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Conserved domains on  [gi|502864106|ref|WP_013099082|]
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MULTISPECIES: GMP/IMP nucleotidase [Enterobacter]

Protein Classification

GMP/IMP nucleotidase( domain architecture ID 10014936)

GMP/IMP nucleotidase similar to Escherichia coli GMP/IMP nucleotidase YrfG, which catalyzes the dephosphorylation of different purine nucleotides (GMP and IMP) and also hydrolyzes flavin mononucleotide (FMN)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK14988 PRK14988
GMP/IMP nucleotidase; Provisional
 1-224 1.08e-172

GMP/IMP nucleotidase; Provisional


:

Pssm-ID: 237882 [Multi-domain]  Cd Length: 224  Bit Score: 473.43  E-value: 1.08e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106   1 MHLDIAWQEVDTVLLDMDGTLLDLAFDNYFWQKLVPETYGEQQGISPAEAQEFIRSQYSAVQHTLNWYCLDYWSERLGLD 80
Cdd:PRK14988   1 MHIDIAWQDVDTVLLDMDGTLLDLAFDNYFWQKLVPETLGAQRGISPQEAQEYIRQEYHAVQHTLNWYCLDYWSERLGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  81 ICAMTTAQGPRAVLREDTVPFLDALKASGKRRILLTNAHPHNLAVKLEHTGLASHLDLLLSTHTFGYPKEDQRLWHAVKE 160
Cdd:PRK14988  81 ICAMTTEQGPRAVLREDTVPFLEALKASGKRRILLTNAHPHNLAVKLEHTGLDAHLDLLLSTHTFGYPKEDQRLWQAVAE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502864106 161 ETGLQPERTLFIDDSEPILDSAAAFGIRYCLGVTNPDSGLADKSYLRHPGLGDYRQMIPSLTVK 224
Cdd:PRK14988 161 HTGLKAERTLFIDDSEPILDAAAQFGIRYCLGVTNPDSGIAEKQYQRHPSLNDYRRLIPSLMLR 224
 
Name Accession Description Interval E-value
PRK14988 PRK14988
GMP/IMP nucleotidase; Provisional
 1-224 1.08e-172

GMP/IMP nucleotidase; Provisional


Pssm-ID: 237882 [Multi-domain]  Cd Length: 224  Bit Score: 473.43  E-value: 1.08e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106   1 MHLDIAWQEVDTVLLDMDGTLLDLAFDNYFWQKLVPETYGEQQGISPAEAQEFIRSQYSAVQHTLNWYCLDYWSERLGLD 80
Cdd:PRK14988   1 MHIDIAWQDVDTVLLDMDGTLLDLAFDNYFWQKLVPETLGAQRGISPQEAQEYIRQEYHAVQHTLNWYCLDYWSERLGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  81 ICAMTTAQGPRAVLREDTVPFLDALKASGKRRILLTNAHPHNLAVKLEHTGLASHLDLLLSTHTFGYPKEDQRLWHAVKE 160
Cdd:PRK14988  81 ICAMTTEQGPRAVLREDTVPFLEALKASGKRRILLTNAHPHNLAVKLEHTGLDAHLDLLLSTHTFGYPKEDQRLWQAVAE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502864106 161 ETGLQPERTLFIDDSEPILDSAAAFGIRYCLGVTNPDSGLADKSYLRHPGLGDYRQMIPSLTVK 224
Cdd:PRK14988 161 HTGLKAERTLFIDDSEPILDAAAQFGIRYCLGVTNPDSGIAEKQYQRHPSLNDYRRLIPSLMLR 224
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 12-191 4.69e-37

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: 127.92  E-value: 4.69e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106   12 TVLLDMDGTLLDLAFD-----NYFWQKLVPETYGEQQGISPAEAQEFIRSQYSAVQHTLNWYCLDYwserlGLDICAMTT 86
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAiakliNREELGLVPDELGVSAVGRLELALRRFKAQYGRTISPEDAQLLYK-----QLFYEQIEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106   87 AQGprAVLREDTVPFLDALKASGKRRILLTNAHPHnLAVKLEHTGLASHLDLLLSTHTFGYPKEDQRLWHAVKEETGLQP 166
Cdd:TIGR01509  76 EAK--LKPLPGVRALLEALRARGKKLALLTNSPRA-HKLVLALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLEP 152

                         170       180
                  ....*....|....*....|....*
gi 502864106  167 ERTLFIDDSEPILDSAAAFGIRYCL 191
Cdd:TIGR01509 153 SECVFVDDSPAGIEAAKAAGMHTVG 177
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 10-191 4.34e-34

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: 121.29  E-value: 4.34e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  10 VDTVLLDMDGTLLDLAFDNYFWQKLVPETYGEqqgisPAEAQEFIRSQYSAVQHTLNWY---------CLDYWSERLGLD 80
Cdd:COG1011    1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGL-----LDEAEELAEAYRAIEYALWRRYergeitfaeLLRRLLEELGLD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  81 ICAMTTAQ-----GPRAVLREDTVPFLDALKASGKRRILLTNAHPHNLAVKLEHTGLASHLDLLLSTHTFGYPKEDQRLW 155
Cdd:COG1011   76 LAEELAEAflaalPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIF 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 502864106 156 HAVKEETGLQPERTLFIDDSEPI-LDSAAAFGIRYCL 191
Cdd:COG1011  156 ELALERLGVPPEEALFVGDSPETdVAGARAAGMRTVW 192
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 10-186 6.53e-20

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: 83.79  E-value: 6.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106   10 VDTVLLDMDGTLLDLAFDNY-FWQKLVPETYgeqQGISPAEAQEFIRSQYSAVQHTLNWYCLDYWsERLGLDICAMTTAQ 88
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTeAIAELASEHP---LAKAIVAAAEDLPIPVEDFTARLLLGKRDWL-EELDILRGLVETLE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106   89 GPRAV-----------------LREDTVPFLDALKASGKRRILLTNAHPHNLAVKLEHTGLASHLDLLLSTHTFGYPKED 151
Cdd:pfam00702  77 AEGLTvvlvellgvialadelkLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPK 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 502864106  152 QRLWHAVKEETGLQPERTLFIDDSEPILDSAAAFG 186
Cdd:pfam00702 157 PEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 98-191 3.05e-15

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: 68.96  E-value: 3.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  98 TVPFLDALKASGKRRILLTNAHPHNLAVKLEHTGLASHLDLLLSTHTFGYPKEDQRLWHAVKEETGLQPERTLFIDDSEP 177
Cdd:cd01427   12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSEN 91

                         90
                 ....*....|....
gi 502864106 178 ILDSAAAFGIRYCL 191
Cdd:cd01427   92 DIEAARAAGGRTVA 105
 
Name Accession Description Interval E-value
PRK14988 PRK14988
GMP/IMP nucleotidase; Provisional
 1-224 1.08e-172

GMP/IMP nucleotidase; Provisional


Pssm-ID: 237882 [Multi-domain]  Cd Length: 224  Bit Score: 473.43  E-value: 1.08e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106   1 MHLDIAWQEVDTVLLDMDGTLLDLAFDNYFWQKLVPETYGEQQGISPAEAQEFIRSQYSAVQHTLNWYCLDYWSERLGLD 80
Cdd:PRK14988   1 MHIDIAWQDVDTVLLDMDGTLLDLAFDNYFWQKLVPETLGAQRGISPQEAQEYIRQEYHAVQHTLNWYCLDYWSERLGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  81 ICAMTTAQGPRAVLREDTVPFLDALKASGKRRILLTNAHPHNLAVKLEHTGLASHLDLLLSTHTFGYPKEDQRLWHAVKE 160
Cdd:PRK14988  81 ICAMTTEQGPRAVLREDTVPFLEALKASGKRRILLTNAHPHNLAVKLEHTGLDAHLDLLLSTHTFGYPKEDQRLWQAVAE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502864106 161 ETGLQPERTLFIDDSEPILDSAAAFGIRYCLGVTNPDSGLADKSYLRHPGLGDYRQMIPSLTVK 224
Cdd:PRK14988 161 HTGLKAERTLFIDDSEPILDAAAQFGIRYCLGVTNPDSGIAEKQYQRHPSLNDYRRLIPSLMLR 224
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 12-191 4.69e-37

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: 127.92  E-value: 4.69e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106   12 TVLLDMDGTLLDLAFD-----NYFWQKLVPETYGEQQGISPAEAQEFIRSQYSAVQHTLNWYCLDYwserlGLDICAMTT 86
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAiakliNREELGLVPDELGVSAVGRLELALRRFKAQYGRTISPEDAQLLYK-----QLFYEQIEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106   87 AQGprAVLREDTVPFLDALKASGKRRILLTNAHPHnLAVKLEHTGLASHLDLLLSTHTFGYPKEDQRLWHAVKEETGLQP 166
Cdd:TIGR01509  76 EAK--LKPLPGVRALLEALRARGKKLALLTNSPRA-HKLVLALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLEP 152

                         170       180
                  ....*....|....*....|....*
gi 502864106  167 ERTLFIDDSEPILDSAAAFGIRYCL 191
Cdd:TIGR01509 153 SECVFVDDSPAGIEAAKAAGMHTVG 177
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 10-191 4.34e-34

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: 121.29  E-value: 4.34e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  10 VDTVLLDMDGTLLDLAFDNYFWQKLVPETYGEqqgisPAEAQEFIRSQYSAVQHTLNWY---------CLDYWSERLGLD 80
Cdd:COG1011    1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGL-----LDEAEELAEAYRAIEYALWRRYergeitfaeLLRRLLEELGLD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  81 ICAMTTAQ-----GPRAVLREDTVPFLDALKASGKRRILLTNAHPHNLAVKLEHTGLASHLDLLLSTHTFGYPKEDQRLW 155
Cdd:COG1011   76 LAEELAEAflaalPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIF 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 502864106 156 HAVKEETGLQPERTLFIDDSEPI-LDSAAAFGIRYCL 191
Cdd:COG1011  156 ELALERLGVPPEEALFVGDSPETdVAGARAAGMRTVW 192
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 10-186 6.53e-20

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: 83.79  E-value: 6.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106   10 VDTVLLDMDGTLLDLAFDNY-FWQKLVPETYgeqQGISPAEAQEFIRSQYSAVQHTLNWYCLDYWsERLGLDICAMTTAQ 88
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTeAIAELASEHP---LAKAIVAAAEDLPIPVEDFTARLLLGKRDWL-EELDILRGLVETLE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106   89 GPRAV-----------------LREDTVPFLDALKASGKRRILLTNAHPHNLAVKLEHTGLASHLDLLLSTHTFGYPKED 151
Cdd:pfam00702  77 AEGLTvvlvellgvialadelkLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPK 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 502864106  152 QRLWHAVKEETGLQPERTLFIDDSEPILDSAAAFG 186
Cdd:pfam00702 157 PEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
10-202 7.08e-16

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 73.32  E-value: 7.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  10 VDTVLLDMDGTLLD---LAFDnyFWQKLVpETYGEQqgISPAEAQEFI-RSQYSAVQHTLNWYCLDYWSERLGLDICAMT 85
Cdd:COG0637    2 IKAVIFDMDGTLVDsepLHAR--AWREAF-AELGID--LTEEEYRRLMgRSREDILRYLLEEYGLDLPEEELAARKEELY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  86 TA--QGPRAVLREDTVPFLDALKASGKRRILLTNAHPHNLAVKLEHTGLASHLDLLLSTHTFGYPKEDQRLWHAVKEETG 163
Cdd:COG0637   77 REllAEEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAERLG 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 502864106 164 LQPERTLFIDDSEPILDSAAAFGIRyCLGVTNPDSGLAD 202
Cdd:COG0637  157 VDPEECVVFEDSPAGIRAAKAAGMR-VVGVPDGGTAEEE 194
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 98-191 3.05e-15

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: 68.96  E-value: 3.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  98 TVPFLDALKASGKRRILLTNAHPHNLAVKLEHTGLASHLDLLLSTHTFGYPKEDQRLWHAVKEETGLQPERTLFIDDSEP 177
Cdd:cd01427   12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSEN 91

                         90
                 ....*....|....
gi 502864106 178 ILDSAAAFGIRYCL 191
Cdd:cd01427   92 DIEAARAAGGRTVA 105
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 10-202 1.54e-13

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: 66.60  E-value: 1.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  10 VDTVLLDMDGTLLDLAFDNYFwqklvpETYGEQQGISPAEAqeFIRSQYSAVQHTLN---WYCLDYW---SERLGLDICA 83
Cdd:cd02603    1 IRAVLFDFGGVLIDPDPAAAV------ARFEALTGEPSEFV--LDTEGLAGAFLELErgrITEEEFWeelREELGRPLSA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  84 MTTAQGPRA--VLREDTVPFLDALKASGKRRILLTNAHPHnlAVKLEHTGLA---SHLDLLLSTHTFGYPKEDQRLWHAV 158
Cdd:cd02603   73 ELFEELVLAavDPNPEMLDLLEALRAKGYKVYLLSNTWPD--HFKFQLELLPrrgDLFDGVVESCRLGVRKPDPEIYQLA 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 502864106 159 KEETGLQPERTLFIDDSEPILDSAAAFGIRYCLgVTNPDSGLAD 202
Cdd:cd02603  151 LERLGVKPEEVLFIDDREENVEAARALGIHAIL-VTDAEDALRE 193
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
10-194 1.59e-13

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 66.88  E-value: 1.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  10 VDTVLLDMDGTLLD--LAFDNYFWQKLvpETYGEQQgISPAEAQEFI-RSQYSAVQHTLNWY-------CLDYWSERLGL 79
Cdd:COG0546    1 IKLVLFDLDGTLVDsaPDIAAALNEAL--AELGLPP-LDLEELRALIgLGLRELLRRLLGEDpdeeleeLLARFRELYEE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  80 DICAMTTaqgpravLREDTVPFLDALKASGKRRILLTNAHPHNLAVKLEHTGLASHLDLLLSTHTFGYPKED-QRLWHAV 158
Cdd:COG0546   78 ELLDETR-------LFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKpEPLLEAL 150

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 502864106 159 kEETGLQPERTLFIDDSEPILDSAAAFGIRyCLGVT 194
Cdd:COG0546  151 -ERLGLDPEEVLMVGDSPHDIEAARAAGVP-FIGVT 184
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 69-191 5.48e-09

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: 54.20  E-value: 5.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  69 CLDYWSERLGLDICAMTTAQGPRAVLR----EDTVPFLDALKASGKRRILLTNAHPHNLAVKLEHTGLASHLDLLLSTHT 144
Cdd:cd02588   63 ALRATAAELGLELDESDLDELGDAYLRlppfPDVVAGLRRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAED 142

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 502864106 145 FGYPKEDQRLWHAVKEETGLQPERTLFIDDSEPILDSAAAFGIRYCL 191
Cdd:cd02588  143 VRAYKPAPAVYELAAERLGVPPDEILHVASHAWDLAGARALGLRTAW 189
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 92-195 2.84e-08

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: 51.08  E-value: 2.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  92 AVLREDTVPFLDALKASGKRRILLTNAHPHNLA-VKLEHTGLASHLDLLLSTHTFGYPKEDQRLWHAVKEETGLQPERTL 170
Cdd:cd07505   40 LKLKPGVVELLDALKAAGIPVAVATSSSRRNVElLLLELGLLRGYFDVIVSGDDVERGKPAPDIYLLAAERLGVDPERCL 119

                         90       100
                 ....*....|....*....|....*
gi 502864106 171 FIDDSEPILDSAAAFGIRyCLGVTN 195
Cdd:cd07505  120 VFEDSLAGIEAAKAAGMT-VVAVPD 143
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 12-191 6.02e-08

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: 50.71  E-value: 6.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  12 TVLLDMDGTL----------LDLAFDNYFWQKLvpetygeqqGISPAEAQEFIRSQYSAVQHTLNWYCL-------DYWS 74
Cdd:cd02604    1 VWFFDLDNTLyplstglfdqIQARITEFVATKL---------GLSPEEARRLRKSYYKEYGTTLRGLMAehgidpdEFLD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  75 ERLG-LDICAMTtaqgPRAVLREdtvpFLDALKAsgkRRILLTNAH-PHNLAVkLEHTGLASHLDLLLSTHTFGY-PKED 151
Cdd:cd02604   72 RVVHlILYDHLK----PDPKLRN----LLLALPG---RKIIFTNASkNHAIRV-LKRLGLADLFDGIFDIEYAGPdPKPH 139

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 502864106 152 QRLWHAVKEETGLQPERTLFIDDSEPILDSAAAFGIRYCL 191
Cdd:cd02604  140 PAAFEKAIREAGLDPKRAAFFDDSIRNLLAAKALGMKTVL 179
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
13-190 1.81e-07

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 49.51  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106   13 VLLDMDGTLLD----------LAFDNYFWQKLVPETYGEQQGISPAEA--QEFIRSQYSAVQHTLnwycLDYWSERLGLD 80
Cdd:pfam13419   1 IIFDFDGTLLDteeliiksfnYLLEEFGYGELSEEEILKFIGLPLREIfrYLGVSEDEEEKIEFY----LRKYNEELHDK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106   81 ICAmttaqgpravLREDTVPFLDALKASGKRRILLTNAHPHNLAVKLEHTGLASHLDLLLSTHTFGYPKEDQRLWHAVKE 160
Cdd:pfam13419  77 LVK----------PYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALE 146

                         170       180       190
                  ....*....|....*....|....*....|
gi 502864106  161 ETGLQPERTLFIDDSEPILDSAAAFGIRYC 190
Cdd:pfam13419 147 QLGLKPEEVIYVGDSPRDIEAAKNAGIKVI 176
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 12-176 2.54e-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: 48.93  E-value: 2.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106   12 TVLLDMDGTLLDLAFdnyFWQKLVPETYgEQQGISPAEAQEFIRsQYSAVQHTLNWYCLDYWSERLGLdicAMTTAQGPR 91
Cdd:TIGR01549   1 AILFDIDGTLVDIKF---AIRRAFPQTF-EEFGLDPASFKALKQ-AGGLAEEEWYRIATSALEELQGR---FWSEYDAEE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106   92 AvLREDTVPFLDALKASGKRRILLTNAHPHNLAVKLEHTGLASHLDLLLSTHTFGYpKEDQRLWHAVKEETGLQPErTLF 171
Cdd:TIGR01549  73 A-YIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEPGS-KPEPEIFLAALESLGVPPE-VLH 149


                  ....*
gi 502864106  172 IDDSE 176
Cdd:TIGR01549 150 VGDNL 154
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
102-194 1.05e-06

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 47.88  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106 102 LDALKASGKRRILLTNAhPHNLAVK-LEHTGLASHLDLLLSTHTFGYPKEDQR-LWHAVkEETGLQPERTLFIDDSEPIL 179
Cdd:PRK13222 102 LAALKAAGYPLAVVTNK-PTPFVAPlLEALGIADYFSVVIGGDSLPNKKPDPApLLLAC-EKLGLDPEEMLFVGDSRNDI 179

                         90
                 ....*....|....*
gi 502864106 180 DSAAAFGIRyCLGVT 194
Cdd:PRK13222 180 QAARAAGCP-SVGVT 193
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 89-194 5.80e-05

subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli 6-phosphogluconate phosphatase YieH; This subfamily includes Escherichia coli YieH/HAD3 an 6-phosphogluconate phosphatase, which can hydrolyzed purines and pyrimidines as secondary substrates. It belongs 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), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate, and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate. 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: 319828 [Multi-domain]  Cd Length: 141  Bit Score: 41.54  E-value: 5.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  89 GPRAVLREDTVPFLDAlkasgkrrillTNAHPHNLAVKLEHTGLASHLD-LLLSTHTFGYPKEDQRLW-HAVKEeTGLQP 166
Cdd:cd07526   46 GAAAALSALTLPFCVA-----------SNSSRERLTHSLGLAGLLAYFEgRIFSASDVGRGKPAPDLFlHAAAQ-MGVAP 113

                         90       100
                 ....*....|....*....|....*...
gi 502864106 167 ERTLFIDDSEPILDSAAAFGIRyCLGVT 194
Cdd:cd07526  114 ERCLVIEDSPTGVRAALAAGMT-VFGFT 140
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 102-191 1.37e-03

haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter sphaeroides CbbZ; Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319815 [Multi-domain]  Cd Length: 214  Bit Score: 38.45  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106 102 LDALKASGKRRILLTNAhPHNLAVK-LEHTGLASHLDLLLSTHTFGYPKEDQRLWHAVKEETGLQPERTLFIDDSEPILD 180
Cdd:cd07512   95 LERLRAAGWRLAICTNK-PEAPARAlLSALGLADLFAAVVGGDTLPQRKPDPAPLRAAIRRLGGDVSRALMVGDSETDAA 173

                         90
                 ....*....|.
gi 502864106 181 SAAAFGIRYCL 191
Cdd:cd07512  174 TARAAGVPFVL 184
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 94-175 2.94e-03

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: 36.37  E-value: 2.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  94 LREDTVPFLDALKAsGKRRILLTNAHPHNLAVKLEHTGLASHLDLLLSTHTFGYPKEDQRLWHAVKEETGLQPERTLFID 173
Cdd:cd04305   10 LLPGAKELLEELKK-GYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLMVG 88


                 ..
gi 502864106 174 DS 175
Cdd:cd04305   89 DS 90
HAD_EP cd01629
Enolase-phosphatase similar to human enolase-phosphatase E1 and and Xanthomonas oryzae pv. ...
 12-193 3.65e-03

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: 37.14  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  12 TVLLDMDGTLLDLAF--DN---YFWQKLV---------PETYGEQQGISPAEAQEFIRSQYSAVQHtlnwycLDYWSERl 77
Cdd:cd01629    1 AILLDIEGTTTPISFvkDVlfpYARERLPdflaehwedPEVKEDVLAAAAEAEGEAEASIEAVVAN------LLDWMDE- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  78 GLDICAMTTAQGP-----------RAVLREDTVPFLDALKASGKRrilltnahphnLAV---------KL--EHTglaSH 135
Cdd:cd01629   74 DRKATPLKALQGLiwregyesgelKGHLYPDVVPALRRWHAAGLR-----------LYIyssgsvaaqKLlfGHS---DA 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502864106 136 LDL--LLSTH---TFGyPKEDQRLWHAVKEETGLQPERTLFIDDSEPILDSAAAFGIRYCLGV 193
Cdd:cd01629  140 GDLtpLFSGYfdtTIG-PKREAASYRKIAEAIGVPPAEILFLSDVVAELDAAKEAGLQTVLLV 201
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 98-187 5.50e-03

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: 35.73  E-value: 5.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  98 TVPFLDALKASGKRRILLTNAHPHnLAVKLEHTGLASHLDLLLSTHTFGYPKEDQRLWHAVKEETGLQPERTLFIDDSeP 177
Cdd:cd16415   12 AVETLKDLKEKGLKLAVVSNFDRR-LRELLEALGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPEEALHVGDD-L 89

                         90
                 ....*....|
gi 502864106 178 ILDSAAAFGI 187
Cdd:cd16415   90 KNDYLGARAV 99
PRK09456 PRK09456
?-D-glucose-1-phosphatase; Provisional
 87-188 6.94e-03

?-D-glucose-1-phosphatase; Provisional


Pssm-ID: 181872 [Multi-domain]  Cd Length: 199  Bit Score: 36.55  E-value: 6.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864106  87 AQGPRAV---LREDTVPFLDALKASGKRRILLTNAH-------PHnlavklEHTGLASHLDLLLSTHTFGYPKEDQRLWH 156
Cdd:PRK09456  75 AHGWQAVfvaLRPEVIAIMHKLREQGHRVVVLSNTNrlhttfwPE------EYPEVRAAADHIYLSQDLGMRKPEARIYQ 148

                         90       100       110
                 ....*....|....*....|....*....|..
gi 502864106 157 AVKEETGLQPERTLFIDDSEPILDSAAAFGIR 188
Cdd:PRK09456 149 HVLQAEGFSAADAVFFDDNADNIEAANALGIT 180
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 101-144 8.22e-03

Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.


Pssm-ID: 433132  Cd Length: 101  Bit Score: 34.75  E-value: 8.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 502864106  101 FLDALKASGKRRILLTNA---HPHNLAVKLEHTGLASHLDLLLSTHT 144
Cdd:pfam13344  22 ALRALRAAGKPVVFVTNNssrSREEYAEKLRKLGFDIDEDEIITSGT 68
 
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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