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 446793467    4 DWIFFDADETLFTFDSFTG--LQRMFLDYSVTFTAEDFQDYQAVNKPLWVDYQNGVITSLQLQHGRFESWAERLNVE--P 79
Cdd:TIGR02254   2 KTLLFDLDDTILDFQAAEAlaLRLLFEDQGIPLTEDMFAQYKEINQGLWRAYEEGKITKDEVVNTRFSALLKEYNTEadE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446793467   80 GKLNEAFINAMAEICTPLPGAVSLLNAIRGNAKIGIITNGFSALQQVRLERTGLRDYFDLLVISEEVGVAKPNKKIFDYA 159
Cdd:TIGR02254  82 ALLNQKYLRFLEEGHQLLPGAFELMENLQQKFRLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDKEIFNYA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446793467  160 LEQAGNPDRSRVLMVGDTAESDILGGINAGLATCWLNAHHREQPEGIAPTWTVSSLHELEQLL 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 446793467  95 TPLPGAVSLLNAIRGNAKIGIITNGFSALQQVRLERTGLRDYFDLLVISEEVGVAKPNKKIFDYALEQAGNPdRSRVLMV 174
Cdd:cd04305    9 TLLPGAKELLEELKKGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVK-PEETLMV 87

                         90       100
                 ....*....|....*....|..
gi 446793467 175 GDTAESDILGGINAGLATCWLN 196
Cdd:cd04305   88 GDSLESDILGAKNAGIKTVWFN 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 446793467    4 DWIFFDADETLFTFDSFTG--LQRMFLDYSVTFTAEDFQDYQAVNKPLWVDYQNGVITSLQLQHGRFESWAERLNVE--P 79
Cdd:TIGR02254   2 KTLLFDLDDTILDFQAAEAlaLRLLFEDQGIPLTEDMFAQYKEINQGLWRAYEEGKITKDEVVNTRFSALLKEYNTEadE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446793467   80 GKLNEAFINAMAEICTPLPGAVSLLNAIRGNAKIGIITNGFSALQQVRLERTGLRDYFDLLVISEEVGVAKPNKKIFDYA 159
Cdd:TIGR02254  82 ALLNQKYLRFLEEGHQLLPGAFELMENLQQKFRLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDKEIFNYA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446793467  160 LEQAGNPDRSRVLMVGDTAESDILGGINAGLATCWLNAHHREQPEGIAPTWTVSSLHELEQLL 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 446793467  95 TPLPGAVSLLNAIRGNAKIGIITNGFSALQQVRLERTGLRDYFDLLVISEEVGVAKPNKKIFDYALEQAGNPdRSRVLMV 174
Cdd:cd04305    9 TLLPGAKELLEELKKGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVK-PEETLMV 87

                         90       100
                 ....*....|....*....|..
gi 446793467 175 GDTAESDILGGINAGLATCWLN 196
Cdd:cd04305   88 GDSLESDILGAKNAGIKTVWFN 109

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446793467  84 EAFINAMAEICTPLPGAVSLLNAIRG-NAKIGIITNGFSALQQVRLERTGLRDYFDLLVISEEVGVAKPNKKIFDYALEQ 162
Cdd:COG0546   73 ELYEEELLDETRLFPGVRELLEALKArGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALER 152

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446793467 163 AGNpDRSRVLMVGDTaESDILGGINAGLATCWLN--AHHREQPEGIAPTWTVSSLHELEQLL 222
Cdd:COG0546  153 LGL-DPEEVLMVGDS-PHDIEAARAAGVPFIGVTwgYGSAEELEAAGADYVIDSLAELLALL 212

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446793467   6 IFFDADETLFtfDS----FTGLQRMFLDYSVTFTAEDFQDYQAVNKPLWVDYqngvitsLQLQHGRFESWAERLNvepgK 81
Cdd:COG0637    5 VIFDMDGTLV--DSeplhARAWREAFAELGIDLTEEEYRRLMGRSREDILRY-------LLEEYGLDLPEEELAA----R 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446793467  82 LNEAFINAMA-EICTPLPGAVSLLNAIRGNA-KIGIITNGFSALQQVRLERTGLRDYFDLLVISEEVGVAKPNKKIFDYA 159
Cdd:COG0637   72 KEELYRELLAeEGLPLIPGVVELLEALKEAGiKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLA 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446793467 160 LEQAG-NPdrSRVLMVGDtAESDILGGINAGLATCWLNAHHREQPEGIAPTWTVSSLHEL 218
Cdd:COG0637  152 AERLGvDP--EECVVFED-SPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208

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 446793467 112 KIGIITNGFSALQQVrLERTGLRDYFDLLVISEEVGVAKPNKKIFDYALEQAGNPDrSRVLMVGDTAESDILGGINAGLA 191
Cdd:cd16415   25 KLAVVSNFDRRLREL-LEALGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSP-EEALHVGDDLKNDYLGARAVGWH 102

                         90
                 ....*....|....*...
gi 446793467 192 TCWLnahHREQPEGIAPT 209
Cdd:cd16415  103 ALLV---DREGALHELPS 117

Haloacid dehalogenase-like hydrolase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446793467   73 ERLNVEPGKLNEAFINAMA-EICTPLPGAVSLLNAIR-GNAKIGIITNGFSALQQVRLERTGLRDYFDLLVISEEVGVAK 150
Cdd:pfam13419  56 EDEEEKIEFYLRKYNEELHdKLVKPYPGIKELLEELKeQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKK 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 446793467  151 PNKKIFDYALEQAGNpDRSRVLMVGDTaESDILGGINAGLATCW 194
Cdd:pfam13419 136 PDPDPILKALEQLGL-KPEEVIYVGDS-PRDIEAAKNAGIKVIA 177

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 446793467   56 GVITSLQLQHGRFESWAERLNVEPGKLNEAFINAMAEicTPLPGAVSLLNAIRG-NAKIGIITNGfSALQQVRLERTGLR 134
Cdd:TIGR01509  43 LALRRFKAQYGRTISPEDAQLLYKQLFYEQIEEEAKL--KPLPGVRALLEALRArGKKLALLTNS-PRAHKLVLALLGLR 119

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446793467  135 DYFDLLVISEEVGVAKPNKKIFDYALEQAGNPDrSRVLMVGDtAESDILGGINAGLATCWL 195
Cdd:TIGR01509 120 DLFDVVIDSSDVGLGKPDPDIYLQALKALGLEP-SECVFVDD-SPAGIEAAKAAGMHTVGV 178

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 446793467 100 AVSLLNAIRG-NAKIGIITNGFSALQQVRLERTGLRDYFDLLVISEEVGVAKPNKKIFDYALEQAGnPDRSRVLMVGDTa 178
Cdd:cd01427   12 AVELLKRLRAaGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLG-VDPEEVLFVGDS- 89

                         90
                 ....*....|....*..
gi 446793467 179 ESDILGGINAGLATCWL 195
Cdd:cd01427   90 ENDIEAARAAGGRTVAV 106

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 446793467   5 WIFFDADETLFTFDSFTGLQRMFLDysvTFTAEDFQDYQAVNKPLWVDYQNGVITSLQLqhgrfesWAE-RLNVEPGKLN 83
Cdd:cd02603    3 AVLFDFGGVLIDPDPAAAVARFEAL---TGEPSEFVLDTEGLAGAFLELERGRITEEEF-------WEElREELGRPLSA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446793467  84 EAFINAMAEICTPLPGAVSLLNAIRG-NAKIGIITNGFSALQQVRLERTGLR-DYFDLLVISEEVGVAKPNKKIFDYALE 161
Cdd:cd02603   73 ELFEELVLAAVDPNPEMLDLLEALRAkGYKVYLLSNTWPDHFKFQLELLPRRgDLFDGVVESCRLGVRKPDPEIYQLALE 152

                        170       180       190
                 ....*....|....*....|....*....|..
gi 446793467 162 QAG-NPDrsRVLMVGDTAESdILGGINAGLAT 192
Cdd:cd02603  153 RLGvKPE--EVLFIDDREEN-VEAARALGIHA 181

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446793467    6 IFFDADETLFTFDSFTG-LQRMFLDYSVTFTAEDFQ---DYQAVNKPL--WVDYQngvitslQLQHGRFESWAERLNVEP 79
Cdd:TIGR01428   4 LVFDVYGTLFDVHSVAErAAELYGGRGEALSQLWRQkqlEYSWLRTLMgpYKDFW-------DLTREALRYLLGRLGLED 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446793467   80 GK-LNEAFINAMAEIcTPLPGAVSLLNAIR-GNAKIGIITNGFSALQQVRLERTGLRDYFDLLVISEEVGVAKPNKKIFD 157
Cdd:TIGR01428  77 DEsAADRLAEAYLRL-PPHPDVPAGLRALKeRGYRLAILSNGSPAMLKSLVKHAGLDDPFDAVLSADAVRAYKPAPQVYQ 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 446793467  158 YALEQAGNPdRSRVLMVgdtAES--DILGGINAGLATCWLN 196
Cdd:TIGR01428 156 LALEALGVP-PDEVLFV---ASNpwDLGGAKKFGFKTAWIN 192

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 446793467  82 LNEAFIN----AMAEICTPLPGAVSLLNAIRG-NAKIGIITNGFSALQQVRLERTGLRDYFDLLVISEEVGVAKPNKKIF 156
Cdd:cd07512   69 LLARFLDhyeaDPPGLTRPYPGVIEALERLRAaGWRLAICTNKPEAPARALLSALGLADLFAAVVGGDTLPQRKPDPAPL 148

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446793467 157 DYALEQAGNpDRSRVLMVGDTaESDILGGINAGL 190
Cdd:cd07512  149 RAAIRRLGG-DVSRALMVGDS-ETDAATARAAGV 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
                 ....*....|....*....|....*....|....*....|...
gi 446793467 150 KPNKKIFDYALEQAGNPDRSRVLMVGDTAESDILGGINAGLAT 192
Cdd:cd07525  183 KPHPPIYDLALARLGRPAKARILAVGDGLHTDILGANAAGLDS 225

pyrophosphatase PpaX; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446793467  92 EICTPLPGAVSLLNAI-RGNAKIGIITNGFSALQQVRLERTGLRDYFDLLVISEEVGVAKPNKKIFDYALEQAGNpDRSR 170
Cdd:PRK13288  79 ELVTEYETVYETLKTLkKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPDPEPVLKALELLGA-KPEE 157

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446793467 171 VLMVGDTAEsDILGGINAGLATCwlnahhreqpeGIAptWTVSSLHELEQL 221
Cdd:PRK13288 158 ALMVGDNHH-DILAGKNAGTKTA-----------GVA--WTIKGREYLEQY 194

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 446793467  95 TPLPGAVSLLNAIR-GNAKIGIITNGFSALQQVRLERTGLRDYFDLLVISEEVGVAKPNKKIFDYALEQAG-NPdrSRVL 172
Cdd:cd16417   87 HLYPGVKEGLAALKaQGYPLACVTNKPERFVAPLLEALGISDYFSLVLGGDSLPEKKPDPAPLLHACEKLGiAP--AQML 164

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446793467 173 MVGDTAeSDILGGINAGLATCWL----NahHREQPEGIAPTWTVSSLHEL 218
Cdd:cd16417  165 MVGDSR-NDILAARAAGCPSVGLtygyN--YGEDIAASGPDAVIDSLAEL 211

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446793467 116 ITNGfsalqQVRLERTGLRDYFDLLVISEEVGVAKPNKKIFDYALEQAGNPDRsRVLMVGDTAESDILGGINAGLATCWL 195
Cdd:PRK10748 134 ITNG-----NAQPELFGLGDYFEFVLRAGPHGRSKPFSDMYHLAAEKLNVPIG-EILHVGDDLTTDVAGAIRCGMQACWI 207

                 .
gi 446793467 196 N 196
Cdd:PRK10748 208 N 208

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 446793467  55 NGVITSLQLQHGRFESWAERLNVEPGKLneafinAMAEICTPLPGAVSLLNAIRGN-AKIGIITNGF-SALQQVRLERTG 132
Cdd:cd07505    7 DGVLIDTEPLHRQAWQLLERKNALLLEL------IASEGLKLKPGVVELLDALKAAgIPVAVATSSSrRNVELLLLELGL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446793467 133 LRDYFDLLVISEEVGVAKPNKKIFDYALEQAG-NPDRSRVLmvgdtaEsDILGGINAGLA---TCW 194
Cdd:cd07505   81 LRGYFDVIVSGDDVERGKPAPDIYLLAAERLGvDPERCLVF------E-DSLAGIEAAKAagmTVV 139

Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; Degradation of the ubiquitous natural phosphonate 2-aminoethylphosphonate (AEP) into useable forms of nitrogen, carbon, and phosphorus is a two-step metabolic pathway. The first step, catalyzed by AEP transaminase, involves the transfer of NH3 from AEP to pyruvate, yielding phosphonoacetaldehyde (P-Ald) and alanine. In the second step, phosphonatase catalyzes the hydrolytic P-C bond cleavage of P-Ald to form orthophosphate and acetaldehyde. 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 446793467  69 ESWAERLNVEPGK-----LNEAF----INAMAEICTPLPGAVSLLNAIRGNA-KIGIITNGFSALQQVRLERTGLRDYF- 137
Cdd:cd02586   63 EAWRAVFGRLPTEadvdaLYEEFepilIASLAEYSSPIPGVLEVIAKLRARGiKIGSTTGYTREMMDIVLPEAAAQGYRp 142

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446793467 138 DLLVISEEVGVAKPNKKIFDYALEQAGNPDRSRVLMVGDTAeSDILGGINAGLAT 192
Cdd:cd02586  143 DSLVTPDDVPAGRPYPWMCYKNAIELGVYDVAAVVKVGDTV-PDIKEGLNAGMWT 196

beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446793467    6 IFFDADETLFTFDS--FTGLQRMFLDYSVTFTAEdfqdyqavnkplWVDYQNGVitslqlqhGRFESWAERLNVEPGKLN 83
Cdd:TIGR02009   4 VIFDMDGVITDTAPlhAQAWKHIAAKYGISFDKQ------------YNESLKGL--------SREDILRAILKLRGDGLS 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446793467   84 EAFINAMAE-------------ICTPLPGAVSLLNAIRgNAKIGIITNGFSALQQVRLERTGLRDYFDLLVISEEVGVAK 150
Cdd:TIGR02009  64 LEEIHQLAErknelyrellrltGVAVLPGIRNLLKRLK-AKGIAVGLGSSSKNAPRILAKLGLRDYFDAIVDASEVKNGK 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 446793467  151 PNKKIFDYALEQAG-NPDRSRVLmvgdtaeSDILGGINAGLAT 192
Cdd:TIGR02009 143 PHPETFLLAAELLGvPPNECIVF-------EDALAGVQAARAA 178

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446793467  95 TPL-PGAVSLLNAI-RGNAKIGIIT-NGFSALQQVrLERTGLRDYFDLLVISEEvGVAKPNKKIFDYALEQAGnPDRSRV 171
Cdd:cd07533   83 EPLfPGVREALDALaAQGVLLAVATgKSRRGLDRV-LEQHGLGGYFDATRTADD-TPSKPHPEMLREILAELG-VDPSRA 159

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446793467 172 LMVGDTAeSDILGGINAG---LATCWlNAHHREQPEGIAPTWTVSSLHEL 218
Cdd:cd07533  160 VMVGDTA-YDMQMAANAGahaVGVAW-GYHSLEDLRSAGADAVVDHFSEL 207

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 446793467  61 LQLQHGR--FESWAErlnVEPGKLNEAFINA--------MAEICTPLPGAVSLLNAIRGN-AKIGIITNGFSALQQVRLE 129
Cdd:cd07527   36 LKVSHGRraIDVIRK---LAPDDADIELVLAleteepesYPEGVIAIPGAVDLLASLPAAgDRWAIVTSGTRALAEARLE 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446793467 130 RTGLRDYfDLLVISEEVGVAKPNKKIFDYALEQAGNPDRSRVlmVGDTAESDILGGINAGLATCWLNA-HHREQPEGIAP 208
Cdd:cd07527  113 AAGLPHP-EVLVTADDVKNGKPDPEPYLLGAKLLGLDPSDCV--VFEDAPAGIKAGKAAGARVVAVNTsHDLEQLEAAGA 189

                 ....*..
gi 446793467 209 TWTVSSL 215
Cdd:cd07527  190 DLVVEDL 196