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Conserved domains on  [gi|503938244|ref|WP_014172238|]
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MULTISPECIES: glucose-1-phosphatase [Enterobacter]

Protein Classification

glucose-1-phosphatase( domain architecture ID 10013243)

glucose-1-phosphatase similar to Escherichia coli alpha-D-glucose 1-phosphate phosphatase YihX that catalyzes the dephosphorylation of alpha-D-glucose 1-phosphate (Glc1P) and, to a lesser extent, of other sugar phosphates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09456 PRK09456
?-D-glucose-1-phosphatase; Provisional
 1-199 1.93e-158

?-D-glucose-1-phosphatase; Provisional


:

Pssm-ID: 181872 [Multi-domain]  Cd Length: 199  Bit Score: 435.24  E-value: 1.93e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244   1 MLYIFDLGNVIVDIDFNRVLGAWSDFSRVPLATLKQSFAMGETFHQHERGEISDEEFAERLCHEMDVPLSYEQFSHGWQA 80
Cdd:PRK09456   1 MLYIFDLGNVIVDIDFNRVLGVWSDLSRVPLATLKKRFTMGEAFHQHERGEISDEAFAEALCHEMALSLSYEQFAHGWQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244  81 VFVAIRPDVIAIMHKLREQGHRVVVLSNTNRLHTTFWPDEYPEVQAAADKIYLSQEMGMRKPEARIYQAVLQAEGFTAAD 160
Cdd:PRK09456  81 VFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTTFWPEEYPEVRAAADHIYLSQDLGMRKPEARIYQHVLQAEGFSAAD 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 503938244 161 AVFFDDNADNIEGANQLGITSILVTGKETIPNYFAKQLC 199
Cdd:PRK09456 161 AVFFDDNADNIEAANALGITSILVTDKQTIPDYFAKVLC 199
 
Name Accession Description Interval E-value
PRK09456 PRK09456
?-D-glucose-1-phosphatase; Provisional
 1-199 1.93e-158

?-D-glucose-1-phosphatase; Provisional


Pssm-ID: 181872 [Multi-domain]  Cd Length: 199  Bit Score: 435.24  E-value: 1.93e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244   1 MLYIFDLGNVIVDIDFNRVLGAWSDFSRVPLATLKQSFAMGETFHQHERGEISDEEFAERLCHEMDVPLSYEQFSHGWQA 80
Cdd:PRK09456   1 MLYIFDLGNVIVDIDFNRVLGVWSDLSRVPLATLKKRFTMGEAFHQHERGEISDEAFAEALCHEMALSLSYEQFAHGWQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244  81 VFVAIRPDVIAIMHKLREQGHRVVVLSNTNRLHTTFWPDEYPEVQAAADKIYLSQEMGMRKPEARIYQAVLQAEGFTAAD 160
Cdd:PRK09456  81 VFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTTFWPEEYPEVRAAADHIYLSQDLGMRKPEARIYQHVLQAEGFSAAD 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 503938244 161 AVFFDDNADNIEGANQLGITSILVTGKETIPNYFAKQLC 199
Cdd:PRK09456 161 AVFFDDNADNIEAANALGITSILVTDKQTIPDYFAKVLC 199
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 4-189 1.19e-62

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: 192.56  E-value: 1.19e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244   4 IFDLGNVIVDIDFNRVLGAWSDFSRVPLATLKQSFAMGETFHQHERGEISDEEFAERLCHEMDVPLSYEQFSHGWQAVFV 83
Cdd:cd02603    5 LFDFGGVLIDPDPAAAVARFEALTGEPSEFVLDTEGLAGAFLELERGRITEEEFWEELREELGRPLSAELFEELVLAAVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244  84 aIRPDVIAIMHKLREQGHRVVVLSNTNRLHTTFWPDEYPEVQAAADKIYLSQEMGMRKPEARIYQAVLQAEGFTAADAVF 163
Cdd:cd02603   85 -PNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLPRRGDLFDGVVESCRLGVRKPDPEIYQLALERLGVKPEEVLF 163

                        170       180
                 ....*....|....*....|....*.
gi 503938244 164 FDDNADNIEGANQLGITSILVTGKET 189
Cdd:cd02603  164 IDDREENVEAARALGIHAILVTDAED 189
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 4-184 1.48e-41

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: 138.32  E-value: 1.48e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244    4 IFDLGNVIVDIDF-NRVLGAWSDFSRVPLATLKQSF-AMGETFHQHER---GEISDEEFAERLCHEMdvplsYEQFSHGW 78
Cdd:TIGR01509   3 LFDLDGVLVDTEFaIAKLINREELGLVPDELGVSAVgRLELALRRFKAqygRTISPEDAQLLYKQLF-----YEQIEEEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244   79 QAvfvAIRPDVIAIMHKLREQGHRVVVLSNTNRLHTTFwpDEYPEVQAAADKIYLSQEMGMRKPEARIYQAVLQAEGFTA 158
Cdd:TIGR01509  78 KL---KPLPGVRALLEALRARGKKLALLTNSPRAHKLV--LALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLEP 152

                         170       180
                  ....*....|....*....|....*.
gi 503938244  159 ADAVFFDDNADNIEGANQLGITSILV 184
Cdd:TIGR01509 153 SECVFVDDSPAGIEAAKAAGMHTVGV 178
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 1-185 2.48e-39

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: 134.00  E-value: 2.48e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244   1 MLYIFDLGNVIVDIDFNRVLGAWSDFSRVPLATLKQSFA------MGETFHQHERGEISDEEFAERLCHEMDVPLS---Y 71
Cdd:COG1011    2 KAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAeayraiEYALWRRYERGEITFAELLRRLLEELGLDLAeelA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244  72 EQFSHGWQAvFVAIRPDVIAIMHKLREQGHRVVVLSNTNRLHTTFWPDEYPeVQAAADKIYLSQEMGMRKPEARIYQAVL 151
Cdd:COG1011   82 EAFLAALPE-LVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLG-LDDLFDAVVSSEEVGVRKPDPEIFELAL 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 503938244 152 QAEGFTAADAVFFDDNAD-NIEGANQLGITSILVT 185
Cdd:COG1011  160 ERLGVPPEEALFVGDSPEtDVAGARAAGMRTVWVN 194
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 2-178 8.31e-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: 58.37  E-value: 8.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244    2 LYIFDLGNVIVDI-----DFNRVLGAWSDFSRVPLATLKQSFAMGETFHQH--------ERGEISDEEFAERLCHEMDVP 68
Cdd:pfam00702   3 AVVFDLDGTLTDGepvvtEAIAELASEHPLAKAIVAAAEDLPIPVEDFTARlllgkrdwLEELDILRGLVETLEAEGLTV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244   69 LSYEQFSHGWQAVFVAIRPDVIAIMHKLREQGHRVVVLSNTNRLHTTfWPDEYPEVQAAADKIYLSQEMGMRKPEARIYQ 148
Cdd:pfam00702  83 VLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAE-ALLRLLGLDDYFDVVISGDDVGVGKPKPEIYL 161

                         170       180       190
                  ....*....|....*....|....*....|
gi 503938244  149 AVLQAEGFTAADAVFFDDNADNIEGANQLG 178
Cdd:pfam00702 162 AALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
 
Name Accession Description Interval E-value
PRK09456 PRK09456
?-D-glucose-1-phosphatase; Provisional
 1-199 1.93e-158

?-D-glucose-1-phosphatase; Provisional


Pssm-ID: 181872 [Multi-domain]  Cd Length: 199  Bit Score: 435.24  E-value: 1.93e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244   1 MLYIFDLGNVIVDIDFNRVLGAWSDFSRVPLATLKQSFAMGETFHQHERGEISDEEFAERLCHEMDVPLSYEQFSHGWQA 80
Cdd:PRK09456   1 MLYIFDLGNVIVDIDFNRVLGVWSDLSRVPLATLKKRFTMGEAFHQHERGEISDEAFAEALCHEMALSLSYEQFAHGWQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244  81 VFVAIRPDVIAIMHKLREQGHRVVVLSNTNRLHTTFWPDEYPEVQAAADKIYLSQEMGMRKPEARIYQAVLQAEGFTAAD 160
Cdd:PRK09456  81 VFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTTFWPEEYPEVRAAADHIYLSQDLGMRKPEARIYQHVLQAEGFSAAD 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 503938244 161 AVFFDDNADNIEGANQLGITSILVTGKETIPNYFAKQLC 199
Cdd:PRK09456 161 AVFFDDNADNIEAANALGITSILVTDKQTIPDYFAKVLC 199
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 4-189 1.19e-62

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: 192.56  E-value: 1.19e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244   4 IFDLGNVIVDIDFNRVLGAWSDFSRVPLATLKQSFAMGETFHQHERGEISDEEFAERLCHEMDVPLSYEQFSHGWQAVFV 83
Cdd:cd02603    5 LFDFGGVLIDPDPAAAVARFEALTGEPSEFVLDTEGLAGAFLELERGRITEEEFWEELREELGRPLSAELFEELVLAAVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244  84 aIRPDVIAIMHKLREQGHRVVVLSNTNRLHTTFWPDEYPEVQAAADKIYLSQEMGMRKPEARIYQAVLQAEGFTAADAVF 163
Cdd:cd02603   85 -PNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLELLPRRGDLFDGVVESCRLGVRKPDPEIYQLALERLGVKPEEVLF 163

                        170       180
                 ....*....|....*....|....*.
gi 503938244 164 FDDNADNIEGANQLGITSILVTGKET 189
Cdd:cd02603  164 IDDREENVEAARALGIHAILVTDAED 189
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 4-184 1.48e-41

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: 138.32  E-value: 1.48e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244    4 IFDLGNVIVDIDF-NRVLGAWSDFSRVPLATLKQSF-AMGETFHQHER---GEISDEEFAERLCHEMdvplsYEQFSHGW 78
Cdd:TIGR01509   3 LFDLDGVLVDTEFaIAKLINREELGLVPDELGVSAVgRLELALRRFKAqygRTISPEDAQLLYKQLF-----YEQIEEEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244   79 QAvfvAIRPDVIAIMHKLREQGHRVVVLSNTNRLHTTFwpDEYPEVQAAADKIYLSQEMGMRKPEARIYQAVLQAEGFTA 158
Cdd:TIGR01509  78 KL---KPLPGVRALLEALRARGKKLALLTNSPRAHKLV--LALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLEP 152

                         170       180
                  ....*....|....*....|....*.
gi 503938244  159 ADAVFFDDNADNIEGANQLGITSILV 184
Cdd:TIGR01509 153 SECVFVDDSPAGIEAAKAAGMHTVGV 178
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 1-185 2.48e-39

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: 134.00  E-value: 2.48e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244   1 MLYIFDLGNVIVDIDFNRVLGAWSDFSRVPLATLKQSFA------MGETFHQHERGEISDEEFAERLCHEMDVPLS---Y 71
Cdd:COG1011    2 KAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAeayraiEYALWRRYERGEITFAELLRRLLEELGLDLAeelA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244  72 EQFSHGWQAvFVAIRPDVIAIMHKLREQGHRVVVLSNTNRLHTTFWPDEYPeVQAAADKIYLSQEMGMRKPEARIYQAVL 151
Cdd:COG1011   82 EAFLAALPE-LVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLG-LDDLFDAVVSSEEVGVRKPDPEIFELAL 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 503938244 152 QAEGFTAADAVFFDDNAD-NIEGANQLGITSILVT 185
Cdd:COG1011  160 ERLGVPPEEALFVGDSPEtDVAGARAAGMRTVWVN 194
HAD-1A3-hyp TIGR02247
epoxide hydrolase N-terminal domain-like phosphatase; This model represents a small clade of ...
 4-189 8.22e-20

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: 82.95  E-value: 8.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244    4 IFDLGNVIVDIDFnrVLGAWSDFSRVPLA--TLKQSFAMGETFHQH----ERGEISDEEFAERLCHEM------DVPLSy 71
Cdd:TIGR02247   6 IFDFGGVLLPSPG--VMRRWETERGLPGLkdFIVTVNITGPDFNPWartfERGELTAEAFDGLFRHEYglrlghDVRIA- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244   72 eQFSHGWQAVFVAIRPDVIAIMHKLREQGHRVVVLsnTNRLHT------TFWPDEypeVQAAADKIYLSQEMGMRKPEAR 145
Cdd:TIGR02247  83 -PVFPLLYGENTKLRPSMMAAIKTLRAKGFKTACI--TNNFPTdhsaeeALLPGD---IMALFDAVVESCLEGLRKPDPR 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 503938244  146 IYQAVLQAEGFTAADAVFFDDNADNIEGANQLGITSILVTGKET 189
Cdd:TIGR02247 157 IYQLMLERLGVAPEECVFLDDLGSNLKPAAALGITTIKVSDEEQ 200
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 2-178 8.31e-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: 58.37  E-value: 8.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244    2 LYIFDLGNVIVDI-----DFNRVLGAWSDFSRVPLATLKQSFAMGETFHQH--------ERGEISDEEFAERLCHEMDVP 68
Cdd:pfam00702   3 AVVFDLDGTLTDGepvvtEAIAELASEHPLAKAIVAAAEDLPIPVEDFTARlllgkrdwLEELDILRGLVETLEAEGLTV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244   69 LSYEQFSHGWQAVFVAIRPDVIAIMHKLREQGHRVVVLSNTNRLHTTfWPDEYPEVQAAADKIYLSQEMGMRKPEARIYQ 148
Cdd:pfam00702  83 VLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAE-ALLRLLGLDDYFDVVISGDDVGVGKPKPEIYL 161

                         170       180       190
                  ....*....|....*....|....*....|
gi 503938244  149 AVLQAEGFTAADAVFFDDNADNIEGANQLG 178
Cdd:pfam00702 162 AALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 89-184 3.50e-10

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: 55.09  E-value: 3.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244  89 VIAIMHKLREQGHRVVVLSNTNRLHTTFWPDEYpEVQAAADKIYLSQEMGMRKPEARIYQAVLQAEGFTAADAVFFDDNA 168
Cdd:cd01427   12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKL-GLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSE 90

                         90
                 ....*....|....*.
gi 503938244 169 DNIEGANQLGITSILV 184
Cdd:cd01427   91 NDIEAARAAGGRTVAV 106
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 47-193 5.97e-10

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: 56.51  E-value: 5.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244  47 HERGEISDEEFAERLCHEMdvplsyeqfsHGWQAvFvairPDVIAIMHKLREQGHRVVVLSNTNrlhttfwPDEYPEVQA 126
Cdd:cd02588   69 AELGLELDESDLDELGDAY----------LRLPP-F----PDVVAGLRRLREAGYRLAILSNGS-------PDLIEDVVA 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503938244 127 AA------DKIYLSQEMGMRKPEARIYQAVLQAEGFTAADAVFFDDNADNIEGANQLGITSILVTGKETIPNY 193
Cdd:cd02588  127 NAglrdlfDAVLSAEDVRAYKPAPAVYELAAERLGVPPDEILHVASHAWDLAGARALGLRTAWINRPGEVPDP 199
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
2-185 1.39e-09

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 55.32  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244   2 LYIFDLGNVIVDID------FNRVLgAWSDFSRVPLATLKQSFAMGetfhqhergeisDEEFAERLCHEmDVPLSYEQFS 75
Cdd:COG0546    3 LVLFDLDGTLVDSApdiaaaLNEAL-AELGLPPLDLEELRALIGLG------------LRELLRRLLGE-DPDEELEELL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244  76 HGWQAVFVAIR-------PDVIAIMHKLREQGHRVVVLSNTNR------LHTTFWpDEYPEVQAAADkiylsqEMGMRKP 142
Cdd:COG0546   69 ARFRELYEEELldetrlfPGVRELLEALKARGIKLAVVTNKPRefaerlLEALGL-DDYFDAIVGGD------DVPPAKP 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 503938244 143 EARIYQAVLQAEGFTAADAVFFDDNADNIEGANQLGITSILVT 185
Cdd:COG0546  142 KPEPLLEALERLGLDPEEVLMVGDSPHDIEAARAAGVPFIGVT 184
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 21-184 1.58e-08

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: 52.34  E-value: 1.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244   21 GAWSDFSRVPLATLKQSFAmgetfhqhERGEISDEEFAERLCHEMdvplsyeqfsHGWQAvfvaiRPDVIAIMHKLREQG 100
Cdd:TIGR01428  52 GPYKDFWDLTREALRYLLG--------RLGLEDDESAADRLAEAY----------LRLPP-----HPDVPAGLRALKERG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244  101 HRVVVLSNTNrlhttfwPDEYPEVQAAA------DKIYLSQEMGMRKPEARIYQAVLQAEGFTAADAVFFDDNADNIEGA 174
Cdd:TIGR01428 109 YRLAILSNGS-------PAMLKSLVKHAglddpfDAVLSADAVRAYKPAPQVYQLALEALGVPPDEVLFVASNPWDLGGA 181

                         170
                  ....*....|
gi 503938244  175 NQLGITSILV 184
Cdd:TIGR01428 182 KKFGFKTAWI 191
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 87-182 5.28e-08

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: 49.08  E-value: 5.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244  87 PDVIAIMHKLREqGHRVVVLSN------TNRLHTTfwpdeypEVQAAADKIYLSQEMGMRKPEARIYQAVLQAEGFTAAD 160
Cdd:cd04305   12 PGAKELLEELKK-GYKLGIITNgptevqWEKLEQL-------GIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEE 83

                         90       100
                 ....*....|....*....|...
gi 503938244 161 AVFFDDNADN-IEGANQLGITSI 182
Cdd:cd04305   84 TLMVGDSLESdILGAKNAGIKTV 106
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
4-195 2.68e-07

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 49.05  E-value: 2.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244   4 IFDLGNVIVDidfnrvlgawsdFSRVPLATLKQSFA-MGETFHQHERGEI---SDEEFAERLCHEMDVPLSYEQFSHGWQ 79
Cdd:COG0637    6 IFDMDGTLVD------------SEPLHARAWREAFAeLGIDLTEEEYRRLmgrSREDILRYLLEEYGLDLPEEELAARKE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244  80 AVF--------VAIRPDVIAIMHKLREQGHRVVVLSNTNR-----LHTTFWPDEYPEVQAAADkiylsqEMGMRKPEARI 146
Cdd:COG0637   74 ELYrellaeegLPLIPGVVELLEALKEAGIKIAVATSSPRenaeaVLEAAGLLDYFDVIVTGD------DVARGKPDPDI 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 503938244 147 YQAVLQAEGFTAADAVFFDDNADNIEGANQLGITSILVTGKETIPNYFA 195
Cdd:COG0637  148 YLLAAERLGVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGGTAEEELA 196
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
3-184 4.15e-07

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 47.96  E-value: 4.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244    3 YIFDLGNVIVDidfnrvlgawsdfsRVPLatLKQSFAmgETFHQHERGEISDEEFA-----------ERLCHEMDVPLSY 71
Cdd:pfam13419   1 IIFDFDGTLLD--------------TEEL--IIKSFN--YLLEEFGYGELSEEEILkfiglplreifRYLGVSEDEEEKI 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244   72 EQFSHGWQAVF----VAIRPDVIAIMHKLREQGHRVVVLSNTNR-----------LHTTFwpdeypevqaaaDKIYLSQE 136
Cdd:pfam13419  63 EFYLRKYNEELhdklVKPYPGIKELLEELKEQGYKLGIVTSKSRenveeflkqlgLEDYF------------DVIVGGDD 130

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 503938244  137 MGMRKPEARIYQAVLQAEGFTAADAVFFDDNADNIEGANQLGITSILV 184
Cdd:pfam13419 131 VEGKKPDPDPILKALEQLGLKPEEVIYVGDSPRDIEAAKNAGIKVIAV 178
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 2-178 4.41e-07

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 47.78  E-value: 4.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244    2 LYIFDLGNVIVDIDFnrvlgawsdfsrVPLAtlkqsfAMGETFHQHERGEISDEEF------AERLCHEMDVPLSYEQFS 75
Cdd:TIGR01549   1 AILFDIDGTLVDIKF------------AIRR------AFPQTFEEFGLDPASFKALkqagglAEEEWYRIATSALEELQG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244   76 HGWQAVFV--AIRPDVIAIMHKLREQGHRVVVLSNTN--------RLHTTFWPDEYpevqaaadkIYLSQEMGmRKPEAR 145
Cdd:TIGR01549  63 RFWSEYDAeeAYIRGAADLLARLKSAGIKLGIISNGSlraqklllRLFGLGDYFEL---------ILVSDEPG-SKPEPE 132

                         170       180       190
                  ....*....|....*....|....*....|...
gi 503938244  146 IYQAVLQAEGfTAADAVFFDDNADNIEGANQLG 178
Cdd:TIGR01549 133 IFLAALESLG-VPPEVLHVGDNLNDIEGARNAG 164
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 141-184 5.09e-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: 42.24  E-value: 5.09e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 503938244 141 KPEARIYQAVLQAEGFTAADAVFFDDNADNIEGANQLGITSILV 184
Cdd:cd02604  137 KPHPAAFEKAIREAGLDPKRAAFFDDSIRNLLAAKALGMKTVLV 180
Acid_PPase pfam12689
Acid Phosphatase; This family contains phosphatase enzymes and other proteins of the HAD ...
 87-186 5.92e-05

Acid Phosphatase; This family contains phosphatase enzymes and other proteins of the HAD superfamily. It includes MDP-1 which is a eukaryotic magnesium-dependent acid phosphatase.


Pssm-ID: 372256  Cd Length: 169  Bit Score: 41.83  E-value: 5.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244   87 PDVIAIMHKLREQGHRVVVLSNTNR-------LHTTFWPDEyPEVQAAADKIYLSQEMGmRKPEARIYQAVLQAEGFTAA 159
Cdd:pfam12689  48 PDVPSILQELKTRGVTLAAASRTDApdwarelLKLLHINDG-PGDTVPAIDYFDDLEIY-PGSKTKHFTKILKKSGIPYS 125

                          90       100
                  ....*....|....*....|....*..
gi 503938244  160 DAVFFDDNADNIEGANQLGITSILVTG 186
Cdd:pfam12689 126 DMLFFDDESRNIDVVSRLGVTFVLVPD 152
PRK14988 PRK14988
GMP/IMP nucleotidase; Provisional
 83-179 6.73e-05

GMP/IMP nucleotidase; Provisional


Pssm-ID: 237882 [Multi-domain]  Cd Length: 224  Bit Score: 42.01  E-value: 6.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244  83 VAIRPDVIAIMHKLREQGHRVVVLSNTNRlHTTFWPDEYPEVQAAADKIYLSQEMGMRKPEARIYQAVLQAEGFTAADAV 162
Cdd:PRK14988  92 AVLREDTVPFLEALKASGKRRILLTNAHP-HNLAVKLEHTGLDAHLDLLLSTHTFGYPKEDQRLWQAVAEHTGLKAERTL 170

                         90
                 ....*....|....*..
gi 503938244 163 FFDDNADNIEGANQLGI 179
Cdd:PRK14988 171 FIDDSEPILDAAAQFGI 187
Hydrolase_like pfam13242
HAD-hyrolase-like;
139-187 8.18e-05

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 39.52  E-value: 8.18e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 503938244  139 MRKPEARIYQAVLQAEGFTAADAVFF-DDNADNIEGANQLGITSILV-TGK 187
Cdd:pfam13242   2 CGKPNPGMLERALARLGLDPERTVMIgDRLDTDILGAREAGARTILVlTGV 52
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
76-169 2.98e-04

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 40.48  E-value: 2.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244  76 HGWQAVfvairPDVIAIMHKLREQGHRVVVLSNTnrlhTTFWPDEYPE------VQAAADKIYLS-----QEMGMRKPEA 144
Cdd:COG0647   21 RGDEPI-----PGAVEALARLRAAGKPVLFLTNN----SSRTPEDVAEklrrlgIPVAEDEIVTSgdataAYLAERHPGA 91

                         90       100       110
                 ....*....|....*....|....*....|..
gi 503938244 145 RIY-------QAVLQAEGFTAADavffDDNAD 169
Cdd:COG0647   92 RVYvigeeglREELEEAGLTLVD----DEEPD 119
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 59-186 4.31e-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: 39.14  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244  59 ERLCHEM--DVPLSYEQFSHGWQAVFVAIRPDVIAIMHKLREQGHRVVVLSNTNRLHTTFWPDEYPEVQAAADKIYLSQE 136
Cdd:cd07505   14 EPLHRQAwqLLERKNALLLELIASEGLKLKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLRGYFDVIVSGDD 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 503938244 137 MGMRKPEARIYQAVLQAEGFTAADAVFFDDNADNIEGANQLGITSILVTG 186
Cdd:cd07505   94 VERGKPAPDIYLLAAERLGVDPERCLVFEDSLAGIEAAKAAGMTVVAVPD 143
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 87-184 4.50e-04

Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the uncharacterized protein Bacillus subtilis YqeG; 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: 319853 [Multi-domain]  Cd Length: 108  Bit Score: 38.40  E-value: 4.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244  87 PDVIAIMHKLREQGHRVVVLSNTnrlhttfWPDEYPEVQAAADKIYLSqemGMRKPEARIYQAVLQAEGFTA------AD 160
Cdd:cd16416   20 PEVKAWLADLKEAGIKVVLVSNN-------NERRVAKVIEKLDLPFVA---RAGKPRPRAFRRALKEMDLPPeqvamvGD 89

                         90       100
                 ....*....|....*....|....
gi 503938244 161 AVFFDdnadnIEGANQLGITSILV 184
Cdd:cd16416   90 QLFTD-----ILGGNRAGLYTILV 108
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 85-185 1.10e-03

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]


Pssm-ID: 273742 [Multi-domain]  Cd Length: 135  Bit Score: 37.77  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244   85 IRPDVIAIMHKLREQGHRVVVLSNTNRLHTTFWPDEYP--------EVQAAADKIYLSQemGMRKPEARIYQAVL-QAEG 155
Cdd:TIGR01662  26 LYPEVPDALAELKEAGYKVVIVTNQSGIGRGYFSRSFSgrvarrleELGVPIDILYACP--GCRKPKPGMFLEALkRFNE 103

                          90       100       110
                  ....*....|....*....|....*....|.
gi 503938244  156 FTAADAVFFDDNADN-IEGANQLGITSILVT 185
Cdd:TIGR01662 104 IDPEESVYVGDQDLTdLQAAKRVGLATILVA 134
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 2-111 1.87e-03

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 37.89  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244   2 LYIFDLGNVIVDIDfnrVLGAWSDF----SRVPLATLKQSFAmgETFHQHERGEISDEEFAER---LCHEMDVPlSYEQF 74
Cdd:COG0560    5 LAVFDLDGTLIAGE---SIDELARFlgrrGLVDRREVLEEVA--AITERAMAGELDFEESLRFrvaLLAGLPEE-ELEEL 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 503938244  75 SHGWQAVFVAIRPDVIAIMHKLREQGHRVVVLSNTNR 111
Cdd:COG0560   79 AERLFEEVPRLYPGARELIAEHRAAGHKVAIVSGGFT 115
HAD_MDP-1_like cd07501
eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to ...
 83-184 3.94e-03

eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to Bacillus cereus phosphonoacetaldehyde hydrolase and Streptomyces FkbH; This family includes eukaryotic magnesium-dependent phosphatase-1 (MDP-1) which is most likely a phosphotyrosine phosphatase catalyzing the dephosphorylation of tyrosine-phosphorylated proteins, Bacillus cereus phosphonoacetaldehyde hydrolase (phosphonatase)which catalyzes the hydrolysis of phosphonoacetaldehyde to acetaldehyde and phosphate using Mg(II) as cofactor, and sequences annotated as FkbH including BafAIV an FkbH-like protein from Streptomyces griseus encoded in ORF12 of the bafilomycin synthesis gene cluster. 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: 319804 [Multi-domain]  Cd Length: 129  Bit Score: 36.17  E-value: 3.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244  83 VAIRPDVIAIMHKLREQGHRVVVLSNTN-------RLHTTFWPDEYPEVQaaadkIYlsqemgmrkPEARI--YQAVLQA 153
Cdd:cd07501   33 VSLYPDAQEILKELKERGILLAVASRNNefdhaneVLEKLDLKELFDAFE-----IY---------PGSKSshFRKIAKE 98

                         90       100       110
                 ....*....|....*....|....*....|.
gi 503938244 154 EGFTAADAVFFDDNADNIEGANQLGITSILV 184
Cdd:cd07501   99 LGIGFDSMVFFDDEPRNREEVSEGGVTCILV 129
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 51-185 5.15e-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: 36.49  E-value: 5.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938244  51 EISDEEFAERLCHEMDvplsyeQFSHGWQAVFVAIRPDVIAIMHKLREQGHRVVVLSNTNRlHTT------FWPDEYPEV 124
Cdd:cd02616   53 EKIDPDKLEDMVEEFR------KYYREHNDDLTKEYPGVYETLARLKSQGIKLGVVTTKLR-ETAlkglklLGLDKYFDV 125

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503938244 125 QAAADkiylsqEMGMRKPEARIYQAVLQAEGFTAADAVFFDDNADNIEGANQLGITSILVT 185
Cdd:cd02616  126 IVGGD------DVTHHKPDPEPVLKALELLGAEPEEALMVGDSPHDILAGKNAGVKTVGVT 180
TM0315 COG3462
Uncharacterized protein, contains short C-terminal (SHOCT) domain [Function unknown];
30-61 6.25e-03

Uncharacterized protein, contains short C-terminal (SHOCT) domain [Function unknown];


Pssm-ID: 442685  Cd Length: 80  Bit Score: 34.50  E-value: 6.25e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 503938244  30 PLATLKQSFAmgetfhqheRGEISDEEFAERL 61
Cdd:COG3462   52 ALEILKERYA---------RGEIDEEEYERRK 74
 
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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