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        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241564 121 SQPFLRWARRKGLIVGLVSNAEyRYQEVILPSFGLSkAEWDFGVFSGIEGIEKPDPRIFTLALERAGnnIAPEEVLHIGD 200
Cdd:cd16415  12 AVETLKDLKEKGLKLAVVSNFD-RRLRELLEALGLD-DYFDFVVFSYEVGYEKPDPRIFQKALERLG--VSPEEALHVGD 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15241564 201 SMRKDYVPAKSIGMHALLVDRFKTEaakdwieagaIVLPDLVAVQQLLESD 251
Cdd:cd16415  88 DLKNDYLGARAVGWHALLVDREGAL----------HELPSLANLLERLLEL 128

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 15241564     9 LRCITVDVTGTLIAYKGELGDYYCMAAkaiglpcpDYKRVHEGFKLAYTDMAQKYPCFGFHAKMPNIVWWKTcvRDSFVK 88
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELA--------SEHPLAKAIVAAAEDLPIPVEDFTARLLLGKRDWLEE--LDILRG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241564    89 AGYEYDEETFEKIFRRIYSTFGSAAPYSVFQDSQPFLRWARRKGLIVGLVSNAEYRYQEVILPSFGLSKAeWDFGVFSGI 168
Cdd:pfam00702  71 LVETLEAEGLTVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDY-FDVVISGDD 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 15241564   169 EGIEKPDPRIFTLALERAGnnIAPEEVLHIGDSMRkDYVPAKSIG 213
Cdd:pfam00702 150 VGVGKPKPEIYLAALERLG--VKPEEVLMVGDGVN-DIPAAKAAG 191

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        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241564 121 SQPFLRWARRKGLIVGLVSNAEyRYQEVILPSFGLSkAEWDFGVFSGIEGIEKPDPRIFTLALERAGnnIAPEEVLHIGD 200
Cdd:cd16415  12 AVETLKDLKEKGLKLAVVSNFD-RRLRELLEALGLD-DYFDFVVFSYEVGYEKPDPRIFQKALERLG--VSPEEALHVGD 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15241564 201 SMRKDYVPAKSIGMHALLVDRFKTEaakdwieagaIVLPDLVAVQQLLESD 251
Cdd:cd16415  88 DLKNDYLGARAVGWHALLVDREGAL----------HELPSLANLLERLLEL 128

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 15241564     9 LRCITVDVTGTLIAYKGELGDYYCMAAkaiglpcpDYKRVHEGFKLAYTDMAQKYPCFGFHAKMPNIVWWKTcvRDSFVK 88
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELA--------SEHPLAKAIVAAAEDLPIPVEDFTARLLLGKRDWLEE--LDILRG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241564    89 AGYEYDEETFEKIFRRIYSTFGSAAPYSVFQDSQPFLRWARRKGLIVGLVSNAEYRYQEVILPSFGLSKAeWDFGVFSGI 168
Cdd:pfam00702  71 LVETLEAEGLTVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDY-FDVVISGDD 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 15241564   169 EGIEKPDPRIFTLALERAGnnIAPEEVLHIGDSMRkDYVPAKSIG 213
Cdd:pfam00702 150 VGVGKPKPEIYLAALERLG--VKPEEVLMVGDGVN-DIPAAKAAG 191

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 15241564 130 RKGLIVGLVSNAEYRYQEVILPSFGLSKaEWDFGVFSGIEGIEKPDPRIFTLALERAGnnIAPEEVLHIGDSMRKDYVPA 209
Cdd:cd04305  22 KKGYKLGIITNGPTEVQWEKLEQLGIHK-YFDHIVISEEVGVQKPNPEIFDYALNQLG--VKPEETLMVGDSLESDILGA 98

                ....*..
gi 15241564 210 KSIGMHA 216
Cdd:cd04305  99 KNAGIKT 105

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 15241564 122 QPFLRWARRKGLIVGLVSNAEYRYQEVILPSFGLSKaEWDFGVFSGIEGIEKPDPRIFTLALERAGnnIAPEEVLHIGDS 201
Cdd:cd01427  13 VELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGD-LFDGIIGSDGGGTPKPKPKPLLLLLLKLG--VDPEEVLFVGDS 89

                        90
                ....*....|....*...
gi 15241564 202 mRKDYVPAKSIGMHALLV 219
Cdd:cd01427  90 -ENDIEAARAAGGRTVAV 106

epoxide hydrolase N-terminal domain-like phosphatase; This model represents a small clade of sequences including C. elegans and mammalian sequences as well as a small number of bacteria. In eukaryotes, this domain exists as an N-terminal fusion to the soluble epoxide hydrolase enzyme and has recently been shown to be an active phosphatase, although the nature of the biological substrate is unclear. 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 (although the first motif is unusual in the replacement of the more common aspartate with glycine...). 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241564    77 WWKTCVRDsfvkagyEYDEETFEKIFRRIYS----TFGSAAPYSV---------FQDSQPFLRWARRKGLIVGLVSNAEY 143
Cdd:TIGR02247  49 WARTFERG-------ELTAEAFDGLFRHEYGlrlgHDVRIAPVFPllygentklRPSMMAAIKTLRAKGFKTACITNNFP 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241564   144 RYQEVILPSFGLS-KAEWDFGVFSGIEGIEKPDPRIFTLALERAGnnIAPEEVLHIgDSMRKDYVPAKSIGMHALLVDRF 222
Cdd:TIGR02247 122 TDHSAEEALLPGDiMALFDAVVESCLEGLRKPDPRIYQLMLERLG--VAPEECVFL-DDLGSNLKPAAALGITTIKVSDE 198

                  ..
gi 15241564   223 KT 224
Cdd:TIGR02247 199 EQ 200

Haloacid dehalogenase-like hydrolase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241564    83 RDSFVKAGYEYDEETFEKIFRRIYSTFGSAAPYSVFQDSQPFLRWARRKGLIVGLVSNAEYRYQEVILPSFGLSKAeWDF 162
Cdd:pfam13419  46 REIFRYLGVSEDEEEKIEFYLRKYNEELHDKLVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDY-FDV 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15241564   163 GVFSGIEGIEKPDPRIFTLALERagNNIAPEEVLHIGDSMRkDYVPAKSIGMHALLV 219
Cdd:pfam13419 125 IVGGDDVEGKKPDPDPILKALEQ--LGLKPEEVIYVGDSPR-DIEAAKNAGIKVIAV 178

HAD-hyrolase-like;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15241564   173 KPDPRIFTLALERAGnnIAPEEVLHIGDSMRKDYVPAKSIGMHALLVDR--FKTEAAKDWIEAGAIVLPDL 241
Cdd:pfam13242   4 KPNPGMLERALARLG--LDPERTVMIGDRLDTDILGAREAGARTILVLTgvTRPADLEKAPIRPDYVVDDL 72

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 15241564   123 PFLRWARRKGLIVGLVSNAeYRYQEVILPSFGLSKAEwDFGVFSGIEGIEKPDPRIFTLALERAGnnIAPEEVLHIGDS- 201
Cdd:TIGR01509  87 ALLEALRARGKKLALLTNS-PRAHKLVLALLGLRDLF-DVVIDSSDVGLGKPDPDIYLQALKALG--LEPSECVFVDDSp 162

                          90       100
                  ....*....|....*....|
gi 15241564   202 --MRkdyvPAKSIGMHALLV 219
Cdd:TIGR01509 163 agIE----AAKAAGMHTVGV 178

Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 15241564 173 KPDPRIFTLALERAGnnIAPEEVLHIGDSMRKDYVPAKSIGMHALLV 219
Cdd:COG0647 186 KPSPPIYELALERLG--VDPERVLMVGDRLDTDILGANAAGLDTLLV 230

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 15241564 123 PFLRWARRKGLIVGLVSNAEYRYQEVILPSFGlskaEWDFGVFSGI-EGIE-KPDPRIFTLALERAGnnIAPEEVLHIGD 200
Cdd:cd16421  14 ELLKALRQKGIKLAVLSNKPNEAVQVLVEELF----PGSFDFVLGEkEGIRrKPDPT*ALECAKVLG--VPPDEVLYVGD 87

                        90
                ....*....|....*....
gi 15241564 201 SmRKDYVPAKSIGMHALLV 219
Cdd:cd16421  88 S-GVDMQTARNAGMDEIGV 105

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 15241564 161 DFGVF-SGIE---GIE-----KPDPRIFTLALERAGnnIAPEEVLHIGDSMRKDYVPAKSIGMHALLVdrfKTEAAKDWI 231
Cdd:cd07509 151 DPGAFvTGLEyatGIKatvvgKPSPEFFLSALRSLG--VDPEEAVMIGDDLRDDVGGAQACGMRGILV---RTGKYRPSD 225

                        90
                ....*....|..
gi 15241564 232 EAGAIVLPDLVA 243
Cdd:cd07509 226 EKKPNVPPDLTA 237

dUMP phosphatase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241564  136 GLVSNAEYRYQEVILPSFGLSKAeWDFGVFSGIEGIEKPDPRIFTLALERAGnNIAPEEVLHIGDSMRKDYVPAKSIGMH 215
Cdd:PRK09449 114 GIITNGFTELQQVRLERTGLRDY-FDLLVISEQVGVAKPDVAIFDYALEQMG-NPDRSRVLMVGDNLHSDILGGINAGID 191

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
                ....*....|....*....|....*....|....*....|....*..
gi 15241564 173 KPDPRIFTLALERAGnnIAPEEVLHIGDSMRKDYVPAKSIGMHALLV 219
Cdd:cd07508 197 KPSPWLGELALEKFG--IDPERVLFVGDRLATDVLFGKACGFQTLLV 241

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p; This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and CMP. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241564 140 NAEYRYQEVILPSFGLSkaewdfGVFSGIEGIE------KPDPRIFTLALERAGnnIAPEEVLHIGDSMRkDYVPAKSIG 213
Cdd:cd02604 104 NASKNHAIRVLKRLGLA------DLFDGIFDIEyagpdpKPHPAAFEKAIREAG--LDPKRAAFFDDSIR-NLLAAKALG 174

                ....*...
gi 15241564 214 MHALLVDR 221
Cdd:cd02604 175 MKTVLVGP 182

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; 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 15241564 146 QEVILPSFGLSkaewDFgvFSGIEGIEKPDPRIFTLALERAGnnIAPEEVLHIGDSMRKDYVPAKSIGMHALLV 219
Cdd:cd07515  46 QEQKLARSGLS----DY--FDAVEVVSEKDPDTYRRVLSRYG--IGPERFVMVGNSLRSDILPVLAAGGWGVHI 111