?-D-glucose-1-phosphatase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548985859   1 MLYIFDLGNVIVDIDFNRVLGAWSDLTRIPLASLKKSFHMGEAFHQHERGEISDEAFAEALCHEMALPLSYEQFSHGWQA 80
Cdd:PRK09456    1 MLYIFDLGNVIVDIDFNRVLGVWSDLSRVPLATLKKRFTMGEAFHQHERGEISDEAFAEALCHEMALSLSYEQFAHGWQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548985859  81 VFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTSFWPEEYPEIRDAADHIYLSQDLGMRKPEARIYQHVLQAEGFSPSD 160
Cdd:PRK09456   81 VFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTTFWPEEYPEVRAAADHIYLSQDLGMRKPEARIYQHVLQAEGFSAAD 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1548985859 161 TVFFDDNADNIEGANQLGITSILVKDKTTIPDYFAKVLC 199
Cdd:PRK09456  161 AVFFDDNADNIEAANALGITSILVTDKQTIPDYFAKVLC 199

?-D-glucose-1-phosphatase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548985859   1 MLYIFDLGNVIVDIDFNRVLGAWSDLTRIPLASLKKSFHMGEAFHQHERGEISDEAFAEALCHEMALPLSYEQFSHGWQA 80
Cdd:PRK09456    1 MLYIFDLGNVIVDIDFNRVLGVWSDLSRVPLATLKKRFTMGEAFHQHERGEISDEAFAEALCHEMALSLSYEQFAHGWQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548985859  81 VFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTSFWPEEYPEIRDAADHIYLSQDLGMRKPEARIYQHVLQAEGFSPSD 160
Cdd:PRK09456   81 VFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTTFWPEEYPEVRAAADHIYLSQDLGMRKPEARIYQHVLQAEGFSAAD 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1548985859 161 TVFFDDNADNIEGANQLGITSILVKDKTTIPDYFAKVLC 199
Cdd:PRK09456  161 AVFFDDNADNIEAANALGITSILVTDKQTIPDYFAKVLC 199

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 1548985859   4 IFDLGNVIVDIDF-NRVLGAWSDLTRIPLASLKKSF-HMGEAFHQHER---GEISDEAFAEALCHEMalplsYEQFSHGW 78
Cdd:TIGR01509   3 LFDLDGVLVDTEFaIAKLINREELGLVPDELGVSAVgRLELALRRFKAqygRTISPEDAQLLYKQLF-----YEQIEEEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548985859  79 QAvfvALRPEVIAIMHKLREQGHRVVVLSNTNRLHTSFwpEEYPEIRDAADHIYLSQDLGMRKPEARIYQHVLQAEGFSP 158
Cdd:TIGR01509  78 KL---KPLPGVRALLEALRARGKKLALLTNSPRAHKLV--LALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLEP 152

                         170       180
                  ....*....|....*....|....*.
gi 1548985859 159 SDTVFFDDNADNIEGANQLGITSILV 184
Cdd:TIGR01509 153 SECVFVDDSPAGIEAAKAAGMHTVGV 178

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 1548985859   2 LYIFDLGNVIVDIDFnRVLGAWSDLT----------------RIPLASLKKSFHMGEAfhQHERGEISDEAFAEALCHEM 65
Cdd:pfam00702   3 AVVFDLDGTLTDGEP-VVTEAIAELAsehplakaivaaaedlPIPVEDFTARLLLGKR--DWLEELDILRGLVETLEAEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548985859  66 ALPLSYEQFSHGWQAVFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTSFWPEEYpEIRDAADHIYLSQDLGMRKPEAR 145
Cdd:pfam00702  80 LTVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLL-GLDDYFDVVISGDDVGVGKPKPE 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1548985859 146 IYQHVLQAEGFSPSDTVFFDDNADNIEGANQLG 178
Cdd:pfam00702 159 IYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191

?-D-glucose-1-phosphatase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548985859   1 MLYIFDLGNVIVDIDFNRVLGAWSDLTRIPLASLKKSFHMGEAFHQHERGEISDEAFAEALCHEMALPLSYEQFSHGWQA 80
Cdd:PRK09456    1 MLYIFDLGNVIVDIDFNRVLGVWSDLSRVPLATLKKRFTMGEAFHQHERGEISDEAFAEALCHEMALSLSYEQFAHGWQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548985859  81 VFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTSFWPEEYPEIRDAADHIYLSQDLGMRKPEARIYQHVLQAEGFSPSD 160
Cdd:PRK09456   81 VFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTTFWPEEYPEVRAAADHIYLSQDLGMRKPEARIYQHVLQAEGFSAAD 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1548985859 161 TVFFDDNADNIEGANQLGITSILVKDKTTIPDYFAKVLC 199
Cdd:PRK09456  161 AVFFDDNADNIEAANALGITSILVTDKQTIPDYFAKVLC 199

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 1548985859   4 IFDLGNVIVDIDF-NRVLGAWSDLTRIPLASLKKSF-HMGEAFHQHER---GEISDEAFAEALCHEMalplsYEQFSHGW 78
Cdd:TIGR01509   3 LFDLDGVLVDTEFaIAKLINREELGLVPDELGVSAVgRLELALRRFKAqygRTISPEDAQLLYKQLF-----YEQIEEEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548985859  79 QAvfvALRPEVIAIMHKLREQGHRVVVLSNTNRLHTSFwpEEYPEIRDAADHIYLSQDLGMRKPEARIYQHVLQAEGFSP 158
Cdd:TIGR01509  78 KL---KPLPGVRALLEALRARGKKLALLTNSPRAHKLV--LALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLEP 152

                         170       180
                  ....*....|....*....|....*.
gi 1548985859 159 SDTVFFDDNADNIEGANQLGITSILV 184
Cdd:TIGR01509 153 SECVFVDDSPAGIEAAKAAGMHTVGV 178

epoxide hydrolase N-terminal domain-like phosphatase; This model represents a small clade of sequences including C. elegans and mammalian sequences as well as a small number of bacteria. In eukaryotes, this domain exists as an N-terminal fusion to the soluble epoxide hydrolase enzyme and has recently been shown to be an active phosphatase, although the nature of the biological substrate is unclear. These appear to be members of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases by general homology and the conservation of all of the recognized catalytic motifs (although the first motif is unusual in the replacement of the more common aspartate with glycine...). The variable domain is found in between motifs 1 and 2, indicating membership in subfamily I and phylogeny and prediction of the alpha helical nature of the variable domain (by PSI-PRED) indicate membership in subfamily IA.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548985859   4 IFDLGNVIVDIDFnrVLGAWSDLTRIPLAS--LKKSFHMGEAFHQH----ERGEISDEAFAEALCHEMALPLSYE----Q 73
Cdd:TIGR02247   6 IFDFGGVLLPSPG--VMRRWETERGLPGLKdfIVTVNITGPDFNPWartfERGELTAEAFDGLFRHEYGLRLGHDvriaP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548985859  74 FSHGWQAVFVALRPEVIAIMHKLREQGHRVVVLsnTNRLHTSFWPEEY---PEIRDAADHIYLSQDLGMRKPEARIYQHV 150
Cdd:TIGR02247  84 VFPLLYGENTKLRPSMMAAIKTLRAKGFKTACI--TNNFPTDHSAEEAllpGDIMALFDAVVESCLEGLRKPDPRIYQLM 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1548985859 151 LQAEGFSPSDTVFFDDNADNIEGANQLGITSILVKDKTTIPDYFAKVL 198
Cdd:TIGR02247 162 LERLGVAPEECVFLDDLGSNLKPAAALGITTIKVSDEEQAIHDLEKAT 209

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 1548985859  89 VIAIMHKLREQGHRVVVLSNTNRLHTSFWPEEYpEIRDAADHIYLSQDLGMRKPEARIYQHVLQAEGFSPSDTVFFDDNA 168
Cdd:cd01427    12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKL-GLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSE 90

                          90
                  ....*....|....*.
gi 1548985859 169 DNIEGANQLGITSILV 184
Cdd:cd01427    91 NDIEAARAAGGRTVAV 106

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 1548985859  47 HERGEISDEAFAEALCHEMalplsyeqfsHGWQAvFvalrPEVIAIMHKLREQGHRVVVLSNTNRlHTSFWPEEYPEIRD 126
Cdd:cd02588    69 AELGLELDESDLDELGDAY----------LRLPP-F----PDVVAGLRRLREAGYRLAILSNGSP-DLIEDVVANAGLRD 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1548985859 127 AADHIYLSQDLGMRKPEARIYQHVLQAEGFSPSDTVFFDDNADNIEGANQLGITSILVKDKTTIPDY 193
Cdd:cd02588   133 LFDAVLSAEDVRAYKPAPAVYELAAERLGVPPDEILHVASHAWDLAGARALGLRTAWINRPGEVPDP 199

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 1548985859   2 LYIFDLGNVIVDIDFNrvlgawsdltrIPLAslkksfhMGEAFHQHERGEISDEAF------AEALCHEMALPLSYEQFS 75
Cdd:TIGR01549   1 AILFDIDGTLVDIKFA-----------IRRA-------FPQTFEEFGLDPASFKALkqagglAEEEWYRIATSALEELQG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548985859  76 HGWQAVFV--ALRPEVIAIMHKLREQGHRVVVLSNTNRLHTSFWpEEYPEIRDAADHIYLSQDLGmRKPEARIYQHVLQA 153
Cdd:TIGR01549  63 RFWSEYDAeeAYIRGAADLLARLKSAGIKLGIISNGSLRAQKLL-LRLFGLGDYFELILVSDEPG-SKPEPEIFLAALES 140

                         170       180
                  ....*....|....*....|....*
gi 1548985859 154 EGFSPsDTVFFDDNADNIEGANQLG 178
Cdd:TIGR01549 141 LGVPP-EVLHVGDNLNDIEGARNAG 164

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548985859   4 IFDLGNVIVDidFNRV-LGAWSDLtripLASLkkSFHMGEAFHQHERGeISDEAFAEALCHEMALPLSYEQFSHGWQAVF 82
Cdd:COG0637     6 IFDMDGTLVD--SEPLhARAWREA----FAEL--GIDLTEEEYRRLMG-RSREDILRYLLEEYGLDLPEEELAARKEELY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548985859  83 --------VALRPEVIAIMHKLREQGHRVVVLSNTNR-----LHTSFwpeeypEIRDAADHIYLSQDLGMRKPEARIYQH 149
Cdd:COG0637    77 rellaeegLPLIPGVVELLEALKEAGIKIAVATSSPRenaeaVLEAA------GLLDYFDVIVTGDDVARGKPDPDIYLL 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1548985859 150 VLQAEGFSPSDTVFFDDNADNIEGANQLGITSILVKDKTTIPDYFAKV 197
Cdd:COG0637   151 AAERLGVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGA 198

beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; This family represents the beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. Family members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. It belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548985859  69 LSYEQFSHGWQAVFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTSFWPEEYPEIRDAADHIYLSQDLGMRKPEARIYQ 148
Cdd:cd07505    26 RKNALLLELIASEGLKLKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLRGYFDVIVSGDDVERGKPAPDIYL 105

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1548985859 149 HVLQAEGFSPSDTVFFDDNADNIEGANQLGITSILVKD 186
Cdd:cd07505   106 LAAERLGVDPERCLVFEDSLAGIEAAKAAGMTVVAVPD 143

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 1548985859  85 LRPEVIAIMHKLREQGHRVVVLSNTNRLHTSFWPEEYPEIRDA--------ADHIYLSQdlGMRKPEARIYQHVL-QAEG 155
Cdd:TIGR01662  26 LYPEVPDALAELKEAGYKVVIVTNQSGIGRGYFSRSFSGRVARrleelgvpIDILYACP--GCRKPKPGMFLEALkRFNE 103

                          90       100       110
                  ....*....|....*....|....*....|
gi 1548985859 156 FSPSDTVFFDDNADN-IEGANQLGITSILV 184
Cdd:TIGR01662 104 IDPEESVYVGDQDLTdLQAAKRVGLATILV 133

subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides xylulose-1,5-bisphosphate phosphatase CbbY; This family includes Rhodobacter sphaeroides and Arabidopsis thaliana xylulose-1,5-bisphosphate phosphatase CbbY which convert xylulose-1,5-bisphosphate (a potent inhibitor of Ribulose-1,5-bisphosphate carboxylase/oxygenase, Rubisco), to the non-inhibitory compound xylulose-5-phosphate. 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 1548985859  83 VALRPEVIAIMHKLREQGHRVVVLSNTNRLHTS-----FWPEEYPEIRDAadhIYLSQDLGMRKPEARIYQHVLQAEGFS 157
Cdd:cd07528    94 LPLRPGVARLIDEAKAAGVRLAIATTTSPANVDallsaLLGPERRAIFDA---IAAGDDVAEKKPDPDIYLLALERLGVS 170

                          90       100
                  ....*....|....*....|....*.
gi 1548985859 158 PSDTVFFDDNADNIEGANQLGITSIL 183
Cdd:cd07528   171 PSDCLAIEDSAIGLQAAKAAGLPCIV 196

eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to Bacillus cereus phosphonoacetaldehyde hydrolase and Streptomyces FkbH; This family includes eukaryotic magnesium-dependent phosphatase-1 (MDP-1) which is most likely a phosphotyrosine phosphatase catalyzing the dephosphorylation of tyrosine-phosphorylated proteins, Bacillus cereus phosphonoacetaldehyde hydrolase (phosphonatase)which catalyzes the hydrolysis of phosphonoacetaldehyde to acetaldehyde and phosphate using Mg(II) as cofactor, and sequences annotated as FkbH including BafAIV an FkbH-like protein from Streptomyces griseus encoded in ORF12 of the bafilomycin synthesis gene cluster. 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 1548985859  83 VALRPEVIAIMHKLREQGHRVVVLSNTN-------RLHTSFWPE--EYPEI--RDAADHIylsqdlgmrkpeariyQHVL 151
Cdd:cd07501    33 VSLYPDAQEILKELKERGILLAVASRNNefdhaneVLEKLDLKElfDAFEIypGSKSSHF----------------RKIA 96

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1548985859 152 QAEGFSPSDTVFFDDNADNIEGANQLGITSILV 184
Cdd:cd07501    97 KELGIGFDSMVFFDDEPRNREEVSEGGVTCILV 129

HAD-hyrolase-like;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1548985859 139 MRKPEARIYQHVLQAEGFSPSDTVFF-DDNADNIEGANQLGITSILVK 185
Cdd:pfam13242   2 CGKPNPGMLERALARLGLDPERTVMIgDRLDTDILGAREAGARTILVL 49

GMP/IMP nucleotidase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1548985859  83 VALRPEVIAIMHKLREQGHRVVVLSNTNRlHTSFWPEEYPEIRDAADHIYLSQDLGMRKPEARIYQHVLQAEGFSPSDTV 162
Cdd:PRK14988   92 AVLREDTVPFLEALKASGKRRILLTNAHP-HNLAVKLEHTGLDAHLDLLLSTHTFGYPKEDQRLWQAVAEHTGLKAERTL 170

                          90
                  ....*....|....*..
gi 1548985859 163 FFDDNADNIEGANQLGI 179
Cdd:PRK14988  171 FIDDSEPILDAAAQFGI 187

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 1548985859  87 PEVIAIMHKLREQGHRVVVLSNTNrlhTSFWPE--EYPEIRDAADHIYLSQDLGMRKPEARIYQHVLQAEGFSPSDTVFF 164
Cdd:cd04302    84 PGIPELLEKLKAAGYRLYVATSKP---EVFARRilEHFGLDEYFDGIAGASLDGSRVHKADVIRYALDTLGIAPEQAVMI 160

                          90       100
                  ....*....|....*....|
gi 1548985859 165 DDNADNIEGANQLGITSILV 184
Cdd:cd04302   161 GDRKHDIIGARANGIDSIGV 180