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Conserved domains on  [gi|219689097|ref|NP_001137276|]
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phosphoethanolamine/phosphocholine phosphatase isoform 1 [Homo sapiens]

Protein Classification

HAD family hydrolase( domain architecture ID 10536425)

HAD (haloacid dehalogenase) family hydrolase; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

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. ...
 52-289 3.55e-133

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: 376.71  E-value: 3.55e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097   52 FLLTFDFDETIVDENSDDSIVRAAPGQRLPESLRATYREGFYNEYMQRVFKYLGEQGVRPRDLSAIYEAIPLSPGMSDLL 131
Cdd:pfam06888   1 ILVVFDFDKTIIDVDSDNWVVDELPTTQLFEQLRPTMPKGFWNELMDRVMKELHDQGVSIADIKAVLRSIPLVPGMVRLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097  132 QFVAKQGACFEVILISDANTFGVESSLRAAGHHSLFRRILSNPSGPDARGLLALRPFHTHSCARCPANMCKHKVLSDYLR 211
Cdd:pfam06888  81 KFLAKNGLGCDLIIISDANSFFIETILRAAGLHDLFSEIFTNPASVDARGRLTVLPYHDHSCNLCPSNMCKGKVLDEIVA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219689097  212 ERAHDGVHFERLFYVGDGANDFCPMGLLAGGDVAFPRRGYPMHRLIQEaqkaEPSSFRASVVPWETAADVRLHLQQVL 289
Cdd:pfam06888 161 SQAREGVRYERVIYVGDGANDFCPSLRLRECDVAMPRKGFPLWKLISE----NPLLLKASVVEWSSGAELEEILLQLI 234
 
Name Accession Description Interval E-value
Put_Phosphatase pfam06888
Putative Phosphatase; This family contains a number of putative eukaryotic acid phosphatases. ...
 52-289 3.55e-133

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: 376.71  E-value: 3.55e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097   52 FLLTFDFDETIVDENSDDSIVRAAPGQRLPESLRATYREGFYNEYMQRVFKYLGEQGVRPRDLSAIYEAIPLSPGMSDLL 131
Cdd:pfam06888   1 ILVVFDFDKTIIDVDSDNWVVDELPTTQLFEQLRPTMPKGFWNELMDRVMKELHDQGVSIADIKAVLRSIPLVPGMVRLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097  132 QFVAKQGACFEVILISDANTFGVESSLRAAGHHSLFRRILSNPSGPDARGLLALRPFHTHSCARCPANMCKHKVLSDYLR 211
Cdd:pfam06888  81 KFLAKNGLGCDLIIISDANSFFIETILRAAGLHDLFSEIFTNPASVDARGRLTVLPYHDHSCNLCPSNMCKGKVLDEIVA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219689097  212 ERAHDGVHFERLFYVGDGANDFCPMGLLAGGDVAFPRRGYPMHRLIQEaqkaEPSSFRASVVPWETAADVRLHLQQVL 289
Cdd:pfam06888 161 SQAREGVRYERVIYVGDGANDFCPSLRLRECDVAMPRKGFPLWKLISE----NPLLLKASVVEWSSGAELEEILLQLI 234
HAD_Pase cd16418
phosphatases, similar to human PHOSPHO1 and PHOSPHO2 phosphatases; belongs to the haloacid ...
 127-245 4.66e-65

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: 199.87  E-value: 4.66e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097 127 MSDLLQFVAKQgACFEVILISDANTFGVESSLRAAGHHSLFRRILSNPSGPDARGLLALRP-FHTHSCARCPANMCKHKV 205
Cdd:cd16418   12 MVDLIKFLAKN-DGFELIIISDANSFFIEEWLEAAGFHDLFSKIFTNPASFDANGNLTVRPyFHSHSCLLCPSNMCKGKV 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 219689097 206 LSDYLRERAHDGVHFERLFYVGDGANDFCPMGLLAGGDVA 245
Cdd:cd16418   91 LEEYVASRAQDSVHYERVIYVGDGANDFCPVLRLRKGDVA 130
DKMTPPase-SF TIGR01489
2,3-diketo-5-methylthio-1-phosphopentane phosphatase; This phosphatase is a member of the IB ...
 52-248 2.17e-41

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: 141.42  E-value: 2.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097   52 FLLTFDFDETIVDENSDDSIVRAAPGQRLPESLRATYREGFYNEYMQRVFKYLGEQGVRPRDLSAIYEAIPLSPGMSDLL 131
Cdd:TIGR01489   2 VVVVSDFDGTITLNDSDDWITDKFGPPEANRLLDGVLSKTLSIKFMDRRMKGLLPSGLKEDEILEVLKSAPIDPGFKEFI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097  132 QFVAKQGacFEVILISDANTFGVESSLRAAGHHSLFRRILSNPSGPDARGLLALRPFHTHSCARCPANMCKHKVLsDYLR 211
Cdd:TIGR01489  82 AFIKEHG--IDFIVISDGNDFFIDPVLEGIGEKDVFIEIYSNPASFDNDGRHIVWPHHCHGCCSCPCGCCKGKVI-HKLS 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 219689097  212 ERAhdgvhFERLFYVGDGANDFCPMGLLaggDVAFPR 248
Cdd:TIGR01489 159 EPK-----YQHIIYIGDGVTDVCPAKLS---DVVFAK 187
MtnX COG4359
2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase (methionine salvage) [Amino acid ...
 57-286 2.96e-12

2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase (methionine salvage) [Amino acid transport and metabolism];


Pssm-ID: 443493 [Multi-domain]  Cd Length: 209  Bit Score: 64.46  E-value: 2.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097  57 DFDETIVDENSDDSIVR--AAPG-QRLPESLRA---TYREGfyneyMQRVFKYLGeqgVRPRDLSAIYEAIPLSPGMSDL 130
Cdd:COG4359    7 DFDGTITEKDVIDAILErfAPPGwEEIEDDWLAgeiSSREC-----LGRQFALLP---ASKEELDALLENIEIDPGFKEF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097 131 LQFVAKQGacFEVILISDANTFGVESSLRAAGHHSLfrRILSNPSGPDARGLlALRPFHTHSCARCPANMCKHKVLSDYL 210
Cdd:COG4359   79 VQFCRERG--IPLYIVSDGLDFYIEPILERYGLSDV--PIYANRLVFDGGGI-RIEFPYADPDCSNGCGTCKCAVIRKLK 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219689097 211 RErahdgvhFERLFYVGDGANDFCPmGLLAggDVAFPRrgypmHRLIQEAQKAepssfRASVVPWETAADVRLHLQ 286
Cdd:COG4359  154 SD-------GYKVIYIGDGRSDFCA-AKLA--DLVFAK-----GKLLEYCREN-----GIPHTPFETFADVIAYLK 209
 
Name Accession Description Interval E-value
Put_Phosphatase pfam06888
Putative Phosphatase; This family contains a number of putative eukaryotic acid phosphatases. ...
 52-289 3.55e-133

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: 376.71  E-value: 3.55e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097   52 FLLTFDFDETIVDENSDDSIVRAAPGQRLPESLRATYREGFYNEYMQRVFKYLGEQGVRPRDLSAIYEAIPLSPGMSDLL 131
Cdd:pfam06888   1 ILVVFDFDKTIIDVDSDNWVVDELPTTQLFEQLRPTMPKGFWNELMDRVMKELHDQGVSIADIKAVLRSIPLVPGMVRLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097  132 QFVAKQGACFEVILISDANTFGVESSLRAAGHHSLFRRILSNPSGPDARGLLALRPFHTHSCARCPANMCKHKVLSDYLR 211
Cdd:pfam06888  81 KFLAKNGLGCDLIIISDANSFFIETILRAAGLHDLFSEIFTNPASVDARGRLTVLPYHDHSCNLCPSNMCKGKVLDEIVA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219689097  212 ERAHDGVHFERLFYVGDGANDFCPMGLLAGGDVAFPRRGYPMHRLIQEaqkaEPSSFRASVVPWETAADVRLHLQQVL 289
Cdd:pfam06888 161 SQAREGVRYERVIYVGDGANDFCPSLRLRECDVAMPRKGFPLWKLISE----NPLLLKASVVEWSSGAELEEILLQLI 234
HAD_Pase cd16418
phosphatases, similar to human PHOSPHO1 and PHOSPHO2 phosphatases; belongs to the haloacid ...
 127-245 4.66e-65

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: 199.87  E-value: 4.66e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097 127 MSDLLQFVAKQgACFEVILISDANTFGVESSLRAAGHHSLFRRILSNPSGPDARGLLALRP-FHTHSCARCPANMCKHKV 205
Cdd:cd16418   12 MVDLIKFLAKN-DGFELIIISDANSFFIEEWLEAAGFHDLFSKIFTNPASFDANGNLTVRPyFHSHSCLLCPSNMCKGKV 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 219689097 206 LSDYLRERAHDGVHFERLFYVGDGANDFCPMGLLAGGDVA 245
Cdd:cd16418   91 LEEYVASRAQDSVHYERVIYVGDGANDFCPVLRLRKGDVA 130
DKMTPPase-SF TIGR01489
2,3-diketo-5-methylthio-1-phosphopentane phosphatase; This phosphatase is a member of the IB ...
 52-248 2.17e-41

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: 141.42  E-value: 2.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097   52 FLLTFDFDETIVDENSDDSIVRAAPGQRLPESLRATYREGFYNEYMQRVFKYLGEQGVRPRDLSAIYEAIPLSPGMSDLL 131
Cdd:TIGR01489   2 VVVVSDFDGTITLNDSDDWITDKFGPPEANRLLDGVLSKTLSIKFMDRRMKGLLPSGLKEDEILEVLKSAPIDPGFKEFI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097  132 QFVAKQGacFEVILISDANTFGVESSLRAAGHHSLFRRILSNPSGPDARGLLALRPFHTHSCARCPANMCKHKVLsDYLR 211
Cdd:TIGR01489  82 AFIKEHG--IDFIVISDGNDFFIDPVLEGIGEKDVFIEIYSNPASFDNDGRHIVWPHHCHGCCSCPCGCCKGKVI-HKLS 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 219689097  212 ERAhdgvhFERLFYVGDGANDFCPMGLLaggDVAFPR 248
Cdd:TIGR01489 159 EPK-----YQHIIYIGDGVTDVCPAKLS---DVVFAK 187
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 53-239 3.72e-19

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: 82.79  E-value: 3.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097   53 LLTFDFDETIVDENSDDSIV-RAAPGQRLPESLRATYREGF--YNEYMQRVFKYLGeqGVRPRDL--SAIYEAIPLSPGM 127
Cdd:TIGR01488   1 LAIFDFDGTLTRQDSLIDLLaKLLGTNDEVIELTRLAPSGRisFEDALGRRLALLH--RSRSEEVakEFLARQVALRPGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097  128 SDLLQFVAKQGAcfEVILISDANTFGVESSLRAAGhhslFRRILSNPSGPDARGLLALRPfhthSCARCPANMCKHKVLS 207
Cdd:TIGR01488  79 RELISWLKERGI--DTVIVSGGFDFFVEPVAEKLG----IDDVFANRLEFDDNGLLTGPI----EGQVNPEGECKGKVLK 148

                         170       180       190
                  ....*....|....*....|....*....|..
gi 219689097  208 DYLRERahdGVHFERLFYVGDGANDFCPMGLL 239
Cdd:TIGR01488 149 ELLEES---KITLKKIIAVGDSVNDLPMLKLA 177
MtnX COG4359
2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase (methionine salvage) [Amino acid ...
 57-286 2.96e-12

2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase (methionine salvage) [Amino acid transport and metabolism];


Pssm-ID: 443493 [Multi-domain]  Cd Length: 209  Bit Score: 64.46  E-value: 2.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097  57 DFDETIVDENSDDSIVR--AAPG-QRLPESLRA---TYREGfyneyMQRVFKYLGeqgVRPRDLSAIYEAIPLSPGMSDL 130
Cdd:COG4359    7 DFDGTITEKDVIDAILErfAPPGwEEIEDDWLAgeiSSREC-----LGRQFALLP---ASKEELDALLENIEIDPGFKEF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097 131 LQFVAKQGacFEVILISDANTFGVESSLRAAGHHSLfrRILSNPSGPDARGLlALRPFHTHSCARCPANMCKHKVLSDYL 210
Cdd:COG4359   79 VQFCRERG--IPLYIVSDGLDFYIEPILERYGLSDV--PIYANRLVFDGGGI-RIEFPYADPDCSNGCGTCKCAVIRKLK 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219689097 211 RErahdgvhFERLFYVGDGANDFCPmGLLAggDVAFPRrgypmHRLIQEAQKAepssfRASVVPWETAADVRLHLQ 286
Cdd:COG4359  154 SD-------GYKVIYIGDGRSDFCA-AKLA--DLVFAK-----GKLLEYCREN-----GIPHTPFETFADVIAYLK 209
HAD pfam12710
haloacid dehalogenase-like hydrolase;
56-236 8.25e-10

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 57.16  E-value: 8.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097   56 FDFDETIVDENSDDSIVRAAPGQRLPESLRA-----------TYREGFYNEYMQRVFKYL-GEQGVRPRDLSAIYEAIP- 122
Cdd:pfam12710   3 FDLDGTLLDGDSLFLLIRALLRRGGPDLWRAllvllllallrLLGRLSRAGARELLRALLaGLPEEDAAELERFVAEVAl 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097  123 --LSPGMSDLLQFVAKQGacFEVILISDANTFGVESSLRAAGHHslfrRILSNPSGPDARGLLALRPFHTHSCARCPanm 200
Cdd:pfam12710  83 prLHPGALELLAAHRAAG--DRVVVVTGGLRPLVEPVLAELGFD----EVLATELEVDDGRFTGELRLIGPPCAGEG--- 153

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 219689097  201 cKHKVLSDYLRERAHdGVHFERLFYVGDGANDFcPM 236
Cdd:pfam12710 154 -KVRRLRAWLAARGL-GLDLADSVAYGDSPSDL-PM 186
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 49-246 2.97e-09

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: 56.00  E-value: 2.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097  49 APRFLLTFDFDETIVDENSDDSIVRAApGQRLPESLRAT----------YREGF--YNEYMQRVFKYLgeQGVRPRDLSA 116
Cdd:COG0560    1 RKMRLAVFDLDGTLIAGESIDELARFL-GRRGLVDRREVleevaaiterAMAGEldFEESLRFRVALL--AGLPEEELEE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097 117 IYEAI-----PLSPGMSDLLQFVAKQGacFEVILISDANTFGVESSLRAAGhhslFRRILSNPSgPDARGLL--ALRPFH 189
Cdd:COG0560   78 LAERLfeevpRLYPGARELIAEHRAAG--HKVAIVSGGFTFFVEPIAERLG----IDHVIANEL-EVEDGRLtgEVVGPI 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 219689097 190 THSCArcpanmcKHKVLSDYLRERahdGVHFERLFYVGDGANDFcPMGLLAGGDVAF 246
Cdd:COG0560  151 VDGEG-------KAEALRELAAEL---GIDLEQSYAYGDSANDL-PMLEAAGLPVAV 196
HAD_Pase cd07524
phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like ...
 57-287 7.34e-07

phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like superfamily; Bacillus subtilis recycles two toxic byproducts of polyamine metabolism, methylthioadenosine and methylthioribose, into methionine by a salvage pathway. The sixth reaction in this pathway is catalyzed by B. subtilis MtnX: the dephosphorylation of 2- hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HKMTP- 1-P) into 1,2-dihydroxy-3-keto-5-methylthiopentene. The hydrolysis of HK-MTP-1-P is a two-step mechanism involving the formation of a transiently phosphorylated aspartyl intermediate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319826 [Multi-domain]  Cd Length: 211  Bit Score: 48.87  E-value: 7.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097  57 DFDETIVDENSDDSIVR--AAPGQRLPE------SLRATYREGFyneymQRVFKYLGEQgVRPRDLSAIYEAIPLSPGMS 128
Cdd:cd07524    5 DFDGTITENDNIIYLMDefAPPLEEWEAlkegvlSQTLSFREGV-----GQMFELLPSS-LKDEIIEFLEKTAKIRPGFK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097 129 DLLQFVAKQGacFEVILISDANTFGVESSLraAGHHSLFRRILSNpsGPDARGllaLRPFHT--HSC-ARCPANMCKHKV 205
Cdd:cd07524   79 EFVAFCQEHG--IPFIIVSGGMDFFIEPLL--EGLVIEKIAIYCN--GSDFSG---EQIHIDwpHECdCTNGCGCCKSSI 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097 206 LSDYLRERAHdgvhferLFYVGDGANDFcPMGLLAggDVAFPRRGypmhrLIQEAQkAEpssfRASVVPWETAADVRLHL 285
Cdd:cd07524  150 IRKYSKPRPF-------IIVIGDSVTDL-EAAKEA--DLVFARDG-----LILKCE-EE----NLPYPPFETFTDIDIHL 209


                 ..
gi 219689097 286 QQ 287
Cdd:cd07524  210 QL 211
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 54-172 5.16e-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: 46.56  E-value: 5.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097  54 LTFDFDETIVDENSDDSIVRAAPGQRL-----PESLRATYREGFYN-------------EYMQRVFKYLGEQGVRP---R 112
Cdd:COG1011    4 VLFDLDGTLLDFDPVIAEALRALAERLglldeAEELAEAYRAIEYAlwrryergeitfaELLRRLLEELGLDLAEElaeA 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097 113 DLSAIYEAIPLSPGMSDLLQFVAKQGacFEVILISDANTFGVESSLRAAGHHSLFRRILS 172
Cdd:COG1011   84 FLAALPELVEPYPDALELLEALKARG--YRLALLTNGSAELQEAKLRRLGLDDLFDAVVS 141
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
56-232 7.00e-04

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 39.91  E-value: 7.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097  56 FDFDETIVDENSD--DSIVRAAPGQRLPESLRATYREGFYN---EYMQRVFKYLGEQGVRP--RDLSAIYEA-----IPL 123
Cdd:COG0546    6 FDLDGTLVDSAPDiaAALNEALAELGLPPLDLEELRALIGLglrELLRRLLGEDPDEELEEllARFRELYEEelldeTRL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097 124 SPGMSDLLQFVAKQGacFEVILISDANTFGVESSLRAAGHHSLFRRILS----NPSGPDARGLLALrpfhthsCARCpan 199
Cdd:COG0546   86 FPGVRELLEALKARG--IKLAVVTNKPREFAERLLEALGLDDYFDAIVGgddvPPAKPKPEPLLEA-------LERL--- 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 219689097 200 mckhkvlsdylrerahdGVHFERLFYVGDGAND 232
Cdd:COG0546  154 -----------------GLDPEEVLMVGDSPHD 169
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 129-243 2.73e-03

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: 36.60  E-value: 2.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219689097 129 DLLQFVAKQGacFEVILISDANTFGVESSLRAAGHHSLFRRILSNPSGPDARGllalrpfhthscarcpanmcKHKVLSD 208
Cdd:cd01427   14 ELLKRLRAAG--IKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKP--------------------KPKPLLL 71

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 219689097 209 YLReraHDGVHFERLFYVGDGANDFcPMGLLAGGD 243
Cdd:cd01427   72 LLL---KLGVDPEEVLFVGDSENDI-EAARAAGGR 102
 
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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