Enolase-phosphatase similar to human enolase-phosphatase E1 and and Xanthomonas oryzae pv. Oryzae enolase-phosphatase Xep; Enolase-phosphatase E1 (also called MASA) is a bifunctional enolase- phosphatase which promotes the conversion of 2,3-diketo-5-methylthio-1-phosphopentane to 1,2-dihydroxy-3-keto-5-methylthiopentene anion (an aci-reductone) in the methionine salvage pathway. The catalytic reaction is carried out continuously by enolization and dephosphorylation, and the enolase activity cannot be classified as typical enzymatic enolization. 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 896198647   4 AIVTDIEGTTSDIRFVHQVLFPYARERLADFVRRHAAESEVASP-LAALRAEIDQPQADLDALIAALYRFMDEDRKSTAL 82
Cdd:cd01629    1 AILLDIEGTTTPISFVKDVLFPYARERLPDFLAEHWEDPEVKEDvLAAAAEAEGEAEASIEAVVANLLDWMDEDRKATPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896198647  83 KALQGIIWRSGYREGDFRGHLYPEVAGQLAAWQRQGVKLYVYSSGSVEAQKLLFGHSDAGDLQPLFSGYFDTHVGAKRET 162
Cdd:cd01629   81 KALQGLIWREGYESGELKGHLYPDVVPALRRWHAAGLRLYIYSSGSVAAQKLLFGHSDAGDLTPLFSGYFDTTIGPKREA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 896198647 163 ASYRNIAQAIGIAPDELLFLSDIHQELDAAQAAGWHTCQLIRD 205
Cdd:cd01629  161 ASYRKIAEAIGVPPAEILFLSDVVAELDAAKEAGLQTVLLVRP 203

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 896198647    2 IRAIVTDIEGTTSDIRFVHQVLFPYARERLADFVRRHAAESEVASPLAALRAEIDQPQADLDA---LIAALYRFMDEDRK 78
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAEDLPIPVEDFTARLLLGKRDWLEeldILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896198647   79 STALKALQGIIWRSGyregdfRGHLYPEVAGQLAAWQRQGVKLYVYSSGSVEAQKLLFGHSDAGDLQPLFSGYFDTHVGa 158
Cdd:pfam00702  81 TVVLVELLGVIALAD------ELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVG- 153

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 896198647  159 KRETASYRNIAQAIGIAPDELLFLSDIHQELDAAQAAG 196
Cdd:pfam00702 154 KPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191

Enolase-phosphatase similar to human enolase-phosphatase E1 and and Xanthomonas oryzae pv. Oryzae enolase-phosphatase Xep; Enolase-phosphatase E1 (also called MASA) is a bifunctional enolase- phosphatase which promotes the conversion of 2,3-diketo-5-methylthio-1-phosphopentane to 1,2-dihydroxy-3-keto-5-methylthiopentene anion (an aci-reductone) in the methionine salvage pathway. The catalytic reaction is carried out continuously by enolization and dephosphorylation, and the enolase activity cannot be classified as typical enzymatic enolization. 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 896198647   4 AIVTDIEGTTSDIRFVHQVLFPYARERLADFVRRHAAESEVASP-LAALRAEIDQPQADLDALIAALYRFMDEDRKSTAL 82
Cdd:cd01629    1 AILLDIEGTTTPISFVKDVLFPYARERLPDFLAEHWEDPEVKEDvLAAAAEAEGEAEASIEAVVANLLDWMDEDRKATPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896198647  83 KALQGIIWRSGYREGDFRGHLYPEVAGQLAAWQRQGVKLYVYSSGSVEAQKLLFGHSDAGDLQPLFSGYFDTHVGAKRET 162
Cdd:cd01629   81 KALQGLIWREGYESGELKGHLYPDVVPALRRWHAAGLRLYIYSSGSVAAQKLLFGHSDAGDLTPLFSGYFDTTIGPKREA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 896198647 163 ASYRNIAQAIGIAPDELLFLSDIHQELDAAQAAGWHTCQLIRD 205
Cdd:cd01629  161 ASYRKIAEAIGVPPAEILFLSDVVAELDAAKEAGLQTVLLVRP 203

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 896198647    4 AIVTDIEGTTSDIRFVHQVLFPYARERladfvrrhaaesevasplaalraeIDQPQADLDALIAA--LYRFMDEDRKSTA 81
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEE------------------------FGLDPASFKALKQAggLAEEEWYRIATSA 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896198647   82 LKALQGIIWrSGYREGDFRGHLYPEVagqLAAWQRQGVKLYVYSSGSVEAQKLLFGHSDAGDLQPLFSGyfDTHVGAKRE 161
Cdd:TIGR01549  57 LEELQGRFW-SEYDAEEAYIRGAADL---LARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILV--SDEPGSKPE 130

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 896198647  162 TASYRNIAQAIGIaPDELLFLSDIHQELDAAQAAG 196
Cdd:TIGR01549 131 PEIFLAALESLGV-PPEVLHVGDNLNDIEGARNAG 164

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 896198647   2 IRAIVTDIEGttsdirfvhqVLFPYARERLadfVRRHAAESEVASPLAALRAEIDQPQADLDALIAALYRFMDEDRKSTA 81
Cdd:cd02603    1 IRAVLFDFGG----------VLIDPDPAAA---VARFEALTGEPSEFVLDTEGLAGAFLELERGRITEEEFWEELREELG 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896198647  82 LKALQGIIWRsgyrEGDFRGHLYPEVAGQLAAWQRQGVKLYVYSSGSVeaqkllFGHSDAGDLQPLFSGYFD-----THV 156
Cdd:cd02603   68 RPLSAELFEE----LVLAAVDPNPEMLDLLEALRAKGYKVYLLSNTWP------DHFKFQLELLPRRGDLFDgvvesCRL 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 896198647 157 G-AKRETASYRNIAQAIGIAPDELLFLSDIHQELDAAQAAGWHT 199
Cdd:cd02603  138 GvRKPDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGIHA 181

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896198647   2 IRAIVTDIEGTTSDirfVHQVLFPYARERLADFVRRHAaesevasPLAALRAEIDQPqadLDALIAALYRFMDEDRKSTA 81
Cdd:COG0546    1 IKLVLFDLDGTLVD---SAPDIAAALNEALAELGLPPL-------DLEELRALIGLG---LRELLRRLLGEDPDEELEEL 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896198647  82 LKAlqgiiWRSGYRE-GDFRGHLYPEVAGQLAAWQRQGVKLYVYSSGSVEAQKLLFGHSdagDLQPLFSGYF--DTHVGA 158
Cdd:COG0546   68 LAR-----FRELYEEeLLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEAL---GLDDYFDAIVggDDVPPA 139

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 896198647 159 KRETASYRNIAQAIGIAPDELLFLSDIHQELDAAQAAGWHTC 200
Cdd:COG0546  140 KPKPEPLLEALERLGLDPEEVLMVGDSPHDIEAARAAGVPFI 181

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 896198647   3 RAIVTDIEGTTSDIRFVHQV---LFPYARERLADFVRRHAAESEVASPLAalRAEIDQPQADLDALIAALYRFMDEDRKS 79
Cdd:cd02588    1 KALVFDVYGTLIDWHSGLAAaerAFPGRGEELSRLWRQKQLEYTWLVTLM--GPYVDFDELTRDALRATAAELGLELDES 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896198647  80 TAlkalqgIIWRSGYRegdfRGHLYPEVAGQLAAWQRQGVKLYVYSSGSVEAQKLLFGHSDAGDlqplfsgYFDTHVGA- 158
Cdd:cd02588   79 DL------DELGDAYL----RLPPFPDVVAGLRRLREAGYRLAILSNGSPDLIEDVVANAGLRD-------LFDAVLSAe 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 896198647 159 -----KRETASYRNIAQAIGIAPDELLFLSDIHQELDAAQAAGWHTC 200
Cdd:cd02588  142 dvrayKPAPAVYELAAERLGVPPDEILHVASHAWDLAGARALGLRTA 188

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 896198647 111 LAAWQRQGVKLYVYSSGSVEAQKLLFGHSDAGDlqpLFSGYF--DTHVGAKRETASYRNIAQAIGIAPDELLFLSDIHQE 188
Cdd:cd01427   16 LKRLRAAGIKLAIVTNRSREALRALLEKLGLGD---LFDGIIgsDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSEND 92

                         90
                 ....*....|..
gi 896198647 189 LDAAQAAGWHTC 200
Cdd:cd01427   93 IEAARAAGGRTV 104

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; 5'-nucleotidases dephosphorylate nucleoside 5'-monophosphates to nucleosides and inorganic phosphate. Purified Pseudomonas aeruginosa PA0065 displayed high activity toward 5'-UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low activity against 5'-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 896198647  44 VASPLAALRaEIDQPQADLDALI-----------AALYRFMDEDrkstALKALQgiIWRSGYRE-GDFRGHLYPEVAGQL 111
Cdd:cd04302   18 TASVQYALE-ELGIPVPDESELRrfigppledsfRELLPFDEEE----AQRAVD--AYREYYKEkGLFENEVYPGIPELL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896198647 112 AAWQRQGVKLYVYSS-GSVEAQKLL--FGhsdagdLQPLFSGYF----DTHVGAKRETASYrnIAQAIGIAPDELLFLSD 184
Cdd:cd04302   91 EKLKAAGYRLYVATSkPEVFARRILehFG------LDEYFDGIAgaslDGSRVHKADVIRY--ALDTLGIAPEQAVMIGD 162

                        170
                 ....*....|..
gi 896198647 185 IHQELDAAQAAG 196
Cdd:cd04302  163 RKHDIIGARANG 174