Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino acid transport and metabolism]; Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily is part of the Pathway/BioSystem: Histidine biosynthesis

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518666937   1 MKLLILDRDGVINIDSDaYIKSVEEWIPLPGAIEAIAQLSKAGWTVAIATNQSGIARGYYDVATLDAMHARLRELVAQQG 80
Cdd:COG0241    3 KKAVFLDRDGTINEDVG-YVKSPEEFEFLPGVLEALARLNEAGYRLVVVTNQSGIGRGLFTEEDLNAVHAKMLELLAAEG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518666937  81 GEVGLIVYCPHGPDEGCACRKPKPGMLQTIAAHYGADLTQCWFVGDSLGDLQAAQTVDSQPVLVKTGKGLLTLAKELPvn 160
Cdd:COG0241   82 GRIDAIYYCPHHPDDNCDCRKPKPGMLLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGCKGILVLTGKGAEELAEALP-- 159

                        170
                 ....*....|....*
gi 518666937 161 TLIFDDLAAVAAELI 175
Cdd:COG0241  160 DTVADDLAEAVDYLL 174

histidinol-phosphate phosphatase family domain; This domain is found in authentic histidinol-phosphate phosphatases which are sometimes found as stand-alone entities and sometimes as fusions with imidazoleglycerol-phosphate dehydratase (TIGR01261). Additionally, a family of proteins including YaeD from E. coli (TIGR00213) and various other proteins are closely related but may not have the same substrate specificity. This domain is a member of the haloacid-dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. This superfamily is distinguished by the presence of three motifs: an N-terminal motif containing the nucleophilic aspartate, a central motif containing an conserved serine or threonine, and a C-terminal motif containing a conserved lysine (or arginine) and conserved aspartates. More specifically, the domian modelled here is a member of subfamily III of the HAD-superfamily by virtue of lacking a "capping" domain in either of the two common positions, between motifs 1 and 2, or between motifs 2 and 3.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518666937    2 KLLILDRDGVINIDSDA-YIKSVEEWIPLPGAIEAIAQLSKAGWTVAIATNQSGIARGYYDVATLDAMHARLRELVAQQG 80
Cdd:TIGR01656   1 PALFLDRDGVINEDTVSdYPRSLDDWQLRPGAVPALLTLRAAGYTVVVVTNQSGIGRGYFSAEAFRAPNGRLLELLRQLG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518666937   81 GEVGLIVYCPHGPDEGCACRKPKPGMLQTIAAHYGADLTQCWFVGDSLGDLQAAQTVDSQPVLVKTG 147
Cdd:TIGR01656  81 VAVDGVLFCPHHPADNCSCRKPKPGLILEALKRLGVDASRSLVVGDRLRDLQAARNAGAAAGLLVSG 147

Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino acid transport and metabolism]; Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily is part of the Pathway/BioSystem: Histidine biosynthesis

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518666937   1 MKLLILDRDGVINIDSDaYIKSVEEWIPLPGAIEAIAQLSKAGWTVAIATNQSGIARGYYDVATLDAMHARLRELVAQQG 80
Cdd:COG0241    3 KKAVFLDRDGTINEDVG-YVKSPEEFEFLPGVLEALARLNEAGYRLVVVTNQSGIGRGLFTEEDLNAVHAKMLELLAAEG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518666937  81 GEVGLIVYCPHGPDEGCACRKPKPGMLQTIAAHYGADLTQCWFVGDSLGDLQAAQTVDSQPVLVKTGKGLLTLAKELPvn 160
Cdd:COG0241   82 GRIDAIYYCPHHPDDNCDCRKPKPGMLLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGCKGILVLTGKGAEELAEALP-- 159

                        170
                 ....*....|....*
gi 518666937 161 TLIFDDLAAVAAELI 175
Cdd:COG0241  160 DTVADDLAEAVDYLL 174

histidinol-phosphate phosphatase family domain; This domain is found in authentic histidinol-phosphate phosphatases which are sometimes found as stand-alone entities and sometimes as fusions with imidazoleglycerol-phosphate dehydratase (TIGR01261). Additionally, a family of proteins including YaeD from E. coli (TIGR00213) and various other proteins are closely related but may not have the same substrate specificity. This domain is a member of the haloacid-dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. This superfamily is distinguished by the presence of three motifs: an N-terminal motif containing the nucleophilic aspartate, a central motif containing an conserved serine or threonine, and a C-terminal motif containing a conserved lysine (or arginine) and conserved aspartates. More specifically, the domian modelled here is a member of subfamily III of the HAD-superfamily by virtue of lacking a "capping" domain in either of the two common positions, between motifs 1 and 2, or between motifs 2 and 3.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518666937    2 KLLILDRDGVINIDSDA-YIKSVEEWIPLPGAIEAIAQLSKAGWTVAIATNQSGIARGYYDVATLDAMHARLRELVAQQG 80
Cdd:TIGR01656   1 PALFLDRDGVINEDTVSdYPRSLDDWQLRPGAVPALLTLRAAGYTVVVVTNQSGIGRGYFSAEAFRAPNGRLLELLRQLG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518666937   81 GEVGLIVYCPHGPDEGCACRKPKPGMLQTIAAHYGADLTQCWFVGDSLGDLQAAQTVDSQPVLVKTG 147
Cdd:TIGR01656  81 VAVDGVLFCPHHPADNCSCRKPKPGLILEALKRLGVDASRSLVVGDRLRDLQAARNAGAAAGLLVSG 147

HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme. [Unknown function, Enzymes of unknown specificity]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518666937    2 KLLILDRDGVINIDSDaYIKSVEEWIPLPGAIEAIAQLSKAGWTVAIATNQSGIARGYYDvatlDAMHARLRELVAQQGG 81
Cdd:TIGR01662   1 KAVVLDLDGTLTDDVP-YVSDEDERILYPEVPDALAELKEAGYKVVIVTNQSGIGRGYFS----RSFSGRVARRLEELGV 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518666937   82 EVGLIVYCPHgpdegcaCRKPKPGMLQTIAAHY-GADLTQCWFVGDSLG-DLQAAQTVDSQPVLV 144
Cdd:TIGR01662  76 PIDILYACPG-------CRKPKPGMFLEALKRFnEIDPEESVYVGDQDLtDLQAAKRVGLATILV 133

histidinol-phosphatase; This model describes histidinol phosphatase. All known examples in the scope of this model are bifunctional proteins with a histidinol phosphatase domain followed by an imidazoleglycerol-phosphate dehydratase domain. These enzymatic domains catalyze the ninth and seventh steps, respectively, of histidine biosynthesis. [Amino acid biosynthesis, Histidine family]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518666937    2 KLLILDRDGVInID---SDAYIKSVEEWIPLPGAIEAIAQLSKAGWTVAIATNQSGIARGYYDVATLDAMHARLRELVAQ 78
Cdd:TIGR01261   2 KILFIDRDGTL-IEeppSDFQVDALEKLRFEKGVIPALLKLKKAGYKFVMVTNQDGLGTPSFPQADFDGPHNLMLQIFRS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 518666937   79 QGGEVGLIVYCPHGPDEGCACRKPKPGMLQTIAAHYGADLTQCWFVGDSLGDLQAAQ 135
Cdd:TIGR01261  81 QGIIFDDVLICPHFPDDNCDCRKPKIKLLEPYLKKNLIDKARSYVIGDRETDMQLAE 137

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518666937  28 PLPGAIEAIAQLSKAGWTVAIATNqsgiargyydvatldAMHARLRELVAQqggeVGLIVYCPH--GPDEGCAcRKPKPG 105
Cdd:COG0546   85 LFPGVRELLEALKARGIKLAVVTN---------------KPREFAERLLEA----LGLDDYFDAivGGDDVPP-AKPKPE 144

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518666937 106 MLQTIAAHYGADLTQCWFVGDSLGDLQAAQTVDSQPVLVKTGKGLLT-LAKELPvnTLIFDDLAAVAAEL 174
Cdd:COG0546  145 PLLEALERLGLDPEEVLMVGDSPHDIEAARAAGVPFIGVTWGYGSAEeLEAAGA--DYVIDSLAELLALL 212

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518666937  17 DAYIKSVEEWIPL-PGAIEAIAQLSKAGWTVAIATNqsgiarGYYDVATLDAMHARLRELVAqqggevGLIVYCPHGpde 95
Cdd:COG1011   82 EAFLAALPELVEPyPDALELLEALKARGYRLALLTN------GSAELQEAKLRRLGLDDLFD------AVVSSEEVG--- 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518666937  96 gcaCRKPKPGMLQTIAAHYGADLTQCWFVGDSL-GDLQAAQTVDSQPVLVkTGKGLLTLAKELPvnTLIFDDLAAVAAEL 174
Cdd:COG1011  147 ---VRKPDPEIFELALERLGVPPEEALFVGDSPeTDVAGARAAGMRTVWV-NRSGEPAPAEPRP--DYVISDLAELLELL 220

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 518666937  32 AIEAIAQLSKAGWTVAIATNQSgiargyydvatLDAMHARLRELVAQQGGEVGLIVycphgpdEGCACRKPKPGMLQTIA 111
Cdd:cd01427   12 AVELLKRLRAAGIKLAIVTNRS-----------REALRALLEKLGLGDLFDGIIGS-------DGGGTPKPKPKPLLLLL 73

                         90       100       110
                 ....*....|....*....|....*....|...
gi 518666937 112 AHYGADLTQCWFVGDSLGDLQAAQTVDSQPVLV 144
Cdd:cd01427   74 LKLGVDPEEVLFVGDSENDIEAARAAGGRTVAV 106

Polynucleotide kinase 3 phosphatase; Polynucleotide kinase 3 phosphatases play a role in the repair of single breaks in DNA induced by DNA-damaging agents such as gamma radiation and camptothecin.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518666937   30 PGAIEAIAQLSKAGWTVAIATNQSGIARGyyDVATLDAMHARLRELVAQQGGEvgLIVYCPHGPDEgcaCRKPKPGMLQT 109
Cdd:pfam08645  32 PSVPEKLKKLHEDGYKIVIFTNQGGIGRK--GKKSLEKFKNKIEAILKKLGVP--LQVYAATKKDI---YRKPNTGMWDE 104

                          90       100
                  ....*....|....*....|....
gi 518666937  110 IAAHYGA----DLTQCWFVGDSLG 129
Cdd:pfam08645 105 MKKDYNDgveiDLEKSFYVGDAAG 128

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518666937  30 PGAIEAIAQLSKAGWTVAIAtnqSG--------IARGY---YDVATldamharlrELVAQQG---GEV-GLIVYcphgpD 94
Cdd:COG0560   91 PGARELIAEHRAAGHKVAIV---SGgftffvepIAERLgidHVIAN---------ELEVEDGrltGEVvGPIVD-----G 153

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 518666937  95 EGcacrkpKPGMLQTIAAHYGADLTQCWFVGDSLGDLQ 132
Cdd:COG0560  154 EG------KAEALRELAAELGIDLEQSYAYGDSANDLP 185

2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate salvage pathway in higher organisms (photorespiration in plants). Phosphoglycolate results from the oxidase activity of RubisCO in the Calvin cycle when concentrations of carbon dioxide are low relative to oxygen. In Ralstonia (Alcaligenes) eutropha and Rhodobacter sphaeroides, the PGP gene (CbbZ) is located on an operon along with other Calvin cycle enzymes including RubisCO. The only other pertinent experimental evidence concerns the gene from E. coli. The in vitro activity of the Ralstonia and Escherichia enzymes was determined with crude cell extracts of strains containing PGP on expression plasmids and compared to controls. In E. coli, however, there does not appear to be a functional Calvin cycle (RubisCO is absent), although the E. coli PGP gene (gph) is on the same operon (dam) with ribulose-5-phosphate-3-epimerase (rpe), a gene in the pentose-phosphate pathway (along with other, unrelated genes). The E. coli enzyme is not expressed under normal laboratory conditions; the pathway to which it belongs has not been determined. In fact, the possibility exists, although unlikely, that the E. coli enzyme and others within this equivalog have as their physiological substrate another, closely related molecule. The other seed chosen for this model, from Xylella fastidiosa has no experimental evidence, but is a plant pathogen and thus may obtain phosphoglycolate from its host. This model has been restricted to encompass only proteobacteria as no related PGP has been verified outside of this clade. Sequences from Aquifex aeolicus and Treponema pallidum fall between the trusted and noise cutoffs. Just below the noise cutoff is a gene which is part of the operon for the biosynthesis of the blue pigment, indigoidine, from Erwinia (Pectobacterium) chrysanthemi, a plant pathogen. It does not seem likely, considering the proposed biosynthetic mechanism, that the dephosphorylation of phosphoglycolate or a closely related compound is required. Possibly, this gene is fortuitously located in this operon, or has an indirect relationship to the necessity for the biosynthesis of this compound. Sequences from 11 species have been annotated as PGP or putative PGP but fall below the noise cutoff. None of these have experimental validation. This enzyme is a member of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolase enzymes (pfam00702). [Energy metabolism, Sugars]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518666937   28 PLPGAIEAIAQLSKAGWTVAIATNQSgiargyydvatldamharlRELVAQQGGEVGLIVYCPH--GPDEgCACRKPKPG 105
Cdd:TIGR01449  86 VFPGVEATLGALRAKGLRLGLVTNKP-------------------TPLARPLLELLGLAKYFSVliGGDS-LAQRKPHPD 145

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 518666937  106 MLQTIAAHYGADLTQCWFVGDSLGDLQAAQTVDSQPVLVKTG 147
Cdd:TIGR01449 146 PLLLAAERLGVAPQQMVYVGDSRVDIQAARAAGCPSVLLTYG 187

polynucleotide 3'-phosphatase domain similar to the phosphatase domain of the bifunctional enzyme polynucleotide 5'-kinase/3'-phosphatase; Polynucleotide 3'-phosphatase (PNP) domain. This domain dephosphorylates single-stranded as well as double-stranded 3'-phospho termini. It is found in bifunctional enzyme polynucleotide kinase/phosphatase (PNKP) which contain both kinase and phosphatase domains. PNKP plays a key role in both base excision repair and non-homologous end-joining DNA repair pathway. DNA strand breaks can result from DNA damage by ionizing radiation and chemical agents, such as alkylating agents or anticancer agents. Such DNA damage often results in DNA strands with 5'-hydroxyl and 3'-phosphate termini. However, the repair of DNA damage by DNA polymerases and ligases requires 5'-phosphate and 3'-hydroxyl termini. PNKP acts as a 5'-kinase/3'-phosphatase to create 5'-phosphate/3'-hydroxyl termini, which are a necessary prerequisite for ligation during repair. 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 518666937  21 KSVEEW-IPLPGAIEAIAQLSKAGWTVAIATNQSGIARGYydvATLDAMHARLRELVAQQGgeVGLIVYCPHGPDegcAC 99
Cdd:cd01625   22 TNASDWqILYPSVPEKLKALHKDGYKIVIFTNQGGIVRGK---LTPEVFKGKIEAILEKLG--VPIQVYAATKKG---KY 93

                         90       100       110
                 ....*....|....*....|....*....|....
gi 518666937 100 RKPKPGMLQTIAAH----YGADLTQCWFVGDSLG 129
Cdd:cd01625   94 RKPVTGMWDHLKEDlnsgIPINLKDSFYVGDAAG 127

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 518666937   29 LPGAIEAIAQLSKAGWTVAIATNqsgiargyydvATLDAMharlrELVAQQGGEVGLIVYcPHGPDEGCacRKPKPGMLQ 108
Cdd:TIGR01549  75 IRGAADLLARLKSAGIKLGIISN-----------GSLRAQ-----KLLLRLFGLGDYFEL-ILVSDEPG--SKPEPEIFL 135

                          90       100
                  ....*....|....*....|....*..
gi 518666937  109 TIAAHYGADlTQCWFVGDSLGDLQAAQ 135
Cdd:TIGR01549 136 AALESLGVP-PEVLHVGDNLNDIEGAR 161

Haloacid dehalogenase-like hydrolase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518666937   28 PLPGAIEAIAQLSKAGWTVAIATNqsgiarGYYDVATLDAMHARLREL--VAQQGGEVGLivycphgpdegcacRKPKPG 105
Cdd:pfam13419  80 PYPGIKELLEELKEQGYKLGIVTS------KSRENVEEFLKQLGLEDYfdVIVGGDDVEG--------------KKPDPD 139

                          90       100       110
                  ....*....|....*....|....*....|
gi 518666937  106 MLQTIAAHYGADLTQCWFVGDSLGDLQAAQ 135
Cdd:pfam13419 140 PILKALEQLGLKPEEVIYVGDSPRDIEAAK 169

haloacid dehalogenase-like hydrolase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518666937   30 PGAIEAIAQLSKAGWTVAIATnqsgiargyydvATLDAMharLRELVAQQGG--------EVGLIVYCPHGPDEGCACRK 101
Cdd:pfam12710  87 PGALELLAAHRAAGDRVVVVT------------GGLRPL---VEPVLAELGFdevlatelEVDDGRFTGELRLIGPPCAG 151

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 518666937  102 P-KPGMLQ--TIAAHYGADLTQCWFVGDSLGDLQAAQ 135
Cdd:pfam12710 152 EgKVRRLRawLAARGLGLDLADSVAYGDSPSDLPMLR 188