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 1388116063   6 LFDLDQTLLNFHASEYIGLKKIIESNGQTFTDELYQYFKKRNKELWMEYEKENITKNQLFETRFRLLFEKCNVDTsnmDL 85
Cdd:TIGR02254   5 LFDLDDTILDFQAAEALALRLLFEDQGIPLTEDMFAQYKEINQGLWRAYEEGKITKDEVVNTRFSALLKEYNTEA---DE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388116063  86 LKINGEFIKIMSQNGVLMKGALEFLKKLRNDIpnsKIIIITNGAKLNAEGRIESTGLNAYYDDIFISEVIGVNKPSIEFF 165
Cdd:TIGR02254  82 ALLNQKYLRFLEEGHQLLPGAFELMENLQQKF---RLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDKEIF 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388116063 166 NIVLNAINEP-KESCIVIGDSLTSDMLGAKNAGLTSCWFIPeeanDIDKNMKEYDINYKASSFDELYDVL 234
Cdd:TIGR02254 159 NYALERMPKFsKEEVLMIGDSLTADIKGGQNAGLDTCWMNP----DMHPNPDDIIPTYEIRSLEELYEIL 224

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 1388116063   6 LFDLDQTLLNFHASEYIGLKKIIESNGQTFTDELYQYFKKRNKELWMEYEKENITKNQLFETRFRLLFEKCNVDTsnmDL 85
Cdd:TIGR02254   5 LFDLDDTILDFQAAEALALRLLFEDQGIPLTEDMFAQYKEINQGLWRAYEEGKITKDEVVNTRFSALLKEYNTEA---DE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388116063  86 LKINGEFIKIMSQNGVLMKGALEFLKKLRNDIpnsKIIIITNGAKLNAEGRIESTGLNAYYDDIFISEVIGVNKPSIEFF 165
Cdd:TIGR02254  82 ALLNQKYLRFLEEGHQLLPGAFELMENLQQKF---RLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDKEIF 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388116063 166 NIVLNAINEP-KESCIVIGDSLTSDMLGAKNAGLTSCWFIPeeanDIDKNMKEYDINYKASSFDELYDVL 234
Cdd:TIGR02254 159 NYALERMPKFsKEEVLMIGDSLTADIKGGQNAGLDTCWMNP----DMHPNPDDIIPTYEIRSLEELYEIL 224

dUMP phosphatase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388116063   6 LFDLDQTLLNFHAseYIGLKKIIESNGQTFTDELYQYFKKRNKELWMEYEKENITKNQLFETRFRLLFEKCNVDTsnmdl 85
Cdd:PRK09449    7 LFDADETLFHFDA--FAGLQRMFSRYGVDFTAEDFQDYQAVNKPLWVDYQNGAITALQLQHTRFESWAEKLNVTP----- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388116063  86 LKINGEFIKIMSQNGVLMKGALEFLKKLRNDIpnsKIIIITNG-AKLNAEgRIESTGLNAYYDDIFISEVIGVNKPSIEF 164
Cdd:PRK09449   80 GELNSAFLNAMAEICTPLPGAVELLNALRGKV---KMGIITNGfTELQQV-RLERTGLRDYFDLLVISEQVGVAKPDVAI 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388116063 165 FNIVLNAINEP-KESCIVIGDSLTSDMLGAKNAGLTSCWFipeeanDIDKNMKEYDIN--YKASSFDELYDVLKK 236
Cdd:PRK09449  156 FDYALEQMGNPdRSRVLMVGDNLHSDILGGINAGIDTCWL------NAHGREQPEGIAptYQVSSLSELEQLLCK 224

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 1388116063   5 FLFDLDQTLLNFH----------ASEYIGLKKIIE-SNGQTFTDELYQYFKKRNKELWMEYEKENITKNQLFETRFRLLF 73
Cdd:pfam00702   4 VVFDLDGTLTDGEpvvteaiaelASEHPLAKAIVAaAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGLTVV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388116063  74 ekcnvdtsnmdLLKINGEFIkiMSQNGVLMKGALEFLKKLRNdiPNSKIIIITNGAKLNAEGRIESTGLNAYYDDIFISE 153
Cdd:pfam00702  84 -----------LVELLGVIA--LADELKLYPGAAEALKALKE--RGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGD 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1388116063 154 VIGVNKPSIEFFNIVLNAINEPKESCIVIGDSLTsDMLGAKNAG 197
Cdd:pfam00702 149 DVGVGKPKPEIYLAALERLGVKPEEVLMVGDGVN-DIPAAKAAG 191

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 1388116063   6 LFDLDQTLLNFHASEYIGLKKIIESNGQTFTDELYQYFKKRNKELWMEYEKENITKNQLFETRFRLLFEKCNVDTsnmDL 85
Cdd:TIGR02254   5 LFDLDDTILDFQAAEALALRLLFEDQGIPLTEDMFAQYKEINQGLWRAYEEGKITKDEVVNTRFSALLKEYNTEA---DE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388116063  86 LKINGEFIKIMSQNGVLMKGALEFLKKLRNDIpnsKIIIITNGAKLNAEGRIESTGLNAYYDDIFISEVIGVNKPSIEFF 165
Cdd:TIGR02254  82 ALLNQKYLRFLEEGHQLLPGAFELMENLQQKF---RLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAGIQKPDKEIF 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388116063 166 NIVLNAINEP-KESCIVIGDSLTSDMLGAKNAGLTSCWFIPeeanDIDKNMKEYDINYKASSFDELYDVL 234
Cdd:TIGR02254 159 NYALERMPKFsKEEVLMIGDSLTADIKGGQNAGLDTCWMNP----DMHPNPDDIIPTYEIRSLEELYEIL 224

dUMP phosphatase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388116063   6 LFDLDQTLLNFHAseYIGLKKIIESNGQTFTDELYQYFKKRNKELWMEYEKENITKNQLFETRFRLLFEKCNVDTsnmdl 85
Cdd:PRK09449    7 LFDADETLFHFDA--FAGLQRMFSRYGVDFTAEDFQDYQAVNKPLWVDYQNGAITALQLQHTRFESWAEKLNVTP----- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388116063  86 LKINGEFIKIMSQNGVLMKGALEFLKKLRNDIpnsKIIIITNG-AKLNAEgRIESTGLNAYYDDIFISEVIGVNKPSIEF 164
Cdd:PRK09449   80 GELNSAFLNAMAEICTPLPGAVELLNALRGKV---KMGIITNGfTELQQV-RLERTGLRDYFDLLVISEQVGVAKPDVAI 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388116063 165 FNIVLNAINEP-KESCIVIGDSLTSDMLGAKNAGLTSCWFipeeanDIDKNMKEYDIN--YKASSFDELYDVLKK 236
Cdd:PRK09449  156 FDYALEQMGNPdRSRVLMVGDNLHSDILGGINAGIDTCWL------NAHGREQPEGIAptYQVSSLSELEQLLCK 224

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388116063   5 FLFDLDQTLLNFHASEYIGLKKIIESNGQTFTDELYQYFK-KRNKELWmeyekenitknqlfetrfRLLFEKCNVDTSNM 83
Cdd:COG0637     5 VIFDMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMgRSREDIL------------------RYLLEEYGLDLPEE 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388116063  84 DLLK-INGEFIKIMSQNGV-LMKGALEFLKKLR-NDIPnskIIIITNGAKLNAEGRIESTGLNAYYDDIFISEVIGVNKP 160
Cdd:COG0637    67 ELAArKEELYRELLAEEGLpLIPGVVELLEALKeAGIK---IAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKP 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388116063 161 SIEFFNIVLNAINEPKESCIVIGDSLTsDMLGAKNAGLTsCWFIPEEAnDIDKNMKEYDinYKASSFDEL 230
Cdd:COG0637   144 DPDIYLLAAERLGVDPEECVVFEDSPA-GIRAAKAAGMR-VVGVPDGG-TAEEELAGAD--LVVDDLAEL 208

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 1388116063   5 FLFDLDQTLLNfhaSEYIGLKKIIESNGQTFTDELYQYFKKRNKELWMEYEKENITKNQlfETRFRLLFEKcnvdtsNMD 84
Cdd:TIGR01509   2 ILFDLDGVLVD---TEFAIAKLINREELGLVPDELGVSAVGRLELALRRFKAQYGRTIS--PEDAQLLYKQ------LFY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388116063  85 LLKINGEFIKIMsqngvlmKGALEFLKKLRndIPNSKIIIITNGAKlNAEGRIESTGLNAYYDDIFISEVIGVNKPSIEF 164
Cdd:TIGR01509  71 EQIEEEAKLKPL-------PGVRALLEALR--ARGKKLALLTNSPR-AHKLVLALLGLRDLFDVVIDSSDVGLGKPDPDI 140

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1388116063 165 FNIVLNAINEPKESCIVIGDSLtSDMLGAKNAGLTSCW 202
Cdd:TIGR01509 141 YLQALKALGLEPSECVFVDDSP-AGIEAAKAAGMHTVG 177

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 1388116063 106 ALEFLKKLRNDipNSKIIIITN-GAKLnaEGRIESTGLNAYYDDIFISEVIGVNKPSIEFFNIVLNAINEPKESCIVIGD 184
Cdd:cd16415    12 AVETLKDLKEK--GLKLAVVSNfDRRL--RELLEALGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPEEALHVGD 87

                          90       100
                  ....*....|....*....|....
gi 1388116063 185 SLTSDMLGAKNAGLTSCWFIPEEA 208
Cdd:cd16415    88 DLKNDYLGARAVGWHALLVDREGA 111

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 1388116063 100 GVLMkgALEFLKKLRNDipNSKIIIITNGAKLNAEGRIESTGLNAYYDDIFISEVIGVNKPSIEFFNIVLNAINEPKESC 179
Cdd:cd01427     8 GTLL--AVELLKRLRAA--GIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEV 83

                          90       100
                  ....*....|....*....|....
gi 1388116063 180 IVIGDSLTsDMLGAKNAGLTSCWF 203
Cdd:cd01427    84 LFVGDSEN-DIEAARAAGGRTVAV 106

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

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1388116063 153 EVIGvnKPSIEFFNIVLNAINEPKESCIVIGDSLTSDMLGAKNAGLTSCW 202
Cdd:COG0647   182 LVVG--KPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLL 229

Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural subclass of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The classes 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. Class I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Class II consists of sequences in which the capping domain is found between the second and third motifs. Class III sequences have no capping domain in iether of these positions. The Class IIA capping domain is predicted by PSI-PRED to consist of a mixed alpha-beta fold with the basic pattern: Helix-Helix-Helix-Sheet-Helix-Loop-Sheet-Helix-Sheet-Helix. Presently, this subfamily encompasses a single equivalog model (TIGR01452) for the eukaryotic phosphoglycolate phosphatase, as well as four hypothetical equivalogs covering closely related sequences (TIGR01456 and TIGR01458 in eukaryotes, TIGR01457 in gram positive bacteria and TIGR01459 in gram negative bacteria). The Escherishia coli NagD gene and the Bacillus subtilus AraL gene are members of this subfamily but are not members of the any of the presently defined equivalogs within it. NagD is part of the NAG operon responsible for N-acetylglucosamine metabolism. The function of this gene is unknown. Genes from several organisms have been annotated as NagD, or NagD-like. However, without data on the presence of other members of this pathway, (such as in the case of Yersinia pestis) these assignments should not be given great weight. The AraL gene is similar: it is part of the L-arabinose operon, but the function is unknown. A gene from Halobacterium has been annotated as AraL, but no other Ara operon genes have been annotated. Many of the genes in this subfamily have been annotated as "pNPPase" "4-nitrophenyl phosphatase" or "NPPase". These all refer to the same activity versus a common lab test compound used to determine phosphatase activity. There is no evidence that this activity is physiologically relevant. [Unknown function, Enzymes of unknown specificity]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388116063 114 RNDIPnskiIIITNGAKLNAEG----RIESTGLNAYYDDIFISEVIGVNKPSIEFFNIVLN-AINEPKESCIVIGDSLTS 188
Cdd:TIGR01460 143 EGDVP----FIAANRDDLVRLGdgrfRPGAGAIAAGIKELSGREPTVVGKPSPAIYRAALNlLQARPERRDVMVGDNLRT 218

                          90
                  ....*....|....
gi 1388116063 189 DMLGAKNAGLTSCW 202
Cdd:TIGR01460 219 DILGAKNAGFDTLL 232

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388116063 110 LKKLRNDipNSKIIIITNGAKLNAEGRIESTGLNAYYDDIFISEVIGVNKPSIEFFNIVLNAINEPKESCIVIGDSlTSD 189
Cdd:cd02588   100 LRRLREA--GYRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAEDVRAYKPAPAVYELAAERLGVPPDEILHVASH-AWD 176

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1388116063 190 MLGAKNAGLTSCWfIPEEANDIDKNMKEYDInyKASSFDELYD 232
Cdd:cd02588   177 LAGARALGLRTAW-INRPGEVPDPLGPAPDF--VVPDLGELAD 216

inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP); LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1388116063 153 EVIGvnKPSIEFFNIVLNAINEPKESCIVIGDSLTSDMLGAKNAGLTS 200
Cdd:cd07509   168 TVVG--KPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRG 213

Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the uncharacterized protein Bacillus subtilis YqeG; 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 1388116063 107 LEFLKKLRNDipNSKIIIITNGAKLNAEGRIESTGLNayyddiFISeviGVNKPSIEFFNIVLNAINEPKESCIVIGDSL 186
Cdd:cd16416    23 KAWLADLKEA--GIKVVLVSNNNERRVAKVIEKLDLP------FVA---RAGKPRPRAFRRALKEMDLPPEQVAMVGDQL 91

                          90
                  ....*....|....
gi 1388116063 187 TSDMLGAKNAGLTS 200
Cdd:cd16416    92 FTDILGGNRAGLYT 105

HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins is a member of the IIIA subfamily of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of this subfamily (TIGR01662) and most characterized members of the HAD superfamily are phosphatases. HAD superfamily phosphatases contain active site residues in several conserved catalytic motifs, all of which are found conserved here. This family consists of sequences from fungi, plants, cyanobacteria, gram-positive bacteria and Deinococcus. There is presently no characterization of any sequence in this family.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388116063 121 KIIIITNGAKlnaEGRI----ESTGLNAYYddifiseviGVNKPSIEFFNIVLNAINEPKESCIVIGDSLTSDMLGAKNA 196
Cdd:TIGR01668  61 KLLIVSNNAG---EQRAkaveKALGIPVLP---------HAVKPPGCAFRRAHPEMGLTSEQVAVVGDRLFTDVMGGNRN 128

                  ....*....
gi 1388116063 197 GLTSCWFIP 205
Cdd:TIGR01668 129 GSYTILVEP 137

Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388116063 106 ALEFLKKLRN-DIpnsKIIIITNgaklNAEGRI----ESTGLNAYYddifiseviGVNKPSIEFFNIVLNAINEPKESCI 180
Cdd:COG2179    49 VIEWLEELKEaGF---KVCIVSN----NSEKRVkrfaEKLGIPYIA---------RAKKPLPRGFRKALKLMGLPPEETA 112

                          90       100
                  ....*....|....*....|
gi 1388116063 181 VIGDSLTSDMLGAKNAGLTS 200
Cdd:COG2179   113 VVGDQLFTDVLGGNRAGLYT 132

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388116063  87 KINGEFIKIMSQNGVL--MKGALEFLKKLR-NDIpnsKIIIITNGAKLNAEGRIESTGLNAYYDDIFISEVIGVNKPSIE 163
Cdd:cd16423    28 RRNELIKRQFSEKTDLppIEGVKELLEFLKeKGI---KLAVASSSPRRWIEPHLERLGLLDYFEVIVTGDDVEKSKPDPD 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1388116063 164 FFNIVLNAINEPKESCIVIGDSlTSDMLGAKNAGLTsCWFIPEEAND 210
Cdd:cd16423   105 LYLEAAERLGVNPEECVVIEDS-RNGVLAAKAAGMK-CVGVPNPVTG 149

UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar phosphatase; Bacillus subtilis AraL is a phosphatase displaying activity towards different sugar phosphate substrates; it is encoded by the arabinose metabolic operon araABDLMNPQ-abfA and may play a role in the dephosphorylation of substrates related to l-arabinose metabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388116063 153 EVIgVNKPSIEFFNIVLNAINEPKESCIVIGDSLTSDMLGAKNAGLTSCWFIPEEANDIDKNMKEYDINYKASSFDEL 230
Cdd:cd07531   175 EVV-VGKPSEVMAREALDILGLDAKDCAIVGDQIDVDIAMGKAIGMETALVLTGVTTRENLDRHGYKPDYVLNSIKDL 251

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 1388116063 154 VIGvnKPSIEFFNIVLNAINEPKESCIVIGDSLTSDMLGAKNAGLTS 200
Cdd:cd07510   201 VVG--KPSRFMFDCISSKFSIDPARTCMVGDRLDTDILFGQNCGLKT 245

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 1388116063 106 ALEFLKKLRNDIpnSKIIIITNGAKLNAEGRIESTGLNAYYDDIFISEVIGVNKPSIEFFNIVLNAINEPKEScIVIGDS 185
Cdd:TIGR01428  97 VPAGLRALKERG--YRLAILSNGSPAMLKSLVKHAGLDDPFDAVLSADAVRAYKPAPQVYQLALEALGVPPDE-VLFVAS 173

                          90
                  ....*....|....*..
gi 1388116063 186 LTSDMLGAKNAGLTSCW 202
Cdd:TIGR01428 174 NPWDLGGAKKFGFKTAW 190

HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of the IIA subfamily (TIGR01460) of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. One sequence (GP|10716807) has been annotated as a "phospholysine phosphohistidine inorganic pyrophosphatase," probably in reference to studies on similarly described (but unsequenced) enzymes from bovine and rat tissues. However, the supporting information for this annotation has never been published. [Unknown function, Enzymes of unknown specificity]

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1388116063 153 EVIGVNKPSIEFFNIVLNAINEPKESCIVIGDSLTSDMLGAKNAGL 198
Cdd:TIGR01458 173 KATVVGKPSKTFFLEALRATGCEPEEAVMIGDDCRDDVGGAQDCGM 218

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 1388116063 110 LKKLRNDIPNSKIIIiTNGAKLNAEGRIESTGLNAYYDDIF-ISEVIGVNKPSIEFFNIVLNAINEPKESCIVIGDSLtS 188
Cdd:cd02604    88 LRNLLLALPGRKIIF-TNASKNHAIRVLKRLGLADLFDGIFdIEYAGPDPKPHPAAFEKAIREAGLDPKRAAFFDDSI-R 165

                          90
                  ....*....|....
gi 1388116063 189 DMLGAKNAGLTSCW 202
Cdd:cd02604   166 NLLAAKALGMKTVL 179