uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1; 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 1032574204   4 ILFDKDGTLIEFDHswekigvRLVNSFLDTF-----PVANKEATLRKLGVvkdtispdsvmgsgSLDEIVHAFNDESGKD 78
Cdd:cd07533     2 VIFDWDGTLADSQH-------NIVAAMTAAFadlglPVPSAAEVRSIIGL--------------SLDEAIARLLPMATPA 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032574204  79 VSKWTRDTSQA---LVDSREPENNWIDGVYDMIQSLRYEGYKIGIVTSDSEKGMTQFLEETHSKDAFDlVISTEAHAAEK 155
Cdd:cd07533    61 LVAVAERYKEAfdiLRLLPEHAEPLFPGVREALDALAAQGVLLAVATGKSRRGLDRVLEQHGLGGYFD-ATRTADDTPSK 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032574204 156 PNPEVLKPLFDHYDVKPEDVAIVGDTNNDMKTKVNAKLGlAIGVLSGIAKKEELVD--ADYVIE 217
Cdd:cd07533   140 PHPEMLREILAELGVDPSRAVMVGDTAYDMQMAANAGAH-AVGVAWGYHSLEDLRSagADAVVD 202

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 1032574204   3 WILFDKDGTLIEFDHSWEKIGVRLVNSFlDTFPVANKEatLRKLGVVKDTISPDsvMGSGSLDEIVHAFndESGKDVSKW 82
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEF-GLDPASFKA--LKQAGGLAEEEWYR--IATSALEELQGRF--WSEYDAEEA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032574204  83 trdtsqalvdsrepennWIDGVYDMIQSLRYEGYKIGIVTSDSEKGMTQFLEETHSKDAFDLvISTEAHAAEKPNPEVLK 162
Cdd:TIGR01549  74 -----------------YIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFEL-ILVSDEPGSKPEPEIFL 135

                         170       180
                  ....*....|....*....|....*
gi 1032574204 163 PLFDHYDVkPEDVAIVGDTNNDMKT 187
Cdd:TIGR01549 136 AALESLGV-PPEVLHVGDNLNDIEG 159

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032574204   4 ILFDKDGTLIEFDHSWEKIGVRLvnsfldtfpvankeatLRKLGVvkdTISPD---SVMGsGSLDEIVHAFNDESGKDVS 80
Cdd:COG0637     5 VIFDMDGTLVDSEPLHARAWREA----------------FAELGI---DLTEEeyrRLMG-RSREDILRYLLEEYGLDLP 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032574204  81 -----KWTRDTSQALVDSREPEnnWIDGVYDMIQSLRYEGYKIGIVTSDSEKGMTQFLEETHSKDAFDLVISTEAHAAEK 155
Cdd:COG0637    65 eeelaARKEELYRELLAEEGLP--LIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGK 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032574204 156 PNPEV-LKPLfDHYDVKPEDVAIVGDTNNDMKTKVNAKLgLAIGVLSGIAKKEELVDADYVIET 218
Cdd:COG0637   143 PDPDIyLLAA-ERLGVDPEECVVFEDSPAGIRAAKAAGM-RVVGVPDGGTAEEELAGADLVVDD 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 1032574204   1 MEWILFDKDGTLIEFDHSWEKIGVRLVNSFLDtfpVANKEATLRKLGVVKDTISPDSVMGSGSLDEIVHAFNDESGKDVS 80
Cdd:COG1011     1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGL---LDEAEELAEAYRAIEYALWRRYERGEITFAELLRRLLEELGLDLA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032574204  81 KWTRDtsqALVDSREPENNWIDGVYDMIQSLRYEGYKIGIVTSDSEKGMTQFLEETHSKDAFDLVISTEAHAAEKPNPEV 160
Cdd:COG1011    78 EELAE---AFLAALPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEI 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032574204 161 LKPLFDHYDVKPEDVAIVGDT-NNDMKTkvnAK-LGL-AIGVLSGIAKKEELVDADYVIETAVSVPEVL 226
Cdd:COG1011   155 FELALERLGVPPEEALFVGDSpETDVAG---ARaAGMrTVWVNRSGEPAPAEPRPDYVISDLAELLELL 220

Haloacid dehalogenase-like hydrolase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032574204   4 ILFDKDGTLIEFDHSWEKIGVRLVNSFldTFPVANKEATLRKLGVvkdtispdsvmgsgSLDEIVHAFNDESGKDV--SK 81
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEF--GYGELSEEEILKFIGL--------------PLREIFRYLGVSEDEEEkiEF 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032574204  82 WTRDTSQALVDSR-EPennwIDGVYDMIQSLRYEGYKIGIVTSDSEKGMTQFLEETHSKDAFDLVISTEAHAAEKPNPEV 160
Cdd:pfam13419  65 YLRKYNEELHDKLvKP----YPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDP 140

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1032574204 161 LKPLFDHYDVKPEDVAIVGDTNNDMKTKVNA 191
Cdd:pfam13419 141 ILKALEQLGLKPEEVIYVGDSPRDIEAAKNA 171

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 1032574204 101 IDG---VYDMIQSLRYEGYKIGIVTSDSEKGMTQFLEETHSKDAFDLVISTEAHAAEKPNPEVLKPLFDHYDVKPEDVAI 177
Cdd:cd01427     6 LDGtllAVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLF 85

                          90       100
                  ....*....|....*....|...
gi 1032574204 178 VGDTNNDMKTkvnAKLGLAIGVL 200
Cdd:cd01427    86 VGDSENDIEA---ARAAGGRTVA 105

pyrophosphatase PpaX; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032574204   4 ILFDKDGTLIEFDhswEKIgvrlVNSFLDTFPVANKEATLRKlgvvkdtispDSVMGSG-SLDEIVHAFNDESGKDVSKW 82
Cdd:PRK13288    6 VLFDLDGTLINTN---ELI----ISSFLHTLKTYYPNQYKRE----------DVLPFIGpSLHDTFSKIDESKVEEMITT 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032574204  83 TRDTSQALVDSREPEnnwIDGVYDMIQSLRYEGYKIGIVTSDSEKGMTQFLEETHSKDAFDLVISTEAHAAEKPNPE-VL 161
Cdd:PRK13288   69 YREFNHEHHDELVTE---YETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPDPEpVL 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032574204 162 KPLfDHYDVKPEDVAIVGDTNNDMKTKVNAKLGLAiGVLSGIAKKEEL--VDADYVIET 218
Cdd:PRK13288  146 KAL-ELLGAKPEEALMVGDNHHDILAGKNAGTKTA-GVAWTIKGREYLeqYKPDFMLDK 202

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 1032574204 101 IDGVYDMIQSLRyEGYKIGIVTSdsekGMTQF----LEETHSKDAFDLVISTEAHAAEKPNPEVLKPLFDHYDVKPEDVA 176
Cdd:cd04305    11 LPGAKELLEELK-KGYKLGIITN----GPTEVqwekLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETL 85

                          90
                  ....*....|....*.
gi 1032574204 177 IVGDT-NNDMKTKVNA 191
Cdd:cd04305    86 MVGDSlESDILGAKNA 101

haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter sphaeroides 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 1032574204   4 ILFDKDGTLIefdhswekigvrlvnsflDTFP--VANKEATLRKLGVVkdTISPDSV---MGSGSLDEIVHAFNdESGKD 78
Cdd:cd07512     2 VIFDLDGTLI------------------DSAPdlHAALNAVLAAEGLA--PLSLAEVrsfVGHGAPALIRRAFA-AAGED 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032574204  79 VSKWTRDTS-QALVDSREP----ENNWIDGVYDMIQSLRYEGYKIGIVTSDSEKGMTQFLEETHSKDAFDLVISTEAHAA 153
Cdd:cd07512    61 LDGPLHDALlARFLDHYEAdppgLTRPYPGVIEALERLRAAGWRLAICTNKPEAPARALLSALGLADLFAAVVGGDTLPQ 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1032574204 154 EKPNPEVLKPLFDHYDVKPEDVAIVGDTNNDMKTKVNAKL 193
Cdd:cd07512   141 RKPDPAPLRAAIRRLGGDVSRALMVGDSETDAATARAAGV 180

Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGP; 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 1032574204   4 ILFDKDGTLiefdhswekigvrlVNSFLDTFPVANkeATLRKLGvvKDTISPDSV---MGSGSlDEIVH-AFNDESGKDV 79
Cdd:cd16417     2 VAFDLDGTL--------------VDSAPDLAEAAN--AMLAALG--LPPLPEETVrtwIGNGA-DVLVErALTGAREAEP 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032574204  80 SKWTRDTSQALVDSREPENNWI-----DGVYDMIQSLRYEGYKIGIVTSDSEKGMTQFLEETHSKDAFDLVISTEAHAAE 154
Cdd:cd16417    63 DEELFKEARALFDRHYAETLSVhshlyPGVKEGLAALKAQGYPLACVTNKPERFVAPLLEALGISDYFSLVLGGDSLPEK 142

                         170       180       190
                  ....*....|....*....|....*....|
gi 1032574204 155 KPNPEVLKPLFDHYDVKPEDVAIVGDTNND 184
Cdd:cd16417   143 KPDPAPLLHACEKLGIAPAQMLMVGDSRND 172

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 1032574204 104 VYDMIQSLRYEGYKIGIVtSDSEKGMTQFLEETHSKDAFDLVISTEAHAAEKPNPEVLKPLFDHYDVKPEDVAIVGDTNN 183
Cdd:cd16421    12 ILELLKALRQKGIKLAVL-SNKPNEAVQVLVEELFPGSFDFVLGEKEGIRRKPDPT*ALECAKVLGVPPDEVLYVGDSGV 90

                          90
                  ....*....|....*.
gi 1032574204 184 DMKTKVNAKLgLAIGV 199
Cdd:cd16421    91 DMQTARNAGM-DEIGV 105

noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including YjjG from E. coli and YfnB from B. subtilis. YjjG has been shown to act as a house-cleaning enzyme, cleaving nucleotides with non-canonical nucleotide bases. This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterized by three conserved sequence motifs. By virtue of an alpha helical domain in-between the first and second conserved motif, this family is a member of subfamily IA (TIGR01549).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032574204   2 EWILFDKDGTLIEFDHSwEKIGVRLVnsFLDT-FPVANKEATLRKlgVVKDTISPDSVMGSGSLDEIVHA--------FN 72
Cdd:TIGR02254   2 KTLLFDLDDTILDFQAA-EALALRLL--FEDQgIPLTEDMFAQYK--EINQGLWRAYEEGKITKDEVVNTrfsallkeYN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032574204  73 DESgkDVSKWTRDTSQALVDsrepENNWIDGVYDMIQSLRYEgYKIGIVTSDSEKGMTQFLEETHSKDAFDLVISTEAHA 152
Cdd:TIGR02254  77 TEA--DEALLNQKYLRFLEE----GHQLLPGAFELMENLQQK-FRLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDAG 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1032574204 153 AEKPNPEVlkplFDH-----YDVKPEDVAIVGDT-NNDMKTKVNAKL 193
Cdd:TIGR02254 150 IQKPDKEI----FNYalermPKFSKEEVLMIGDSlTADIKGGQNAGL 192

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 1032574204 100 WIDGVYDMIQSLRYEGYKIGIVTSDSEKGMTQFLEETH-SKDAFDLVISTEAHAAEKPNPEV----LKPLfdhyDVKPED 174
Cdd:cd07505    42 LKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGlLRGYFDVIVSGDDVERGKPAPDIyllaAERL----GVDPER 117

                  ....*....
gi 1032574204 175 VAIVGDTNN 183
Cdd:cd07505   118 CLVFEDSLA 126

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 1032574204   1 MEWILFDKDGTLIEFDhswekiGVRLVNSFldtfpvanKEATLRKLGVVKDTISPDSVM-----GSGSLDEIVHAFNDES 75
Cdd:cd02603     1 IRAVLFDFGGVLIDPD------PAAAVARF--------EALTGEPSEFVLDTEGLAGAFlelerGRITEEEFWEELREEL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032574204  76 GKDVSKwtrDTSQALVDSREPENnwiDGVYDMIQSLRYEGYKIGIVTSDSEKGMTQFLEETHSKDA-FDLVI-STEAHAA 153
Cdd:cd02603    67 GRPLSA---ELFEELVLAAVDPN---PEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLPRRGDlFDGVVeSCRLGVR 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032574204 154 eKPNPEVLKPLFDHYDVKPEDVAIVgDtnnDMKTKVNA--KLGL-AIGVLSGIAKKEEL 209
Cdd:cd02603   141 -KPDPEIYQLALERLGVKPEEVLFI-D---DREENVEAarALGIhAILVTDAEDALREL 194

N-acetylmuramic acid 6-phosphate phosphatase MupP;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032574204 102 DGVYDMIQSLRYEGYKIGIVTSdseKgMTQF----LEETHSKDAFDLVISTEAHAAEKPNPEVLKPLFDHYDVKPEDVAI 177
Cdd:PRK13222   96 PGVKETLAALKAAGYPLAVVTN---K-PTPFvaplLEALGIADYFSVVIGGDSLPNKKPDPAPLLLACEKLGLDPEEMLF 171

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1032574204 178 VGDTNNDMKTKVNAklGLA-IGVLSGIAKKE--ELVDADYVIETAVSVPEVL 226
Cdd:PRK13222  172 VGDSRNDIQAARAA--GCPsVGVTYGYNYGEpiALSEPDVVIDHFAELLPLL 221

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to uncharacterized Drosophila melanogaster rhythmically expressed gene 2 protein and human haloacid dehalogenase-like hydrolase domain-containing protein 3; 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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032574204 104 VYDMIQSLRYEGYKIGIVtSDSEKGMTQFLEETHSKDAFDLVISTEAHAAEKPNPEVLKPLFDHYDVKPEDVAIVGDT 181
Cdd:cd16415    12 AVETLKDLKEKGLKLAVV-SNFDRRLRELLEALGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPEEALHVGDD 88

dUMP phosphatase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032574204 102 DGVYDMIQSLrYEGYKIGIVTSdsekGMTQF----LEETHSKDAFDLVISTEAHAAEKPNPEVLKPLFDHYDVKP-EDVA 176
Cdd:PRK09449   98 PGAVELLNAL-RGKVKMGIITN----GFTELqqvrLERTGLRDYFDLLVISEQVGVAKPDVAIFDYALEQMGNPDrSRVL 172

                  ....*
gi 1032574204 177 IVGDT 181
Cdd:PRK09449  173 MVGDN 177

haloacid dehalogenase superfamily, subfamily IA hydrolase, TIGR01548; This model represents a small and phylogenetically curious clade of sequences. Sequences are found from Halobacterium (an archaeon), Nostoc and Synechococcus (cyanobacteria) and Phytophthora (a stramenophile eukaryote). 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. 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. All but the Halobacterium sequence currently found are annotated as "Imidazoleglycerol-phosphate dehydratase", however, the source of the annotation could not be traced and significant homology could not be found between any of these sequences and known IGPD's.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032574204 106 DMIQSLRYEGYKIGIVTSDSEKGMTQFLEETHSKDAFDLVISTEaHAAEKPNPEVLKPLFDHYDVKPEDVAIVGDTNNDM 185
Cdd:TIGR01548 113 GLLRELHRAPKGMAVVTGRPRKDAAKFLTTHGLEILFPVQIWME-DCPPKPNPEPLILAAKALGVEACHAAMVGDTVDDI 191

                  ....*.
gi 1032574204 186 KTKVNA 191
Cdd:TIGR01548 192 ITGRKA 197

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 1032574204   4 ILFDKDGTLIEFDHswekIGVRLVNSFLDTF---PVANKE-ATLRKLgvvkdtispdsvmgsgSLDEIVhafndeSGKDV 79
Cdd:cd04303     2 IIFDFDGTLADSFP----WFLSILNQLAARHgfkTVDEEEiEQLRQL----------------SSREIL------KQLGV 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032574204  80 SKW-----TRDTSQALVDsREPENNWIDGVYDMIQSLRYEGYKIGIVTSDSEKGMTQFLEETHskdafdlVISTEAHAAE 154
Cdd:cd04303    56 PLWklpliAKDFRRLMAE-AAPELALFPGVEDMLRALHARGVRLAVVSSNSEENIRRVLGPEE-------LISLFAVIEG 127

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032574204 155 KP---NPEVLKPLFDHYDVKPEDVAIVGDTNNDmktkVNA--KLGLAIGVLS-GIAKKEELVDA--DYVIET 218
Cdd:cd04303   128 SSlfgKAKKIRRVLRRTKITAAQVIYVGDETRD----IEAarKVGLAFAAVSwGYAKPEVLKALapDHMLED 195

phosphoglycolate phosphatase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032574204 103 GVYDMIQSLRYEGYKIGIVTSDSEKGMTQFLEETHSKDAFDLVISTEAHAAEKpnpEVLKPLFDHYDVKPEDVAIVGDTN 182
Cdd:PRK13225  146 GVADLLAQLRSRSLCLGILSSNSRQNIEAFLQRQGLRSLFSVVQAGTPILSKR---RALSQLVAREGWQPAAVMYVGDET 222

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1032574204 183 NDMKTKVNAKLgLAIGVLSGIAKKEELVDA--DYVIETAvsvPEVLKKYTQ 231
Cdd:PRK13225  223 RDVEAARQVGL-IAVAVTWGFNDRQSLVAAcpDWLLETP---SDLLQAVTQ 269

Haloacid dehalogenase superfamily, subfamily IA, variant 2 with 3rd motif like haloacid dehalogenase; 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 2 (this model) is distinctive of the type II haloacid dehalogenases, and nearly all of the sequences are also part of the HAD, type II equivalog model (TIGR01428). 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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032574204 106 DMIQSLRyegyKIGIVTSDSEKGMTQFLEETHSKDAFDLVISTEAHAAEKPNPEVLKPLFDHYDVKPEDVAIV 178
Cdd:TIGR01493  94 DSAAALA----RVAILSNASHWAFDQFAQQAGLPWYFDRAFSVDTVRAYKPDPVVYELVFDTVGLPPDRVLMV 162

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032574204 108 IQSLRYEGYKIGIVTSDSEKGMTQFLEETHSKDAFDLVISTEAHAAEKPNPEVLKPLFDHYDVKPEDV 175
Cdd:cd02588   100 LRRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAEDVRAYKPAPAVYELAAERLGVPPDEI 167

UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase and Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase; Escherichia coli UmpH/NagD is a ribonucleoside tri-, di-, and monophosphatase with a preference for purines, it shows peak activity with UMP and functions in UMP-degradation. It is also an effective phosphatase with AMP, GMP and CMP. Mycobacterium tuberculosis phosphatase, Rv1692 is a glycerol 3-phosphate phosphatase. Rv1692 is the final enzyme involved in glycerophospholipid recycling/catabolism. This 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 1032574204 155 KPNPEVLKPLFDHYDVKPEDVAIVGDT-NNDMKTKVNAKLGlAIGVLSGIAKKEELVD----ADYVIE 217
Cdd:cd07530   177 KPEPIMMRAALEKLGLKSEETLMVGDRlDTDIAAGIAAGID-TLLVLTGVTTREDLAKppyrPTYIVP 243