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Conserved domains on  [gi|2524880393|ref|WP_286833799|]
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MULTISPECIES: phosphoserine phosphatase SerB [Proteiniphilum]

Protein Classification

phosphoserine phosphatase SerB( domain architecture ID 18727198)

phosphoserine phosphatase SerB is a HAD (haloacid dehalogenase) family hydrolase that catalyzes the dephosphorylation of phosphoserine (P-Ser); also catalyzes the hydrolysis of phosphothreonine (P-Thr)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 194-373 4.07e-99

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: 292.91  E-value: 4.07e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 194 LICFDMDSTLIQTEVIDELAERAGVGDKVRAITEQAMHGEIDFEESFRQRVKLLEGLDVSVMKEIAENLPITEGLGRLMK 273
Cdd:cd07500     1 LIVFDMDSTLIQQEVIDELAAEAGVGEEVAAITERAMRGELDFEESLRERVALLKGLPESVLDEVYERLTLTPGAEELIQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 274 VLQKVGFKTAILSGGFSYFGNYLKEKYGFDYMYANELEIKNGKLTGNYLGDVVDGRRKAELLRLIAQVEKIDLRQTVAVG 353
Cdd:cd07500    81 TLKAKGYKTAVVSGGFTYFTDRLAEELGLDYAFANELEIKDGKLTGKVLGPIVDAQRKAETLQELAARLGIPLEQTVAVG 160

                         170       180
                  ....*....|....*....|
gi 2524880393 354 DGANDLPMLGIAGLGIAFHA 373
Cdd:cd07500   161 DGANDLPMLKAAGLGIAFHA 180
ACT COG3830
ACT domain, binds amino acids and other small ligands [Signal transduction mechanisms];
4-213 4.66e-64

ACT domain, binds amino acids and other small ligands [Signal transduction mechanisms];


:

Pssm-ID: 443042 [Multi-domain]  Cd Length: 212  Bit Score: 204.55  E-value: 4.66e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393   4 NSEIILLNINGEDKPGLTAALTEILAKHDAFILDIGQSDIHRNLSLGILFKSKNNNS--GEIMKDLLFKAYEMDVNIRFT 81
Cdd:COG3830     1 MSMKALITVTGKDRPGITAAVSGVLAEHGVNILDISQTVIHGYFTMGMLVDLPESSAsfEELQKDLEAAGEELGVEVRVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393  82 PISAERYSNWVGMQGKNRYIITLLGRILTARQIAAVSKIIAEQNLNIDNIVRLTGRIPLDEKQRAAKSCVELSVRGTPNN 161
Cdd:COG3830    81 HEDIFDYMHRIGRQGVVRYILTLLARAITAEAIAAVAAIVAINGLNIDRITRLSGRLELDSGPDADVACVELAARGLAED 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2524880393 162 RQQMQEAFLELTSSLNFDISFQEESMFRRMRRLICFDMDSTLIQTEVIDELA 213
Cdd:COG3830   161 VAAAVAVALALARELRRDIAFQDDDRFRRRRRILVFDMDATLEEVEVEVELA 212
 
Name Accession Description Interval E-value
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 194-373 4.07e-99

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: 292.91  E-value: 4.07e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 194 LICFDMDSTLIQTEVIDELAERAGVGDKVRAITEQAMHGEIDFEESFRQRVKLLEGLDVSVMKEIAENLPITEGLGRLMK 273
Cdd:cd07500     1 LIVFDMDSTLIQQEVIDELAAEAGVGEEVAAITERAMRGELDFEESLRERVALLKGLPESVLDEVYERLTLTPGAEELIQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 274 VLQKVGFKTAILSGGFSYFGNYLKEKYGFDYMYANELEIKNGKLTGNYLGDVVDGRRKAELLRLIAQVEKIDLRQTVAVG 353
Cdd:cd07500    81 TLKAKGYKTAVVSGGFTYFTDRLAEELGLDYAFANELEIKDGKLTGKVLGPIVDAQRKAETLQELAARLGIPLEQTVAVG 160

                         170       180
                  ....*....|....*....|
gi 2524880393 354 DGANDLPMLGIAGLGIAFHA 373
Cdd:cd07500   161 DGANDLPMLKAAGLGIAFHA 180
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 179-397 4.41e-92

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: 276.54  E-value: 4.41e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 179 DISFQEESMFRRMRRLICFDMDSTLIQTEVIDELAERAGVGDKVRAITEQAMHGEIDFEESFRQRVKLLEGLDVSVMKEI 258
Cdd:TIGR00338   1 DIAHSELSPLLRSKKLVVFDMDSTLINAETIDEIAKIAGVEEEVSEITERAMRGELDFKASLRERVALLKGLPVELLKEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 259 AENLPITEGLGRLMKVLQKVGFKTAILSGGFSYFGNYLKEKYGFDYMYANELEIKNGKLTGNYLGDVVDGRRKAELLRLI 338
Cdd:TIGR00338  81 RENLPLTEGAEELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDAAFANRLEVEDGKLTGLVEGPIVDASYKGKTLLIL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2524880393 339 AQVEKIDLRQTVAVGDGANDLPMLGIAGLGIAFHAKPKVKQNADQSLSTVGIDGILYFL 397
Cdd:TIGR00338 161 LRKEGISPENTVAVGDGANDLSMIKAAGLGIAFNAKPKLQQKADICINKKDLTDILPLL 219
serB PRK11133
phosphoserine phosphatase; Provisional
 194-381 1.91e-88

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 271.05  E-value: 1.91e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 194 LICFDMDSTLIQTEVIDELAERAGVGDKVRAITEQAMHGEIDFEESFRQRVKLLEGLDVSVMKEIAENLPITEGLGRLMK 273
Cdd:PRK11133  112 LLVMDMDSTAIQIECIDEIAKLAGTGEEVAEVTERAMRGELDFEASLRQRVATLKGADANILQQVRENLPLMPGLTELVL 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 274 VLQKVGFKTAILSGGFSYFGNYLKEKYGFDYMYANELEIKNGKLTGNYLGDVVDGRRKAELLRLIAQVEKIDLRQTVAVG 353
Cdd:PRK11133  192 KLQALGWKVAIASGGFTYFADYLRDKLRLDAAVANELEIMDGKLTGNVLGDIVDAQYKADTLTRLAQEYEIPLAQTVAIG 271

                         170       180
                  ....*....|....*....|....*...
gi 2524880393 354 DGANDLPMLGIAGLGIAFHAKPKVKQNA 381
Cdd:PRK11133  272 DGANDLPMIKAAGLGIAYHAKPKVNEQA 299
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 190-399 2.91e-83

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: 253.99  E-value: 2.91e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 190 RMRRLICFDMDSTLIQTEVIDELAERAG---------VGDKVRAITEQAMHGEIDFEESFRQRVKLLEGLDVSVMKEIAE 260
Cdd:COG0560     1 RKMRLAVFDLDGTLIAGESIDELARFLGrrglvdrreVLEEVAAITERAMAGELDFEESLRFRVALLAGLPEEELEELAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 261 NL-----PITEGLGRLMKVLQKVGFKTAILSGGFSYFGNYLKEKYGFDYMYANELEIKNGKLTGNYLGDVVDGRRKAELL 335
Cdd:COG0560    81 RLfeevpRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEVVGPIVDGEGKAEAL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524880393 336 RLIAQVEKIDLRQTVAVGDGANDLPMLGIAGLGIAFHAKPKVKQNADQSLSTvgidGILYFLGY 399
Cdd:COG0560   161 RELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAADRERGW----PVLDLLGD 220
ACT COG3830
ACT domain, binds amino acids and other small ligands [Signal transduction mechanisms];
4-213 4.66e-64

ACT domain, binds amino acids and other small ligands [Signal transduction mechanisms];


Pssm-ID: 443042 [Multi-domain]  Cd Length: 212  Bit Score: 204.55  E-value: 4.66e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393   4 NSEIILLNINGEDKPGLTAALTEILAKHDAFILDIGQSDIHRNLSLGILFKSKNNNS--GEIMKDLLFKAYEMDVNIRFT 81
Cdd:COG3830     1 MSMKALITVTGKDRPGITAAVSGVLAEHGVNILDISQTVIHGYFTMGMLVDLPESSAsfEELQKDLEAAGEELGVEVRVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393  82 PISAERYSNWVGMQGKNRYIITLLGRILTARQIAAVSKIIAEQNLNIDNIVRLTGRIPLDEKQRAAKSCVELSVRGTPNN 161
Cdd:COG3830    81 HEDIFDYMHRIGRQGVVRYILTLLARAITAEAIAAVAAIVAINGLNIDRITRLSGRLELDSGPDADVACVELAARGLAED 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2524880393 162 RQQMQEAFLELTSSLNFDISFQEESMFRRMRRLICFDMDSTLIQTEVIDELA 213
Cdd:COG3830   161 VAAAVAVALALARELRRDIAFQDDDRFRRRRRILVFDMDATLEEVEVEVELA 212
ACT_PSP_2 cd04871
ACT domains found N-terminal of phosphoserine phosphatase (PSP, SerB); The ACT_PSP_2 CD ...
 101-184 1.12e-33

ACT domains found N-terminal of phosphoserine phosphatase (PSP, SerB); The ACT_PSP_2 CD includes the second of the two ACT domains found N-terminal of phosphoserine phosphatase (PSP, SerB). PSPs belong to the L-2-haloacid dehalogenase-like protein superfamily. PSP is involved in serine metabolism; serine is synthesized from phosphoglycerate through sequential reactions catalyzed by 3-phosphoglycerate dehydrogenase (SerA), 3-phosphoserine aminotransferase (SerC), and SerB. Members of this CD belong to the superfamily of ACT regulatory domains


Pssm-ID: 153143  Cd Length: 84  Bit Score: 120.87  E-value: 1.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 101 IITLLGRILTARQIAAVSKIIAEQNLNIDNIVRLTGRIPLDEKQRAAKSCVELSVRGTPNNRQQMQEAFLELTSSLNFDI 180
Cdd:cd04871     1 IVTLLGRPLTAEQLAAVTRVVADQGLNIDRIRRLSGRVPLEEQDDSPKACVEFSVRGQPADLEALRAALLELASELNVDI 80


                  ....
gi 2524880393 181 SFQE 184
Cdd:cd04871    81 AFQR 84
ACT_6 pfam13740
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains.
 6-81 1.86e-25

ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains.


Pssm-ID: 433446 [Multi-domain]  Cd Length: 76  Bit Score: 98.40  E-value: 1.86e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524880393   6 EIILLNINGEDKPGLTAALTEILAKHDAFILDIGQSDIHRNLSLGILFKSKNNNSGEIMKDLLFKAYEMDVNIRFT 81
Cdd:pfam13740   1 EILLITATGPDRPGLTASLTAVLAEHGCNILDSGQAVIHNRLSLGLLVSGPWDALARLEKDLLFLAHELGLTVRFK 76
HAD pfam12710
haloacid dehalogenase-like hydrolase;
195-362 1.69e-19

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 85.66  E-value: 1.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 195 ICFDMDSTLIQTEVIDELAE---RAGVGDKVRAITEQAMH------GEIDFEESFRQRVKLLEGLDVSVMKEIAENLP-- 263
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRallRRGGPDLWRALLVLLLLallrllGRLSRAGARELLRALLAGLPEEDAAELERFVAev 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 264 ----ITEGLGRLMKVLQKVGFKTAILSGGFSYFGNYLKEKYGFDYMYANELEIKNGKLTGN--YLGDVVDGRRKAELLR- 336
Cdd:pfam12710  81 alprLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDGRFTGElrLIGPPCAGEGKVRRLRa 160

                         170       180
                  ....*....|....*....|....*..
gi 2524880393 337 -LIAQVEKIDLRQTVAVGDGANDLPML 362
Cdd:pfam12710 161 wLAARGLGLDLADSVAYGDSPSDLPML 187
 
Name Accession Description Interval E-value
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 194-373 4.07e-99

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: 292.91  E-value: 4.07e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 194 LICFDMDSTLIQTEVIDELAERAGVGDKVRAITEQAMHGEIDFEESFRQRVKLLEGLDVSVMKEIAENLPITEGLGRLMK 273
Cdd:cd07500     1 LIVFDMDSTLIQQEVIDELAAEAGVGEEVAAITERAMRGELDFEESLRERVALLKGLPESVLDEVYERLTLTPGAEELIQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 274 VLQKVGFKTAILSGGFSYFGNYLKEKYGFDYMYANELEIKNGKLTGNYLGDVVDGRRKAELLRLIAQVEKIDLRQTVAVG 353
Cdd:cd07500    81 TLKAKGYKTAVVSGGFTYFTDRLAEELGLDYAFANELEIKDGKLTGKVLGPIVDAQRKAETLQELAARLGIPLEQTVAVG 160

                         170       180
                  ....*....|....*....|
gi 2524880393 354 DGANDLPMLGIAGLGIAFHA 373
Cdd:cd07500   161 DGANDLPMLKAAGLGIAFHA 180
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 179-397 4.41e-92

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: 276.54  E-value: 4.41e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 179 DISFQEESMFRRMRRLICFDMDSTLIQTEVIDELAERAGVGDKVRAITEQAMHGEIDFEESFRQRVKLLEGLDVSVMKEI 258
Cdd:TIGR00338   1 DIAHSELSPLLRSKKLVVFDMDSTLINAETIDEIAKIAGVEEEVSEITERAMRGELDFKASLRERVALLKGLPVELLKEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 259 AENLPITEGLGRLMKVLQKVGFKTAILSGGFSYFGNYLKEKYGFDYMYANELEIKNGKLTGNYLGDVVDGRRKAELLRLI 338
Cdd:TIGR00338  81 RENLPLTEGAEELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDAAFANRLEVEDGKLTGLVEGPIVDASYKGKTLLIL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2524880393 339 AQVEKIDLRQTVAVGDGANDLPMLGIAGLGIAFHAKPKVKQNADQSLSTVGIDGILYFL 397
Cdd:TIGR00338 161 LRKEGISPENTVAVGDGANDLSMIKAAGLGIAFNAKPKLQQKADICINKKDLTDILPLL 219
serB PRK11133
phosphoserine phosphatase; Provisional
 194-381 1.91e-88

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 271.05  E-value: 1.91e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 194 LICFDMDSTLIQTEVIDELAERAGVGDKVRAITEQAMHGEIDFEESFRQRVKLLEGLDVSVMKEIAENLPITEGLGRLMK 273
Cdd:PRK11133  112 LLVMDMDSTAIQIECIDEIAKLAGTGEEVAEVTERAMRGELDFEASLRQRVATLKGADANILQQVRENLPLMPGLTELVL 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 274 VLQKVGFKTAILSGGFSYFGNYLKEKYGFDYMYANELEIKNGKLTGNYLGDVVDGRRKAELLRLIAQVEKIDLRQTVAVG 353
Cdd:PRK11133  192 KLQALGWKVAIASGGFTYFADYLRDKLRLDAAVANELEIMDGKLTGNVLGDIVDAQYKADTLTRLAQEYEIPLAQTVAIG 271

                         170       180
                  ....*....|....*....|....*...
gi 2524880393 354 DGANDLPMLGIAGLGIAFHAKPKVKQNA 381
Cdd:PRK11133  272 DGANDLPMIKAAGLGIAYHAKPKVNEQA 299
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 190-399 2.91e-83

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: 253.99  E-value: 2.91e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 190 RMRRLICFDMDSTLIQTEVIDELAERAG---------VGDKVRAITEQAMHGEIDFEESFRQRVKLLEGLDVSVMKEIAE 260
Cdd:COG0560     1 RKMRLAVFDLDGTLIAGESIDELARFLGrrglvdrreVLEEVAAITERAMAGELDFEESLRFRVALLAGLPEEELEELAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 261 NL-----PITEGLGRLMKVLQKVGFKTAILSGGFSYFGNYLKEKYGFDYMYANELEIKNGKLTGNYLGDVVDGRRKAELL 335
Cdd:COG0560    81 RLfeevpRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEVVGPIVDGEGKAEAL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524880393 336 RLIAQVEKIDLRQTVAVGDGANDLPMLGIAGLGIAFHAKPKVKQNADQSLSTvgidGILYFLGY 399
Cdd:COG0560   161 RELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAADRERGW----PVLDLLGD 220
ACT COG3830
ACT domain, binds amino acids and other small ligands [Signal transduction mechanisms];
4-213 4.66e-64

ACT domain, binds amino acids and other small ligands [Signal transduction mechanisms];


Pssm-ID: 443042 [Multi-domain]  Cd Length: 212  Bit Score: 204.55  E-value: 4.66e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393   4 NSEIILLNINGEDKPGLTAALTEILAKHDAFILDIGQSDIHRNLSLGILFKSKNNNS--GEIMKDLLFKAYEMDVNIRFT 81
Cdd:COG3830     1 MSMKALITVTGKDRPGITAAVSGVLAEHGVNILDISQTVIHGYFTMGMLVDLPESSAsfEELQKDLEAAGEELGVEVRVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393  82 PISAERYSNWVGMQGKNRYIITLLGRILTARQIAAVSKIIAEQNLNIDNIVRLTGRIPLDEKQRAAKSCVELSVRGTPNN 161
Cdd:COG3830    81 HEDIFDYMHRIGRQGVVRYILTLLARAITAEAIAAVAAIVAINGLNIDRITRLSGRLELDSGPDADVACVELAARGLAED 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2524880393 162 RQQMQEAFLELTSSLNFDISFQEESMFRRMRRLICFDMDSTLIQTEVIDELA 213
Cdd:COG3830   161 VAAAVAVALALARELRRDIAFQDDDRFRRRRRILVFDMDATLEEVEVEVELA 212
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 194-365 2.59e-37

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: 133.63  E-value: 2.59e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 194 LICFDMDSTLIQTE-VIDELAERAGVGDKVRAITEQAMHGEIDFEESFRQRVKLLEGL-DVSVMKE-IAENLPITEGLGR 270
Cdd:TIGR01488   1 LAIFDFDGTLTRQDsLIDLLAKLLGTNDEVIELTRLAPSGRISFEDALGRRLALLHRSrSEEVAKEfLARQVALRPGARE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 271 LMKVLQKVGFKTAILSGGFSYFGNYLKEKYGFDYMYANELEI-KNGKLTGNYLGDV-VDGRRKAELLRLIAQVEKIDLRQ 348
Cdd:TIGR01488  81 LISWLKERGIDTVIVSGGFDFFVEPVAEKLGIDDVFANRLEFdDNGLLTGPIEGQVnPEGECKGKVLKELLEESKITLKK 160

                         170
                  ....*....|....*..
gi 2524880393 349 TVAVGDGANDLPMLGIA 365
Cdd:TIGR01488 161 IIAVGDSVNDLPMLKLA 177
ACT_PSP_2 cd04871
ACT domains found N-terminal of phosphoserine phosphatase (PSP, SerB); The ACT_PSP_2 CD ...
 101-184 1.12e-33

ACT domains found N-terminal of phosphoserine phosphatase (PSP, SerB); The ACT_PSP_2 CD includes the second of the two ACT domains found N-terminal of phosphoserine phosphatase (PSP, SerB). PSPs belong to the L-2-haloacid dehalogenase-like protein superfamily. PSP is involved in serine metabolism; serine is synthesized from phosphoglycerate through sequential reactions catalyzed by 3-phosphoglycerate dehydrogenase (SerA), 3-phosphoserine aminotransferase (SerC), and SerB. Members of this CD belong to the superfamily of ACT regulatory domains


Pssm-ID: 153143  Cd Length: 84  Bit Score: 120.87  E-value: 1.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 101 IITLLGRILTARQIAAVSKIIAEQNLNIDNIVRLTGRIPLDEKQRAAKSCVELSVRGTPNNRQQMQEAFLELTSSLNFDI 180
Cdd:cd04871     1 IVTLLGRPLTAEQLAAVTRVVADQGLNIDRIRRLSGRVPLEEQDDSPKACVEFSVRGQPADLEALRAALLELASELNVDI 80


                  ....
gi 2524880393 181 SFQE 184
Cdd:cd04871    81 AFQR 84
HAD_PSP_eu cd04309
phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human ...
 195-382 5.03e-27

phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human PSP, EC 3.1.3.3, catalyzes the third and final of the L-serine biosynthesis pathway, the Mg2+-dependent hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, L-serine is a precursor for the biosynthesis of glycine. HPSP regulates the levels of glycine and D-serine (converted from L-serine), the putative co-agonists for the glycine site of the NMDA receptor in the brain. Plant 3-PSP catalyzes the conversion of 3-phosphoserine to serine in the last step of the plastidic pathway of serine biosynthesis. 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: 319801 [Multi-domain]  Cd Length: 202  Bit Score: 106.60  E-value: 5.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 195 ICFDMDSTLIQTEVIDELAERAGVGDKVRAITEQAMHGEIDFEESFRQRVKLLEGLDVSVMKEIAENLP-ITEGLGRLMK 273
Cdd:cd04309     3 VCFDVDSTVIQEEGIDELAKFCGVGDEVAELTRRAMGGSIPFRDALRKRLAIINPTKEQVDEFLEEHPPrLTPGVEELVS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 274 VLQKVGFKTAILSGGFSYFGNYLKEKYGF--DYMYANELEI-KNGKLTG---NYLGDVVDGRRKA-ELLRliaqvEKIDL 346
Cdd:cd04309    83 RLKARGVEVYLISGGFRELIEPVASQLGIplENVFANRLLFdFNGEYAGfdeTQPTSRSGGKAKViEQLK-----EKHHY 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2524880393 347 RQTVAVGDGANDLPMLGIAGLGIAFHA---KPKVKQNAD 382
Cdd:cd04309   158 KRVIMIGDGATDLEACPPADAFIGFGGnviREKVKARAD 196
ACT_PSP_1 cd04870
CT domains found N-terminal of phosphoserine phosphatase (PSP, SerB); The ACT_PSP_1 CD ...
 9-82 1.48e-25

CT domains found N-terminal of phosphoserine phosphatase (PSP, SerB); The ACT_PSP_1 CD includes the first of the two ACT domains found N-terminal of phosphoserine phosphatase (PSP, SerB). PSPs belong to the L-2-haloacid dehalogenase-like protein superfamily. PSP is involved in serine metabolism; serine is synthesized from phosphoglycerate through sequential reactions catalyzed by 3-phosphoglycerate dehydrogenase (SerA), 3-phosphoserine aminotransferase (SerC), and SerB. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153142  Cd Length: 75  Bit Score: 98.47  E-value: 1.48e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524880393   9 LLNINGEDKPGLTAALTEILAKHDAFILDIGQSDIHRNLSLGILFKSK-NNNSGEIMKDLLFKAYEMDVNIRFTP 82
Cdd:cd04870     1 LITVTGPDRPGLTSALTEVLAAHGVRILDVGQAVIHGRLSLGILVQIPdSADSEALLKDLLFKAHELGLQVRFEP 75
ACT_6 pfam13740
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains.
 6-81 1.86e-25

ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains.


Pssm-ID: 433446 [Multi-domain]  Cd Length: 76  Bit Score: 98.40  E-value: 1.86e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524880393   6 EIILLNINGEDKPGLTAALTEILAKHDAFILDIGQSDIHRNLSLGILFKSKNNNSGEIMKDLLFKAYEMDVNIRFT 81
Cdd:pfam13740   1 EILLITATGPDRPGLTASLTAVLAEHGCNILDSGQAVIHNRLSLGLLVSGPWDALARLEKDLLFLAHELGLTVRFK 76
PLN02954 PLN02954
phosphoserine phosphatase
 195-382 7.18e-22

phosphoserine phosphatase


Pssm-ID: 215514 [Multi-domain]  Cd Length: 224  Bit Score: 93.22  E-value: 7.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 195 ICFDMDSTLIQTEVIDELAERAGVGDKVRAITEQAMHGEIDFEESFRQRVKLLEGLDVSVMKEIAENLP-ITEGLGRLMK 273
Cdd:PLN02954   15 VCFDVDSTVCVDEGIDELAEFCGAGEAVAEWTAKAMGGSVPFEEALAARLSLFKPSLSQVEEFLEKRPPrLSPGIPELVK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 274 VLQKVGFKTAILSGGFSYFGNYLKEKYGF--DYMYANELEIKNgklTGNYLG-DVVD------GRRKAellrlIAQVEKI 344
Cdd:PLN02954   95 KLRARGTDVYLVSGGFRQMIAPVAAILGIppENIFANQILFGD---SGEYAGfDENEptsrsgGKAEA-----VQHIKKK 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2524880393 345 DLRQTVA-VGDGANDLP--MLGIAGLGIAF---HAKPKVKQNAD 382
Cdd:PLN02954  167 HGYKTMVmIGDGATDLEarKPGGADLFIGYggvQVREAVAAKAD 210
HAD pfam12710
haloacid dehalogenase-like hydrolase;
195-362 1.69e-19

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 85.66  E-value: 1.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 195 ICFDMDSTLIQTEVIDELAE---RAGVGDKVRAITEQAMH------GEIDFEESFRQRVKLLEGLDVSVMKEIAENLP-- 263
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRallRRGGPDLWRALLVLLLLallrllGRLSRAGARELLRALLAGLPEEDAAELERFVAev 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 264 ----ITEGLGRLMKVLQKVGFKTAILSGGFSYFGNYLKEKYGFDYMYANELEIKNGKLTGN--YLGDVVDGRRKAELLR- 336
Cdd:pfam12710  81 alprLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDGRFTGElrLIGPPCAGEGKVRRLRa 160

                         170       180
                  ....*....|....*....|....*..
gi 2524880393 337 -LIAQVEKIDLRQTVAVGDGANDLPML 362
Cdd:pfam12710 161 wLAARGLGLDLADSVAYGDSPSDLPML 187
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 197-366 3.33e-17

HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase (TIGR00338). Due to this relationship, several of these sequences have been annotated as "phosphoserine phosphatase related proteins," or "Phosphoserine phosphatase-family enzymes." There is presently no evidence that any of the enzymes in this model possess PSPase activity. OMNI|NTL01ML1250 is annotated as a "possible transferase," however this is due to the C-terminal domain found on this sequence which is homologous to a group of glycerol-phosphate acyltransferases (between trusted and noise to TIGR00530). A subset of these sequences including OMNI|CC1962, the Caulobacter crescentus CicA protein cluster together and may represent a separate equivalog. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273654 [Multi-domain]  Cd Length: 202  Bit Score: 79.31  E-value: 3.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 197 FDMDSTLIQTEVIDE-LAERAGVGD--------KVRAiteQAMH--GEIDFEESfRQRVKLLE---GLDVSVMKEIAE-- 260
Cdd:TIGR01490   4 FDFDGTLTAKDTLFIfLKFLASKNIlfeelrlpKVLA---RFEFflNRGLDYMA-YYRAFALDalaGLLEEDVRAIVEef 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 261 -NLPITEGL----GRLMKVLQKVGFKTAILSGGFSYFGNYLKEKYGFDYMYANEL-EIKNGKLTGNYLGDVVDGRRKAEL 334
Cdd:TIGR01490  80 vNQKIESILypeaRDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTRLeESEDGIYTGNIDGNNCKGEGKVHA 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2524880393 335 LRLIAQVEKIDLRQTVAVGDGANDLPMLGIAG 366
Cdd:TIGR01490 160 LAELLAEEQIDLKDSYAYGDSISDLPLLSLVG 191
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 193-366 3.64e-16

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: 76.47  E-value: 3.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 193 RLICFDMDSTLIQ-----TEVIDELA-----------ERAGVGDKVRAITEQAMHGEIDFEES---FRQRVKLLEGLDVS 253
Cdd:pfam00702   2 KAVVFDLDGTLTDgepvvTEAIAELAsehplakaivaAAEDLPIPVEDFTARLLLGKRDWLEEldiLRGLVETLEAEGLT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 254 V-------MKEIAENLPITEGLGRLMKVLQKVGFKTAILSGGFSYFGNYLKEKYGFDYMYANELEIkngkltgnylGDVV 326
Cdd:pfam00702  82 VvlvellgVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISG----------DDVG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2524880393 327 DGRRKAELLRLIAQVEKIDLRQTVAVGDGANDLPMLGIAG 366
Cdd:pfam00702 152 VGKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 197-366 1.46e-14

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). 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: 319796 [Multi-domain]  Cd Length: 195  Bit Score: 71.95  E-value: 1.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 197 FDMDSTLIQTEV-------IDELAERAGVGD--KVRAITEQAMhGEIDfEESFRQRVK-----LLEGLDVSV---MKEIA 259
Cdd:cd02612     4 FDLDGTLIAGDSffaflrfKGIAERRAPLEEllLLRLMALYAL-GRLD-GAGMEALLGfatagLAGELAALVeefVEEYI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 260 ENLPITEGLgRLMKVLQKVGFKTAILSGGFSYFGNYLKEKYGFDYMYANELEIKNGKLTGNYLGDVVDGRRKAELLRLIA 339
Cdd:cd02612    82 LRVLYPEAR-ELIAWHKAAGHDVVLISASPEELVAPIARKLGIDNVLGTQLETEDGRYTGRIIGPPCYGEGKVKRLREWL 160

                         170       180
                  ....*....|....*....|....*..
gi 2524880393 340 QVEKIDLRQTVAVGDGANDLPMLGIAG 366
Cdd:cd02612   161 AEEGIDLKDSYAYSDSINDLPMLEAVG 187
HAD_ThrH_like cd02607
bifunctional phosphoserine phosphatase/phosphoserine:homoserine phosphotransferase, similar to ...
 196-388 3.48e-11

bifunctional phosphoserine phosphatase/phosphoserine:homoserine phosphotransferase, similar to Pseudomonas aeruginosa ThrH; This family includes Pseudomonas aeruginosa ThrH which is a duel activity enzyme having both phosphoserine phosphatase and phosphoserine:homoserine phosphotransferase activities, i.e. it can dephosphorylate phosphoserine, and can transfer phosphate from phosphoserine to homoserine. 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: 319793 [Multi-domain]  Cd Length: 195  Bit Score: 61.91  E-value: 3.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 196 CFDMDSTLIqTEVIDELAERAGVgDKVRAITEqamhgEI-DFEESFRQRVKLLE--GLDVSVMKEIAENLPITEGLGRLM 272
Cdd:cd02607     5 CLDLEGVLV-PEIWIAFAEKTGI-DALKATTR-----DIpDYDVLMKQRLRILDehGLKLADIQEVIATLKPLEGAVEFV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 273 KVLqKVGFKTAILSGGFSYFGNYLKEKYGFDYMYANELEIKNGKLTGNYLGDVVDGRRkaelLRLIAQveKIDLRQTVAV 352
Cdd:cd02607    78 DWL-RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHKLQTDDDDRVVGYQLRQKDPKR----QSVIAV--KSLYYRVIAA 150

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2524880393 353 GDGANDLPMLGIAGLGIAFHAKPKVKQNADQSLSTV 388
Cdd:cd02607   151 GDSYNDTTMLSEAHAGILFHAPENVIREFPQFPAVH 186
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 331-397 5.03e-11

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 61.30  E-value: 5.03e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524880393 331 KAELLRLIAQVEKIDLRQTVAVGDGANDLPMLGIAGLGIAF-HAKPKVKQNADQSLSTVGIDGILYFL 397
Cdd:COG0561   122 KGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMgNAPPEVKAAADYVTGSNDEDGVAEAL 189
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 306-397 4.56e-10

Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 59.59  E-value: 4.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 306 YANELEIKNGKLTGNYLGDVVDGRRKAELLRLIAQVEKIDLRQTVAVGDGANDLPMLGIAGLGIAFH-AKPKVKQNADQS 384
Cdd:TIGR00099 164 LELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGnADEELKALADYV 243

                          90
                  ....*....|...
gi 2524880393 385 LSTVGIDGILYFL 397
Cdd:TIGR00099 244 TDSNNEDGVALAL 256
thrH PRK13582
bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;
193-383 5.25e-10

bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;


Pssm-ID: 237437 [Multi-domain]  Cd Length: 205  Bit Score: 58.79  E-value: 5.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 193 RLICFDMDSTLIqTEVIDELAERAGVgDKVRAITEQamhgEIDFEESFRQRVKLLE--GLDVS-VMKEIAENLPIT---E 266
Cdd:PRK13582    2 EIVCLDLEGVLV-PEIWIAFAEKTGI-PELRATTRD----IPDYDVLMKQRLDILDehGLGLAdIQEVIATLDPLPgavE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 267 GLGRLMKVLQKVgfktaILSGGFSYFGNYLKEKYGFDYMYANELEI-KNGKLTGnYLGDVVDGRRKAellrlIAQVEKID 345
Cdd:PRK13582   76 FLDWLRERFQVV-----ILSDTFYEFAGPLMRQLGWPTLFCHSLEVdEDGMITG-YDLRQPDGKRQA-----VKALKSLG 144

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2524880393 346 LRqTVAVGDGANDLPMLGIAGLGIAFHAKPKVKQNADQ 383
Cdd:PRK13582  145 YR-VIAAGDSYNDTTMLGEADAGILFRPPANVIAEFPQ 181
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 331-397 1.58e-09

haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes.


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 58.02  E-value: 1.58e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2524880393 331 KAELLRLIAQVEKIDLRQTVAVGDGANDLPMLGIAGLGIAFH-AKPKVKQNADQSLSTVGIDGILYFL 397
Cdd:pfam08282 188 KGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGnASPEVKAAADYVTDSNNEDGVAKAL 255
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 331-382 4.87e-08

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-phosphate. 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: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 53.75  E-value: 4.87e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2524880393 331 KAELLRLIAQVEKIDLRQTVAVGDGANDLPMLGIAGLGIAF-HAKPKVKQNAD 382
Cdd:cd07516   184 KGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMgNAIDEVKEAAD 236
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 324-397 5.60e-08

phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. 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: 319819 [Multi-domain]  Cd Length: 213  Bit Score: 53.00  E-value: 5.60e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524880393 324 DVVD-GRRKAELLRLIAQVEKIDLRQTVAVGDGANDLPMLGIAGLGIAF-HAKPKVKQNADQSLSTVGIDGILYFL 397
Cdd:cd07517   134 DVIPkGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMgNAHEELKEIADYVTKDVDEDGILKAL 209
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 193-397 1.42e-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: 48.87  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 193 RLICFDMDSTLIQ-----TEVIDELAERAGVGDKVRAITE-----------QAMHGEIDFEESFRQRVKLLeGLDVS--- 253
Cdd:COG1011     2 KAVLFDLDGTLLDfdpviAEALRALAERLGLLDEAEELAEayraieyalwrRYERGEITFAELLRRLLEEL-GLDLAeel 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 254 ---VMKEIAENLPITEGLGRLMKVLQKVGFKTAILSGGFSYFGNYLKEKYGFDymyaneleikngkltgNYLGDVVD--- 327
Cdd:COG1011    81 aeaFLAALPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLD----------------DLFDAVVSsee 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524880393 328 -GRRK--AELLRLIAQVEKIDLRQTVAVGD-GANDLpmLGIAGLGI-AFHAKPKVKQNADQSLSTVGIDGILYFL 397
Cdd:COG1011   145 vGVRKpdPEIFELALERLGVPPEEALFVGDsPETDV--AGARAAGMrTVWVNRSGEPAPAEPRPDYVISDLAELL 217
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
193-359 3.30e-06

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 47.62  E-value: 3.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 193 RLICFDMDSTLIQT-----EVIDELAERAG------------VGDKVRAITEQAMHGEID--FEESFRQRVKLLEgldvs 253
Cdd:COG0546     2 KLVLFDLDGTLVDSapdiaAALNEALAELGlppldleelralIGLGLRELLRRLLGEDPDeeLEELLARFRELYE----- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 254 vmKEIAENLPITEGLGRLMKVLQKVGFKTAILSGGFSYFGNYLKEKYG----FDYMYANEleikngkltgnylgDVVDGR 329
Cdd:COG0546    77 --EELLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGlddyFDAIVGGD--------------DVPPAK 140

                         170       180       190
                  ....*....|....*....|....*....|
gi 2524880393 330 RKAELLRLIAQVEKIDLRQTVAVGDGANDL 359
Cdd:COG0546   141 PKPEPLLEALERLGLDPEEVLMVGDSPHDI 170
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 331-382 4.65e-06

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 47.28  E-value: 4.65e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2524880393 331 KAELLRLIAQVEKIDLRQTVAVGDGANDLPMLGIAGLGIAF-HAKPKVKQNAD 382
Cdd:PRK01158  158 KGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVaNADEELKEAAD 210
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 267-382 8.12e-06

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily phosphatases [Cell wall/membrane/envelope biogenesis, General function prediction only];


Pssm-ID: 441384 [Multi-domain]  Cd Length: 170  Bit Score: 45.81  E-value: 8.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 267 GLGrlMKVLQKVGFKTAILSGGFSyfgNYLKEKygfdymyANELEIKngkltgnylgDVVDGRR-KAELLRLIAQVEKID 345
Cdd:COG1778    41 GLG--IKLLRKAGIKVAIITGRDS---PAVRRR-------AEELGIT----------HVYQGVKdKLEALEELLAKLGLS 98

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2524880393 346 LRQTVAVGDGANDLPMLGIAGLGIA-FHAKPKVKQNAD 382
Cdd:COG1778    99 PEEVAYIGDDLPDLPVMRRVGLSVApADAHPEVKAAAD 136
COG4087 COG4087
Soluble P-type ATPase [General function prediction only];
341-370 1.44e-05

Soluble P-type ATPase [General function prediction only];


Pssm-ID: 443263 [Multi-domain]  Cd Length: 156  Bit Score: 44.77  E-value: 1.44e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 2524880393 341 VEKIDLRQTVAVGDGANDLPMLGIAGLGIA 370
Cdd:COG4087    86 VEKLGAETTVAIGNGRNDVLMLKEAALGIA 115
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 328-397 1.79e-05

phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), and Pyrococcus horikoshii PH1421, a magnesium-dependent phosphatase; belongs to the haloacid dehalogenase-like superfamily; Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PGPase) catalyzes the magnesium-dependent dephosphorylation of phosphoglycolate. This family also includes Pyrococcus horikoshii OT3 PH1421, a magnesium-dependent phosphatase. 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: 319816 [Multi-domain]  Cd Length: 139  Bit Score: 44.12  E-value: 1.79e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524880393 328 GRRKAELLRLIAQVEKIDLRQTVAVGDGANDLPMLGIAGLGIAF-HAKPKVKQNADQSLSTVGIDGILYFL 397
Cdd:cd07514    65 GVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVaNADEELKEAADYVTDASYGDGVLEAI 135
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 271-371 1.98e-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: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 271 LMKVLQKVGFKTAILSGGFSYFGNYLKEKYG----FDYMYANEleikngkltgnylgDVVDGRRKAELLRLIAQVEKIDL 346
Cdd:cd01427    15 LLKRLRAAGIKLAIVTNRSREALRALLEKLGlgdlFDGIIGSD--------------GGGTPKPKPKPLLLLLLKLGVDP 80

                          90       100
                  ....*....|....*....|....*.
gi 2524880393 347 RQTVAVGDGANDLPMLGIAG-LGIAF 371
Cdd:cd01427    81 EEVLFVGDSENDIEAARAAGgRTVAV 106
Put_Phosphatase pfam06888
Putative Phosphatase; This family contains a number of putative eukaryotic acid phosphatases. ...
 193-371 6.27e-05

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: 43.90  E-value: 6.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 193 RLICFDMDSTLIQ----TEVIDELaeragvGDKVRAITEQAMHgEIDFEESFRQRV-KLLEGLDVSV--MKEIAENLPIT 265
Cdd:pfam06888   1 ILVVFDFDKTIIDvdsdNWVVDEL------PTTQLFEQLRPTM-PKGFWNELMDRVmKELHDQGVSIadIKAVLRSIPLV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 266 EGLGRLMKVLQK--VGFKTAILSGGFSYFGNYLKEKYG----FDYMYANELEI-KNGKLT-GNYL-------------GD 324
Cdd:pfam06888  74 PGMVRLIKFLAKngLGCDLIIISDANSFFIETILRAAGlhdlFSEIFTNPASVdARGRLTvLPYHdhscnlcpsnmckGK 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2524880393 325 VVDgRRKAELLRliaqvEKIDLRQTVAVGDGANDL-PMLGIAGLGIAF 371
Cdd:pfam06888 154 VLD-EIVASQAR-----EGVRYERVIYVGDGANDFcPSLRLRECDVAM 195
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 220-383 1.37e-04

sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP equivalog model (TIGR01485), encompassing plants and cyanobacteria, as well as those archaeal sequences which are the closest relatives (TIGR01487). It remains to be shown whether these archaeal sequences catalyze the same reaction as SPP.


Pssm-ID: 273650 [Multi-domain]  Cd Length: 225  Bit Score: 42.84  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 220 DKVRAITEqaMHGEIDFEESFRQR-VKLLEGLDVSVMKEIAENLpiteglgRLMKVLQKVGFKTAILSGGFSYfGN---Y 295
Cdd:TIGR01482  87 DIVIAKTF--PFSRLKVQYPRRASlVKMRYGIDVDTVREIIKEL-------GLNLVAVDSGFDIHILPQGVNK-GVavkK 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524880393 296 LKEKYGFDYmyaneleikngkltgnylgdvvdgrrkaellrliaqvekidlRQTVAVGDGANDLPMLGIAGLGIAF-HAK 374
Cdd:TIGR01482 157 LKEKLGIKP------------------------------------------GETLVCGDSENDIDLFEVPGFGVAVaNAQ 194


                  ....*....
gi 2524880393 375 PKVKQNADQ 383
Cdd:TIGR01482 195 PELKEWADY 203
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 331-395 6.38e-04

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 41.22  E-value: 6.38e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524880393 331 KAELLRLIAQVEKIDLRQTVAVGDGANDLPMLGIAGLGIAF-HAKPKVKQNADQSLSTVGIDGILY 395
Cdd:PRK10513  197 KGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAMgNAIPSVKEVAQFVTKSNLEDGVAF 262
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 324-382 1.59e-03

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 40.01  E-value: 1.59e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524880393 324 DVVD----GRRKAELLRLIAQVEKIDLRQTVAVGDGANDLPMLGIAGLGIAF-HAKPKVKQNAD 382
Cdd:PRK10530  189 DQVDiarkGNSKGKRLTQWVEAQGWSMKNVVAFGDNFNDISMLEAAGLGVAMgNADDAVKARAD 252
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 344-382 1.91e-03

Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli YbiV can act as both a sugar phosphatase and as a phosphotransferase. 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: 319820 [Multi-domain]  Cd Length: 184  Bit Score: 39.10  E-value: 1.91e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2524880393 344 IDLRQTVAVGDGANDLPMLGIAGLGIAF-HAKPKVKQNAD 382
Cdd:cd07518   129 ISPDEVMAFGDGGNDIEMLKYAGYSYAMeNAPEEVKAAAK 168
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 317-370 2.38e-03

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 38.90  E-value: 2.38e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2524880393 317 LTGNYLGDVVD-GRRKAELLRLIAQVEKIDLRQTVAVGDGANDLPMLGIAGLGIA 370
Cdd:TIGR01484 152 YSGKTDLEVLPaGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVA 206
 
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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