inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP); LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. 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 568951595   2 SNPNCVVIADAGEAFSYQNMNRAFQVLmeLENPVLISLGKGRYYKETSGLMLDVGGYMKALEYACGIKAEVVGKPSPEFF 81
Cdd:cd07509  101 SDPNAVVIGDAGEHFNYQTLNRAFRLL--LDGAPLIALHKGRYYKRKDGLALDPGAFVTGLEYATGIKATVVGKPSPEFF 178

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951595  82 KSALQAIGVEAHQAIMIGDDIVGDVGGAQQCGMRALQVRTGKFRPGDEHHPEVQADGYVDNLAEAVDLLL 151
Cdd:cd07509  179 LSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRGILVRTGKYRPSDEKKPNVPPDLTADSFADAVDHIL 248

HAD-hyrolase-like;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568951595   72 VVGKPSPEFFKSALQAIGVEAHQAIMIGDDIVGDVGGAQQCGMRALQVRTGKFRPGDEHHPEVQADGYVDNLAEA 146
Cdd:pfam13242   1 VCGKPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILVLTGVTRPADLEKAPIRPDYVVDDLAEA 75

inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP); LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. 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 568951595   2 SNPNCVVIADAGEAFSYQNMNRAFQVLmeLENPVLISLGKGRYYKETSGLMLDVGGYMKALEYACGIKAEVVGKPSPEFF 81
Cdd:cd07509  101 SDPNAVVIGDAGEHFNYQTLNRAFRLL--LDGAPLIALHKGRYYKRKDGLALDPGAFVTGLEYATGIKATVVGKPSPEFF 178

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951595  82 KSALQAIGVEAHQAIMIGDDIVGDVGGAQQCGMRALQVRTGKFRPGDEHHPEVQADGYVDNLAEAVDLLL 151
Cdd:cd07509  179 LSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRGILVRTGKYRPSDEKKPNVPPDLTADSFADAVDHIL 248

HAD-hyrolase-like;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568951595   72 VVGKPSPEFFKSALQAIGVEAHQAIMIGDDIVGDVGGAQQCGMRALQVRTGKFRPGDEHHPEVQADGYVDNLAEA 146
Cdd:pfam13242   1 VCGKPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILVLTGVTRPADLEKAPIRPDYVVDDLAEA 75

Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural subclass of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The classes 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. Class I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Class II consists of sequences in which the capping domain is found between the second and third motifs. Class III sequences have no capping domain in iether of these positions. The Class IIA capping domain is predicted by PSI-PRED to consist of a mixed alpha-beta fold with the basic pattern: Helix-Helix-Helix-Sheet-Helix-Loop-Sheet-Helix-Sheet-Helix. Presently, this subfamily encompasses a single equivalog model (TIGR01452) for the eukaryotic phosphoglycolate phosphatase, as well as four hypothetical equivalogs covering closely related sequences (TIGR01456 and TIGR01458 in eukaryotes, TIGR01457 in gram positive bacteria and TIGR01459 in gram negative bacteria). The Escherishia coli NagD gene and the Bacillus subtilus AraL gene are members of this subfamily but are not members of the any of the presently defined equivalogs within it. NagD is part of the NAG operon responsible for N-acetylglucosamine metabolism. The function of this gene is unknown. Genes from several organisms have been annotated as NagD, or NagD-like. However, without data on the presence of other members of this pathway, (such as in the case of Yersinia pestis) these assignments should not be given great weight. The AraL gene is similar: it is part of the L-arabinose operon, but the function is unknown. A gene from Halobacterium has been annotated as AraL, but no other Ara operon genes have been annotated. Many of the genes in this subfamily have been annotated as "pNPPase" "4-nitrophenyl phosphatase" or "NPPase". These all refer to the same activity versus a common lab test compound used to determine phosphatase activity. There is no evidence that this activity is physiologically relevant. [Unknown function, Enzymes of unknown specificity]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951595    6 CVVIADAGEAFSYQNMNRAFQVLMELENPVLIS-------LGKGRYYketsglmLDVGGYMKALEYACGIKAEVVGKPSP 78
Cdd:TIGR01460 119 AAVIVGEPSDFSYDELAKAAYLLAEGDVPFIAAnrddlvrLGDGRFR-------PGAGAIAAGIKELSGREPTVVGKPSP 191

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 568951595   79 EFFKSALQAIGVEAHQ-AIMIGDDIVGDVGGAQQCGMRALQVRTG 122
Cdd:TIGR01460 192 AIYRAALNLLQARPERrDVMVGDNLRTDILGAKNAGFDTLLVLTG 236

haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this UmpH/NagD family include Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase , Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase, human PGP phosphoglycolate phosphatase, Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase, Bacillus AraL a putative sugar phosphatase, and Plasmodium falciparum para nitrophenyl phosphate phosphatase PNPase. 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 568951595   8 VIADAGEAFSYQNMNRAfqvLMELENP--VLISLGKGRYYK-ETSGLMLDVGGYMKALEYACGIKAEVVGKPSPEFFKSA 84
Cdd:cd07508  130 VIVGSDFKLNFAKLRKA---CRYLRNPgcLFIATAPDRIHPlKDGGPIPGTGAFAAAVEAATGRQPLVLGKPSPWLGELA 206

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568951595  85 LQAIGVEAHQAIMIGDDIVGDVGGAQQCGMRALQVRTGKFRPGD---EHHPEVQADGYVDNLAE 145
Cdd:cd07508  207 LEKFGIDPERVLFVGDRLATDVLFGKACGFQTLLVLTGVTTLEDlqaYIDHELVPDYYADSLAD 270

Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568951595  74 GKPSPEFFKSALQAIGVEAHQAIMIGDDIVgDVGGAQQCGMRALQVRTGkFRPGDEHHpEVQADGYVDNLAEAVDLLLK 152
Cdd:COG0546  139 AKPKPEPLLEALERLGLDPEEVLMVGDSPH-DIEAARAAGVPFIGVTWG-YGSAEELE-AAGADYVIDSLAELLALLAE 214

Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino acid transport and metabolism]; Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily is part of the Pathway/BioSystem: Histidine biosynthesis

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568951595  75 KPSPEFFKSALQAIGVEAHQAIMIGdDIVGDVGGAQQCGMRALQVRTGKfrpGDEHHPEVQADGYVDNLAEAVDLLLK 152
Cdd:COG0241  102 KPKPGMLLQAAERLGIDLSNSYMIG-DRLSDLQAAKAAGCKGILVLTGK---GAEELAEALPDTVADDLAEAVDYLLA 175

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
                 ....*....|....*....|....*....|....*....|....
gi 568951595  73 VGKPSPEFFKSALQAIGVEAHQAIMIGDDIVGDVGGAQQCGMRA 116
Cdd:cd04305   62 VQKPNPEIFDYALNQLGVKPEETLMVGDSLESDILGAKNAGIKT 105

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 568951595    6 CVVIADAGEAFSYQNMNRAFQVLMELENPVLISLGKgryYKETSGLMLDVGGYMKALEYACGIKAEVVGKPSPEFFKSAL 85
Cdd:pfam00702  88 LGVIALADELKLYPGAAEALKALKERGIKVAILTGD---NPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIYLAAL 164

                          90       100
                  ....*....|....*....|....*...
gi 568951595   86 QAIGVEAHQAIMIGDDIVgDVGGAQQCG 113
Cdd:pfam00702 165 ERLGVKPEEVLMVGDGVN-DIPAAKAAG 191

HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all eukaryotes. One sequence (GP|13344995) is called "Cat Eye Syndrome critical region protein 5" (CECR5). This gene has been cloned from a pericentromere region of human chromosome 22 believed to be the location of the gene or genes responsible for Cat Eye Syndrome. This is one of a number of candidate genes. The Schizosaccharomyces pombe sequence (EGAD|138276) is annotated as "phosphatidyl synthase," however this is due entirely to a C-terminal region of the protein (outside the region of similarity of this model) which is highly homologous to a family of CDP-alcohol phosphatidyltransferases. (Thus, the annotation of GP|4226073 from C. elegans as similar to phosphatidyl synthase, is a mistake as this gene does not contain the C-terminal portion). The physical connection of the phosphatidyl synthase and the HAD-superfamily hydrolase domain in S. pombe may, however, be an important clue to the substrate for the hydrolases in this equivalog.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951595   39 LGKGRYYKETSGLMLDVGGymKALEYacgikaEVVGKPSPEFFKSALQAIGVEA-------------HQAIMIGDDIVGD 105
Cdd:TIGR01456 205 FGQGAFRLLLERIYLELNG--KPLQY------YTLGKPTKLTYDFAEDVLIDWEkrlsgtkpstspfHALYMVGDNPASD 276

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568951595  106 VGGAQQCGMRALQVRTGKFRPGDEHHpEVQADGYVDNLAEAVDLLL 151
Cdd:TIGR01456 277 IIGAQNYGWFSCLVKTGVYNGGDDLK-ECKPTLIVNDVFDAVTKIL 321

UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium falciparum PNPase; Plasmodium falciparum para nitrophenyl phosphate phosphatase (PNPase) catalyzes the dephosphorylation of thiamine monophosphate to thiamine, other substrates on which its active are nucleotides, phosphorylated sugars, pyridoxal-5-phosphate, and paranitrophenyl phosphate. 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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951595   3 NPNCVVIA-DagEAFSYQNMNRAFQVLMeleNPVLISLGKGR--YYKETSGLML-DVGGYMKALEYACGIKAEVVGKPSP 78
Cdd:cd07532  135 DVGAVVVGrD--EHFSYPKLMKACNYLR---NPDVLFLATNMdaTFPGPVGRVIpGAGAMVAAIEAVSGRKPLVLGKPNP 209

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568951595  79 EFFKSALQAIGVEAHQAIMIGDDIVGDVGGAQQCGMRALQVRTG 122
Cdd:cd07532  210 QILNFLMKSGVIKPERTLMIGDRLKTDILFANNCGFQSLLVGTG 253

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
                 ....*....|....*....|....*....|....*....|....*..
gi 568951595  73 VGKPSPEFFKSALQAIGVEAHQAIMIgDDIVGDVGGAQQCGMRALQV 119
Cdd:cd02603  139 VRKPDPEIYQLALERLGVKPEEVLFI-DDREENVEAARALGIHAILV 184

N-acetylmuramic acid 6-phosphate phosphatase MupP;

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568951595  75 KPSPEFFKSALQAIGVEAHQAIMIGDDIVgDVGGAQQCGMRALQVRTGkFRPGdEHHPEVQADGYVDNLAEAVDLL 150
Cdd:PRK13222 149 KPDPAPLLLACEKLGLDPEEMLFVGDSRN-DIQAARAAGCPSVGVTYG-YNYG-EPIALSEPDVVIDHFAELLPLL 221

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 568951595  35 VLISlgkGRYYKETSGLM--LDVGGYMKALEYACGIkaeVVGKPSPEFFKSALQAIGVEAHQAIMIGDDiVGDVGGAQQC 112
Cdd:cd01427   27 AIVT---NRSREALRALLekLGLGDLFDGIIGSDGG---GTPKPKPKPLLLLLLKLGVDPEEVLFVGDS-ENDIEAARAA 99

                 ....*..
gi 568951595 113 GMRALQV 119
Cdd:cd01427  100 GGRTVAV 106

HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme. [Unknown function, Enzymes of unknown specificity]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951595    3 NPNCVVIADAGEAFSYQNMNRAFQVLMELENPVLI---SLGKGRYYKETSglmldVGGYMKALEYACGIKAEVVG----- 74
Cdd:TIGR01662  12 TDDVPYVSDEDERILYPEVPDALAELKEAGYKVVIvtnQSGIGRGYFSRS-----FSGRVARRLEELGVPIDILYacpgc 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568951595   75 -KPSPEFFKSAL-QAIGVEAHQAIMIGDDIVGDVGGAQQCGMRALQVRT 121
Cdd:TIGR01662  87 rKPKPGMFLEALkRFNEIDPEESVYVGDQDLTDLQAAKRVGLATILVAP 135

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568951595  75 KPSPEFFKSALQAIGVEAHQAIMIGDDIVgDVGGAQQCGMRALQVRTGkfrPGDEHHPEVQADGYVDNLAEAVDLL 150
Cdd:cd07512  142 KPDPAPLRAAIRRLGGDVSRALMVGDSET-DAATARAAGVPFVLVTFG---YRHAPVAELPHDAVFSDFDALPDLL 213

HAD-IIA family hydrolase;

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568951595  56 GGYMKALEYACGIKAEVVGKPSPEFFKSALQAIGVEAHQAIMIGDDIVGDVGGAQQCGMRALQVRTG 122
Cdd:PRK10444 155 GALCAGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILVLSG 221

Haloacid dehalogenase-like hydrolase;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568951595   75 KPSPEFFKSALQAIGVEAHQAIMIGDDIVgDVGGAQQCGMRALQV 119
Cdd:pfam13419 135 KPDPDPILKALEQLGLKPEEVIYVGDSPR-DIEAAKNAGIKVIAV 178

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
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568951595  70 AEVV--GKPSPEFFKSALQAIGVEAHQAIMIGDDIVGdVGGAQQCGMRALQVRT 121
Cdd:cd07505   91 GDDVerGKPAPDIYLLAAERLGVDPERCLVFEDSLAG-IEAAKAAGMTVVAVPD 143

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568951595  84 ALQAIGVEAHQAIMIGD---DIVgdvgGAQQCGMRALQVRTGkFrpGDEHhpEVQADGyVDNLAEAVDLLLKY 153
Cdd:cd04302  146 ALDTLGIAPEQAVMIGDrkhDII----GARANGIDSIGVLYG-Y--GSED--ELEEAG-ATYIVETPAELLEL 208

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
                 ....*....|....*....|....*....|....*....|....*....|
gi 568951595  68 IKAEVVG--KPSPEFFKSALQAIGVEAHQAIMIGDDIvGDVGGAQQCGMR 115
Cdd:cd02588  138 LSAEDVRayKPAPAVYELAAERLGVPPDEILHVASHA-WDLAGARALGLR 186

HAD-IIIA family hydrolase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568951595  75 KPSPEFFKSALQAIGVEAHQAIMIGDDIVGDVGGAQQCGMRALqVRTG-------KFRpgdEHHPEVQADGYVDNLAEAV 147
Cdd:PRK06769  93 KPSTGMLLQAAEKHGLDLTQCAVIGDRWTDIVAAAKVNATTIL-VRTGagydalhTYR---DKWAHIEPNYIAENFEDAV 168

                 ....*
gi 568951595 148 DLLLK 152
Cdd:PRK06769 169 NWILN 173