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 490522783   4 AIVTDIEGTTTDIRFVHNVLFPYARERLERFIRS-GEQREPVNLLLNELRGEIHAPAASVDQLIETLFKFMDEDRKSPAL 82
Cdd:cd01629    1 AILLDIEGTTTPISFVKDVLFPYARERLPDFLAEhWEDPEVKEDVLAAAAEAEGEAEASIEAVVANLLDWMDEDRKATPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522783  83 KSIQGYIWREGYVNGDFTGHLYPDVVPALRRWSAQDIDIYIYSSGSVPAQKLLFSHSDEGDVTELLSGFFDTHVGAKRQV 162
Cdd:cd01629   81 KALQGLIWREGYESGELKGHLYPDVVPALRRWHAAGLRLYIYSSGSVAAQKLLFGHSDAGDLTPLFSGYFDTTIGPKREA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 490522783 163 SSYRNISMKTGVPVHQMLFLSDIREELDAAREAGWKTVQLIR 204
Cdd:cd01629  161 ASYRKIAEAIGVPPAEILFLSDVVAELDAAKEAGLQTVLLVR 202

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 490522783    2 IRAIVTDIEGTTTDIRFVHNVLFPYARERLERFIRSGEQREPVNLLLNELRGEIHAPAASVDQLIETLFKFMD---EDRK 78
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVEtleAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522783   79 SPALKSIQGYIWREGyvngdfTGHLYPDVVPALRRWSAQDIDIYIYSSGSVPAQKLLFSHSDEGDVTELLSGFFDTHVGa 158
Cdd:pfam00702  81 TVVLVELLGVIALAD------ELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVG- 153

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 490522783  159 KRQVSSYRNISMKTGVPVHQMLFLSDIREELDAAREAG 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 490522783   4 AIVTDIEGTTTDIRFVHNVLFPYARERLERFIRS-GEQREPVNLLLNELRGEIHAPAASVDQLIETLFKFMDEDRKSPAL 82
Cdd:cd01629    1 AILLDIEGTTTPISFVKDVLFPYARERLPDFLAEhWEDPEVKEDVLAAAAEAEGEAEASIEAVVANLLDWMDEDRKATPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522783  83 KSIQGYIWREGYVNGDFTGHLYPDVVPALRRWSAQDIDIYIYSSGSVPAQKLLFSHSDEGDVTELLSGFFDTHVGAKRQV 162
Cdd:cd01629   81 KALQGLIWREGYESGELKGHLYPDVVPALRRWHAAGLRLYIYSSGSVAAQKLLFGHSDAGDLTPLFSGYFDTTIGPKREA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 490522783 163 SSYRNISMKTGVPVHQMLFLSDIREELDAAREAGWKTVQLIR 204
Cdd:cd01629  161 ASYRKIAEAIGVPPAEILFLSDVVAELDAAKEAGLQTVLLVR 202

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 490522783    4 AIVTDIEGTTTDIRFVHNVLFPYARERLERFIRSGEQrepvnllLNELRGeihapaasvdqLIETLFKfmdeDRKSPALK 83
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFGLDPASFKA-------LKQAGG-----------LAEEEWY----RIATSALE 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522783   84 SIQGYIWREGyvngdFTGHLY-PDVVPALRRWSAQDIDIYIYSSGSVPAQKLLFSHSDEGDVTELLSGffDTHVGAKRQV 162
Cdd:TIGR01549  59 ELQGRFWSEY-----DAEEAYiRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILV--SDEPGSKPEP 131

                         170       180       190
                  ....*....|....*....|....*....|....
gi 490522783  163 SSYRNISMKTGVPVHqMLFLSDIREELDAAREAG 196
Cdd:TIGR01549 132 EIFLAALESLGVPPE-VLHVGDNLNDIEGARNAG 164

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 490522783    2 IRAIVTDIEGTTTDIRFVHNVLFPYARERLERFIRSGEQREPVNLLLNELRGEIHAPAASVDQLIETLFKFMD---EDRK 78
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVEtleAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522783   79 SPALKSIQGYIWREGyvngdfTGHLYPDVVPALRRWSAQDIDIYIYSSGSVPAQKLLFSHSDEGDVTELLSGFFDTHVGa 158
Cdd:pfam00702  81 TVVLVELLGVIALAD------ELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVG- 153

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 490522783  159 KRQVSSYRNISMKTGVPVHQMLFLSDIREELDAAREAG 196
Cdd:pfam00702 154 KPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191

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 490522783   2 IRAIVTDIEGtttdirfvhnVLFPYARER-LERFIRSGeqREPVNLLLNELRGEIHAPAASVDQLieTLFKFMDEDRKSP 80
Cdd:cd02603    1 IRAVLFDFGG----------VLIDPDPAAaVARFEALT--GEPSEFVLDTEGLAGAFLELERGRI--TEEEFWEELREEL 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522783  81 ALKSIQGYIWREGYVNGDFtghlYPDVVPALRRWSAQDIDIYIYSSGSVPAQKLLFSHSDEgdvtelLSGFFD-----TH 155
Cdd:cd02603   67 GRPLSAELFEELVLAAVDP----NPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLPR------RGDLFDgvvesCR 136

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490522783 156 VG-AKRQVSSYRNISMKTGVPVHQMLFLSDIREELDAAREAGWKTVQLIRGE 206
Cdd:cd02603  137 LGvRKPDPEIYQLALERLGVKPEEVLFIDDREENVEAARALGIHAILVTDAE 188

MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.

                          10
                  ....*....|....
gi 490522783    3 RAIVTDIEGTTTDI 16
Cdd:pfam12631 119 RAIVTDIPGTTRDV 132