Enolase-phosphatase similar to human enolase-phosphatase E1 and and Xanthomonas oryzae pv. Oryzae enolase-phosphatase Xep; Enolase-phosphatase E1 (also called MASA) is a bifunctional enolase- phosphatase which promotes the conversion of 2,3-diketo-5-methylthio-1-phosphopentane to 1,2-dihydroxy-3-keto-5-methylthiopentene anion (an aci-reductone) in the methionine salvage pathway. The catalytic reaction is carried out continuously by enolization and dephosphorylation, and the enolase activity cannot be classified as typical enzymatic enolization. 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 464100234   4 HVVYDIEGTTSSTGFVHDTLYPYSRERFAAYIDEHGHDPQV-IAQLDAVRELAGEPDADVERIVWWLNHWLDDDQKVTPL 82
Cdd:cd01629    1 AILLDIEGTTTPISFVKDVLFPYARERLPDFLAEHWEDPEVkEDVLAAAAEAEGEAEASIEAVVANLLDWMDEDRKATPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464100234  83 KAFQGWIWTDGFAAGDLTSHFFADSIPAIRRHHAEGRTLSIFSSGSVSAQLAWFGNTPDGSLLDLFSHHFDTeNIGPKRV 162
Cdd:cd01629   81 KALQGLIWREGYESGELKGHLYPDVVPALRRWHAAGLRLYIYSSGSVAAQKLLFGHSDAGDLTPLFSGYFDT-TIGPKRE 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 464100234 163 TESYDLIASRLGAPADEIVFFSDLVAELDAARDAGWHTVGVRRQG 207
Cdd:cd01629  160 AASYRKIAEAIGVPPAEILFLSDVVAELDAAKEAGLQTVLLVRPG 204

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 464100234    5 VVYDIEGTTSSTGFVHDTLYPYSRERFAAYIDEHGHDPQVIAQLDAVRELAGepdadVERIVWWLNHWLDDDQKVTPLKA 84
Cdd:pfam00702   4 VVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAEDLPIPVEDFTARLL-----LGKRDWLEELDILRGLVETLEAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464100234   85 FQGWIWT--DGFAAGDLTSHFFADSIPAIRRHHAEGRTLSIFSSGSVSAQLAWFGNTPDGSLLDLFSHHFDTENIGPKRv 162
Cdd:pfam00702  79 GLTVVLVelLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKP- 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 464100234  163 tESYDLIASRLGAPADEIVFFSDLVAELDAARDAG 197
Cdd:pfam00702 158 -EIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191

Enolase-phosphatase similar to human enolase-phosphatase E1 and and Xanthomonas oryzae pv. Oryzae enolase-phosphatase Xep; Enolase-phosphatase E1 (also called MASA) is a bifunctional enolase- phosphatase which promotes the conversion of 2,3-diketo-5-methylthio-1-phosphopentane to 1,2-dihydroxy-3-keto-5-methylthiopentene anion (an aci-reductone) in the methionine salvage pathway. The catalytic reaction is carried out continuously by enolization and dephosphorylation, and the enolase activity cannot be classified as typical enzymatic enolization. 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 464100234   4 HVVYDIEGTTSSTGFVHDTLYPYSRERFAAYIDEHGHDPQV-IAQLDAVRELAGEPDADVERIVWWLNHWLDDDQKVTPL 82
Cdd:cd01629    1 AILLDIEGTTTPISFVKDVLFPYARERLPDFLAEHWEDPEVkEDVLAAAAEAEGEAEASIEAVVANLLDWMDEDRKATPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464100234  83 KAFQGWIWTDGFAAGDLTSHFFADSIPAIRRHHAEGRTLSIFSSGSVSAQLAWFGNTPDGSLLDLFSHHFDTeNIGPKRV 162
Cdd:cd01629   81 KALQGLIWREGYESGELKGHLYPDVVPALRRWHAAGLRLYIYSSGSVAAQKLLFGHSDAGDLTPLFSGYFDT-TIGPKRE 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 464100234 163 TESYDLIASRLGAPADEIVFFSDLVAELDAARDAGWHTVGVRRQG 207
Cdd:cd01629  160 AASYRKIAEAIGVPPAEILFLSDVVAELDAAKEAGLQTVLLVRPG 204

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 464100234  21 DTLYPYS---RERFAAYIDEHGHDPQVIAQLDAVRELAGEPDADVERIVWWLNHWLDDDQKVTPLKAFQGWIwtDGFAAG 97
Cdd:COG1011   10 GTLLDFDpviAEALRALAERLGLLDEAEELAEAYRAIEYALWRRYERGEITFAELLRRLLEELGLDLAEELA--EAFLAA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464100234  98 -DLTSHFFADSIPAIRRHHAEGRTLSIFSSGSVSAQLAWFGNTPdgsLLDLFSHHFDTENIG-PKRVTESYDLIASRLGA 175
Cdd:COG1011   88 lPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLG---LDDLFDAVVSSEEVGvRKPDPEIFELALERLGV 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 464100234 176 PADEIVFFSD-LVAELDAARDAGWHTVGVRRQGDQYFDQGVGDHlAIFSFDEI 227
Cdd:COG1011  165 PPEEALFVGDsPETDVAGARAAGMRTVWVNRSGEPAPAEPRPDY-VISDLAEL 216

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 464100234 104 FADSIPAIRRHHAEGRTLSIFSSGSVSAQLAWFGNTpdgSLLDLFSHHFDTENIGP-KRVTESYDLIASRLGAPADEIVF 182
Cdd:cd02588   93 FPDVVAGLRRLREAGYRLAILSNGSPDLIEDVVANA---GLRDLFDAVLSAEDVRAyKPAPAVYELAAERLGVPPDEILH 169

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 464100234 183 FSDLVAELDAARDAGWHTVGVRRQGdQYFDQGVGD 217
Cdd:cd02588  170 VASHAWDLAGARALGLRTAWINRPG-EVPDPLGPA 203

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464100234  108 IPAIRRHHAEGRTLSIFSSG--SVSAQLAWFGntpdgsLLDLFSHHFDTENIG-PKRVTESYDLIASRLGAPADEIVFFS 184
Cdd:TIGR01509  86 RALLEALRARGKKLALLTNSprAHKLVLALLG------LRDLFDVVIDSSDVGlGKPDPDIYLQALKALGLEPSECVFVD 159

                          90
                  ....*....|....*....
gi 464100234  185 DLVAELDAARDAGWHTVGV 203
Cdd:TIGR01509 160 DSPAGIEAAKAAGMHTVGV 178

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464100234 108 IPAIRRHHAEGRTLSIFSSGSVSAQLAWFGNtpdGSLLDLFSHHFDTENIG-PKRVTESYDLIASRLGAPADEIVFFSDL 186
Cdd:cd01427   13 VELLKRLRAAGIKLAIVTNRSREALRALLEK---LGLGDLFDGIIGSDGGGtPKPKPKPLLLLLLKLGVDPEEVLFVGDS 89

                         90
                 ....*....|....*..
gi 464100234 187 VAELDAARDAGWHTVGV 203
Cdd:cd01427   90 ENDIEAARAAGGRTVAV 106

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 464100234 110 AIRRHHAEGRTLSIFSSGSVSAQLAWFGNtpdgslLDLFSHHFDT-----ENIGPKRVTESYDLIASRLGAPADEIVFFS 184
Cdd:cd07505   49 LLDALKAAGIPVAVATSSSRRNVELLLLE------LGLLRGYFDVivsgdDVERGKPAPDIYLLAAERLGVDPERCLVFE 122

                         90       100
                 ....*....|....*....|
gi 464100234 185 DLVAELDAARDAGWHTVGVR 204
Cdd:cd07505  123 DSLAGIEAAKAAGMTVVAVP 142