?-D-glucose-1-phosphatase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A         8 MLYIFDLGNVIVDIDFNRVLGAWSDLTRIPLASLKKSFHMGEAFHQHERGEISDEAFAEALCHEMALPLSYEQFSHGWQA 87
Cdd:PRK09456   1 MLYIFDLGNVIVDIDFNRVLGVWSDLSRVPLATLKKRFTMGEAFHQHERGEISDEAFAEALCHEMALSLSYEQFAHGWQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A        88 VFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTTFWPEEYPEIRDAADHIYLSQDLGMRKPEARIYQHVLQAEGFSPSD 167
Cdd:PRK09456  81 VFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTTFWPEEYPEVRAAADHIYLSQDLGMRKPEARIYQHVLQAEGFSAAD 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
2B0C_A       168 TVFFDDNADNIEGANQLGITSILVKDKTTIPDYFAKVLC 206
Cdd:PRK09456 161 AVFFDDNADNIEAANALGITSILVTDKQTIPDYFAKVLC 199

?-D-glucose-1-phosphatase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A         8 MLYIFDLGNVIVDIDFNRVLGAWSDLTRIPLASLKKSFHMGEAFHQHERGEISDEAFAEALCHEMALPLSYEQFSHGWQA 87
Cdd:PRK09456   1 MLYIFDLGNVIVDIDFNRVLGVWSDLSRVPLATLKKRFTMGEAFHQHERGEISDEAFAEALCHEMALSLSYEQFAHGWQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A        88 VFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTTFWPEEYPEIRDAADHIYLSQDLGMRKPEARIYQHVLQAEGFSPSD 167
Cdd:PRK09456  81 VFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTTFWPEEYPEVRAAADHIYLSQDLGMRKPEARIYQHVLQAEGFSAAD 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
2B0C_A       168 TVFFDDNADNIEGANQLGITSILVKDKTTIPDYFAKVLC 206
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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A         11 IFDLGNVIVDIDF-NRVLGAWSDLTRIPLASLKKSF-HMGEAFHQHER---GEISDEAFAEALCHEMalplsYEQFSHGW 85
Cdd:TIGR01509   3 LFDLDGVLVDTEFaIAKLINREELGLVPDELGVSAVgRLELALRRFKAqygRTISPEDAQLLYKQLF-----YEQIEEEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A         86 QAvfvALRPEVIAIMHKLREQGHRVVVLSNTNRLHTTFwpEEYPEIRDAADHIYLSQDLGMRKPEARIYQHVLQAEGFSP 165
Cdd:TIGR01509  78 KL---KPLPGVRALLEALRARGKKLALLTNSPRAHKLV--LALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLEP 152

                         170       180
                  ....*....|....*....|....*.
2B0C_A        166 SDTVFFDDNADNIEGANQLGITSILV 191
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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A          9 LYIFDLGNVIVDIDFnRVLGAWSDLT----------------RIPLASLKKSFHMGEAfhQHERGEISDEAFAEALCHEM 72
Cdd:pfam00702   3 AVVFDLDGTLTDGEP-VVTEAIAELAsehplakaivaaaedlPIPVEDFTARLLLGKR--DWLEELDILRGLVETLEAEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A         73 ALPLSYEQFSHGWQAVFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTTFWPEEYpEIRDAADHIYLSQDLGMRKPEAR 152
Cdd:pfam00702  80 LTVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLL-GLDDYFDVVISGDDVGVGKPKPE 158

                         170       180       190
                  ....*....|....*....|....*....|...
2B0C_A        153 IYQHVLQAEGFSPSDTVFFDDNADNIEGANQLG 185
Cdd:pfam00702 159 IYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191

?-D-glucose-1-phosphatase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A         8 MLYIFDLGNVIVDIDFNRVLGAWSDLTRIPLASLKKSFHMGEAFHQHERGEISDEAFAEALCHEMALPLSYEQFSHGWQA 87
Cdd:PRK09456   1 MLYIFDLGNVIVDIDFNRVLGVWSDLSRVPLATLKKRFTMGEAFHQHERGEISDEAFAEALCHEMALSLSYEQFAHGWQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A        88 VFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTTFWPEEYPEIRDAADHIYLSQDLGMRKPEARIYQHVLQAEGFSPSD 167
Cdd:PRK09456  81 VFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTTFWPEEYPEVRAAADHIYLSQDLGMRKPEARIYQHVLQAEGFSAAD 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
2B0C_A       168 TVFFDDNADNIEGANQLGITSILVKDKTTIPDYFAKVLC 206
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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A         11 IFDLGNVIVDIDF-NRVLGAWSDLTRIPLASLKKSF-HMGEAFHQHER---GEISDEAFAEALCHEMalplsYEQFSHGW 85
Cdd:TIGR01509   3 LFDLDGVLVDTEFaIAKLINREELGLVPDELGVSAVgRLELALRRFKAqygRTISPEDAQLLYKQLF-----YEQIEEEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A         86 QAvfvALRPEVIAIMHKLREQGHRVVVLSNTNRLHTTFwpEEYPEIRDAADHIYLSQDLGMRKPEARIYQHVLQAEGFSP 165
Cdd:TIGR01509  78 KL---KPLPGVRALLEALRARGKKLALLTNSPRAHKLV--LALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLEP 152

                         170       180
                  ....*....|....*....|....*.
2B0C_A        166 SDTVFFDDNADNIEGANQLGITSILV 191
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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A         11 IFDLGNVIVDIDFnrVLGAWSDLTRIPLAS--LKKSFHMGEAFHQH----ERGEISDEAFAEALCHEMALPLSYE----Q 80
Cdd:TIGR02247   6 IFDFGGVLLPSPG--VMRRWETERGLPGLKdfIVTVNITGPDFNPWartfERGELTAEAFDGLFRHEYGLRLGHDvriaP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A         81 FSHGWQAVFVALRPEVIAIMHKLREQGHRVVVLsnTNRLHTTFWPEEY---PEIRDAADHIYLSQDLGMRKPEARIYQHV 157
Cdd:TIGR02247  84 VFPLLYGENTKLRPSMMAAIKTLRAKGFKTACI--TNNFPTDHSAEEAllpGDIMALFDAVVESCLEGLRKPDPRIYQLM 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
2B0C_A        158 LQAEGFSPSDTVFFDDNADNIEGANQLGITSILVKDKTTIPDYFAKVL 205
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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A       96 VIAIMHKLREQGHRVVVLSNTNRLHTTFWPEEYpEIRDAADHIYLSQDLGMRKPEARIYQHVLQAEGFSPSDTVFFDDNA 175
Cdd:cd01427  12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKL-GLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSE 90

                        90
                ....*....|....*.
2B0C_A      176 DNIEGANQLGITSILV 191
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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A       54 HERGEISDEAFAEALCHEMalplsyeqfsHGWQAvFvalrPEVIAIMHKLREQGHRVVVLSNTNRlHTTFWPEEYPEIRD 133
Cdd:cd02588  69 AELGLELDESDLDELGDAY----------LRLPP-F----PDVVAGLRRLREAGYRLAILSNGSP-DLIEDVVANAGLRD 132

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
2B0C_A      134 AADHIYLSQDLGMRKPEARIYQHVLQAEGFSPSDTVFFDDNADNIEGANQLGITSILVKDKTTIPDY 200
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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A          9 LYIFDLGNVIVDIDFNrvlgawsdltrIPLAslkksfhMGEAFHQHERGEISDEAF------AEALCHEMALPLSYEQFS 82
Cdd:TIGR01549   1 AILFDIDGTLVDIKFA-----------IRRA-------FPQTFEEFGLDPASFKALkqagglAEEEWYRIATSALEELQG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A         83 HGWQAVFV--ALRPEVIAIMHKLREQGHRVVVLSNTNRLHTTFWpEEYPEIRDAADHIYLSQDLGmRKPEARIYQHVLQA 160
Cdd:TIGR01549  63 RFWSEYDAeeAYIRGAADLLARLKSAGIKLGIISNGSLRAQKLL-LRLFGLGDYFELILVSDEPG-SKPEPEIFLAALES 140

                         170       180
                  ....*....|....*....|....*
2B0C_A        161 EGFSPsDTVFFDDNADNIEGANQLG 185
Cdd:TIGR01549 141 LGVPP-EVLHVGDNLNDIEGARNAG 164

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A       11 IFDLGNVIVDidFNRV-LGAWSDLtripLASLkkSFHMGEAFHQHERGeISDEAFAEALCHEMALPLSYEQFSHGWQAVF 89
Cdd:COG0637   6 IFDMDGTLVD--SEPLhARAWREA----FAEL--GIDLTEEEYRRLMG-RSREDILRYLLEEYGLDLPEEELAARKEELY 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A       90 --------VALRPEVIAIMHKLREQGHRVVVLSNTNR------LHTTfwpeeypEIRDAADHIYLSQDLGMRKPEARIYQ 155
Cdd:COG0637  77 rellaeegLPLIPGVVELLEALKEAGIKIAVATSSPRenaeavLEAA-------GLLDYFDVIVTGDDVARGKPDPDIYL 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
2B0C_A      156 HVLQAEGFSPSDTVFFDDNADNIEGANQLGITSILVKDKTTIPDYFAKV 204
Cdd:COG0637 150 LAAERLGVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGA 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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A       76 LSYEQFSHGWQAVFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTTFWPEEYPEIRDAADHIYLSQDLGMRKPEARIYQ 155
Cdd:cd07505  26 RKNALLLELIASEGLKLKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLRGYFDVIVSGDDVERGKPAPDIYL 105

                        90       100       110
                ....*....|....*....|....*....|....*...
2B0C_A      156 HVLQAEGFSPSDTVFFDDNADNIEGANQLGITSILVKD 193
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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A         92 LRPEVIAIMHKLREQGHRVVVLSNTNRLHTTFWPEEYPEIRDA--------ADHIYLSQdlGMRKPEARIYQHVL-QAEG 162
Cdd:TIGR01662  26 LYPEVPDALAELKEAGYKVVIVTNQSGIGRGYFSRSFSGRVARrleelgvpIDILYACP--GCRKPKPGMFLEALkRFNE 103

                          90       100       110
                  ....*....|....*....|....*....|
2B0C_A        163 FSPSDTVFFDDNADN-IEGANQLGITSILV 191
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.

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                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A       90 VALRPEVIAIMHKLREQGHRVVVLSNTNRLHTT-----FWPEEYPEIRDAadhIYLSQDLGMRKPEARIYQHVLQAEGFS 164
Cdd:cd07528  94 LPLRPGVARLIDEAKAAGVRLAIATTTSPANVDallsaLLGPERRAIFDA---IAAGDDVAEKKPDPDIYLLALERLGVS 170

                        90       100
                ....*....|....*....|....*.
2B0C_A      165 PSDTVFFDDNADNIEGANQLGITSIL 190
Cdd:cd07528 171 PSDCLAIEDSAIGLQAAKAAGLPCIV 196

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.

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                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A       94 PEVIAIMHKLREQGHRVVVLSNTnrlhttfWPEEYPEIRDAADHIYLSqdlGMRKPEARIYQHVLQAEGFSPSDTVFFDD 173
Cdd:cd16416  20 PEVKAWLADLKEAGIKVVLVSNN-------NERRVAKVIEKLDLPFVA---RAGKPRPRAFRRALKEMDLPPEQVAMVGD 89

                        90
                ....*....|....*....
2B0C_A      174 NA-DNIEGANQLGITSILV 191
Cdd:cd16416  90 QLfTDILGGNRAGLYTILV 108

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
                ....*....|....*....|....*....|....*....|....
2B0C_A      148 KPEARIYQHVLQAEGFSPSDTVFFDDNADNIEGANQLGITSILV 191
Cdd:cd02604 137 KPHPAAFEKAIREAGLDPKRAAFFDDSIRNLLAAKALGMKTVLV 180

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A       90 VALRPEVIAIMHKLREQGHRVVVLSNTN-------RLHTTFWPE--EYPEI--RDAADHIylsqdlgmrkpeariyQHVL 158
Cdd:cd07501  33 VSLYPDAQEILKELKERGILLAVASRNNefdhaneVLEKLDLKElfDAFEIypGSKSSHF----------------RKIA 96

                        90       100       110
                ....*....|....*....|....*....|...
2B0C_A      159 QAEGFSPSDTVFFDDNADNIEGANQLGITSILV 191
Cdd:cd07501  97 KELGIGFDSMVFFDDEPRNREEVSEGGVTCILV 129

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2B0C_A       94 PEVIAIMHKLREQGHRVVVlsntnrlhTTFWPEEYPE-------IRDAADHIYLSQDLGMRKPEARIYQHVLQAEGFSPS 166
Cdd:cd04302  84 PGIPELLEKLKAAGYRLYV--------ATSKPEVFARrilehfgLDEYFDGIAGASLDGSRVHKADVIRYALDTLGIAPE 155

                        90       100
                ....*....|....*....|....*
2B0C_A      167 DTVFFDDNADNIEGANQLGITSILV 191
Cdd:cd04302 156 QAVMIGDRKHDIIGARANGIDSIGV 180