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Conserved domains on  [gi|506268084|ref|WP_015787859|]
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HAD family phosphatase [Saccharomonospora viridis]

Protein Classification

HAD family hydrolase( domain architecture ID 10001729)

haloacid dehalogenase (HAD) family hydrolase uses a nucleophilic aspartate in the phosphoryl transfer reaction; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

CATH:  3.30.1240.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|15337123|33940035|37786806
SCOP:  3001890

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 15-237 8.02e-71

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: 217.40  E-value: 8.02e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084  15 PATSAAFFDLDKTIIASSSALAFSKPFLRQGLINRRAALKSAYAQLMFSLSGADANrtERLRAEISRMCAGWDVNQVKAI 94
Cdd:COG0560    1 RKMRLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVLEEVAAITERAMAGELDF--EESLRFRVALLAGLPEEELEEL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084  95 VSETLHDVvsPLVYAEATELIERHKAEGRDVIVLSATGEELVRPIADMLGITHCVGSRMEIVDGRYTGTV-EYYCYGEYK 173
Cdd:COG0560   79 AERLFEEV--PRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEVvGPIVDGEGK 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506268084 174 AIAARRLAAEHGYDLAASHAYTDSSTDLPLLETVGHPHAVNPDKALRRIA-VERGWPVHTFTNPV 237
Cdd:COG0560  157 AEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAAdRERGWPVLDLLGDR 221
 
Name Accession Description Interval E-value
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 15-237 8.02e-71

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: 217.40  E-value: 8.02e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084  15 PATSAAFFDLDKTIIASSSALAFSKPFLRQGLINRRAALKSAYAQLMFSLSGADANrtERLRAEISRMCAGWDVNQVKAI 94
Cdd:COG0560    1 RKMRLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVLEEVAAITERAMAGELDF--EESLRFRVALLAGLPEEELEEL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084  95 VSETLHDVvsPLVYAEATELIERHKAEGRDVIVLSATGEELVRPIADMLGITHCVGSRMEIVDGRYTGTV-EYYCYGEYK 173
Cdd:COG0560   79 AERLFEEV--PRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEVvGPIVDGEGK 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506268084 174 AIAARRLAAEHGYDLAASHAYTDSSTDLPLLETVGHPHAVNPDKALRRIA-VERGWPVHTFTNPV 237
Cdd:COG0560  157 AEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAAdRERGWPVLDLLGDR 221
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 19-219 7.18e-69

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: 211.82  E-value: 7.18e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084   19 AAFFDLDKTIIASSSALAFSKPFLRQGLINRRAALKSAYAQLMFSLsGADANRTERLRAEISRMCAGWDVNQVKAIVSET 98
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASKNILFEELRLPKVLARFEFFL-NRGLDYMAYYRAFALDALAGLLEEDVRAIVEEF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084   99 LHDVVSPLVYAEATELIERHKAEGRDVIVLSATGEELVRPIADMLGITHCVGSRMEIV-DGRYTGTVEY-YCYGEYKAIA 176
Cdd:TIGR01490  80 VNQKIESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTRLEESeDGIYTGNIDGnNCKGEGKVHA 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 506268084  177 ARRLAAEHGYDLAASHAYTDSSTDLPLLETVGHPHAVNPDKAL 219
Cdd:TIGR01490 160 LAELLAEEQIDLKDSYAYGDSISDLPLLSLVGHPYVVNPDKKL 202
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 19-216 3.93e-65

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: 202.15  E-value: 3.93e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084  19 AAFFDLDKTIIASSSALAFSKpflRQGLINRRAALKSAY---AQLMFSLSGADANRTERLRAEISRMCAGWDVNQVKAIV 95
Cdd:cd02612    1 LAFFDLDGTLIAGDSFFAFLR---FKGIAERRAPLEELLllrLMALYALGRLDGAGMEALLGFATAGLAGELAALVEEFV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084  96 SETLHdvvsPLVYAEATELIERHKAEGRDVIVLSATGEELVRPIADMLGITHCVGSRMEIVDGRYTGTVEYY-CYGEYKA 174
Cdd:cd02612   78 EEYIL----RVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDNVLGTQLETEDGRYTGRIIGPpCYGEGKV 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 506268084 175 IAARRLAAEHGYDLAASHAYTDSSTDLPLLETVGHPHAVNPD 216
Cdd:cd02612  154 KRLREWLAEEGIDLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD pfam12710
haloacid dehalogenase-like hydrolase;
20-205 5.52e-36

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 127.26  E-value: 5.52e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084   20 AFFDLDKTIIASSSALAFSKPFLRQGLINRRAALKSAYAQLMF-SLSGADANRTERLRAEISRMCAGWDVNQVKAIVSET 98
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGPDLWRALLVLLLLALLrLLGRLSRAGARELLRALLAGLPEEDAAELERFVAEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084   99 LHDVVSPlvyaEATELIERHKAEGRDVIVLSATGEELVRPIADMLGITHCVGSRMEIVDGRYTGTVEYY---CYGEYKAI 175
Cdd:pfam12710  81 ALPRLHP----GALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDGRFTGELRLIgppCAGEGKVR 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 506268084  176 AARRLAAEHGY--DLAASHAYTDSSTDLPLLE 205
Cdd:pfam12710 157 RLRAWLAARGLglDLADSVAYGDSPSDLPMLR 188
PRK08238 PRK08238
UbiA family prenyltransferase;
103-242 2.46e-06

UbiA family prenyltransferase;


Pssm-ID: 236195 [Multi-domain]  Cd Length: 479  Bit Score: 48.33  E-value: 2.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084 103 VSPLVYAEAT-ELIERHKAEGRDVIVLSATGEELVRPIADMLGI-THCVGSrmeivDGRYTgtveyyCYGEYKAIAARRL 180
Cdd:PRK08238  68 VATLPYNEEVlDYLRAERAAGRKLVLATASDERLAQAVAAHLGLfDGVFAS-----DGTTN------LKGAAKAAALVEA 136

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506268084 181 AAEHGYDLAAshaytDSSTDLPLLETVGHPHAVNPDKALRRiAVERGWPVHTFTNPVSPRAR 242
Cdd:PRK08238 137 FGERGFDYAG-----NSAADLPVWAAARRAIVVGASPGVAR-AARALGPVERVFPPRPARLR 192
 
Name Accession Description Interval E-value
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 15-237 8.02e-71

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: 217.40  E-value: 8.02e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084  15 PATSAAFFDLDKTIIASSSALAFSKPFLRQGLINRRAALKSAYAQLMFSLSGADANrtERLRAEISRMCAGWDVNQVKAI 94
Cdd:COG0560    1 RKMRLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVLEEVAAITERAMAGELDF--EESLRFRVALLAGLPEEELEEL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084  95 VSETLHDVvsPLVYAEATELIERHKAEGRDVIVLSATGEELVRPIADMLGITHCVGSRMEIVDGRYTGTV-EYYCYGEYK 173
Cdd:COG0560   79 AERLFEEV--PRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEVvGPIVDGEGK 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506268084 174 AIAARRLAAEHGYDLAASHAYTDSSTDLPLLETVGHPHAVNPDKALRRIA-VERGWPVHTFTNPV 237
Cdd:COG0560  157 AEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAAdRERGWPVLDLLGDR 221
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 19-219 7.18e-69

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: 211.82  E-value: 7.18e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084   19 AAFFDLDKTIIASSSALAFSKPFLRQGLINRRAALKSAYAQLMFSLsGADANRTERLRAEISRMCAGWDVNQVKAIVSET 98
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASKNILFEELRLPKVLARFEFFL-NRGLDYMAYYRAFALDALAGLLEEDVRAIVEEF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084   99 LHDVVSPLVYAEATELIERHKAEGRDVIVLSATGEELVRPIADMLGITHCVGSRMEIV-DGRYTGTVEY-YCYGEYKAIA 176
Cdd:TIGR01490  80 VNQKIESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTRLEESeDGIYTGNIDGnNCKGEGKVHA 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 506268084  177 ARRLAAEHGYDLAASHAYTDSSTDLPLLETVGHPHAVNPDKAL 219
Cdd:TIGR01490 160 LAELLAEEQIDLKDSYAYGDSISDLPLLSLVGHPYVVNPDKKL 202
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 19-216 3.93e-65

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: 202.15  E-value: 3.93e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084  19 AAFFDLDKTIIASSSALAFSKpflRQGLINRRAALKSAY---AQLMFSLSGADANRTERLRAEISRMCAGWDVNQVKAIV 95
Cdd:cd02612    1 LAFFDLDGTLIAGDSFFAFLR---FKGIAERRAPLEELLllrLMALYALGRLDGAGMEALLGFATAGLAGELAALVEEFV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084  96 SETLHdvvsPLVYAEATELIERHKAEGRDVIVLSATGEELVRPIADMLGITHCVGSRMEIVDGRYTGTVEYY-CYGEYKA 174
Cdd:cd02612   78 EEYIL----RVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDNVLGTQLETEDGRYTGRIIGPpCYGEGKV 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 506268084 175 IAARRLAAEHGYDLAASHAYTDSSTDLPLLETVGHPHAVNPD 216
Cdd:cd02612  154 KRLREWLAEEGIDLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD pfam12710
haloacid dehalogenase-like hydrolase;
20-205 5.52e-36

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 127.26  E-value: 5.52e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084   20 AFFDLDKTIIASSSALAFSKPFLRQGLINRRAALKSAYAQLMF-SLSGADANRTERLRAEISRMCAGWDVNQVKAIVSET 98
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGPDLWRALLVLLLLALLrLLGRLSRAGARELLRALLAGLPEEDAAELERFVAEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084   99 LHDVVSPlvyaEATELIERHKAEGRDVIVLSATGEELVRPIADMLGITHCVGSRMEIVDGRYTGTVEYY---CYGEYKAI 175
Cdd:pfam12710  81 ALPRLHP----GALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDGRFTGELRLIgppCAGEGKVR 156

                         170       180       190
                  ....*....|....*....|....*....|..
gi 506268084  176 AARRLAAEHGY--DLAASHAYTDSSTDLPLLE 205
Cdd:pfam12710 157 RLRAWLAARGLglDLADSVAYGDSPSDLPMLR 188
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 19-207 4.60e-19

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


Pssm-ID: 273653 [Multi-domain]  Cd Length: 177  Bit Score: 82.40  E-value: 4.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084   19 AAFFDLDKTIIASSSALAFSKPFLrqGLINRRAALksaYAQLMfslsgadaNRTERLRAEISRMCAGWDVNQVKAIVSET 98
Cdd:TIGR01488   1 LAIFDFDGTLTRQDSLIDLLAKLL--GTNDEVIEL---TRLAP--------SGRISFEDALGRRLALLHRSRSEEVAKEF 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084   99 LHDVVSPLVYAEatELIERHKAEGRDVIVLSATGEELVRPIADMLGITHCVGSRMEIVD-GRYTGTVEYY--CYGEYKAI 175
Cdd:TIGR01488  68 LARQVALRPGAR--ELISWLKERGIDTVIVSGGFDFFVEPVAEKLGIDDVFANRLEFDDnGLLTGPIEGQvnPEGECKGK 145

                         170       180       190
                  ....*....|....*....|....*....|..
gi 506268084  176 AARRLAAEHGYDLAASHAYTDSSTDLPLLETV 207
Cdd:TIGR01488 146 VLKELLEESKITLKKIIAVGDSVNDLPMLKLA 177
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 88-208 1.64e-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: 47.16  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084  88 VNQVKAIVSETLHDVVSPLVYAE-ATELIERHKAEGRDVIVLSATGEELVRPIADMLGITHCVGSRMEIVDGRYTGTV-E 165
Cdd:cd07500   51 VALLKGLPESVLDEVYERLTLTPgAEELIQTLKAKGYKTAVVSGGFTYFTDRLAEELGLDYAFANELEIKDGKLTGKVlG 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 506268084 166 YYCYGEYKAIAARRLAAEHGYDLAASHAYTDSSTDLPLLETVG 208
Cdd:cd07500  131 PIVDAQRKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAG 173
PRK08238 PRK08238
UbiA family prenyltransferase;
103-242 2.46e-06

UbiA family prenyltransferase;


Pssm-ID: 236195 [Multi-domain]  Cd Length: 479  Bit Score: 48.33  E-value: 2.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084 103 VSPLVYAEAT-ELIERHKAEGRDVIVLSATGEELVRPIADMLGI-THCVGSrmeivDGRYTgtveyyCYGEYKAIAARRL 180
Cdd:PRK08238  68 VATLPYNEEVlDYLRAERAAGRKLVLATASDERLAQAVAAHLGLfDGVFAS-----DGTTN------LKGAAKAAALVEA 136

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506268084 181 AAEHGYDLAAshaytDSSTDLPLLETVGHPHAVNPDKALRRiAVERGWPVHTFTNPVSPRAR 242
Cdd:PRK08238 137 FGERGFDYAG-----NSAADLPVWAAARRAIVVGASPGVAR-AARALGPVERVFPPRPARLR 192
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 21-149 9.49e-04

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: 39.63  E-value: 9.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506268084  21 FFDLDKTII--ASSSALAFSKPFLRQGLINRRAALKSAYAQLMFSLSGADANRTERLRAEISRMCAGWDVNQVKAIVSET 98
Cdd:COG1011    5 LFDLDGTLLdfDPVIAEALRALAERLGLLDEAEELAEAYRAIEYALWRRYERGEITFAELLRRLLEELGLDLAEELAEAF 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 506268084  99 LHDVVSPL-VYAEATELIERHKAEGRDVIVLSATGEELVRPIADMLGITHCV 149
Cdd:COG1011   85 LAALPELVePYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLF 136
serB PRK11133
phosphoserine phosphatase; Provisional
 141-208 1.95e-03

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 39.16  E-value: 1.95e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506268084 141 DMLGITHCVGSRMEIVDGRYTGTVEyycyG-----EYKAIAARRLAAEHGYDLAASHAYTDSSTDLPLLETVG 208
Cdd:PRK11133 216 DKLRLDAAVANELEIMDGKLTGNVL----GdivdaQYKADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAG 284
 
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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