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Conserved domains on  [gi|896567165|ref|WP_049463206|]
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MULTISPECIES: HAD family hydrolase [Stenotrophomonas]

Protein Classification

HAD family hydrolase( domain architecture ID 11552400)

HAD (haloacid dehalogenase) family hydrolase similar to Pseudomonas aeruginosa histidinol-phosphatase that catalyzes the dephosphorylation of histidinol-phosphate to histidinol, the direct precursor of histidine; the HAD (haloacid dehalogenase) family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

EC:  3.1.3.-
Gene Ontology:  GO:0046872|GO:0016791|GO:0016311
PubMed:  16889794|15337123
SCOP:  3001890

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 3-189 8.25e-51

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: 162.48  E-value: 8.25e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165   3 LALFDFDHTVTTCDTYGRFLRRVATAEQLAQ-AWWKVGPWLAAYKLKLISAERIRARVTRLTFSDRHsdDIATLAAGFSR 81
Cdd:cd02612    1 LAFFDLDGTLIAGDSFFAFLRFKGIAERRAPlEELLLLRLMALYALGRLDGAGMEALLGFATAGLAG--ELAALVEEFVE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165  82 EFLPDVVRPEMLEQIRWHKEQQHTVVIVSGSLDLYLRPWCEQLGLQ-LICNRLESQDGRLTGRYAGGDC-GPRKVEHIRR 159
Cdd:cd02612   79 EYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDnVLGTQLETEDGRYTGRIIGPPCyGEGKVKRLRE 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 896567165 160 QF--DLSRYVRIHAYGDSSEDKPMLALAHERW 189
Cdd:cd02612  159 WLaeEGIDLKDSYAYSDSINDLPMLEAVGHPV 190
 
Name Accession Description Interval E-value
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 3-189 8.25e-51

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: 162.48  E-value: 8.25e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165   3 LALFDFDHTVTTCDTYGRFLRRVATAEQLAQ-AWWKVGPWLAAYKLKLISAERIRARVTRLTFSDRHsdDIATLAAGFSR 81
Cdd:cd02612    1 LAFFDLDGTLIAGDSFFAFLRFKGIAERRAPlEELLLLRLMALYALGRLDGAGMEALLGFATAGLAG--ELAALVEEFVE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165  82 EFLPDVVRPEMLEQIRWHKEQQHTVVIVSGSLDLYLRPWCEQLGLQ-LICNRLESQDGRLTGRYAGGDC-GPRKVEHIRR 159
Cdd:cd02612   79 EYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDnVLGTQLETEDGRYTGRIIGPPCyGEGKVKRLRE 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 896567165 160 QF--DLSRYVRIHAYGDSSEDKPMLALAHERW 189
Cdd:cd02612  159 WLaeEGIDLKDSYAYSDSINDLPMLEAVGHPV 190
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-185 7.25e-36

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: 124.95  E-value: 7.25e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165   1 MELALFDFDHTVTTCDT---YGRFLRR---VATAEQLAQAWWkvgpWLAAYKLKLISAERIRARVTRLtFSDRHSDDIAT 74
Cdd:COG0560    3 MRLAVFDLDGTLIAGESideLARFLGRrglVDRREVLEEVAA----ITERAMAGELDFEESLRFRVAL-LAGLPEEELEE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165  75 LAAGFSREFLPdvVRPEMLEQIRWHKEQQHTVVIVSGSLDLYLRPWCEQLGL-QLICNRLESQDGRLTGRYAGGDC-GPR 152
Cdd:COG0560   78 LAERLFEEVPR--LYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIdHVIANELEVEDGRLTGEVVGPIVdGEG 155

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 896567165 153 KVEHIRR-----QFDLSryvRIHAYGDSSEDKPMLALA 185
Cdd:COG0560  156 KAEALRElaaelGIDLE---QSYAYGDSANDLPMLEAA 190
HAD pfam12710
haloacid dehalogenase-like hydrolase;
4-182 1.10e-30

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 110.70  E-value: 1.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165    4 ALFDFDHTVTTCDTyGRFLRRVATAEQLAQAW--WKVGPWLAAYKLKLISAERIRARVTRLTFSDRHSDDIATLAAGFSR 81
Cdd:pfam12710   1 ALFDLDGTLLDGDS-LFLLIRALLRRGGPDLWraLLVLLLLALLRLLGRLSRAGARELLRALLAGLPEEDAAELERFVAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165   82 EFLPdVVRPEMLEQIRWHKEQQHTVVIVSGSLDLYLRPWCEQLGLQ-LICNRLESQDGRLTGRYA--GGDC-GPRKVEHI 157
Cdd:pfam12710  80 VALP-RLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDeVLATELEVDDGRFTGELRliGPPCaGEGKVRRL 158

                         170       180
                  ....*....|....*....|....*....
gi 896567165  158 RRQFDLSRY----VRIHAYGDSSEDKPML 182
Cdd:pfam12710 159 RAWLAARGLgldlADSVAYGDSPSDLPML 187
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 3-185 2.65e-30

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: 110.12  E-value: 2.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165    3 LALFDFDHTVTTCDTYGRFLRRVAtAEQLAQAWWKVGPWLAAYKLKLISAERIRARVtRLTFSDRHSDDIATLAAGFSRE 82
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLA-SKNILFEELRLPKVLARFEFFLNRGLDYMAYY-RAFALDALAGLLEEDVRAIVEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165   83 FLP----DVVRPEMLEQIRWHKEQQHTVVIVSGSLDLYLRPWCEQLGLQ-LICNRL-ESQDGRLTGRYAGGDC-GPRKVE 155
Cdd:TIGR01490  79 FVNqkieSILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDnAIGTRLeESEDGIYTGNIDGNNCkGEGKVH 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 896567165  156 HIRRQFDLSR--YVRIHAYGDSSEDKPMLALA 185
Cdd:TIGR01490 159 ALAELLAEEQidLKDSYAYGDSISDLPLLSLV 190
thrH PRK13582
bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;
91-186 1.94e-07

bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;


Pssm-ID: 237437 [Multi-domain]  Cd Length: 205  Bit Score: 49.16  E-value: 1.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165  91 EMLEQIRwhkeQQHTVVIVSGSLDLYLRPWCEQLGL-QLICNRLE-SQDGRLTG-RYAGGDcgpRKVEHIRRqFDLSRYv 167
Cdd:PRK13582  75 EFLDWLR----ERFQVVILSDTFYEFAGPLMRQLGWpTLFCHSLEvDEDGMITGyDLRQPD---GKRQAVKA-LKSLGY- 145

                         90
                 ....*....|....*....
gi 896567165 168 RIHAYGDSSEDKPMLALAH 186
Cdd:PRK13582 146 RVIAAGDSYNDTTMLGEAD 164
 
Name Accession Description Interval E-value
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 3-189 8.25e-51

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: 162.48  E-value: 8.25e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165   3 LALFDFDHTVTTCDTYGRFLRRVATAEQLAQ-AWWKVGPWLAAYKLKLISAERIRARVTRLTFSDRHsdDIATLAAGFSR 81
Cdd:cd02612    1 LAFFDLDGTLIAGDSFFAFLRFKGIAERRAPlEELLLLRLMALYALGRLDGAGMEALLGFATAGLAG--ELAALVEEFVE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165  82 EFLPDVVRPEMLEQIRWHKEQQHTVVIVSGSLDLYLRPWCEQLGLQ-LICNRLESQDGRLTGRYAGGDC-GPRKVEHIRR 159
Cdd:cd02612   79 EYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDnVLGTQLETEDGRYTGRIIGPPCyGEGKVKRLRE 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 896567165 160 QF--DLSRYVRIHAYGDSSEDKPMLALAHERW 189
Cdd:cd02612  159 WLaeEGIDLKDSYAYSDSINDLPMLEAVGHPV 190
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-185 7.25e-36

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: 124.95  E-value: 7.25e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165   1 MELALFDFDHTVTTCDT---YGRFLRR---VATAEQLAQAWWkvgpWLAAYKLKLISAERIRARVTRLtFSDRHSDDIAT 74
Cdd:COG0560    3 MRLAVFDLDGTLIAGESideLARFLGRrglVDRREVLEEVAA----ITERAMAGELDFEESLRFRVAL-LAGLPEEELEE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165  75 LAAGFSREFLPdvVRPEMLEQIRWHKEQQHTVVIVSGSLDLYLRPWCEQLGL-QLICNRLESQDGRLTGRYAGGDC-GPR 152
Cdd:COG0560   78 LAERLFEEVPR--LYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIdHVIANELEVEDGRLTGEVVGPIVdGEG 155

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 896567165 153 KVEHIRR-----QFDLSryvRIHAYGDSSEDKPMLALA 185
Cdd:COG0560  156 KAEALRElaaelGIDLE---QSYAYGDSANDLPMLEAA 190
HAD pfam12710
haloacid dehalogenase-like hydrolase;
4-182 1.10e-30

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 110.70  E-value: 1.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165    4 ALFDFDHTVTTCDTyGRFLRRVATAEQLAQAW--WKVGPWLAAYKLKLISAERIRARVTRLTFSDRHSDDIATLAAGFSR 81
Cdd:pfam12710   1 ALFDLDGTLLDGDS-LFLLIRALLRRGGPDLWraLLVLLLLALLRLLGRLSRAGARELLRALLAGLPEEDAAELERFVAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165   82 EFLPdVVRPEMLEQIRWHKEQQHTVVIVSGSLDLYLRPWCEQLGLQ-LICNRLESQDGRLTGRYA--GGDC-GPRKVEHI 157
Cdd:pfam12710  80 VALP-RLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDeVLATELEVDDGRFTGELRliGPPCaGEGKVRRL 158

                         170       180
                  ....*....|....*....|....*....
gi 896567165  158 RRQFDLSRY----VRIHAYGDSSEDKPML 182
Cdd:pfam12710 159 RAWLAARGLgldlADSVAYGDSPSDLPML 187
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 3-185 2.65e-30

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: 110.12  E-value: 2.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165    3 LALFDFDHTVTTCDTYGRFLRRVAtAEQLAQAWWKVGPWLAAYKLKLISAERIRARVtRLTFSDRHSDDIATLAAGFSRE 82
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLA-SKNILFEELRLPKVLARFEFFLNRGLDYMAYY-RAFALDALAGLLEEDVRAIVEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165   83 FLP----DVVRPEMLEQIRWHKEQQHTVVIVSGSLDLYLRPWCEQLGLQ-LICNRL-ESQDGRLTGRYAGGDC-GPRKVE 155
Cdd:TIGR01490  79 FVNqkieSILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDnAIGTRLeESEDGIYTGNIDGNNCkGEGKVH 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 896567165  156 HIRRQFDLSR--YVRIHAYGDSSEDKPMLALA 185
Cdd:TIGR01490 159 ALAELLAEEQidLKDSYAYGDSISDLPLLSLV 190
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 3-185 1.46e-24

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: 94.34  E-value: 1.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165    3 LALFDFDHTVTTCDTYGRFLRRVATAEqlaqawWKVGPWLAAYKLKLISaerIRARVTRLTFSDRHSddiatLAAGFSRE 82
Cdd:TIGR01488   1 LAIFDFDGTLTRQDSLIDLLAKLLGTN------DEVIELTRLAPSGRIS---FEDALGRRLALLHRS-----RSEEVAKE 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165   83 FL-PDVVRPEMLEQ-IRWHKEQQHTVVIVSGSLDLYLRPWCEQLGL-QLICNRLESQD-GRLTGRYAGGDC--GPRKVEH 156
Cdd:TIGR01488  67 FLaRQVALRPGARElISWLKERGIDTVIVSGGFDFFVEPVAEKLGIdDVFANRLEFDDnGLLTGPIEGQVNpeGECKGKV 146

                         170       180       190
                  ....*....|....*....|....*....|.
gi 896567165  157 IRRQFDLSRYVR--IHAYGDSSEDKPMLALA 185
Cdd:TIGR01488 147 LKELLEESKITLkkIIAVGDSVNDLPMLKLA 177
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 3-186 3.06e-08

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: 51.59  E-value: 3.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165    3 LALFDFDHTVTtcdtygrflrRVATAEQLAQAWwKVGPWLAAYKLKLISAE-----RIRARVTRLTFSDRHSDDIAtlaa 77
Cdd:TIGR00338  16 LVVFDMDSTLI----------NAETIDEIAKIA-GVEEEVSEITERAMRGEldfkaSLRERVALLKGLPVELLKEV---- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165   78 gfsREFLPdvVRPEMLEQIRWHKEQQHTVVIVSGSLDLYLRPWCEQLGLQ-LICNRLESQDGRLTGRYAG----GDCGPR 152
Cdd:TIGR00338  81 ---RENLP--LTEGAEELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDaAFANRLEVEDGKLTGLVEGpivdASYKGK 155

                         170       180       190
                  ....*....|....*....|....*....|....
gi 896567165  153 KVEHIRRQFDLSrYVRIHAYGDSSEDKPMLALAH 186
Cdd:TIGR00338 156 TLLILLRKEGIS-PENTVAVGDGANDLSMIKAAG 188
thrH PRK13582
bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;
91-186 1.94e-07

bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;


Pssm-ID: 237437 [Multi-domain]  Cd Length: 205  Bit Score: 49.16  E-value: 1.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165  91 EMLEQIRwhkeQQHTVVIVSGSLDLYLRPWCEQLGL-QLICNRLE-SQDGRLTG-RYAGGDcgpRKVEHIRRqFDLSRYv 167
Cdd:PRK13582  75 EFLDWLR----ERFQVVILSDTFYEFAGPLMRQLGWpTLFCHSLEvDEDGMITGyDLRQPD---GKRQAVKA-LKSLGY- 145

                         90
                 ....*....|....*....
gi 896567165 168 RIHAYGDSSEDKPMLALAH 186
Cdd:PRK13582 146 RVIAAGDSYNDTTMLGEAD 164
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
1-178 2.39e-07

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 49.16  E-value: 2.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165   1 MELALFDFDHTVttcdtygrflrrVATAEQLAQAWWKVgpwLAAYKLKLISAERIRARV-------TRLTFSDRHSDDIA 73
Cdd:COG0546    1 IKLVLFDLDGTL------------VDSAPDIAAALNEA---LAELGLPPLDLEELRALIglglrelLRRLLGEDPDEELE 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165  74 TLAAGFSREFLPDVVR--------PEMLEQIrwhKEQQHTVVIVSGSLDLYLRPWCEQLGLqlicnrlesqDGRLTGRYA 145
Cdd:COG0546   66 ELLARFRELYEEELLDetrlfpgvRELLEAL---KARGIKLAVVTNKPREFAERLLEALGL----------DDYFDAIVG 132

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 896567165 146 GGDCGPRK-----VEHIRRQFDLSR----YVrihayGDSSED 178
Cdd:COG0546  133 GDDVPPAKpkpepLLEALERLGLDPeevlMV-----GDSPHD 169
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 90-186 6.07e-07

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: 47.54  E-value: 6.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165  90 PEMLEQIRWHKEQQHTVVIVSGSLDLYLRPWCEQLGLQL-ICNRLESQDGRLTGRYAG----GDCGPRKVEHIRRQFDLS 164
Cdd:cd07500   73 PGAEELIQTLKAKGYKTAVVSGGFTYFTDRLAEELGLDYaFANELEIKDGKLTGKVLGpivdAQRKAETLQELAARLGIP 152

                         90       100
                 ....*....|....*....|..
gi 896567165 165 RYVRIhAYGDSSEDKPMLALAH 186
Cdd:cd07500  153 LEQTV-AVGDGANDLPMLKAAG 173
HAD_ThrH_like cd02607
bifunctional phosphoserine phosphatase/phosphoserine:homoserine phosphotransferase, similar to ...
 93-186 1.74e-05

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: 43.42  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165  93 LEQIRWHKEQQHtVVIVSGSLDLYLRPWCEQLGL-QLICNRLESQDGRLTGRYAGGDCGPRKVEHIrrQFDlSRYVRIHA 171
Cdd:cd02607   74 VEFVDWLRERFQ-VVILSDTFYEFSQPLMRQLGFpTLLCHKLQTDDDDRVVGYQLRQKDPKRQSVI--AVK-SLYYRVIA 149

                         90
                 ....*....|....*
gi 896567165 172 YGDSSEDKPMLALAH 186
Cdd:cd02607  150 AGDSYNDTTMLSEAH 164
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 5-126 3.46e-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: 40.01  E-value: 3.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165   5 LFDFDHTVTTCDT--------YGRFLRRVATAEQLAQAWWKV-GPWLAAYKLKLISAERIRARVtrltFSDRHSDDIATL 75
Cdd:COG1011    5 LFDLDGTLLDFDPviaealraLAERLGLLDEAEELAEAYRAIeYALWRRYERGEITFAELLRRL----LEELGLDLAEEL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 896567165  76 AAGFSREFLPDV-VRPEMLEQIRWHKEQQHTVVIVSGSLDLYLRPWCEQLGL 126
Cdd:COG1011   81 AEAFLAALPELVePYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGL 132
HAD_Pase cd07524
phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like ...
 7-187 2.79e-03

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


Pssm-ID: 319826 [Multi-domain]  Cd Length: 211  Bit Score: 37.31  E-value: 2.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165   7 DFDHTVTTCDTYGRFLRRVATAEQLaqawwkvgpWLAAYKLKLISAERIRARVTRLtFSDRHS---DDIatlaagfsREF 83
Cdd:cd07524    5 DFDGTITENDNIIYLMDEFAPPLEE---------WEALKEGVLSQTLSFREGVGQM-FELLPSslkDEI--------IEF 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896567165  84 LPD--VVRPEMLEQIRWHKEQQHTVVIVSGSLDLYLRPWCEQLGL---QLICNRLESQDGRLTGRY-----AGGDCGPRK 153
Cdd:cd07524   67 LEKtaKIRPGFKEFVAFCQEHGIPFIIVSGGMDFFIEPLLEGLVIekiAIYCNGSDFSGEQIHIDWphecdCTNGCGCCK 146

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 896567165 154 VEHIRRqfdLSRYVRIHAY-GDSSEDkpmLALAHE 187
Cdd:cd07524  147 SSIIRK---YSKPRPFIIViGDSVTD---LEAAKE 175
 
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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