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Conserved domains on  [gi|392891718|ref|NP_001254295|]
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HAD family phosphatase [Caenorhabditis elegans]

Protein Classification

HAD-IA family hydrolase( domain architecture ID 711566)

haloacid dehalogenase (HAD)-IA family hydrolase containing a mannitol dehydrogenase domain, uses a nucleophilic aspartate in the phosphoryl transfer reaction; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

CATH:  3.30.1240.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|15337123|33940035|37786806

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD-1A3-hyp super family cl26186
epoxide hydrolase N-terminal domain-like phosphatase; This model represents a small clade of ...
 1-112 6.50e-63

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.


The actual alignment was detected with superfamily member TIGR02247:

Pssm-ID: 274054 [Multi-domain]  Cd Length: 211  Bit Score: 190.42  E-value: 6.50e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718    1 MQKTVEILHKKGFKTAMLTNNMFLDKEHKETRLPCDL-THFDEVVESCLEHLMKPDARFYHLVEKRLGVKPEEIVFLDDL 79
Cdd:TIGR02247  99 MMAAIKTLRAKGFKTACITNNFPTDHSAEEALLPGDImALFDAVVESCLEGLRKPDPRIYQLMLERLGVAPEECVFLDDL 178

                          90       100       110
                  ....*....|....*....|....*....|...
gi 392891718   80 HENIEAAEKLGWNTILVEDIEKAIHELEGFTKV 112
Cdd:TIGR02247 179 GSNLKPAAALGITTIKVSDEEQAIHDLEKATKL 211
 
Name Accession Description Interval E-value
HAD-1A3-hyp TIGR02247
epoxide hydrolase N-terminal domain-like phosphatase; This model represents a small clade of ...
 1-112 6.50e-63

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.


Pssm-ID: 274054 [Multi-domain]  Cd Length: 211  Bit Score: 190.42  E-value: 6.50e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718    1 MQKTVEILHKKGFKTAMLTNNMFLDKEHKETRLPCDL-THFDEVVESCLEHLMKPDARFYHLVEKRLGVKPEEIVFLDDL 79
Cdd:TIGR02247  99 MMAAIKTLRAKGFKTACITNNFPTDHSAEEALLPGDImALFDAVVESCLEGLRKPDPRIYQLMLERLGVAPEECVFLDDL 178

                          90       100       110
                  ....*....|....*....|....*....|...
gi 392891718   80 HENIEAAEKLGWNTILVEDIEKAIHELEGFTKV 112
Cdd:TIGR02247 179 GSNLKPAAALGITTIKVSDEEQAIHDLEKATKL 211
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 1-107 3.79e-45

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.


Pssm-ID: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 144.79  E-value: 3.79e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718   1 MQKTVEILHKKGFKTAMLTNNMFLDKEHKETRLPCDLTHFDEVVESCLEHLMKPDARFYHLVEKRLGVKPEEIVFLDDLH 80
Cdd:cd02603   89 MLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLPRRGDLFDGVVESCRLGVRKPDPEIYQLALERLGVKPEEVLFIDDRE 168

                         90       100
                 ....*....|....*....|....*..
gi 392891718  81 ENIEAAEKLGWNTILVEDIEKAIHELE 107
Cdd:cd02603  169 ENVEAARALGIHAILVTDAEDALRELA 195
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 4-98 6.27e-22

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 85.85  E-value: 6.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718   4 TVEILHKKGFKTAMLTNNMFLDKEHKETRLPCDlTHFDEVVESCLEHLMKPDARFYHLVEKRLGVKPEEIVFLDD-LHEN 82
Cdd:COG1011  101 LLEALKARGYRLALLTNGSAELQEAKLRRLGLD-DLFDAVVSSEEVGVRKPDPEIFELALERLGVPPEEALFVGDsPETD 179

                         90
                 ....*....|....*.
gi 392891718  83 IEAAEKLGWNTILVED 98
Cdd:COG1011  180 VAGARAAGMRTVWVNR 195
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 3-90 2.85e-11

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.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 57.21  E-value: 2.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718    3 KTVEILHKKGFKTAMLTNNmflDKEHKETRL-PCDLTH-FDEVVESCLEHLMKPDARFYHLVEKRLGVKPEEIVFLDDLH 80
Cdd:pfam00702 105 EALKALKERGIKVAILTGD---NPEAAEALLrLLGLDDyFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGV 181

                          90
                  ....*....|
gi 392891718   81 ENIEAAEKLG 90
Cdd:pfam00702 182 NDIPAAKAAG 191
PRK09456 PRK09456
?-D-glucose-1-phosphatase; Provisional
 4-98 3.62e-11

?-D-glucose-1-phosphatase; Provisional


Pssm-ID: 181872 [Multi-domain]  Cd Length: 199  Bit Score: 56.97  E-value: 3.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718   4 TVEILHK---KGFKTAMLTNNmfldkehkeTRLPCDL--THFDEVVESClEHLM--------KPDARFYHLVEKRLGVKP 70
Cdd:PRK09456  89 VIAIMHKlreQGHRVVVLSNT---------NRLHTTFwpEEYPEVRAAA-DHIYlsqdlgmrKPEARIYQHVLQAEGFSA 158

                         90       100
                 ....*....|....*....|....*...
gi 392891718  71 EEIVFLDDLHENIEAAEKLGWNTILVED 98
Cdd:PRK09456 159 ADAVFFDDNADNIEAANALGITSILVTD 186
 
Name Accession Description Interval E-value
HAD-1A3-hyp TIGR02247
epoxide hydrolase N-terminal domain-like phosphatase; This model represents a small clade of ...
 1-112 6.50e-63

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.


Pssm-ID: 274054 [Multi-domain]  Cd Length: 211  Bit Score: 190.42  E-value: 6.50e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718    1 MQKTVEILHKKGFKTAMLTNNMFLDKEHKETRLPCDL-THFDEVVESCLEHLMKPDARFYHLVEKRLGVKPEEIVFLDDL 79
Cdd:TIGR02247  99 MMAAIKTLRAKGFKTACITNNFPTDHSAEEALLPGDImALFDAVVESCLEGLRKPDPRIYQLMLERLGVAPEECVFLDDL 178

                          90       100       110
                  ....*....|....*....|....*....|...
gi 392891718   80 HENIEAAEKLGWNTILVEDIEKAIHELEGFTKV 112
Cdd:TIGR02247 179 GSNLKPAAALGITTIKVSDEEQAIHDLEKATKL 211
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 1-107 3.79e-45

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.


Pssm-ID: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 144.79  E-value: 3.79e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718   1 MQKTVEILHKKGFKTAMLTNNMFLDKEHKETRLPCDLTHFDEVVESCLEHLMKPDARFYHLVEKRLGVKPEEIVFLDDLH 80
Cdd:cd02603   89 MLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLPRRGDLFDGVVESCRLGVRKPDPEIYQLALERLGVKPEEVLFIDDRE 168

                         90       100
                 ....*....|....*....|....*..
gi 392891718  81 ENIEAAEKLGWNTILVEDIEKAIHELE 107
Cdd:cd02603  169 ENVEAARALGIHAILVTDAEDALRELA 195
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 1-96 6.18e-28

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]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 100.19  E-value: 6.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718    1 MQKTVEILHKKGFKTAMLTNNmflDKEHKETRLPCDL-THFDEVVESCLEHLMKPDARFYHLVEKRLGVKPEEIVFLDDL 79
Cdd:TIGR01509  85 VRALLEALRARGKKLALLTNS---PRAHKLVLALLGLrDLFDVVIDSSDVGLGKPDPDIYLQALKALGLEPSECVFVDDS 161

                          90
                  ....*....|....*..
gi 392891718   80 HENIEAAEKLGWNTILV 96
Cdd:TIGR01509 162 PAGIEAAKAAGMHTVGV 178
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 4-98 6.27e-22

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 85.85  E-value: 6.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718   4 TVEILHKKGFKTAMLTNNMFLDKEHKETRLPCDlTHFDEVVESCLEHLMKPDARFYHLVEKRLGVKPEEIVFLDD-LHEN 82
Cdd:COG1011  101 LLEALKARGYRLALLTNGSAELQEAKLRRLGLD-DLFDAVVSSEEVGVRKPDPEIFELALERLGVPPEEALFVGDsPETD 179

                         90
                 ....*....|....*.
gi 392891718  83 IEAAEKLGWNTILVED 98
Cdd:COG1011  180 VAGARAAGMRTVWVNR 195
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 3-90 2.85e-11

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.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 57.21  E-value: 2.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718    3 KTVEILHKKGFKTAMLTNNmflDKEHKETRL-PCDLTH-FDEVVESCLEHLMKPDARFYHLVEKRLGVKPEEIVFLDDLH 80
Cdd:pfam00702 105 EALKALKERGIKVAILTGD---NPEAAEALLrLLGLDDyFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGV 181

                          90
                  ....*....|
gi 392891718   81 ENIEAAEKLG 90
Cdd:pfam00702 182 NDIPAAKAAG 191
PRK09456 PRK09456
?-D-glucose-1-phosphatase; Provisional
 4-98 3.62e-11

?-D-glucose-1-phosphatase; Provisional


Pssm-ID: 181872 [Multi-domain]  Cd Length: 199  Bit Score: 56.97  E-value: 3.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718   4 TVEILHK---KGFKTAMLTNNmfldkehkeTRLPCDL--THFDEVVESClEHLM--------KPDARFYHLVEKRLGVKP 70
Cdd:PRK09456  89 VIAIMHKlreQGHRVVVLSNT---------NRLHTTFwpEEYPEVRAAA-DHIYlsqdlgmrKPEARIYQHVLQAEGFSA 158

                         90       100
                 ....*....|....*....|....*...
gi 392891718  71 EEIVFLDDLHENIEAAEKLGWNTILVED 98
Cdd:PRK09456 159 ADAVFFDDNADNIEAANALGITSILVTD 186
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 1-96 5.90e-11

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.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 54.71  E-value: 5.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718   1 MQKTVEILHKKGFKTAMLTNNMFLDKEHKETRLPCDLtHFDEVVESCLEHLMKPDARFYHLVEKRLGVKPEEIVFLDDLH 80
Cdd:cd01427   12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGD-LFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSE 90

                         90
                 ....*....|....*.
gi 392891718  81 ENIEAAEKLGWNTILV 96
Cdd:cd01427   91 NDIEAARAAGGRTVAV 106
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 10-94 4.80e-10

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.


Pssm-ID: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 52.54  E-value: 4.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718  10 KKGFKTAMLTNNMFLDKEHKETRLPCDlTHFDEVVESCLEHLMKPDARFYHLVEKRLGVKPEEIVFL-DDLHENIEAAEK 88
Cdd:cd04305   22 KKGYKLGIITNGPTEVQWEKLEQLGIH-KYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLMVgDSLESDILGAKN 100


                 ....*.
gi 392891718  89 LGWNTI 94
Cdd:cd04305  101 AGIKTV 106
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 2-115 3.71e-09

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.


Pssm-ID: 319852 [Multi-domain]  Cd Length: 128  Bit Score: 50.75  E-value: 3.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718   2 QKTVEILHKKGFKTAMLTNnmFldkehkETRLP------CDLTHFDEVVESCLEHLMKPDARFYHLVEKRLGVKPEEIVF 75
Cdd:cd16415   13 VETLKDLKEKGLKLAVVSN--F------DRRLRellealGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPEEALH 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 392891718  76 L-DDLHENIEAAEKLGWNTILVeDIEKAIHELEGFTKVKLI 115
Cdd:cd16415   85 VgDDLKNDYLGARAVGWHALLV-DREGALHELPSLANLLER 124
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 6-97 2.74e-08

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.


Pssm-ID: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 49.57  E-value: 2.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718   6 EILHKKGFKTAMLTN---NMFLDK-EHKETRLPcdlthFDEVVESCLEHLMKPDARFYHLVEKRLGVKPEEIVFL----- 76
Cdd:cd02588  101 RRLREAGYRLAILSNgspDLIEDVvANAGLRDL-----FDAVLSAEDVRAYKPAPAVYELAAERLGVPPDEILHVashaw 175

                         90       100
                 ....*....|....*....|.
gi 392891718  77 DdlhenIEAAEKLGWNTILVE 97
Cdd:cd02588  176 D-----LAGARALGLRTAWIN 191
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
1-96 2.13e-07

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 46.81  E-value: 2.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718    1 MQKTVEILHKKGFKTAMLTNNMFLDKEHKETRLPCDlTHFDEVVESCLEHLMKPDARFYHLVEKRLGVKPEEIVFLDDLH 80
Cdd:pfam13419  84 IKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLE-DYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVIYVGDSP 162

                          90
                  ....*....|....*.
gi 392891718   81 ENIEAAEKLGWNTILV 96
Cdd:pfam13419 163 RDIEAAKNAGIKVIAV 178
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
53-102 3.04e-07

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 47.03  E-value: 3.04e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 392891718  53 KPDARFYHLVEKRLGVKPEEIVFL-DDLHENIEAAEKLGWNTILV-------EDIEKA 102
Cdd:COG0647  186 KPSPPIYELALERLGVDPERVLMVgDRLDTDILGANAAGLDTLLVltgvttaEDLEAA 243
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
4-96 3.26e-07

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 46.46  E-value: 3.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718   4 TVEILHKKGFKTAMLTNnmfldKEHKETRLPCDLT----HFDEVVESCLEHLMKPDARFYHLVEKRLGVKPEEIVFLDDL 79
Cdd:COG0546   92 LLEALKARGIKLAVVTN-----KPREFAERLLEALglddYFDAIVGGDDVPPAKPKPEPLLEALERLGLDPEEVLMVGDS 166

                         90
                 ....*....|....*..
gi 392891718  80 HENIEAAEKLGWNTILV 96
Cdd:COG0546  167 PHDIEAARAAGVPFIGV 183
DREG-2 TIGR02252
REG-2-like, HAD superfamily (subfamily IA) hydrolase; This family of proteins includes ...
 2-95 3.30e-07

REG-2-like, HAD superfamily (subfamily IA) hydrolase; This family of proteins includes uncharacterized sequences from eukaryotes, cyanobacteria and Leptospira as well as the DREG-2 protein from Drosophila melanogaster which has been identified as a rhythmically (diurnally) regulated gene. This family is a member 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. This family is a member of subfamily 1A in which the cap domain consists of a predicted alpha helical bundle found in between the first and second catalytic motifs. A distinctive feature of this family is a conserved tandem pair of tryptophan residues in the cap domain. The most divergent sequences included within the scope of this model are from plants and have "FW" at this position instead. Most likely, these sequences, like the vast majority of HAD sequences, represent phosphatase enzymes.


Pssm-ID: 274056 [Multi-domain]  Cd Length: 203  Bit Score: 46.51  E-value: 3.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718    2 QKTVEILHKKGFKTAMLTNnmFldkehkETRLPCDL------THFDEVVESCLEHLMKPDARFYHLVEKRLGVKPEEIVF 75
Cdd:TIGR02252 111 IKLLKDLRERGLILGVISN--F------DSRLRGLLealgllEYFDFVVTSYEVGAEKPDPKIFQEALERAGISPEEALH 182

                          90       100
                  ....*....|....*....|.
gi 392891718   76 L-DDLHENIEAAEKLGWNTIL 95
Cdd:TIGR02252 183 IgDSLRNDYQGARAAGWRALL 203
Hydrolase_like pfam13242
HAD-hyrolase-like;
53-105 3.74e-07

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 44.14  E-value: 3.74e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392891718   53 KPDARFYHLVEKRLGVKPEEIVFL-DDLHENIEAAEKLGWNTILV-------EDIEKAIHE 105
Cdd:pfam13242   4 KPNPGMLERALARLGLDPERTVMIgDRLDTDILGAREAGARTILVltgvtrpADLEKAPIR 64
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 38-96 2.21e-05

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.


Pssm-ID: 319791 [Multi-domain]  Cd Length: 182  Bit Score: 41.08  E-value: 2.21e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392891718  38 THFDEVVesCLEHL---MKPDARFYHLVEKRLGVKPEEIVFLDDLHENIEAAEKLGWNTILV 96
Cdd:cd02604  121 DLFDGIF--DIEYAgpdPKPHPAAFEKAIREAGLDPKRAAFFDDSIRNLLAAKALGMKTVLV 180
HAD_EP cd01629
Enolase-phosphatase similar to human enolase-phosphatase E1 and and Xanthomonas oryzae pv. ...
 36-96 2.77e-05

Enolase-phosphatase similar to human enolase-phosphatase E1 and and Xanthomonas oryzae pv. Oryzae enolase-phosphatase Xep; Enolase-phosphatase E1 (also called MASA) is a bifunctional enolase- phosphatase which promotes the conversion of 2,3-diketo-5-methylthio-1-phosphopentane to 1,2-dihydroxy-3-keto-5-methylthiopentene anion (an aci-reductone) in the methionine salvage pathway. The catalytic reaction is carried out continuously by enolization and dephosphorylation, and the enolase activity cannot be classified as typical enzymatic enolization. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319768 [Multi-domain]  Cd Length: 204  Bit Score: 40.99  E-value: 2.77e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392891718  36 DLT-----HFDEVVESclehlmKPDARFYHLVEKRLGVKPEEIVFLDDLHENIEAAEKLGWNTILV 96
Cdd:cd01629  141 DLTplfsgYFDTTIGP------KREAASYRKIAEAIGVPPAEILFLSDVVAELDAAKEAGLQTVLL 200
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 1-96 1.42e-04

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.


Pssm-ID: 319799 [Multi-domain]  Cd Length: 201  Bit Score: 39.26  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718   1 MQKTVEILHKKGFKTAMLTNNmflDKEHKETRL-PCDLTHFDEVVESclEHLMKPDARFYHLVeKRLGVKPEEIVFLDDL 79
Cdd:cd04303   84 VEDMLRALHARGVRLAVVSSN---SEENIRRVLgPEELISLFAVIEG--SSLFGKAKKIRRVL-RRTKITAAQVIYVGDE 157

                         90
                 ....*....|....*..
gi 392891718  80 HENIEAAEKLGWNTILV 96
Cdd:cd04303  158 TRDIEAARKVGLAFAAV 174
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 2-98 1.93e-04

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.


Pssm-ID: 319808 [Multi-domain]  Cd Length: 143  Bit Score: 38.37  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718   2 QKTVEILHKKGFKTAMLTNNMFLDKEHKETRLPCDLTHFDEVVESCLEHLMKPDARFYHLVEKRLGVKPEE-IVFLDDLH 80
Cdd:cd07505   47 VELLDALKAAGIPVAVATSSSRRNVELLLLELGLLRGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERcLVFEDSLA 126

                         90
                 ....*....|....*...
gi 392891718  81 eNIEAAEKLGWNTILVED 98
Cdd:cd07505  127 -GIEAAKAAGMTVVAVPD 143
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 8-96 3.62e-04

2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Belongs to the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases (pfam00702), class (subfamily) I. Note that the Type I HAD enzymes have not yet been fully characterized, but clearly utilize a substantially different catalytic mechanism and are thus unlikely to be related.


Pssm-ID: 130495 [Multi-domain]  Cd Length: 198  Bit Score: 38.09  E-value: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718    8 LHKKGFKTAMLTN-----NMFLDKEHKetrlpcdlthfdevVESCLEHLM--------KPDARFYHLVEKRLGVKPEEIV 74
Cdd:TIGR01428 104 LKERGYRLAILSNgspamLKSLVKHAG--------------LDDPFDAVLsadavrayKPAPQVYQLALEALGVPPDEVL 169

                          90       100
                  ....*....|....*....|....*.
gi 392891718   75 FLD----DLHenieAAEKLGWNTILV 96
Cdd:TIGR01428 170 FVAsnpwDLG----GAKKFGFKTAWI 191
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
4-96 4.94e-04

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 37.87  E-value: 4.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718   4 TVEILHKKGFKTAMLTNnmfldkehKETRL--PC----DLTH-FDEVVesCLEHL--MKPDAR-FYHLVEKrLGVKPEEI 73
Cdd:PRK13222 101 TLAALKAAGYPLAVVTN--------KPTPFvaPLlealGIADyFSVVI--GGDSLpnKKPDPApLLLACEK-LGLDPEEM 169

                         90       100
                 ....*....|....*....|...
gi 392891718  74 VFLDDLHENIEAAEKLGWNTILV 96
Cdd:PRK13222 170 LFVGDSRNDIQAARAAGCPSVGV 192
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 53-96 6.17e-04

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.


Pssm-ID: 319812 [Multi-domain]  Cd Length: 248  Bit Score: 37.64  E-value: 6.17e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 392891718  53 KPDARFYHLVEKRLGVKPEEIVFL-DDLHENIEAAEKLGWNTILV 96
Cdd:cd07509  172 KPSPEFFLSALRSLGVDPEEAVMIgDDLRDDVGGAQACGMRGILV 216
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 4-96 8.29e-04

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.


Pssm-ID: 319854 [Multi-domain]  Cd Length: 212  Bit Score: 37.21  E-value: 8.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718   4 TVEILHKKGFKTAMLTNnmfldkehKETRLPCDL-------THFDEVV--ESCLEhlMKPD-ARFYHLVEKrLGVKPEEI 73
Cdd:cd16417   95 GLAALKAQGYPLACVTN--------KPERFVAPLlealgisDYFSLVLggDSLPE--KKPDpAPLLHACEK-LGIAPAQM 163

                         90       100
                 ....*....|....*....|...
gi 392891718  74 VFLDDLHENIEAAEKLGWNTILV 96
Cdd:cd16417  164 LMVGDSRNDILAARAAGCPSVGL 186
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 53-96 2.82e-03

subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p); This subfamily includes Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). GPP1p and GPP2p are involved in glycerol biosynthesis, GPP1 is induced in response to both anaerobic and hyperosmotic stress, GPP2 is induced in response to hyperosmotic or oxidative stress, and during diauxic shift; overexpression of DOG1 or DOG2 confers 2-deoxyglucose resistance. These belong to the beta-phosphoglucomutase-like family whose other 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), and Escherichia coli 6-phosphogluconate phosphatase YieH. 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.


Pssm-ID: 319829 [Multi-domain]  Cd Length: 205  Bit Score: 35.40  E-value: 2.82e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 392891718  53 KPDARFYHLVEKRLGVKPEEIVFLDDLHENIEAAEKLGWNTILV 96
Cdd:cd07527  132 KPDPEPYLLGAKLLGLDPSDCVVFEDAPAGIKAGKAAGARVVAV 175
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 3-96 3.02e-03

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. 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.


Pssm-ID: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 35.33  E-value: 3.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718   3 KTVEILHKKGFKTAMLTNNMFlDKEHKETRLPCDLTHFDEVV--ESCLEHlmKPDARFYHLVEKRLGVKPEEIVFLDDLH 80
Cdd:cd02616   87 ETLARLKSQGIKLGVVTTKLR-ETALKGLKLLGLDKYFDVIVggDDVTHH--KPDPEPVLKALELLGAEPEEALMVGDSP 163

                         90
                 ....*....|....*.
gi 392891718  81 ENIEAAEKLGWNTILV 96
Cdd:cd02616  164 HDILAGKNAGVKTVGV 179
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 4-96 6.89e-03

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 34.62  E-value: 6.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392891718   4 TVEILHKKGFKTAMLTNnmfldKEHKETRLPCDLT----HFDEVV--ESCLEHlmKPDARFYHLVEKRLGVKPEEIVFLD 77
Cdd:PRK13288  90 TLKTLKKQGYKLGIVTT-----KMRDTVEMGLKLTgldeFFDVVItlDDVEHA--KPDPEPVLKALELLGAKPEEALMVG 162

                         90
                 ....*....|....*....
gi 392891718  78 DLHENIEAAEKLGWNTILV 96
Cdd:PRK13288 163 DNHHDILAGKNAGTKTAGV 181
PTZ00445 PTZ00445
p36-lilke protein; Provisional
 59-97 7.89e-03

p36-lilke protein; Provisional


Pssm-ID: 240421  Cd Length: 219  Bit Score: 34.29  E-value: 7.89e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 392891718  59 YHL--VEKRLGVKPEEIVFLDDLHENIEAAEKLGWNTILVE 97
Cdd:PTZ00445 165 YHLkqVCSDFNVNPDEILFIDDDMNNCKNALKEGYIALHVT 205
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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