Haloacid dehalogenase-like hydrolase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434627872   1 DVDGTILDTEKAILKSLQKVLKEELKEDYALQDLKFALGIPGKETLKKLNVK-----NIDVVHPKWAKSVLNFshEVSVF 75
Cdd:pfam13419   4 DFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEILKFIGLPLREIFRYLGVSedeeeKIEFYLRKYNEELHDK--LVKPY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434627872  76 EELESIIKELSFSKLKLGIVTSKTKQELIDEFEPFDLSGHFERIICACDTDKHKPHPEPLLACLKQLDVPNNESVYIGDS 155
Cdd:pfam13419  82 PGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVIYVGDS 161

                         170
                  ....*....|....*..
gi 1434627872 156 IYDMQCAKSAGVKFALA 172
Cdd:pfam13419 162 PRDIEAAKNAGIKVIAV 178

pyrophosphatase PpaX; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434627872   1 DVDGTILDTEKAILKSLQKVLKEELKEDYALQD-LKFaLGIPGKETLKKLNVKNIDvvhpKWAKSVLNFSHE-----VSV 74
Cdd:PRK13288    9 DLDGTLINTNELIISSFLHTLKTYYPNQYKREDvLPF-IGPSLHDTFSKIDESKVE----EMITTYREFNHEhhdelVTE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434627872  75 FEELESIIKELSFSKLKLGIVTSKTKQELIDEFEPFDLSGHFERIICACDTDKHKPHPEPLLACLKQLDVPNNESVYIGD 154
Cdd:PRK13288   84 YETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPDPEPVLKALELLGAKPEEALMVGD 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1434627872 155 SIYDMQCAKSAGVKFALALWGSKTKEGFEK--ADYVLNTPKDILNLI 199
Cdd:PRK13288  164 NHHDILAGKNAGTKTAGVAWTIKGREYLEQykPDFMLDKMSDLLAIV 210

Haloacid dehalogenase-like hydrolase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434627872   1 DVDGTILDTEKAILKSLQKVLKEELKEDYALQDLKFALGIPGKETLKKLNVK-----NIDVVHPKWAKSVLNFshEVSVF 75
Cdd:pfam13419   4 DFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEILKFIGLPLREIFRYLGVSedeeeKIEFYLRKYNEELHDK--LVKPY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434627872  76 EELESIIKELSFSKLKLGIVTSKTKQELIDEFEPFDLSGHFERIICACDTDKHKPHPEPLLACLKQLDVPNNESVYIGDS 155
Cdd:pfam13419  82 PGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVIYVGDS 161

                         170
                  ....*....|....*..
gi 1434627872 156 IYDMQCAKSAGVKFALA 172
Cdd:pfam13419 162 PRDIEAAKNAGIKVIAV 178

pyrophosphatase PpaX; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434627872   1 DVDGTILDTEKAILKSLQKVLKEELKEDYALQD-LKFaLGIPGKETLKKLNVKNIDvvhpKWAKSVLNFSHE-----VSV 74
Cdd:PRK13288    9 DLDGTLINTNELIISSFLHTLKTYYPNQYKREDvLPF-IGPSLHDTFSKIDESKVE----EMITTYREFNHEhhdelVTE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434627872  75 FEELESIIKELSFSKLKLGIVTSKTKQELIDEFEPFDLSGHFERIICACDTDKHKPHPEPLLACLKQLDVPNNESVYIGD 154
Cdd:PRK13288   84 YETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPDPEPVLKALELLGAKPEEALMVGD 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1434627872 155 SIYDMQCAKSAGVKFALALWGSKTKEGFEK--ADYVLNTPKDILNLI 199
Cdd:PRK13288  164 NHHDILAGKNAGTKTAGVAWTIKGREYLEQykPDFMLDKMSDLLAIV 210

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 1434627872   1 DVDGTILDTEKAILKSLQKVLK--------EELKEDYALQDLKFALGIPG---------KETLKKLNVKNIDVVHPKWAK 63
Cdd:COG1011     7 DLDGTLLDFDPVIAEALRALAErlglldeaEELAEAYRAIEYALWRRYERgeitfaellRRLLEELGLDLAEELAEAFLA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434627872  64 SvlnFSHEVSVFEELESIIKELSFSKLKLGIVT--SKTKQELIDEFepFDLSGHFERIICACDTDKHKPHPEPLLACLKQ 141
Cdd:COG1011    87 A---LPELVEPYPDALELLEALKARGYRLALLTngSAELQEAKLRR--LGLDDLFDAVVSSEEVGVRKPDPEIFELALER 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1434627872 142 LDVPNNESVYIGDSIY-DMQCAKSAGVKFALALWGSKTKEGFEKADYVLNTPKDILNLI 199
Cdd:COG1011   162 LGVPPEEALFVGDSPEtDVAGARAAGMRTVWVNRSGEPAPAEPRPDYVISDLAELLELL 220

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 1434627872  73 SVFEELESIIKELSFSKLKLGIVTSKTKQELIDEFEPFDLSGHFERIICACDTDKHKPHPEPLLACLKQLDVPNNESVYI 152
Cdd:TIGR01449  85 SVFPGVEATLGALRAKGLRLGLVTNKPTPLARPLLELLGLAKYFSVLIGGDSLAQRKPHPDPLLLAAERLGVAPQQMVYV 164

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1434627872 153 GDSIYDMQCAKSAGVKFALALWGSKTKEGFE--KADYVLNTPKDILNLI 199
Cdd:TIGR01449 165 GDSRVDIQAARAAGCPSVLLTYGYRYGEAIDllPPDVLYDSLNELPPLL 213

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 1434627872   1 DVDGTILDTEKAILKSLQKVLKEELKEDYALQDLKFALGIPGKETLkklnvkniDVVHPKWAKSVLNFSHEVSV----FE 76
Cdd:TIGR01549   5 DIDGTLVDIKFAIRRAFPQTFEEFGLDPASFKALKQAGGLAEEEWY--------RIATSALEELQGRFWSEYDAeeayIR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434627872  77 ELESIIKELSFSKLKLGIVTSKTKQELIDEFEPFDLSGHFERIICACDTDkHKPHPEPLLACLKQLDVPNnESVYIGDSI 156
Cdd:TIGR01549  77 GAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEPG-SKPEPEIFLAALESLGVPP-EVLHVGDNL 154

                         170
                  ....*....|
gi 1434627872 157 YDMQCAKSAG 166
Cdd:TIGR01549 155 NDIEGARNAG 164

N-acetylmuramic acid 6-phosphate phosphatase MupP;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434627872   1 DVDGTILDTEKAILKSLQKVLKEELKEDYALQD----------------LKFALGIPGKETLKKLnvKNIDVVHpkWAKS 64
Cdd:PRK13222   12 DLDGTLVDSAPDLAAAVNAALAALGLPPAGEERvrtwvgngadvlveraLTWAGREPDEELLEKL--RELFDRH--YAEN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434627872  65 VLNFSHevsVFEELESIIKELSFSKLKLGIVTSKTKQ---ELIDEFepfDLSGHFERIICACDTDKHKPHPEPLLACLKQ 141
Cdd:PRK13222   88 VAGGSR---LYPGVKETLAALKAAGYPLAVVTNKPTPfvaPLLEAL---GIADYFSVVIGGDSLPNKKPDPAPLLLACEK 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434627872 142 LDVPNNESVYIGDSIYDMQCAKSAGVKFALALWGSKTKEGFE--KADYVLNTPKDILNLI 199
Cdd:PRK13222  162 LGLDPEEMLFVGDSRNDIQAARAAGCPSVGVTYGYNYGEPIAlsEPDVVIDHFAELLPLL 221

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 1434627872   1 DVDGTILDTEKAILKSLQKVLKEELKEDYALQDLKFALGIPGKETLKKLNVKNidvvhPKWAKSVLNFSH---------E 71
Cdd:cd04302     5 DLDGTLTDSAEGITASVQYALEELGIPVPDESELRRFIGPPLEDSFRELLPFD-----EEEAQRAVDAYReyykekglfE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434627872  72 VSVFEELESIIKELSFSKLKLGIVTSK---TKQELIDEFEpfdLSGHFERIICAcDTDKHKPHPEPLLA-CLKQLDVPNN 147
Cdd:cd04302    80 NEVYPGIPELLEKLKAAGYRLYVATSKpevFARRILEHFG---LDEYFDGIAGA-SLDGSRVHKADVIRyALDTLGIAPE 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1434627872 148 ESVYIGDSIYDMQCAKSAGVKFALALWG--SKTKEGFEKADYVLNTPKDILNLI 199
Cdd:cd04302   156 QAVMIGDRKHDIIGARANGIDSIGVLYGygSEDELEEAGATYIVETPAELLELL 209

beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434627872   1 DVDGTILDTEKAILKSLQKVLKE---ELKEDYaLQDLKfalGIPGKETLKKLNVKNIDVVHPKWAKSVLNFSHE------ 71
Cdd:TIGR02009   7 DMDGVITDTAPLHAQAWKHIAAKygiSFDKQY-NESLK---GLSREDILRAILKLRGDGLSLEEIHQLAERKNElyrell 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434627872  72 ----VSVFEELESIIKELSFSKLKLGIVTSKTKQELIdeFEPFDLSGHFERIICACDTDKHKPHPEPLLACLKQLDVPNN 147
Cdd:TIGR02009  83 rltgVAVLPGIRNLLKRLKAKGIAVGLGSSSKNAPRI--LAKLGLRDYFDAIVDASEVKNGKPHPETFLLAAELLGVPPN 160

                         170       180
                  ....*....|....*....|....*
gi 1434627872 148 ESVYIGDSIYDMQCAKSAGVkFALA 172
Cdd:TIGR02009 161 ECIVFEDALAGVQAARAAGM-FAVA 184

phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase PGP/CbbZ; Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. 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 1434627872   1 DVDGTILDTEKAILKSLQKVLKEELKEDYALQDLKFALGIPGKETLKKLNVknidvvhPKWA---------KSVLNFSHE 71
Cdd:cd04303     5 DFDGTLADSFPWFLSILNQLAARHGFKTVDEEEIEQLRQLSSREILKQLGV-------PLWKlpliakdfrRLMAEAAPE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434627872  72 VSVFEELESIIKELSFSKLKLGIVTSKTKQELIDEFEPFDLSGHFEriiCACDTD---KHKPhpepLLACLKQLDVPNNE 148
Cdd:cd04303    78 LALFPGVEDMLRALHARGVRLAVVSSNSEENIRRVLGPEELISLFA---VIEGSSlfgKAKK----IRRVLRRTKITAAQ 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1434627872 149 SVYIGDSIYDMQCAKSAGVKFALALWGSKTKEGFEKA--DYVLNTPKDIL 196
Cdd:cd04303   151 VIYVGDETRDIEAARKVGLAFAAVSWGYAKPEVLKALapDHMLEDPEDLI 200

Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGPase; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and phosphate. Members of this family belong 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 (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. 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 1434627872  90 LKLGIVTSK---TKQELIDEFEPfdlsGHFERIICACDTDKHKPHPEPLLACLKQLDVPNNESVYIGDSIYDMQCAKSAG 166
Cdd:cd16421    24 IKLAVLSNKpneAVQVLVEELFP----GSFDFVLGEKEGIRRKPDPT*ALECAKVLGVPPDEVLYVGDSGVDMQTARNAG 99

                  .
gi 1434627872 167 V 167
Cdd:cd16421   100 M 100

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the uncharacterized Lactococcus lactis YsbA; The specific function of Lactococcus lactis YsbA is unknown. Members of this family belong 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 1434627872   1 DVDGTILDTEKAILKSLQKVLKEELKEDYALQDLKFALGIPGKETLKKLNVknIDVVHPKWAKSVLNFSHEVSVFEELES 80
Cdd:cd07523     5 DLDGTLLDSYPAMTKALSETLADFGIPQDLETVYKIIKESSVQFAIQYYAE--VPDLEEEYKELEAEYLAKPILFPGAKA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434627872  81 IIKELSFSKLKLGIVTSKTKQELiDEFEPFDLSGHFERIICACDTDKHKPHPEPLLACLKQLDVPNNESVYIGDSIYDMQ 160
Cdd:cd07523    83 VLRWIKEQGGKNFLMTHRDHSAL-TILKKDGIASYFTEIVTSDNGFPRKPNPEAINYLLNKYQLNPEETVMIGDRELDIE 161

                  ....*...
gi 1434627872 161 CAKSAGVK 168
Cdd:cd07523   162 AGHNAGIS 169

human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. 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 1434627872  75 FEELESIIKELSfSKLKLGIVT---SKTKQELIDEFepfDLSGHFERIICACDTDKHKPHPEPLLACLKQLDVPNNESVY 151
Cdd:cd04305    11 LPGAKELLEELK-KGYKLGIITngpTEVQWEKLEQL---GIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLM 86

                          90
                  ....*....|....*...
gi 1434627872 152 IGDSIY-DMQCAKSAGVK 168
Cdd:cd04305    87 VGDSLEsDILGAKNAGIK 104

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 1434627872  81 IIKELSFSKLKLGIVTSKTKQE---LIDEFEPFDLSGHFERIICACDTDKHKPHPEPLLACLKQLDVPNNESVYIGDSIY 157
Cdd:cd07528   103 LIDEAKAAGVRLAIATTTSPANvdaLLSALLGPERRAIFDAIAAGDDVAEKKPDPDIYLLALERLGVSPSDCLAIEDSAI 182

                          90
                  ....*....|.
gi 1434627872 158 DMQCAKSAGVK 168
Cdd:cd07528   183 GLQAAKAAGLP 193

uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid dehalogenase-like superfamily; This uncharacterized subfamily belongs to the UmpH/NagD phosphatase family and 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434627872 129 KPHPEPLLACLKQLDVPNNESVYIGDSIY-DMQCAKSAGVKFALALWGSKTKEGFEKADY 187
Cdd:cd16422   177 KPNPIILDPVLEKFDYSKEETVMVGDRLYtDIVLGINAGVDSILVLSGETTREDLEDLER 236

subfamily of beta-phosphoglucomutase-like family, similar to Arabidopsis thaliana Gpp1 and Gpp2; This subfamily includes Arabidopsis thaliana AtGpp1 and AtGpp2, and Drosophila GS1-like protein (Dmel\Gs1l) of unknown function. AtGpp1 and AtGpp2 are constitutively expressed in all the Arabidopsis tissues and unaffected under abiotic stress. Overexpression of AtGpp2 in transgenic Arabidopsis plants increases the specific DL-glycerol-3-phosphatase activity and improves the plants tolerance to salt, osmotic and oxidative stress. 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 1434627872   1 DVDGTILDTEKAILKSLQKVLKEELKeDYALQDLKFALGIPGKETLKKL-NVKNIDVvhpKWAKSVLN--------FSHE 71
Cdd:cd07529     7 DMDGLLLDTERIYTETTQEILARYGK-TYTWDVKAKMMGRPASEAARIIvDELKLPM---SLEEEFDEqqealaelFMGT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434627872  72 VSVFEELESIIKELSFSKLKLGIVTS--------KTKQELidefEPFDLSGHferIICACDTD---KHKPHPEPLLACLK 140
Cdd:cd07529    83 AKLMPGAERLLRHLHAHNIPIALATSsctrhfklKTSRHK----ELFSLFHH---VVTGDDPEvkgRGKPAPDIFLVAAK 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1434627872 141 QLDVP--NNESVYI-GDSIYDMQCAKSAGVK 168
Cdd:cd07529   156 RFNEPpkDPSKCLVfEDSPNGVKAAKAAGMQ 186

HAD-hyrolase-like;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1434627872 129 KPHPEPLLACLKQLDVPNNESVYIGDSIY-DMQCAKSAGVKFALALWGSKTKEGFEKA----DYVLNT 191
Cdd:pfam13242   4 KPNPGMLERALARLGLDPERTVMIGDRLDtDILGAREAGARTILVLTGVTRPADLEKApirpDYVVDD 71

histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal domain of the Escherichia coli bifunctional enzyme histidinol-phosphate phosphatase/imidazole-glycerol-phosphate dehydratase, HisB. The N-terminal histidinol-phosphate phosphatase domain catalyzes the dephosphorylation of histidinol phosphate, the eight step of L-histidine biosynthesis. This family also includes Escherichia coli GmhB phosphatase which is highly specific for D-glycero-D-manno-heptose-1,7-bisphosphate, it removes the C(7)phosphate and not the C(1)phosphate, and this is the third essential step of lipopolysaccharide heptose biosynthesis. 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
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1434627872 115 HFERIICACdtdkHKPHPEPLLACLKQLDVPNNESVYIGDSIYDMQCAKSAGVKFAL 171
Cdd:cd07503    89 HHPDDGCPC----RKPKPGMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGCKGIL 141

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 1434627872  70 HEVSVFEELESIIKELSFSKLKLGIVTSKTKQELIDEFEPFDLSGHFERIICACDTDKHKPHPEPLLACLKQLDVPNNES 149
Cdd:cd02588    88 LRLPPFPDVVAGLRRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAEDVRAYKPAPAVYELAAERLGVPPDEI 167

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1434627872 150 VYIGDSIYDMQCAKSAGVKFAlalW----GSKTKEGFEKADYVLNT 191
Cdd:cd02588   168 LHVASHAWDLAGARALGLRTA---WinrpGEVPDPLGPAPDFVVPD 210

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 1434627872  68 FSHEVSVFEELESIIKELSFSKLKLGIVT--SKTKQELIDEFEPFdLSGHFERIICACDTDKHKPHPEPLLACLKQLDVP 145
Cdd:cd02603    79 VLAAVDPNPEMLDLLEALRAKGYKVYLLSntWPDHFKFQLELLPR-RGDLFDGVVESCRLGVRKPDPEIYQLALERLGVK 157

                          90       100
                  ....*....|....*....|.
gi 1434627872 146 NNESVYIGDSIYDMQCAKSAG 166
Cdd:cd02603   158 PEEVLFIDDREENVEAARALG 178