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Conserved domains on  [gi|313151193|ref|NP_001186215|]
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pyridoxal phosphate phosphatase PHOSPHO2 [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. ...
 3-239 1.11e-140

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: 393.66  E-value: 1.11e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193    3 ILLVFDFDNTIIDDNSDTWIVQCAPNKKLPIELRDSYRKGFWTEFMGRVFKYLGDKGVREHEMKRAVTSLPFTPGMVELF 82
Cdd:pfam06888   1 ILVVFDFDKTIIDVDSDNWVVDELPTTQLFEQLRPTMPKGFWNELMDRVMKELHDQGVSIADIKAVLRSIPLVPGMVRLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193   83 NFIRKNKDKFDCIIISDSNSVFIDWVLEAASFHDIFDKVFTNPAAFNSNGHLTVENYHTHSCNRCPKNLCKKVVLIEFVD 162
Cdd:pfam06888  81 KFLAKNGLGCDLIIISDANSFFIETILRAAGLHDLFSEIFTNPASVDARGRLTVLPYHDHSCNLCPSNMCKGKVLDEIVA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313151193  163 KQLQQGVNYTQIVYIGDGGNDVCPVTFLKNDDVAMPRKGYTLQKTLSRmsqNLEPMEYSVVVWSSGVDIISHLQFLI 239
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. ...
 3-239 1.11e-140

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: 393.66  E-value: 1.11e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193    3 ILLVFDFDNTIIDDNSDTWIVQCAPNKKLPIELRDSYRKGFWTEFMGRVFKYLGDKGVREHEMKRAVTSLPFTPGMVELF 82
Cdd:pfam06888   1 ILVVFDFDKTIIDVDSDNWVVDELPTTQLFEQLRPTMPKGFWNELMDRVMKELHDQGVSIADIKAVLRSIPLVPGMVRLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193   83 NFIRKNKDKFDCIIISDSNSVFIDWVLEAASFHDIFDKVFTNPAAFNSNGHLTVENYHTHSCNRCPKNLCKKVVLIEFVD 162
Cdd:pfam06888  81 KFLAKNGLGCDLIIISDANSFFIETILRAAGLHDLFSEIFTNPASVDARGRLTVLPYHDHSCNLCPSNMCKGKVLDEIVA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313151193  163 KQLQQGVNYTQIVYIGDGGNDVCPVTFLKNDDVAMPRKGYTLQKTLSRmsqNLEPMEYSVVVWSSGVDIISHLQFLI 239
Cdd:pfam06888 161 SQAREGVRYERVIYVGDGANDFCPSLRLRECDVAMPRKGFPLWKLISE---NPLLLKASVVEWSSGAELEEILLQLI 234
DKMTPPase-SF TIGR01489
2,3-diketo-5-methylthio-1-phosphopentane phosphatase; This phosphatase is a member of the IB ...
 2-200 1.26e-72

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: 219.61  E-value: 1.26e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193    2 KILLVFDFDNTIIDDNSDTWIVQCAPNKKLPIELRDSYRKGFWTEFMGRVFKYLGDKGVREHEMKRAVTSLPFTPGMVEL 81
Cdd:TIGR01489   1 KVVVVSDFDGTITLNDSDDWITDKFGPPEANRLLDGVLSKTLSIKFMDRRMKGLLPSGLKEDEILEVLKSAPIDPGFKEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193   82 FNFIRKNkdKFDCIIISDSNSVFIDWVLEAASFHDIFDKVFTNPAAFNSNGHLTVENYHTHSCNRCPKNLCKkvvlIEFV 161
Cdd:TIGR01489  81 IAFIKEH--GIDFIVISDGNDFFIDPVLEGIGEKDVFIEIYSNPASFDNDGRHIVWPHHCHGCCSCPCGCCK----GKVI 154

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 313151193  162 DKQLQQGvnYTQIVYIGDGGNDVCPVTFLkndDVAMPRK 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 1.34e-62

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: 191.78  E-value: 1.34e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193  78 MVELFNFIRKNkDKFDCIIISDSNSVFIDWVLEAASFHDIFDKVFTNPAAFNSNGHLTVENY-HTHSCNRCPKNLCKKVV 156
Cdd:cd16418   12 MVDLIKFLAKN-DGFELIIISDANSFFIEEWLEAAGFHDLFSKIFTNPASFDANGNLTVRPYfHSHSCLLCPSNMCKGKV 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 313151193 157 LIEFVDKQLQQGVNYTQIVYIGDGGNDVCPVTFLKNDDVA 196
Cdd:cd16418   91 LEEYVASRAQDSVHYERVIYVGDGANDFCPVLRLRKGDVA 130
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-184 1.51e-12

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: 64.47  E-value: 1.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193   1 MKILLVFDFDNTIIDDNSDTWIVQCAPNKKLPI---------ELRDSYRKGFWT--EFMGRVFKYLgdKGVREHEMKRAV 69
Cdd:COG0560    2 KMRLAVFDLDGTLIAGESIDELARFLGRRGLVDrrevleevaAITERAMAGELDfeESLRFRVALL--AGLPEEELEELA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193  70 TSL-----PFTPGMVELFNFIRKNKDKfdCIIISDSNSVFIDWVleAASFHdiFDKVFTNPAAFNsNGHLT--VENYHTH 142
Cdd:COG0560   80 ERLfeevpRLYPGARELIAEHRAAGHK--VAIVSGGFTFFVEPI--AERLG--IDHVIANELEVE-DGRLTgeVVGPIVD 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 313151193 143 SCNrcpknlcKKVVLIEFVDkqlQQGVNYTQIVYIGDGGNDV 184
Cdd:COG0560  153 GEG-------KAEALRELAA---ELGIDLEQSYAYGDSANDL 184
 
Name Accession Description Interval E-value
Put_Phosphatase pfam06888
Putative Phosphatase; This family contains a number of putative eukaryotic acid phosphatases. ...
 3-239 1.11e-140

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: 393.66  E-value: 1.11e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193    3 ILLVFDFDNTIIDDNSDTWIVQCAPNKKLPIELRDSYRKGFWTEFMGRVFKYLGDKGVREHEMKRAVTSLPFTPGMVELF 82
Cdd:pfam06888   1 ILVVFDFDKTIIDVDSDNWVVDELPTTQLFEQLRPTMPKGFWNELMDRVMKELHDQGVSIADIKAVLRSIPLVPGMVRLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193   83 NFIRKNKDKFDCIIISDSNSVFIDWVLEAASFHDIFDKVFTNPAAFNSNGHLTVENYHTHSCNRCPKNLCKKVVLIEFVD 162
Cdd:pfam06888  81 KFLAKNGLGCDLIIISDANSFFIETILRAAGLHDLFSEIFTNPASVDARGRLTVLPYHDHSCNLCPSNMCKGKVLDEIVA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313151193  163 KQLQQGVNYTQIVYIGDGGNDVCPVTFLKNDDVAMPRKGYTLQKTLSRmsqNLEPMEYSVVVWSSGVDIISHLQFLI 239
Cdd:pfam06888 161 SQAREGVRYERVIYVGDGANDFCPSLRLRECDVAMPRKGFPLWKLISE---NPLLLKASVVEWSSGAELEEILLQLI 234
DKMTPPase-SF TIGR01489
2,3-diketo-5-methylthio-1-phosphopentane phosphatase; This phosphatase is a member of the IB ...
 2-200 1.26e-72

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: 219.61  E-value: 1.26e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193    2 KILLVFDFDNTIIDDNSDTWIVQCAPNKKLPIELRDSYRKGFWTEFMGRVFKYLGDKGVREHEMKRAVTSLPFTPGMVEL 81
Cdd:TIGR01489   1 KVVVVSDFDGTITLNDSDDWITDKFGPPEANRLLDGVLSKTLSIKFMDRRMKGLLPSGLKEDEILEVLKSAPIDPGFKEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193   82 FNFIRKNkdKFDCIIISDSNSVFIDWVLEAASFHDIFDKVFTNPAAFNSNGHLTVENYHTHSCNRCPKNLCKkvvlIEFV 161
Cdd:TIGR01489  81 IAFIKEH--GIDFIVISDGNDFFIDPVLEGIGEKDVFIEIYSNPASFDNDGRHIVWPHHCHGCCSCPCGCCK----GKVI 154

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 313151193  162 DKQLQQGvnYTQIVYIGDGGNDVCPVTFLkndDVAMPRK 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 1.34e-62

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: 191.78  E-value: 1.34e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193  78 MVELFNFIRKNkDKFDCIIISDSNSVFIDWVLEAASFHDIFDKVFTNPAAFNSNGHLTVENY-HTHSCNRCPKNLCKKVV 156
Cdd:cd16418   12 MVDLIKFLAKN-DGFELIIISDANSFFIEEWLEAAGFHDLFSKIFTNPASFDANGNLTVRPYfHSHSCLLCPSNMCKGKV 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 313151193 157 LIEFVDKQLQQGVNYTQIVYIGDGGNDVCPVTFLKNDDVA 196
Cdd:cd16418   91 LEEYVASRAQDSVHYERVIYVGDGANDFCPVLRLRKGDVA 130
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 4-186 2.94e-21

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: 87.02  E-value: 2.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193    4 LLVFDFDNTIIDDNSDTWIV-QCAPNKKLPIELRDSYRKGFWTEF--MGRVFKYLGDKGVREHEMKRAVTSLPFTPGMVE 80
Cdd:TIGR01488   1 LAIFDFDGTLTRQDSLIDLLaKLLGTNDEVIELTRLAPSGRISFEdaLGRRLALLHRSRSEEVAKEFLARQVALRPGARE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193   81 LFNFIRKNKDkfDCIIISDSNSVFIDWVLEAASFHDIfdkvFTNPAAFNSNGHLTVEnyhtHSCNRCPKNLCKKVVLIEf 160
Cdd:TIGR01488  81 LISWLKERGI--DTVIVSGGFDFFVEPVAEKLGIDDV----FANRLEFDDNGLLTGP----IEGQVNPEGECKGKVLKE- 149

                         170       180
                  ....*....|....*....|....*.
gi 313151193  161 vdKQLQQGVNYTQIVYIGDGGNDVCP 186
Cdd:TIGR01488 150 --LLEESKITLKKIIAVGDSVNDLPM 173
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-184 1.51e-12

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: 64.47  E-value: 1.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193   1 MKILLVFDFDNTIIDDNSDTWIVQCAPNKKLPI---------ELRDSYRKGFWT--EFMGRVFKYLgdKGVREHEMKRAV 69
Cdd:COG0560    2 KMRLAVFDLDGTLIAGESIDELARFLGRRGLVDrrevleevaAITERAMAGELDfeESLRFRVALL--AGLPEEELEELA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193  70 TSL-----PFTPGMVELFNFIRKNKDKfdCIIISDSNSVFIDWVleAASFHdiFDKVFTNPAAFNsNGHLT--VENYHTH 142
Cdd:COG0560   80 ERLfeevpRLYPGARELIAEHRAAGHK--VAIVSGGFTFFVEPI--AERLG--IDHVIANELEVE-DGRLTgeVVGPIVD 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 313151193 143 SCNrcpknlcKKVVLIEFVDkqlQQGVNYTQIVYIGDGGNDV 184
Cdd:COG0560  153 GEG-------KAEALRELAA---ELGIDLEQSYAYGDSANDL 184
HAD pfam12710
haloacid dehalogenase-like hydrolase;
5-185 5.39e-08

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 51.38  E-value: 5.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193    5 LVFDFDNTIIDDNSDT-WIVQCAPNKKLPI--ELRDSYRKGFW--------TEFMGRVFKYLGD-KGVREHEMKRAVTSL 72
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFlLIRALLRRGGPDLwrALLVLLLLALLrllgrlsrAGARELLRALLAGlPEEDAAELERFVAEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193   73 P---FTPGMVELFNFIRKNKDKfdCIIISDSNSVFIDWVLEAASFHDIFDKVFtnpaaFNSNGHLTVEN-YHTHSCNRCP 148
Cdd:pfam12710  81 AlprLHPGALELLAAHRAAGDR--VVVVTGGLRPLVEPVLAELGFDEVLATEL-----EVDDGRFTGELrLIGPPCAGEG 153

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 313151193  149 KNLCKKVVLIEfvdkqLQQGVNYTQIVYIGDGGNDVC 185
Cdd:pfam12710 154 KVRRLRAWLAA-----RGLGLDLADSVAYGDSPSDLP 185
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 4-183 7.25e-06

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: 45.23  E-value: 7.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193   4 LLVFDFDNTI-----IDDNSDTW--------IVQCAPNKKLpiELRDSYRKgfwtefmgRVfKYLgdKGVREHEMKRAVT 70
Cdd:cd07500    1 LIVFDMDSTLiqqevIDELAAEAgvgeevaaITERAMRGEL--DFEESLRE--------RV-ALL--KGLPESVLDEVYE 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193  71 SLPFTPGMVELFNFIRKNKDKfdCIIISDSNSVFIDWVLEAASFhdifDKVFTNPAAFnSNGHLTVEnyhthscnrcpkn 150
Cdd:cd07500   68 RLTLTPGAEELIQTLKAKGYK--TAVVSGGFTYFTDRLAEELGL----DYAFANELEI-KDGKLTGK------------- 127

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 313151193 151 lckkvVLIEFVDKQ-----LQQ-----GVNYTQIVYIGDGGND 183
Cdd:cd07500  128 -----VLGPIVDAQrkaetLQElaarlGIPLEQTVAVGDGAND 165
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 5-128 1.00e-05

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: 45.02  E-value: 1.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193   5 LVFDFDNTIIDDNSD---------TWIVQCAPNKKLPIELRDSYRKGF---------WTEFMGRVFKYLG---DKGVREH 63
Cdd:COG1011    4 VLFDLDGTLLDFDPViaealralaERLGLLDEAEELAEAYRAIEYALWrryergeitFAELLRRLLEELGldlAEELAEA 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313151193  64 EMKRAVTSLPFTPGMVELFNFIRKNKdkFDCIIISDSNSVFIDWVLEAASFHDIFDKVFT---------NPAAF 128
Cdd:COG1011   84 FLAALPELVEPYPDALELLEALKARG--YRLALLTNGSAELQEAKLRRLGLDDLFDAVVSseevgvrkpDPEIF 155
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 1-183 8.38e-05

phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate. It catalyzes the last of three steps in the biosynthesis of serine from D-3-phosphoglycerate. Note that this enzyme acts on free phosphoserine, not on phosphoserine residues of phosphoproteins. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273022 [Multi-domain]  Cd Length: 219  Bit Score: 42.34  E-value: 8.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193    1 MKILLVFDFDNTIIDDNSDTWIVQCAPNKKLPIELRDSYRKG---FWTEFMGRVfKYLgdKGVREHEMKRAVTSLPFTPG 77
Cdd:TIGR00338  13 SKKLVVFDMDSTLINAETIDEIAKIAGVEEEVSEITERAMRGeldFKASLRERV-ALL--KGLPVELLKEVRENLPLTEG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193   78 MVELFNFIRKNKDKFdcIIISDSNSVFIDWVLE-------AASFHDIFDKVFTNpaafNSNGHLTVENYHThscnrcpKN 150
Cdd:TIGR00338  90 AEELVKTLKEKGYKV--AVISGGFDLFAEHVKDklgldaaFANRLEVEDGKLTG----LVEGPIVDASYKG-------KT 156

                         170       180       190
                  ....*....|....*....|....*....|...
gi 313151193  151 LCKKvvliefvdkQLQQGVNYTQIVYIGDGGND 183
Cdd:TIGR00338 157 LLIL---------LRKEGISPENTVAVGDGAND 180
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 78-184 1.36e-04

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: 40.07  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193  78 MVELFNFIRKNKDKfdCIIISDSNSVFIDWVLEAASFHDIFDKVFTNPAAFNsnghltvenyhthscnrcPKNLCKKVVL 157
Cdd:cd01427   12 AVELLKRLRAAGIK--LAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGT------------------PKPKPKPLLL 71

                         90       100
                 ....*....|....*....|....*..
gi 313151193 158 IefvdkQLQQGVNYTQIVYIGDGGNDV 184
Cdd:cd01427   72 L-----LLKLGVDPEEVLFVGDSENDI 93
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
4-184 5.73e-03

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 36.83  E-value: 5.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193   4 LLVFDFDNTIIDDNSD--TWIVQCAPNKKLPIELRDSYR-------KGFWTEFMGRVFKYLGD---KGVREHEMKRAVTS 71
Cdd:COG0546    3 LVLFDLDGTLVDSAPDiaAALNEALAELGLPPLDLEELRaliglglRELLRRLLGEDPDEELEellARFRELYEEELLDE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313151193  72 LPFTPGMVELFNFIRKNkdKFDCIIISDSNSVFIDWVLEAASFHDIFDKVFTnpaafnsnghltvenyHTHSCNRCPKNL 151
Cdd:COG0546   83 TRLFPGVRELLEALKAR--GIKLAVVTNKPREFAERLLEALGLDDYFDAIVG----------------GDDVPPAKPKPE 144

                        170       180       190
                 ....*....|....*....|....*....|...
gi 313151193 152 ckkvVLIEFVDkqlQQGVNYTQIVYIGDGGNDV 184
Cdd:COG0546  145 ----PLLEALE---RLGLDPEEVLMVGDSPHDI 170
 
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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