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Conserved domains on  [gi|21312114|ref|NP_082797|]
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pyridoxal phosphate phosphatase PHOSPHO2 [Mus musculus]

Protein Classification

Put_Phosphatase domain-containing protein( domain architecture ID 10536425)

Put_Phosphatase domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Put_Phosphatase pfam06888
Putative Phosphatase; This family contains a number of putative eukaryotic acid phosphatases. ...
 3-239 9.77e-124

Putative Phosphatase; This family contains a number of putative eukaryotic acid phosphatases. Some family members represent the products of the PSI14 phosphatase family in Lycopersicon esculentum (Tomato).


:

Pssm-ID: 284339  Cd Length: 234  Bit Score: 350.52  E-value: 9.77e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114     3 VLLVFDFDNTIIDDNSDTWIVQCAPDKKLPIELQDSYQKGLWTEFMGRVFKYLRDEGVKADELKRAVTSLPFTSGMIELL 82
Cdd:pfam06888   1 ILVVFDFDKTIIDVDSDNWVVDELPTTQLFEQLRPTMPKGFWNELMDRVMKELHDQGVSIADIKAVLRSIPLVPGMVRLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114    83 SFLRMNKDRFDCIIISDSNSIFIDWVLEAAAFHDVFDHVFTNPASFDSSGRLTVKNYHAHSCTRCPKNLCKNTVLGEFID 162
Cdd:pfam06888  81 KFLAKNGLGCDLIIISDANSFFIETILRAAGLHDLFSEIFTNPASVDARGRLTVLPYHDHSCNLCPSNMCKGKVLDEIVA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21312114   163 KQLQKGVRYTRIVYIGDGGNDVCPVTFLKKNDVAMPREGYTLHRtlaKMSQNLEPMESSIVVWSSGVEIISHLQFLI 239
Cdd:pfam06888 161 SQAREGVRYERVIYVGDGANDFCPSLRLRECDVAMPRKGFPLWK---LISENPLLLKASVVEWSSGAELEEILLQLI 234
 
Name Accession Description Interval E-value
Put_Phosphatase pfam06888
Putative Phosphatase; This family contains a number of putative eukaryotic acid phosphatases. ...
 3-239 9.77e-124

Putative Phosphatase; This family contains a number of putative eukaryotic acid phosphatases. Some family members represent the products of the PSI14 phosphatase family in Lycopersicon esculentum (Tomato).


Pssm-ID: 284339  Cd Length: 234  Bit Score: 350.52  E-value: 9.77e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114     3 VLLVFDFDNTIIDDNSDTWIVQCAPDKKLPIELQDSYQKGLWTEFMGRVFKYLRDEGVKADELKRAVTSLPFTSGMIELL 82
Cdd:pfam06888   1 ILVVFDFDKTIIDVDSDNWVVDELPTTQLFEQLRPTMPKGFWNELMDRVMKELHDQGVSIADIKAVLRSIPLVPGMVRLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114    83 SFLRMNKDRFDCIIISDSNSIFIDWVLEAAAFHDVFDHVFTNPASFDSSGRLTVKNYHAHSCTRCPKNLCKNTVLGEFID 162
Cdd:pfam06888  81 KFLAKNGLGCDLIIISDANSFFIETILRAAGLHDLFSEIFTNPASVDARGRLTVLPYHDHSCNLCPSNMCKGKVLDEIVA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21312114   163 KQLQKGVRYTRIVYIGDGGNDVCPVTFLKKNDVAMPREGYTLHRtlaKMSQNLEPMESSIVVWSSGVEIISHLQFLI 239
Cdd:pfam06888 161 SQAREGVRYERVIYVGDGANDFCPSLRLRECDVAMPRKGFPLWK---LISENPLLLKASVVEWSSGAELEEILLQLI 234
DKMTPPase-SF TIGR01489
2,3-diketo-5-methylthio-1-phosphopentane phosphatase; This phosphatase is a member of the IB ...
 2-200 4.15e-88

2,3-diketo-5-methylthio-1-phosphopentane phosphatase; This phosphatase is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. With the exception of OMNI|NTL01BS01361 from B. subtilis and GP|15024582 from Clostridium acetabutylicum, the members of this group are all eukaryotic, spanning metazoa, plants and fungi. The B. subtilus gene (YkrX, renamed MtnX) is part of an operon for the conversion of methylthioribose (MTR) to methionine. It works with the enolase MtnW, a RuBisCO homolog. The combination of MtnW and MtnX achieves the same overall reaction as the enolase-phosphatase MtnC. The function of MtnX was shown by Ashida, et al. (2003) to be 2,3-diketo-5-methylthio-1-phosphopentane phosphatase, rather than 2,3-diketo-5-methylthio-1-phosphopentane phosphatase as proposed earlier. See the Genome Property for methionine salvage for more details. In eukaryotes, methionine salvage from methylthioadenosine also occurs. It seems reasonable that members of this family in eukaryotes fulfill a similar role as in Bacillus. A more specific, equivalog-level model is TIGR03333. Note that SP|P53981 from S. cerevisiae, a member of this family, is annotated as a "probable membrane protein" due to a predicted transmembrane helix. The region in question contains the second of the three conserved HAD superfamily catalytic motifs and thus, considering the fold of the HAD catalytic domain, is unlikely to be a transmembrane region in fact. [Central intermediary metabolism, Other]


Pssm-ID: 213629 [Multi-domain]  Cd Length: 188  Bit Score: 258.90  E-value: 4.15e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114     2 KVLLVFDFDNTIIDDNSDTWIVQCAPDKKLPIELQDSYQKGLWTEFMGRVFKYLRDEGVKADELKRAVTSLPFTSGMIEL 81
Cdd:TIGR01489   1 KVVVVSDFDGTITLNDSDDWITDKFGPPEANRLLDGVLSKTLSIKFMDRRMKGLLPSGLKEDEILEVLKSAPIDPGFKEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114    82 LSFLRMNKdrFDCIIISDSNSIFIDWVLEAAAFHDVFDHVFTNPASFDSSGRLTVKNYHAHSCTRCPKNLCKntvlGEFI 161
Cdd:TIGR01489  81 IAFIKEHG--IDFIVISDGNDFFIDPVLEGIGEKDVFIEIYSNPASFDNDGRHIVWPHHCHGCCSCPCGCCK----GKVI 154

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 21312114   162 DKQLQKGvrYTRIVYIGDGGNDVCPVTFLkknDVAMPRE 200
Cdd:TIGR01489 155 HKLSEPK--YQHIIYIGDGVTDVCPAKLS---DVVFAKE 188
HAD_Pase cd16418
phosphatases, similar to human PHOSPHO1 and PHOSPHO2 phosphatases; belongs to the haloacid ...
 78-196 8.49e-57

phosphatases, similar to human PHOSPHO1 and PHOSPHO2 phosphatases; belongs to the haloacid dehalogenase-like superfamily; This family includes phosphatases with different substrate specificities. Human PHOSPHO1 is a phosphoethanolamine/phosphocholine phosphatase associated with high levels of expression at mineralizing regions of bone and cartilage and is thought to be involved in the generation of inorganic phosphate for bone mineralization. Human PHOSPHO2 is a putative phosphatase which shows high specific activity toward pyridoxal-5-phosphate; PHODPHO2 is not specific to bone but is expressed in a wide range of soft tissues. These belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319855  Cd Length: 130  Bit Score: 177.14  E-value: 8.49e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114  78 MIELLSFLRMNkDRFDCIIISDSNSIFIDWVLEAAAFHDVFDHVFTNPASFDSSGRLTVKNY-HAHSCTRCPKNLCKNTV 156
Cdd:cd16418  12 MVDLIKFLAKN-DGFELIIISDANSFFIEEWLEAAGFHDLFSKIFTNPASFDANGNLTVRPYfHSHSCLLCPSNMCKGKV 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 21312114 157 LGEFIDKQLQKGVRYTRIVYIGDGGNDVCPVTFLKKNDVA 196
Cdd:cd16418  91 LEEYVASRAQDSVHYERVIYVGDGANDFCPVLRLRKGDVA 130
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-184 4.17e-13

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: 66.01  E-value: 4.17e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114   1 MKVLLVFDFDNTIIDDNSDTWIVQCAPDKKLPI---------ELQDSYQKGLWT--EFMGRVFKYLRdeGVKADELKRAV 69
Cdd:COG0560   2 KMRLAVFDLDGTLIAGESIDELARFLGRRGLVDrrevleevaAITERAMAGELDfeESLRFRVALLA--GLPEEELEELA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114  70 TSL-----PFTSGMIELLSFLRMNKDRfdCIIISDSNSIFIDWVleAAAFHdvFDHVFTNPASFDsSGRLT--VKNYHAH 142
Cdd:COG0560  80 ERLfeevpRLYPGARELIAEHRAAGHK--VAIVSGGFTFFVEPI--AERLG--IDHVIANELEVE-DGRLTgeVVGPIVD 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21312114 143 SCTrcpknlcKNTVLGEFIDKQlqkGVRYTRIVYIGDGGNDV 184
Cdd:COG0560 153 GEG-------KAEALRELAAEL---GIDLEQSYAYGDSANDL 184
 
Name Accession Description Interval E-value
Put_Phosphatase pfam06888
Putative Phosphatase; This family contains a number of putative eukaryotic acid phosphatases. ...
 3-239 9.77e-124

Putative Phosphatase; This family contains a number of putative eukaryotic acid phosphatases. Some family members represent the products of the PSI14 phosphatase family in Lycopersicon esculentum (Tomato).


Pssm-ID: 284339  Cd Length: 234  Bit Score: 350.52  E-value: 9.77e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114     3 VLLVFDFDNTIIDDNSDTWIVQCAPDKKLPIELQDSYQKGLWTEFMGRVFKYLRDEGVKADELKRAVTSLPFTSGMIELL 82
Cdd:pfam06888   1 ILVVFDFDKTIIDVDSDNWVVDELPTTQLFEQLRPTMPKGFWNELMDRVMKELHDQGVSIADIKAVLRSIPLVPGMVRLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114    83 SFLRMNKDRFDCIIISDSNSIFIDWVLEAAAFHDVFDHVFTNPASFDSSGRLTVKNYHAHSCTRCPKNLCKNTVLGEFID 162
Cdd:pfam06888  81 KFLAKNGLGCDLIIISDANSFFIETILRAAGLHDLFSEIFTNPASVDARGRLTVLPYHDHSCNLCPSNMCKGKVLDEIVA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21312114   163 KQLQKGVRYTRIVYIGDGGNDVCPVTFLKKNDVAMPREGYTLHRtlaKMSQNLEPMESSIVVWSSGVEIISHLQFLI 239
Cdd:pfam06888 161 SQAREGVRYERVIYVGDGANDFCPSLRLRECDVAMPRKGFPLWK---LISENPLLLKASVVEWSSGAELEEILLQLI 234
DKMTPPase-SF TIGR01489
2,3-diketo-5-methylthio-1-phosphopentane phosphatase; This phosphatase is a member of the IB ...
 2-200 4.15e-88

2,3-diketo-5-methylthio-1-phosphopentane phosphatase; This phosphatase is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. With the exception of OMNI|NTL01BS01361 from B. subtilis and GP|15024582 from Clostridium acetabutylicum, the members of this group are all eukaryotic, spanning metazoa, plants and fungi. The B. subtilus gene (YkrX, renamed MtnX) is part of an operon for the conversion of methylthioribose (MTR) to methionine. It works with the enolase MtnW, a RuBisCO homolog. The combination of MtnW and MtnX achieves the same overall reaction as the enolase-phosphatase MtnC. The function of MtnX was shown by Ashida, et al. (2003) to be 2,3-diketo-5-methylthio-1-phosphopentane phosphatase, rather than 2,3-diketo-5-methylthio-1-phosphopentane phosphatase as proposed earlier. See the Genome Property for methionine salvage for more details. In eukaryotes, methionine salvage from methylthioadenosine also occurs. It seems reasonable that members of this family in eukaryotes fulfill a similar role as in Bacillus. A more specific, equivalog-level model is TIGR03333. Note that SP|P53981 from S. cerevisiae, a member of this family, is annotated as a "probable membrane protein" due to a predicted transmembrane helix. The region in question contains the second of the three conserved HAD superfamily catalytic motifs and thus, considering the fold of the HAD catalytic domain, is unlikely to be a transmembrane region in fact. [Central intermediary metabolism, Other]


Pssm-ID: 213629 [Multi-domain]  Cd Length: 188  Bit Score: 258.90  E-value: 4.15e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114     2 KVLLVFDFDNTIIDDNSDTWIVQCAPDKKLPIELQDSYQKGLWTEFMGRVFKYLRDEGVKADELKRAVTSLPFTSGMIEL 81
Cdd:TIGR01489   1 KVVVVSDFDGTITLNDSDDWITDKFGPPEANRLLDGVLSKTLSIKFMDRRMKGLLPSGLKEDEILEVLKSAPIDPGFKEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114    82 LSFLRMNKdrFDCIIISDSNSIFIDWVLEAAAFHDVFDHVFTNPASFDSSGRLTVKNYHAHSCTRCPKNLCKntvlGEFI 161
Cdd:TIGR01489  81 IAFIKEHG--IDFIVISDGNDFFIDPVLEGIGEKDVFIEIYSNPASFDNDGRHIVWPHHCHGCCSCPCGCCK----GKVI 154

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 21312114   162 DKQLQKGvrYTRIVYIGDGGNDVCPVTFLkknDVAMPRE 200
Cdd:TIGR01489 155 HKLSEPK--YQHIIYIGDGVTDVCPAKLS---DVVFAKE 188
HAD_Pase cd16418
phosphatases, similar to human PHOSPHO1 and PHOSPHO2 phosphatases; belongs to the haloacid ...
 78-196 8.49e-57

phosphatases, similar to human PHOSPHO1 and PHOSPHO2 phosphatases; belongs to the haloacid dehalogenase-like superfamily; This family includes phosphatases with different substrate specificities. Human PHOSPHO1 is a phosphoethanolamine/phosphocholine phosphatase associated with high levels of expression at mineralizing regions of bone and cartilage and is thought to be involved in the generation of inorganic phosphate for bone mineralization. Human PHOSPHO2 is a putative phosphatase which shows high specific activity toward pyridoxal-5-phosphate; PHODPHO2 is not specific to bone but is expressed in a wide range of soft tissues. These belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319855  Cd Length: 130  Bit Score: 177.14  E-value: 8.49e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114  78 MIELLSFLRMNkDRFDCIIISDSNSIFIDWVLEAAAFHDVFDHVFTNPASFDSSGRLTVKNY-HAHSCTRCPKNLCKNTV 156
Cdd:cd16418  12 MVDLIKFLAKN-DGFELIIISDANSFFIEEWLEAAGFHDLFSKIFTNPASFDANGNLTVRPYfHSHSCLLCPSNMCKGKV 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 21312114 157 LGEFIDKQLQKGVRYTRIVYIGDGGNDVCPVTFLKKNDVA 196
Cdd:cd16418  91 LEEYVASRAQDSVHYERVIYVGDGANDFCPVLRLRKGDVA 130
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 4-186 7.67e-20

Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273653 [Multi-domain]  Cd Length: 177  Bit Score: 83.56  E-value: 7.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114     4 LLVFDFDNTIIDDNSDTWIV-QCAPDKKLPIELQDSYQKGlWTEF---MGRVFK---YLRDEGVKADELKRAVTSLPfts 76
Cdd:TIGR01488   1 LAIFDFDGTLTRQDSLIDLLaKLLGTNDEVIELTRLAPSG-RISFedaLGRRLAllhRSRSEEVAKEFLARQVALRP--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114    77 GMIELLSFLRMNKDRfdCIIISDSNSIFIDWVLEAAAFHDvfdhVFTNPASFDSSGRLTVKnyhaHSCTRCPKNLCKNTV 156
Cdd:TIGR01488  77 GARELISWLKERGID--TVIVSGGFDFFVEPVAEKLGIDD----VFANRLEFDDNGLLTGP----IEGQVNPEGECKGKV 146

                         170       180       190
                  ....*....|....*....|....*....|
gi 21312114   157 LGEfidKQLQKGVRYTRIVYIGDGGNDVCP 186
Cdd:TIGR01488 147 LKE---LLEESKITLKKIIAVGDSVNDLPM 173
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-184 4.17e-13

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: 66.01  E-value: 4.17e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114   1 MKVLLVFDFDNTIIDDNSDTWIVQCAPDKKLPI---------ELQDSYQKGLWT--EFMGRVFKYLRdeGVKADELKRAV 69
Cdd:COG0560   2 KMRLAVFDLDGTLIAGESIDELARFLGRRGLVDrrevleevaAITERAMAGELDfeESLRFRVALLA--GLPEEELEELA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114  70 TSL-----PFTSGMIELLSFLRMNKDRfdCIIISDSNSIFIDWVleAAAFHdvFDHVFTNPASFDsSGRLT--VKNYHAH 142
Cdd:COG0560  80 ERLfeevpRLYPGARELIAEHRAAGHK--VAIVSGGFTFFVEPI--AERLG--IDHVIANELEVE-DGRLTgeVVGPIVD 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21312114 143 SCTrcpknlcKNTVLGEFIDKQlqkGVRYTRIVYIGDGGNDV 184
Cdd:COG0560 153 GEG-------KAEALRELAAEL---GIDLEQSYAYGDSANDL 184
HAD pfam12710
haloacid dehalogenase-like hydrolase;
5-185 7.28e-08

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 50.99  E-value: 7.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114     5 LVFDFDNTIIDDNS-----DTWIVQCAPDKKLPIE----LQDSYQKGLWTEFMGRVFKYLRDEGVK---ADELKRAVTSL 72
Cdd:pfam12710   1 ALFDLDGTLLDGDSlflliRALLRRGGPDLWRALLvlllLALLRLLGRLSRAGARELLRALLAGLPeedAAELERFVAEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114    73 P---FTSGMIELLSFLRMNKDRfdCIIISDSNSIFIDWVLEAAAFHDVFD-HVFTNPASFDSSGRLTVKNYHAHSctrcp 148
Cdd:pfam12710  81 AlprLHPGALELLAAHRAAGDR--VVVVTGGLRPLVEPVLAELGFDEVLAtELEVDDGRFTGELRLIGPPCAGEG----- 153

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 21312114   149 knlcKNTVLGEFIDKQLQkGVRYTRIVYIGDGGNDVC 185
Cdd:pfam12710 154 ----KVRRLRAWLAARGL-GLDLADSVAYGDSPSDLP 185
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 5-123 1.94e-06

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: 47.33  E-value: 1.94e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114   5 LVFDFDNTIID-DNSDTWIVQCAPDKKLPIELQDSYQKGLWTEFMGRVFKYLRDEGVKADELKRAVTSLPFTS------- 76
Cdd:COG1011   4 VLFDLDGTLLDfDPVIAEALRALAERLGLLDEAEELAEAYRAIEYALWRRYERGEITFAELLRRLLEELGLDLaeelaea 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114  77 -------------GMIELLSFLRmnKDRFDCIIISDSNSIFIDWVLEAAAFHDVFDHVFT 123
Cdd:COG1011  84 flaalpelvepypDALELLEALK--ARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVS 141
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 78-184 1.26e-05

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: 43.15  E-value: 1.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114  78 MIELLSFLRmnKDRFDCIIISDSNSIFIDWVLEAAAFHDVFDHVFTNPASFDssgrltvknyhahsctrcPKNLCKntvl 157
Cdd:cd01427  12 AVELLKRLR--AAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGT------------------PKPKPK---- 67

                        90       100
                ....*....|....*....|....*..
gi 21312114 158 gEFIDKQLQKGVRYTRIVYIGDGGNDV 184
Cdd:cd01427  68 -PLLLLLLKLGVDPEEVLFVGDSENDI 93
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 4-184 2.52e-05

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: 43.73  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114     4 LLVFDFDNTIIDDNS--DTWIVQCAPDKKLPIELQDSYQKGLW--TEFMGRVF----KYLRDEG---------------- 59
Cdd:pfam00702   3 AVVFDLDGTLTDGEPvvTEAIAELASEHPLAKAIVAAAEDLPIpvEDFTARLLlgkrDWLEELDilrglvetleaegltv 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114    60 --VKADELKRAVTSLPFTSGMIELLSFLRMNKdrFDCIIISDSNSIFIDWVLEAAAFHDVFDHVFTnpASFDSSGrltvk 137
Cdd:pfam00702  83 vlVELLGVIALADELKLYPGAAEALKALKERG--IKVAILTGDNPEAAEALLRLLGLDDYFDVVIS--GDDVGVG----- 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 21312114   138 nyhahsctrCPKNLCKNTVLGEFidkqlqkGVRYTRIVYIGDGGNDV 184
Cdd:pfam00702 154 ---------KPKPEIYLAALERL-------GVKPEEVLMVGDGVNDI 184
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 4-183 3.11e-04

phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. 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: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 40.22  E-value: 3.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114   4 LLVFDFDNTI-----IDDNSDTW--------IVQCAPDKKLpiELQDSYQKglwtefmgRVfKYLrdEGVKADELKRAVT 70
Cdd:cd07500   1 LIVFDMDSTLiqqevIDELAAEAgvgeevaaITERAMRGEL--DFEESLRE--------RV-ALL--KGLPESVLDEVYE 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21312114  71 SLPFTSGMIELLSFLRMNKdrFDCIIISDSNSIFIDWVleAAAFHdvFDHVFTNPASFDsSGRLTVKnyhahsctrcpkn 150
Cdd:cd07500  68 RLTLTPGAEELIQTLKAKG--YKTAVVSGGFTYFTDRL--AEELG--LDYAFANELEIK-DGKLTGK------------- 127

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21312114 151 lckntVLGEFIDKQ-----LQK-----GVRYTRIVYIGDGGND 183
Cdd:cd07500 128 -----VLGPIVDAQrkaetLQElaarlGIPLEQTVAVGDGAND 165
 
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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