phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human PSP, EC 3.1.3.3, catalyzes the third and final of the L-serine biosynthesis pathway, the Mg2+-dependent hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, L-serine is a precursor for the biosynthesis of glycine. HPSP regulates the levels of glycine and D-serine (converted from L-serine), the putative co-agonists for the glycine site of the NMDA receptor in the brain. Plant 3-PSP catalyzes the conversion of 3-phosphoserine to serine in the last step of the plastidic pathway of serine 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        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734332052  41 DAVCFDVDSTVCQDEGIDELAAYLGVGEAVANVTRTAMNGNARFRyrDALAARLQVMKPNHEQLEQFVNISKPKLTVGIR 120
Cdd:cd04309     1 DAVCFDVDSTVIQEEGIDELAKFCGVGDEVAELTRRAMGGSIPFR--DALRKRLAIINPTKEQVDEFLEEHPPRLTPGVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734332052 121 ELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEKSRIYANEILFDKFGKYHGFDTSELTSDSGsketGKPAVIALLKKM 200
Cdd:cd04309    79 ELVSRLKARGVEVYLISGGFRELIEPVASQLGIPLENVFANRLLFDFNGEYAGFDETQPTSRSG----GKAKVIEQLKEK 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1734332052 201 YNYKTVVMVGDGATDVEASPPADAFIGFGGNVIREGVKARAKWYVTDF 248
Cdd:cd04309   155 HHYKRVIMIGDGATDLEACPPADAFIGFGGNVIREKVKARADWYVTDF 202

phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human PSP, EC 3.1.3.3, catalyzes the third and final of the L-serine biosynthesis pathway, the Mg2+-dependent hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, L-serine is a precursor for the biosynthesis of glycine. HPSP regulates the levels of glycine and D-serine (converted from L-serine), the putative co-agonists for the glycine site of the NMDA receptor in the brain. Plant 3-PSP catalyzes the conversion of 3-phosphoserine to serine in the last step of the plastidic pathway of serine 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        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734332052  41 DAVCFDVDSTVCQDEGIDELAAYLGVGEAVANVTRTAMNGNARFRyrDALAARLQVMKPNHEQLEQFVNISKPKLTVGIR 120
Cdd:cd04309     1 DAVCFDVDSTVIQEEGIDELAKFCGVGDEVAELTRRAMGGSIPFR--DALRKRLAIINPTKEQVDEFLEEHPPRLTPGVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734332052 121 ELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEKSRIYANEILFDKFGKYHGFDTSELTSDSGsketGKPAVIALLKKM 200
Cdd:cd04309    79 ELVSRLKARGVEVYLISGGFRELIEPVASQLGIPLENVFANRLLFDFNGEYAGFDETQPTSRSG----GKAKVIEQLKEK 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1734332052 201 YNYKTVVMVGDGATDVEASPPADAFIGFGGNVIREGVKARAKWYVTDF 248
Cdd:cd04309   155 HHYKRVIMIGDGATDLEACPPADAFIGFGGNVIREKVKARADWYVTDF 202

phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate. It catalyzes the last of three steps in the biosynthesis of serine from D-3-phosphoglycerate. Note that this enzyme acts on free phosphoserine, not on phosphoserine residues of phosphoproteins. [Amino acid biosynthesis, Serine family]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734332052  38 RKADAVCFDVDSTVCQDEGIDELAAYLGVGEAVANVTRTAMNGNARFryRDALAARLQVMKPNHEQLEQFVnISKPKLTV 117
Cdd:TIGR00338  12 RSKKLVVFDMDSTLINAETIDEIAKIAGVEEEVSEITERAMRGELDF--KASLRERVALLKGLPVELLKEV-RENLPLTE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734332052 118 GIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEKsrIYANEILFDKfGKYHGFDTSELTsDSGSKetGKPAVIALL 197
Cdd:TIGR00338  89 GAEELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDA--AFANRLEVED-GKLTGLVEGPIV-DASYK--GKTLLILLR 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1734332052 198 KKMYNYKTVVMVGDGATDVEASPPADAFIGFGGNVIREGVK--ARAKWYVTDF 248
Cdd:TIGR00338 163 KEGISPENTVAVGDGANDLSMIKAAGLGIAFNAKPKLQQKAdiCINKKDLTDI 215

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 1734332052  41 DAVCFDVDSTVCQDE----------------GIDELAAYLGVGEAVANVTRTAMNGNARF-------RYRDALAARLQVM 97
Cdd:pfam00702   2 KAVVFDLDGTLTDGEpvvteaiaelasehplAKAIVAAAEDLPIPVEDFTARLLLGKRDWleeldilRGLVETLEAEGLT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734332052  98 KPNHEQLEQFVNISKPKLTVGIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEKSRIYANEILFDKFGKYHgfdts 177
Cdd:pfam00702  82 VVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPK----- 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1734332052 178 eltsdsgsketgkPAVIALLKKMYN--YKTVVMVGDGATDVEA 218
Cdd:pfam00702 157 -------------PEIYLAALERLGvkPEEVLMVGDGVNDIPA 186

phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human PSP, EC 3.1.3.3, catalyzes the third and final of the L-serine biosynthesis pathway, the Mg2+-dependent hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, L-serine is a precursor for the biosynthesis of glycine. HPSP regulates the levels of glycine and D-serine (converted from L-serine), the putative co-agonists for the glycine site of the NMDA receptor in the brain. Plant 3-PSP catalyzes the conversion of 3-phosphoserine to serine in the last step of the plastidic pathway of serine 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        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734332052  41 DAVCFDVDSTVCQDEGIDELAAYLGVGEAVANVTRTAMNGNARFRyrDALAARLQVMKPNHEQLEQFVNISKPKLTVGIR 120
Cdd:cd04309     1 DAVCFDVDSTVIQEEGIDELAKFCGVGDEVAELTRRAMGGSIPFR--DALRKRLAIINPTKEQVDEFLEEHPPRLTPGVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734332052 121 ELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEKSRIYANEILFDKFGKYHGFDTSELTSDSGsketGKPAVIALLKKM 200
Cdd:cd04309    79 ELVSRLKARGVEVYLISGGFRELIEPVASQLGIPLENVFANRLLFDFNGEYAGFDETQPTSRSG----GKAKVIEQLKEK 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1734332052 201 YNYKTVVMVGDGATDVEASPPADAFIGFGGNVIREGVKARAKWYVTDF 248
Cdd:cd04309   155 HHYKRVIMIGDGATDLEACPPADAFIGFGGNVIREKVKARADWYVTDF 202

phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate. It catalyzes the last of three steps in the biosynthesis of serine from D-3-phosphoglycerate. Note that this enzyme acts on free phosphoserine, not on phosphoserine residues of phosphoproteins. [Amino acid biosynthesis, Serine family]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734332052  38 RKADAVCFDVDSTVCQDEGIDELAAYLGVGEAVANVTRTAMNGNARFryRDALAARLQVMKPNHEQLEQFVnISKPKLTV 117
Cdd:TIGR00338  12 RSKKLVVFDMDSTLINAETIDEIAKIAGVEEEVSEITERAMRGELDF--KASLRERVALLKGLPVELLKEV-RENLPLTE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734332052 118 GIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEKsrIYANEILFDKfGKYHGFDTSELTsDSGSKetGKPAVIALL 197
Cdd:TIGR00338  89 GAEELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDA--AFANRLEVED-GKLTGLVEGPIV-DASYK--GKTLLILLR 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1734332052 198 KKMYNYKTVVMVGDGATDVEASPPADAFIGFGGNVIREGVK--ARAKWYVTDF 248
Cdd:TIGR00338 163 KEGISPENTVAVGDGANDLSMIKAAGLGIAFNAKPKLQQKAdiCINKKDLTDI 215

Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences. [Unknown function, Enzymes of unknown specificity]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734332052  42 AVCFDVDSTVC-QDEGIDELAAYLGVGEAVANVTRTAMNGNARFRYRDALAARLQVMKpNHEQLEQFVNISKPKLTVGIR 120
Cdd:TIGR01488   1 LAIFDFDGTLTrQDSLIDLLAKLLGTNDEVIELTRLAPSGRISFEDALGRRLALLHRS-RSEEVAKEFLARQVALRPGAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734332052 121 ELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEksRIYANEILFDKFGKYHGFDTSELTSDSGsketGKPAVIALLKKM 200
Cdd:TIGR01488  80 ELISWLKERGIDTVIVSGGFDFFVEPVAEKLGID--DVFANRLEFDDNGLLTGPIEGQVNPEGE----CKGKVLKELLEE 153

                         170       180
                  ....*....|....*....|....
gi 1734332052 201 YNY--KTVVMVGDGATDVEASPPA 222
Cdd:TIGR01488 154 SKItlKKIIAVGDSVNDLPMLKLA 177

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 1734332052  41 DAVCFDVDSTVCQDE----------------GIDELAAYLGVGEAVANVTRTAMNGNARF-------RYRDALAARLQVM 97
Cdd:pfam00702   2 KAVVFDLDGTLTDGEpvvteaiaelasehplAKAIVAAAEDLPIPVEDFTARLLLGKRDWleeldilRGLVETLEAEGLT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734332052  98 KPNHEQLEQFVNISKPKLTVGIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEKSRIYANEILFDKFGKYHgfdts 177
Cdd:pfam00702  82 VVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPK----- 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1734332052 178 eltsdsgsketgkPAVIALLKKMYN--YKTVVMVGDGATDVEA 218
Cdd:pfam00702 157 -------------PEIYLAALERLGvkPEEVLMVGDGVNDIPA 186

haloacid dehalogenase-like hydrolase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734332052  43 VCFDVDSTVCQDEGIDELAAYLGvgEAVANVTRTAMNGNARFRYRDALAARLQVMK-------------PNHEQLEQFV- 108
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALL--RRGGPDLWRALLVLLLLALLRLLGRLSRAGArellrallaglpeEDAAELERFVa 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734332052 109 NISKPKLTVGIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEksRIYANEILFDKfgkyHGFDTSELTSDSGSKET 188
Cdd:pfam12710  79 EVALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFD--EVLATELEVDD----GRFTGELRLIGPPCAGE 152

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1734332052 189 GKPAVIA--LLKKMYN--YKTVVMVGDGATDVEA 218
Cdd:pfam12710 153 GKVRRLRawLAARGLGldLADSVAYGDSPSDLPM 186

phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like superfamily; Bacillus subtilis recycles two toxic byproducts of polyamine metabolism, methylthioadenosine and methylthioribose, into methionine by a salvage pathway. The sixth reaction in this pathway is catalyzed by B. subtilis MtnX: the dephosphorylation of 2- hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HKMTP- 1-P) into 1,2-dihydroxy-3-keto-5-methylthiopentene. The hydrolysis of HK-MTP-1-P is a two-step mechanism involving the formation of a transiently phosphorylated aspartyl intermediate. 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 1734332052  46 DVDSTVCQDEGIDELAAYLGVGEAVanvtRTAMNG---NARFRYRDALAARLQVMKPN-HEQLEQFVnISKPKLTVGIRE 121
Cdd:cd07524     5 DFDGTITENDNIIYLMDEFAPPLEE----WEALKEgvlSQTLSFREGVGQMFELLPSSlKDEIIEFL-EKTAKIRPGFKE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734332052 122 LVSRLHARGTHVYLVSGGFRRLILPVAELLGIEKSRIYANEILFDKFGKYHGFDTS-ELTSDSGskeTGKPAVIALLKKM 200
Cdd:cd07524    80 FVAFCQEHGIPFIIVSGGMDFFIEPLLEGLVIEKIAIYCNGSDFSGEQIHIDWPHEcDCTNGCG---CCKSSIIRKYSKP 156

                         170       180
                  ....*....|....*....|...
gi 1734332052 201 YNYKtvVMVGDGATDVEASPPAD 223
Cdd:cd07524   157 RPFI--IVIGDSVTDLEAAKEAD 177

2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase; Reviewed

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734332052 101 HEQLEQFVnISKPKLTVGIRELVSRLHARGTHVYLVSGGFRRLILPVAELLgIEKSRIYANEILFDkfGKY------HGF 174
Cdd:PRK09552   62 KEEIIQFL-LETAEIREGFHEFVQFVKENNIPFYVVSGGMDFFVYPLLQGL-IPKEQIYCNGSDFS--GEYititwpHPC 137

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1734332052 175 DTSeLTSDSGskeTGKPAVIALLKKMYNYKtvVMVGDGATDVEASPPAD 223
Cdd:PRK09552  138 DEH-CQNHCG---CCKPSLIRKLSDTNDFH--IVIGDSITDLEAAKQAD 180

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). 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 1734332052  42 AVCFDVDSTVCQDE---------GIDELAAYLGVGEAVANVTRTAMNGNARFRYRDALAArlqVMKPNHEQLEQFVN--- 109
Cdd:cd02612     1 LAFFDLDGTLIAGDsffaflrfkGIAERRAPLEELLLLRLMALYALGRLDGAGMEALLGF---ATAGLAGELAALVEefv 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1734332052 110 --ISKPKLTVGIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEK 155
Cdd:cd02612    78 eeYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDN 125

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 1734332052  42 AVCFDVDSTVC-QDEGIDELAAYLGVGEAVANVTRTAMNG----NARFRYRDALAARLQVMkpnhEQLEQFVNISKPKLt 116
Cdd:TIGR01549   1 AILFDIDGTLVdIKFAIRRAFPQTFEEFGLDPASFKALKQagglAEEEWYRIATSALEELQ----GRFWSEYDAEEAYI- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734332052 117 VGIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEksrIYANEILFDkfgkyhgfdtseltSDSGSKETGKpAVIAL 196
Cdd:TIGR01549  76 RGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLG---DYFELILVS--------------DEPGSKPEPE-IFLAA 137

                         170       180
                  ....*....|....*....|..
gi 1734332052 197 LKKMYNYKTVVMVGDGATDVEA 218
Cdd:TIGR01549 138 LESLGVPPEVLHVGDNLNDIEG 159

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734332052  41 DAVCFDVDSTVCQDEGI-----DELAAYLGVgeavaNVTR---TAMNGNARFRYRDALAARLQVMKPNHEQLEQFVN--- 109
Cdd:COG0637     3 KAVIFDMDGTLVDSEPLharawREAFAELGI-----DLTEeeyRRLMGRSREDILRYLLEEYGLDLPEEELAARKEElyr 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1734332052 110 --ISKPKLTV--GIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEK 155
Cdd:COG0637    78 elLAEEGLPLipGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLD 127