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 2530369125   4 DWIFFDADETLFTFDSFSG--LQRMFLDYSVTFTAEDFQDYQAVNKPLWVDYQNGAITSLQLQHQRFDSWAERLNVP--P 79
Cdd:TIGR02254   2 KTLLFDLDDTILDFQAAEAlaLRLLFEDQGIPLTEDMFAQYKEINQGLWRAYEEGKITKDEVVNTRFSALLKEYNTEadE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530369125  80 GELNDAFMNAMAEICAPLPGAVSLLNALQGKVRMGIITNGFTSLQQTRLERTGLRDHFDLLIISEQVGVAKPDARIFDYA 159
Cdd:TIGR02254  82 ALLNQKYLRFLEEGHQLLPGAFELMENLQQKFRLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDKEIFNYA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2530369125 160 LAQAGNPPRSRVLMVGDTAESDIRGGVNAGLATCWLNAHQRELPADLEPDWTVTSLSELEQLL 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 2530369125  97 LPGAVSLLNALQGKVRMGIITNGFTSLQQTRLERTGLRDHFDLLIISEQVGVAKPDARIFDYALAQAGNPPRsRVLMVGD 176
Cdd:cd04305    11 LPGAKELLEELKKGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPE-ETLMVGD 89

                          90       100
                  ....*....|....*....|
gi 2530369125 177 TAESDIRGGVNAGLATCWLN 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 2530369125   4 DWIFFDADETLFTFDSFSG--LQRMFLDYSVTFTAEDFQDYQAVNKPLWVDYQNGAITSLQLQHQRFDSWAERLNVP--P 79
Cdd:TIGR02254   2 KTLLFDLDDTILDFQAAEAlaLRLLFEDQGIPLTEDMFAQYKEINQGLWRAYEEGKITKDEVVNTRFSALLKEYNTEadE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530369125  80 GELNDAFMNAMAEICAPLPGAVSLLNALQGKVRMGIITNGFTSLQQTRLERTGLRDHFDLLIISEQVGVAKPDARIFDYA 159
Cdd:TIGR02254  82 ALLNQKYLRFLEEGHQLLPGAFELMENLQQKFRLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDKEIFNYA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2530369125 160 LAQAGNPPRSRVLMVGDTAESDIRGGVNAGLATCWLNAHQRELPADLEPDWTVTSLSELEQLL 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 2530369125  97 LPGAVSLLNALQGKVRMGIITNGFTSLQQTRLERTGLRDHFDLLIISEQVGVAKPDARIFDYALAQAGNPPRsRVLMVGD 176
Cdd:cd04305    11 LPGAKELLEELKKGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPE-ETLMVGD 89

                          90       100
                  ....*....|....*....|
gi 2530369125 177 TAESDIRGGVNAGLATCWLN 196
Cdd:cd04305    90 SLESDILGAKNAGIKTVWFN 109

Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530369125   6 IFFDADETLFtfDS----FSGLQRMFLDYSVTFTAEDFQDYQAVNkplwvdyqngAITSLQLQHQRFDswaerLNVPPGE 81
Cdd:COG0637     5 VIFDMDGTLV--DSeplhARAWREAFAELGIDLTEEEYRRLMGRS----------REDILRYLLEEYG-----LDLPEEE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530369125  82 LNDAFMNAMAEICA-----PLPGAVSLLNALQGK-VRMGIITNGFTSLQQTRLERTGLRDHFDLLIISEQVGVAKPDARI 155
Cdd:COG0637    68 LAARKEELYRELLAeeglpLIPGVVELLEALKEAgIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDI 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2530369125 156 FDYALAQAGNPPrSRVLMVGDtAESDIRGGVNAGLATCWLNAHQRELPADLEPDWTVTSLSEL 218
Cdd:COG0637   148 YLLAAERLGVDP-EECVVFED-SPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208

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 2530369125   5 WIFFDADETLFTFD--SFSGLQRMFldysvtftaEDFQDYQAVNKPLwvdyqngaitsLQLQHQRFDSWAERLNVPPGEL 82
Cdd:TIGR01549   1 AILFDIDGTLVDIKfaIRRAFPQTF---------EEFGLDPASFKAL-----------KQAGGLAEEEWYRIATSALEEL 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530369125  83 NDAFMNAMAEICAPLPGAVSLLNALQGK-VRMGIITNGFTSLQQTRLERTGLRDHFDLLIISEQVGvAKPDARIFDYALA 161
Cdd:TIGR01549  61 QGRFWSEYDAEEAYIRGAADLLARLKSAgIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEPG-SKPEPEIFLAALE 139

                         170       180
                  ....*....|....*....|....*...
gi 2530369125 162 QAGNPPrsRVLMVGDTaESDIRGGVNAG 189
Cdd:TIGR01549 140 SLGVPP--EVLHVGDN-LNDIEGARNAG 164

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 2530369125 100 AVSLLNALQGK-VRMGIITNgFTSLQQTRLERTGLRDHFDLLIISEQVGVAKPDARIFDYALAQAGNPPrSRVLMVGDTA 178
Cdd:cd16415    12 AVETLKDLKEKgLKLAVVSN-FDRRLRELLEALGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSP-EEALHVGDDL 89

                          90
                  ....*....|....*...
gi 2530369125 179 ESDIRGGVNAGLATCWLN 196
Cdd:cd16415    90 KNDYLGARAVGWHALLVD 107

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 2530369125   5 WIFFDADETLFTFDSFSGLQ--RMFLDYSVTFT-AEDFQDYQAVNKPLWVDYQNGAITSLQLQHQRFDSWAERLNVPPGE 81
Cdd:TIGR02252   2 LITFDAVGTLLALKEPVGEVycEIARKYGVEVSpDELEQAFRKAFKAMSEAFPNFGFSSGLTPQQWWQKLVRDTFGRAGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530369125  82 LNDAFMNAMAEI-----CAP-----LPGAVSLLNALQGK-VRMGIITNgFTSLQQTRLERTGLRDHFDLLIISEQVGVAK 150
Cdd:TIGR02252  82 PDPESFEKIFEElysyfATPepwqvYPDAIKLLKDLRERgLILGVISN-FDSRLRGLLEALGLLEYFDFVVTSYEVGAEK 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2530369125 151 PDARIFDYALAQAGNPPrSRVLMVGDTAESDIRGGVNAGL 190
Cdd:TIGR02252 161 PDPKIFQEALERAGISP-EEALHIGDSLRNDYQGARAAGW 199

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530369125  91 AEICAPLPGAVSLLNALQGK-VRMGIITNGFTSLQQTRLERTGLRDHFDLLIISEQVGVAKPDARIFDYALAQAGNPPrS 169
Cdd:cd02616    76 DDLTKEYPGVYETLARLKSQgIKLGVVTTKLRETALKGLKLLGLDKYFDVIVGGDDVTHHKPDPEPVLKALELLGAEP-E 154

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2530369125 170 RVLMVGDTaESDIRGGVNAGLATC---WlNAHQRELPADLEPDWTVTSLSEL 218
Cdd:cd02616   155 EALMVGDS-PHDILAGKNAGVKTVgvtW-GYKGREYLKAFNPDFIIDKMSDL 204

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2530369125 150 KPDARIFDYALAQAGnPPRSRVLMVGDTAESDIRGGVNAGLATCW----LNAHQRELPADLEPDWTVTSLSEL 218
Cdd:COG0647   186 KPSPPIYELALERLG-VDPERVLMVGDRLDTDILGANAAGLDTLLvltgVTTAEDLEAAPIRPDYVLDSLAEL 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 2530369125 100 AVSLLNALQGK-VRMGIITNGFTSLQQTRLERTGLRDHFDLLIISEQVGVAKPDARIFDYALAQAGNPPrSRVLMVGDTa 178
Cdd:cd01427    12 AVELLKRLRAAgIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDP-EEVLFVGDS- 89

                          90
                  ....*....|....*..
gi 2530369125 179 ESDIRGGVNAGLATCWL 195
Cdd:cd01427    90 ENDIEAARAAGGRTVAV 106

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 2530369125  84 DAFMNAMAEICAPLPGAVSLLNALQGK-VRMGIITNGFTSLQQTRLERTGLRDHFDLLIISEQVGVAKPDARIFDYALAQ 162
Cdd:cd07512    75 DHYEADPPGLTRPYPGVIEALERLRAAgWRLAICTNKPEAPARALLSALGLADLFAAVVGGDTLPQRKPDPAPLRAAIRR 154

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2530369125 163 AGNPPrSRVLMVGDTaESDIRGGVNAGLATCWLNAHQRELP-ADLEPDWTVTSLSELEQLL 222
Cdd:cd07512   155 LGGDV-SRALMVGDS-ETDAATARAAGVPFVLVTFGYRHAPvAELPHDAVFSDFDALPDLL 213

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 2530369125  98 PGAVSLLNAL-QGKVRMGIITNGFTSLQQTRLERTGLRDHFDLLIISEQVGVAKPDARIFDYALAQAGNPPrSRVLMVGD 176
Cdd:cd16417    90 PGVKEGLAALkAQGYPLACVTNKPERFVAPLLEALGISDYFSLVLGGDSLPEKKPDPAPLLHACEKLGIAP-AQMLMVGD 168

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2530369125 177 TAeSDIRGGVNAGLATCWLN---AHQrELPADLEPDWTVTSLSEL 218
Cdd:cd16417   169 SR-NDILAARAAGCPSVGLTygyNYG-EDIAASGPDAVIDSLAEL 211

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 2530369125 150 KPDARIFDYALAQAGNPPRSRVLMVGDTAESDIRGGVNAGLAT 192
Cdd:cd07525   183 KPHPPIYDLALARLGRPAKARILAVGDGLHTDILGANAAGLDS 225

pyrophosphatase PpaX; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530369125  92 EICAPLPGAVSLLNALQGK-VRMGIITngfTSLQQTR---LERTGLRDHFDLLIISEQVGVAKPDARIFDYALAQAGNPP 167
Cdd:PRK13288   79 ELVTEYETVYETLKTLKKQgYKLGIVT---TKMRDTVemgLKLTGLDEFFDVVITLDDVEHAKPDPEPVLKALELLGAKP 155

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2530369125 168 rSRVLMVGDTAEsDIRGGVNAGLATC---WlNAHQRELPADLEPDWTVTSLSEL 218
Cdd:PRK13288  156 -EEALMVGDNHH-DILAGKNAGTKTAgvaW-TIKGREYLEQYKPDFMLDKMSDL 206

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 2530369125  64 QHQRFDSWAERLNVPPGELndafmnAMAEICAPLPGAVSLLNALQG-KVRMGIITNGFTS-LQQTRLERTGLRDHFDLLI 141
Cdd:cd07505    16 LHRQAWQLLERKNALLLEL------IASEGLKLKPGVVELLDALKAaGIPVAVATSSSRRnVELLLLELGLLRGYFDVIV 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2530369125 142 ISEQVGVAKPDARIFDYALAQAGNPPrSRVLMVGDtAESDIRGGVNAGLAT 192
Cdd:cd07505    90 SGDDVERGKPAPDIYLLAAERLGVDP-ERCLVFED-SLAGIEAAKAAGMTV 138

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 2530369125  87 MNAMAEICAPLPGAVSLLNALQG-KVRMGIITNGFTSLQQTRLERTGLRdHFDLLIISEQVGVAKPDARIFDYALAQAGN 165
Cdd:cd07527    69 PESYPEGVIAIPGAVDLLASLPAaGDRWAIVTSGTRALAEARLEAAGLP-HPEVLVTADDVKNGKPDPEPYLLGAKLLGL 147

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2530369125 166 PPRSRVlmVGDTAESDIRGGVNAGLATCWLNAhqRELPADLEPDWTVTSLSELEQL 221
Cdd:cd07527   148 DPSDCV--VFEDAPAGIKAGKAAGARVVAVNT--SHDLEQLEAAGADLVVEDLSDI 199

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530369125 104 LNALQGKVRMGIITNGftslqQTRLERTGLRDHFDLLIISEQVGVAKPDARIFDYAlAQAGNPPRSRVLMVGDTAESDIR 183
Cdd:PRK10748  122 LKQLAKKWPLVAITNG-----NAQPELFGLGDYFEFVLRAGPHGRSKPFSDMYHLA-AEKLNVPIGEILHVGDDLTTDVA 195

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2530369125 184 GGVNAGLATCWLNAHQREL----PADLEPDWTVTSLSELEQLL 222
Cdd:PRK10748  196 GAIRCGMQACWINPENGDLmqtwDSRLLPHIEISRLASLTSLI 238

UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase and Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase; Escherichia coli UmpH/NagD is a ribonucleoside tri-, di-, and monophosphatase with a preference for purines, it shows peak activity with UMP and functions in UMP-degradation. It is also an effective phosphatase with AMP, GMP and CMP. Mycobacterium tuberculosis phosphatase, Rv1692 is a glycerol 3-phosphate phosphatase. Rv1692 is the final enzyme involved in glycerophospholipid recycling/catabolism. 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2530369125 148 VAKPDARIFDYALAQAGnPPRSRVLMVGDTAESDIRGGVNAGLATCWL--NAHQRELPADLE--PDWTVTSLSE 217
Cdd:cd07530   175 IGKPEPIMMRAALEKLG-LKSEETLMVGDRLDTDIAAGIAAGIDTLLVltGVTTREDLAKPPyrPTYIVPSLRE 247

beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); Lactococcus lactis beta-PGM catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate as an intermediate. In the forward G6P-forming direction, this reaction links polysaccharide phosphorolysis to glycolysis, in the reverse direction, the reaction provides G1P for the biosynthesis of exo-polysaccharides. This subfamily belongs to the beta-phosphoglucomutase-like family whose other members include Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530369125  97 LPGAVSLLNALQGKVrmgiITNGFTSLQ---QTRLERTGLRDHFDLLIISEQVGVAKPDARIFDYALAQAGNPPrSRVLM 173
Cdd:cd02598    51 LPGIASLLVDLKAKG----IKIALASASknaPKILEKLGLAEYFDAIVDGAVLAKGKPDPDIFLAAAEGLGLNP-KDCIG 125

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2530369125 174 VGDtAESDIRGGVNAGLATCWLNAHQRELPAD 205
Cdd:cd02598   126 VED-AQAGIRAIKAAGFLVVGVGREEDLLGAD 156

phosphoglycolate phosphatase

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2530369125 148 VAKPDARIFDYaLAQAGNPPRSRVLMVGDTAESDIRGGVNAGLATC 193
Cdd:PLN02645  228 VGKPSTFMMDY-LANKFGIEKSQICMVGDRLDTDILFGQNGGCKTL 272

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 2530369125   4 DWIFFDADETLFTFDS--FSGLQRMFLDYSVTFTAEDFQDYQAVNKPLWVDYqNGAITSLQLQHQrfdswaerlnVPPGE 81
Cdd:TIGR01993   1 DVWFFDLDNTLYPHSAgiFLQIDRNITEFVAARLKLSPEEARVLRKDYYKEY-GTTLAGLMILHE----------IDADE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530369125  82 LNDAFMNAMA-EICAPLPGAVSLLNALQGkvRMGIITNGFTSLQQTRLERTGLRDHFDLLIISEQVG---VAKPDARIFD 157
Cdd:TIGR01993  70 YLRYVHGRLPyDKLKPDPELRNLLLRLPG--RKIIFTNGDRAHARRALRRLGIEDCFDGIFCFDTANpdlLPKPSPQAYE 147