEVGVPKPDPRIFDYA 159
Cdd:TIGR02254  82 ALLNQKYLRFLEEGHQLLPGAFELMENLQQKFRLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDKEIFNYA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495777498  160 LAQAGNPDRDRVLMVGDTAESDILGGMKAGLSTVWLNAHGRVKPEGIEPTWTVTSLNELEQLL 222
Cdd:TIGR02254 162 LERMPKFSKEEVLMIGDSLTADIKGGQNAGLDTCWMNPDMHPNPDDIIPTYEIRSLEELYEIL 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 495777498  97 LPGAVSLLNALKGKVKLGIITNGFTALQQIRLERTGLRDHFDALVISEEVGVPKPDPRIFDYALAQAGNPdRDRVLMVGD 176
Cdd:cd04305   11 LPGAKELLEELKKGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVK-PEETLMVGD 89

                         90       100
                 ....*....|....*....|
gi 495777498 177 TAESDILGGMKAGLSTVWLN 196
Cdd:cd04305   90 SLESDILGAKNAGIKTVWFN 109

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777498   6 IFFDADETLFtfDSFGGL----QRMFLDYSV-TFTAEDFQDYqaVNKPLWVdyqngAITALqLQHQRFDVWAERLKVspg 80
Cdd:COG0546    4 VLFDLDGTLV--DSAPDIaaalNEALAELGLpPLDLEELRAL--IGLGLRE-----LLRRL-LGEDPDEELEELLAR--- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777498  81 tLNEAFLNAMADICAPLPGAVSLLNALKGK-VKLGIITNGFTALQQIRLERTGLRDHFDALVISEEVGVPKPDPRIFDYA 159
Cdd:COG0546   71 -FRELYEEELLDETRLFPGVRELLEALKARgIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEA 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495777498 160 LAQAGNpDRDRVLMVGDTaESDILGGMKAGLSTVWLN--AHGRVKPEGIEPTWTVTSLNELEQLL 222
Cdd:COG0546  150 LERLGL-DPEEVLMVGDS-PHDIEAARAAGVPFIGVTwgYGSAEELEAAGADYVIDSLAELLALL 212

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 495777498    5 WIFFDADETLFtfDSFGGLQRMFLDysvtfTAEDFQDYQAVNKPLwvdyqngaitaLQLQHQRFDVWAERLKVSPGTLNE 84
Cdd:TIGR01549   1 AILFDIDGTLV--DIKFAIRRAFPQ-----TFEEFGLDPASFKAL-----------KQAGGLAEEEWYRIATSALEELQG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777498   85 AFLNAMADICAPLPGAVSLLNALKGK-VKLGIITNGFTALQQIRLERTGLRDHFDALVISEEVGVpKPDPRIFDYALAQA 163
Cdd:TIGR01549  63 RFWSEYDAEEAYIRGAADLLARLKSAgIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEPGS-KPEPEIFLAALESL 141

                         170       180
                  ....*....|....*....|....*.
gi 495777498  164 GNPdrDRVLMVGDTaESDILGGMKAG 189
Cdd:TIGR01549 142 GVP--PEVLHVGDN-LNDIEGARNAG 164

Haloacid dehalogenase-like hydrolase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777498   73 ERLKVSPGTLNEAFLNAMAD-ICAPLPGAVSLLNALK-GKVKLGIITNGFTALQQIRLERTGLRDHFDALVISEEVGVPK 150
Cdd:pfam13419  56 EDEEEKIEFYLRKYNEELHDkLVKPYPGIKELLEELKeQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKK 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 495777498  151 PDPRIFDYALAQAGNpDRDRVLMVGDTaESDILGGMKAGLSTVW 194
Cdd:pfam13419 136 PDPDPILKALEQLGL-KPEEVIYVGDS-PRDIEAAKNAGIKVIA 177

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 495777498    6 IFFDADETLFtfDSFGGLQRMFLD-YSVTFTAEDFQDYQAVNKPLWVDYQngaiTALQLQHQRFDVWAERLKVSPGTLNE 84
Cdd:pfam00702   4 VVFDLDGTLT--DGEPVVTEAIAElASEHPLAKAIVAAAEDLPIPVEDFT----ARLLLGKRDWLEELDILRGLVETLEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777498   85 AFLNAM----------ADICAPLPGAVSLLNALKGK-VKLGIITNGFTALQQIRLERTGLRDHFDALVISEEVGVPKPDP 153
Cdd:pfam00702  78 EGLTVVlvellgvialADELKLYPGAAEALKALKERgIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKP 157

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 495777498  154 RIFDYALAQAGNpDRDRVLMVGDTAEsDILGGMKAG 189
Cdd:pfam00702 158 EIYLAALERLGV-KPEEVLMVGDGVN-DIPAAKAAG 191

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 495777498    6 IFFDADETLFTFDSFGGLQRMFLDYSVTftaEDFQDYQAVNKPLWvdyqngAITALQLQHQRFDVWAERLKVSPGTLNEA 85
Cdd:TIGR01509   2 ILFDLDGVLVDTEFAIAKLINREELGLV---PDELGVSAVGRLEL------ALRRFKAQYGRTISPEDAQLLYKQLFYEQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777498   86 FLNAMADicAPLPGAVSLLNALKGK-VKLGIITNGFTALQQiRLERTGLRDHFDALVISEEVGVPKPDPRIFDYALAQAG 164
Cdd:TIGR01509  73 IEEEAKL--KPLPGVRALLEALRARgKKLALLTNSPRAHKL-VLALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALG 149

                         170       180       190
                  ....*....|....*....|....*....|.
gi 495777498  165 NPDrDRVLMVGDtAESDILGGMKAGLSTVWL 195
Cdd:TIGR01509 150 LEP-SECVFVDD-SPAGIEAAKAAGMHTVGV 178

Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777498 139 ALVISEEVGVP-----KPDPRIFDYALAQAGnPDRDRVLMVGDTAESDILGGMKAGLSTVW----LNAHGRVKPEGIEPT 209
Cdd:COG0647  170 AAALEAATGGEplvvgKPSPPIYELALERLG-VDPERVLMVGDRLDTDILGANAAGLDTLLvltgVTTAEDLEAAPIRPD 248

                 ....*....
gi 495777498 210 WTVTSLNEL 218
Cdd:COG0647  249 YVLDSLAEL 257

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 495777498 100 AVSLLNALKGK-VKLGIITNGFTALQQIRLERTGLRDHFDALVISEEVGVPKPDPRIFDYALAQAGnPDRDRVLMVGDTa 178
Cdd:cd01427   12 AVELLKRLRAAgIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLG-VDPEEVLFVGDS- 89

                         90
                 ....*....|....*..
gi 495777498 179 ESDILGGMKAGLSTVWL 195
Cdd:cd01427   90 ENDIEAARAAGGRTVAV 106

N-acetylmuramic acid 6-phosphate phosphatase MupP;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777498  90 MADICAPLPGAVSLLNALKGK-VKLGIITNGFTALQQIRLERTGLRDHFDALVISEEVGVPKPDPRIFDYALAQAGNpDR 168
Cdd:PRK13222  88 VAGGSRLYPGVKETLAALKAAgYPLAVVTNKPTPFVAPLLEALGIADYFSVVIGGDSLPNKKPDPAPLLLACEKLGL-DP 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495777498 169 DRVLMVGDTaESDILGGMKAGLSTVWLNaHGRVKPEGI---EPTWTVTSLNELEQLL 222
Cdd:PRK13222 167 EEMLFVGDS-RNDIQAARAAGCPSVGVT-YGYNYGEPIalsEPDVVIDHFAELLPLL 221

HAD-hyrolase-like;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495777498  150 KPDPRIFDYALAQAGnPDRDRVLMVGDTAESDILGGMKAGLSTVW----LNAHGRVKPEGIEPTWTVTSLNEL 218
Cdd:pfam13242   4 KPNPGMLERALARLG-LDPERTVMIGDRLDTDILGAREAGARTILvltgVTRPADLEKAPIRPDYVVDDLAEA 75

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
                 ....*....|....*....|....*....|....*....|....
gi 495777498 150 KPDPRIFDYALAQAGNPDRDRVLMVGDTAESDILGGMKAGLSTV 193
Cdd:cd07525  183 KPHPPIYDLALARLGRPAKARILAVGDGLHTDILGANAAGLDSL 226

beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; This family represents the beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. Family 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. It 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 495777498  89 AMADICAPLPGAVSLLNALKG-KVKLGIITNGFTA-LQQIRLERTGLRDHFDALVISEEVGVPKPDPRIFDYAlAQAGNP 166
Cdd:cd07505   35 IASEGLKLKPGVVELLDALKAaGIPVAVATSSSRRnVELLLLELGLLRGYFDVIVSGDDVERGKPAPDIYLLA-AERLGV 113

                         90       100
                 ....*....|....*....|....*..
gi 495777498 167 DRDRVLMVGDtAESDILGGMKAGLSTV 193
Cdd:cd07505  114 DPERCLVFED-SLAGIEAAKAAGMTVV 139

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 495777498  98 PGAVSLLNALKGK-VKLGIITNGFTALQQIRLERTGLRDHFDALVISEEVGVPKPDPRIFDYALAQAGNPDRDrVLMVGD 176
Cdd:cd16417   90 PGVKEGLAALKAQgYPLACVTNKPERFVAPLLEALGISDYFSLVLGGDSLPEKKPDPAPLLHACEKLGIAPAQ-MLMVGD 168

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 495777498 177 TAeSDILGGMKAGLSTVWLN---AHGRvKPEGIEPTWTVTSLNEL 218
Cdd:cd16417  169 SR-NDILAARAAGCPSVGLTygyNYGE-DIAASGPDAVIDSLAEL 211

pyrimidine 5'-nucleotidase; This family of proteins includes the SDT1/SSM1 gene from yeast which has been shown to code for a pyrimidine (UMP/CMP) 5'nucleotidase. The family spans plants, fungi and a small number of bacteria. These enzymes are members of the haloacid dehalogenase (HAD) superfamily of hydrolases, specifically the IA subfamily (variant 3, TIGR01509).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777498    4 DWIFFDADETLFtfDSFGGL-----QRM--FLDYSVTFTAED--------FQDYQAVNKPLWVDYQNGAITALQLQHQRF 68
Cdd:TIGR01993   1 DVWFFDLDNTLY--PHSAGIflqidRNIteFVAARLKLSPEEarvlrkdyYKEYGTTLAGLMILHEIDADEYLRYVHGRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777498   69 DVwaERLKVSPGTLNeaflnamadicaplpgavsLLNALKGKvkLGIITNGFTALQQIRLERTGLRDHFDALVISEEVG- 147
Cdd:TIGR01993  79 PY--DKLKPDPELRN-------------------LLLRLPGR--KIIFTNGDRAHARRALRRLGIEDCFDGIFCFDTANp 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 495777498  148 --VPKPDPRIFDYALAQAGnPDRDRVLMVGDTAEsDILGGMKAGLSTV 193
Cdd:TIGR01993 136 dlLPKPSPQAYEKALREAG-VDPERAIFFDDSAR-NIAAGKALGMKTV 181

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777498 103 LLNALKGKvkLGIITNGFTALQQIRLERTGLRDHFDALV-ISEEVGVPKPDPRIFDYALAQAGnPDRDRVLMVGDTaESD 181
Cdd:cd02604   91 LLLALPGR--KIIFTNASKNHAIRVLKRLGLADLFDGIFdIEYAGPDPKPHPAAFEKAIREAG-LDPKRAAFFDDS-IRN 166

                         90
                 ....*....|...
gi 495777498 182 ILGGMKAGLSTVW 194
Cdd:cd02604  167 LLAAKALGMKTVL 179

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777498  88 NAMADICAPLPGAVSLLNALKG-KVKLGIITNGFTALQQIRLERTGLRdHFDALVISEEVGVPKPDPRIFDYALAQAGNP 166
Cdd:cd07527   70 ESYPEGVIAIPGAVDLLASLPAaGDRWAIVTSGTRALAEARLEAAGLP-HPEVLVTADDVKNGKPDPEPYLLGAKLLGLD 148

                         90       100       110
                 ....*....|....*....|....*....|.
gi 495777498 167 DRDRVlmVGDTAESDILGGMKAGLSTVWLNA 197
Cdd:cd07527  149 PSDCV--VFEDAPAGIKAGKAAGARVVAVNT 177

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777498  96 PLPGAVSLLNALKGK-VKLGIITNGFTALQQIRLERTGLRDHFDALVISEEVGVPKPDPRIFDYALAQAG 164
Cdd:cd16423   45 PIEGVKELLEFLKEKgIKLAVASSSPRRWIEPHLERLGLLDYFEVIVTGDDVEKSKPDPDLYLEAAERLG 114

UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium falciparum PNPase; Plasmodium falciparum para nitrophenyl phosphate phosphatase (PNPase) catalyzes the dephosphorylation of thiamine monophosphate to thiamine, other substrates on which its active are nucleotides, phosphorylated sugars, pyridoxal-5-phosphate, and paranitrophenyl phosphate. 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
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 495777498 150 KPDPRIFDYaLAQAGNPDRDRVLMVGDTAESDILGGMKAGLSTVWLNAhGRVKPEGIEP 208
Cdd:cd07532  206 KPNPQILNF-LMKSGVIKPERTLMIGDRLKTDILFANNCGFQSLLVGT-GVNSLEDAEK 262

UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase; This subfamily includes the phosphoglycolate phosphatases (human PGP and Arabidopsis thaliana PGLP2) and p-nitrophenylphosphatases (Schizosaccharomyces pombe PHO2 and Saccharomyces PHO13p). It 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
                 ....*....|....*....|....*....|....*....|....*.
gi 495777498 148 VPKPDPRIFDYaLAQAGNPDRDRVLMVGDTAESDILGGMKAGLSTV 193
Cdd:cd07510  202 VGKPSRFMFDC-ISSKFSIDPARTCMVGDRLDTDILFGQNCGLKTL 246