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Conserved domains on  [gi|489917538|ref|WP_003820913|]
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MULTISPECIES: HAD family phosphatase [Bordetella]

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 ...
 4-224 4.81e-82

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: 243.98  E-value: 4.81e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917538   4 RRLALFDLDHTLLPLDSDYQWADFLARTGRAgDPAEARRRNDDLMERYNRGELTAEQAAEFMLGLLAAHSPVELAAWHEE 83
Cdd:COG0560    3 MRLAVFDLDGTLIAGESIDELARFLGRRGLV-DRREVLEEVAAITERAMAGELDFEESLRFRVALLAGLPEEELEELAER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917538  84 FMRDVirPSLTAQAVDVVRGHLAAGDLCALVTATNSFVTAPIARAFGVQHLIATDPEYRDGRYTGRIEGTPSFREGKVVR 163
Cdd:COG0560   82 LFEEV--PRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEVVGPIVDGEGKAEA 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917538 164 VNQWLAGMGLalgDFAESYFYSDSVNDVPLLEAVTRPIAANPSPGLREIA-QARGWQVIDLF 224
Cdd:COG0560  160 LRELAAELGI---DLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAAdRERGWPVLDLL 218
 
Name Accession Description Interval E-value
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 4-224 4.81e-82

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: 243.98  E-value: 4.81e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917538   4 RRLALFDLDHTLLPLDSDYQWADFLARTGRAgDPAEARRRNDDLMERYNRGELTAEQAAEFMLGLLAAHSPVELAAWHEE 83
Cdd:COG0560    3 MRLAVFDLDGTLIAGESIDELARFLGRRGLV-DRREVLEEVAAITERAMAGELDFEESLRFRVALLAGLPEEELEELAER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917538  84 FMRDVirPSLTAQAVDVVRGHLAAGDLCALVTATNSFVTAPIARAFGVQHLIATDPEYRDGRYTGRIEGTPSFREGKVVR 163
Cdd:COG0560   82 LFEEV--PRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEVVGPIVDGEGKAEA 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917538 164 VNQWLAGMGLalgDFAESYFYSDSVNDVPLLEAVTRPIAANPSPGLREIA-QARGWQVIDLF 224
Cdd:COG0560  160 LRELAAELGI---DLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAAdRERGWPVLDLL 218
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 6-206 2.58e-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: 200.61  E-value: 2.58e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917538   6 LALFDLDHTLLPLDSdyqWADFLARTGRAG-DPAEARRRNDDLMERYNRGELTAEQAaEFMLGLLAAHSPVELAAWHEEF 84
Cdd:cd02612    1 LAFFDLDGTLIAGDS---FFAFLRFKGIAErRAPLEELLLLRLMALYALGRLDGAGM-EALLGFATAGLAGELAALVEEF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917538  85 MRDVIRPSLTAQAVDVVRGHLAAGDLCALVTATNSFVTAPIARAFGVQHLIATDPEYRDGRYTGRIEGTPSFREGKVVRV 164
Cdd:cd02612   77 VEEYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDNVLGTQLETEDGRYTGRIIGPPCYGEGKVKRL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 489917538 165 NQWLAGMGLalgDFAESYFYSDSVNDVPLLEAVTRPIAANPS 206
Cdd:cd02612  157 REWLAEEGI---DLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD pfam12710
haloacid dehalogenase-like hydrolase;
7-195 2.88e-43

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 144.21  E-value: 2.88e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917538    7 ALFDLDHTLLPLDSDYQWADFLARTGRAgDPAEARRRNDDLMERYNRGELTAEQAAEFMLGLLAAHSPvELAAWHEEFMR 86
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGP-DLWRALLVLLLLALLRLLGRLSRAGARELLRALLAGLPE-EDAAELERFVA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917538   87 DVIRPSLTAQAVDVVRGHLAAGDLCALVTATNSFVTAPIARAFGVQHLIATDPEYRDGRYTGR--IEGTPSFREGKVVRV 164
Cdd:pfam12710  79 EVALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDGRFTGElrLIGPPCAGEGKVRRL 158

                         170       180       190
                  ....*....|....*....|....*....|.
gi 489917538  165 NQWLAGMGLALgDFAESYFYSDSVNDVPLLE 195
Cdd:pfam12710 159 RAWLAARGLGL-DLADSVAYGDSPSDLPMLR 188
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 6-209 1.77e-42

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: 142.86  E-value: 1.77e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917538    6 LALFDLDHTLLPLDSDYQWADFLAR----TGRAGDPaEARRRnddlMERY-NRGELTAEQAAEFMLGLLAAHSPVELAAW 80
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASknilFEELRLP-KVLAR----FEFFlNRGLDYMAYYRAFALDALAGLLEEDVRAI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917538   81 HEEFMRDVIRPSLTAQAVDVVRGHLAAGDLCALVTATNSFVTAPIARAFGVQHLIATD-PEYRDGRYTGRIEGTPSFREG 159
Cdd:TIGR01490  76 VEEFVNQKIESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTRlEESEDGIYTGNIDGNNCKGEG 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 489917538  160 KVVRVNQWLAGMGLalgDFAESYFYSDSVNDVPLLEAVTRPIAANPSPGL 209
Cdd:TIGR01490 156 KVHALAELLAEEQI---DLKDSYAYGDSISDLPLLSLVGHPYVVNPDKKL 202
 
Name Accession Description Interval E-value
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 4-224 4.81e-82

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: 243.98  E-value: 4.81e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917538   4 RRLALFDLDHTLLPLDSDYQWADFLARTGRAgDPAEARRRNDDLMERYNRGELTAEQAAEFMLGLLAAHSPVELAAWHEE 83
Cdd:COG0560    3 MRLAVFDLDGTLIAGESIDELARFLGRRGLV-DRREVLEEVAAITERAMAGELDFEESLRFRVALLAGLPEEELEELAER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917538  84 FMRDVirPSLTAQAVDVVRGHLAAGDLCALVTATNSFVTAPIARAFGVQHLIATDPEYRDGRYTGRIEGTPSFREGKVVR 163
Cdd:COG0560   82 LFEEV--PRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEVVGPIVDGEGKAEA 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917538 164 VNQWLAGMGLalgDFAESYFYSDSVNDVPLLEAVTRPIAANPSPGLREIA-QARGWQVIDLF 224
Cdd:COG0560  160 LRELAAELGI---DLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAAdRERGWPVLDLL 218
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 6-206 2.58e-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: 200.61  E-value: 2.58e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917538   6 LALFDLDHTLLPLDSdyqWADFLARTGRAG-DPAEARRRNDDLMERYNRGELTAEQAaEFMLGLLAAHSPVELAAWHEEF 84
Cdd:cd02612    1 LAFFDLDGTLIAGDS---FFAFLRFKGIAErRAPLEELLLLRLMALYALGRLDGAGM-EALLGFATAGLAGELAALVEEF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917538  85 MRDVIRPSLTAQAVDVVRGHLAAGDLCALVTATNSFVTAPIARAFGVQHLIATDPEYRDGRYTGRIEGTPSFREGKVVRV 164
Cdd:cd02612   77 VEEYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDNVLGTQLETEDGRYTGRIIGPPCYGEGKVKRL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 489917538 165 NQWLAGMGLalgDFAESYFYSDSVNDVPLLEAVTRPIAANPS 206
Cdd:cd02612  157 REWLAEEGI---DLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD pfam12710
haloacid dehalogenase-like hydrolase;
7-195 2.88e-43

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 144.21  E-value: 2.88e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917538    7 ALFDLDHTLLPLDSDYQWADFLARTGRAgDPAEARRRNDDLMERYNRGELTAEQAAEFMLGLLAAHSPvELAAWHEEFMR 86
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGP-DLWRALLVLLLLALLRLLGRLSRAGARELLRALLAGLPE-EDAAELERFVA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917538   87 DVIRPSLTAQAVDVVRGHLAAGDLCALVTATNSFVTAPIARAFGVQHLIATDPEYRDGRYTGR--IEGTPSFREGKVVRV 164
Cdd:pfam12710  79 EVALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDGRFTGElrLIGPPCAGEGKVRRL 158

                         170       180       190
                  ....*....|....*....|....*....|.
gi 489917538  165 NQWLAGMGLALgDFAESYFYSDSVNDVPLLE 195
Cdd:pfam12710 159 RAWLAARGLGL-DLADSVAYGDSPSDLPMLR 188
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 6-209 1.77e-42

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: 142.86  E-value: 1.77e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917538    6 LALFDLDHTLLPLDSDYQWADFLAR----TGRAGDPaEARRRnddlMERY-NRGELTAEQAAEFMLGLLAAHSPVELAAW 80
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASknilFEELRLP-KVLAR----FEFFlNRGLDYMAYYRAFALDALAGLLEEDVRAI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917538   81 HEEFMRDVIRPSLTAQAVDVVRGHLAAGDLCALVTATNSFVTAPIARAFGVQHLIATD-PEYRDGRYTGRIEGTPSFREG 159
Cdd:TIGR01490  76 VEEFVNQKIESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTRlEESEDGIYTGNIDGNNCKGEG 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 489917538  160 KVVRVNQWLAGMGLalgDFAESYFYSDSVNDVPLLEAVTRPIAANPSPGL 209
Cdd:TIGR01490 156 KVHALAELLAEEQI---DLKDSYAYGDSISDLPLLSLVGHPYVVNPDKKL 202
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 6-197 2.89e-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: 94.73  E-value: 2.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917538    6 LALFDLDHTLLPLDSDYqwaDFLARtgRAGDPAEARrrndDLMERYNRGELTAEQAAEFMLGLLAAHSPVELAawHEEFM 85
Cdd:TIGR01488   1 LAIFDFDGTLTRQDSLI---DLLAK--LLGTNDEVI----ELTRLAPSGRISFEDALGRRLALLHRSRSEEVA--KEFLA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917538   86 RDVirpSLTAQAVDVVRGHLAAGDLCALVTATNSFVTAPIARAFGVQHLIATDPE-YRDGRYTGRIEGTPS-FREGKVVR 163
Cdd:TIGR01488  70 RQV---ALRPGARELISWLKERGIDTVIVSGGFDFFVEPVAEKLGIDDVFANRLEfDDNGLLTGPIEGQVNpEGECKGKV 146

                         170       180       190
                  ....*....|....*....|....*....|....
gi 489917538  164 VNQWLAGMGLalgDFAESYFYSDSVNDVPLLEAV 197
Cdd:TIGR01488 147 LKELLEESKI---TLKKIIAVGDSVNDLPMLKLA 177
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 8-86 1.25e-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: 41.94  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917538   8 LFDLDHTLLPLDSDYQWA--DFLARTGRAGDPAEARRR----NDDLMERYNRGELTAEqaaEFMLGLLAAHSPVELAAWH 81
Cdd:COG1011    5 LFDLDGTLLDFDPVIAEAlrALAERLGLLDEAEELAEAyraiEYALWRRYERGEITFA---ELLRRLLEELGLDLAEELA 81


                 ....*
gi 489917538  82 EEFMR 86
Cdd:COG1011   82 EAFLA 86
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 6-196 3.58e-04

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: 40.22  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917538   6 LALFDLDHTLLpldsDYQWADFLARtgRAGDPAEArrrnDDLMERYNRGELTAEQAAEFMLGLLAAHSpvelaawhEEFM 85
Cdd:cd07500    1 LIVFDMDSTLI----QQEVIDELAA--EAGVGEEV----AAITERAMRGELDFEESLRERVALLKGLP--------ESVL 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917538  86 RDVIRP-SLTAQAVDVVRGHLAAGDLCALVTATNSFVTAPIARAFGVQHLIATDPEYRDGRYTGRIEGTPSFREGKVVRV 164
Cdd:cd07500   63 DEVYERlTLTPGAEELIQTLKAKGYKTAVVSGGFTYFTDRLAEELGLDYAFANELEIKDGKLTGKVLGPIVDAQRKAETL 142

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 489917538 165 NQWLAGMGL------ALGDFAesyfysdsvNDVPLLEA 196
Cdd:cd07500  143 QELAARLGIpleqtvAVGDGA---------NDLPMLKA 171
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 5-63 5.09e-03

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. 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: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 36.94  E-value: 5.09e-03
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gi 489917538   5 RLALFDLDHTLLPLDSDYQWADFLARTGRAGDPAEARRRNDDLMERYNRGELTAEQAAE 63
Cdd:cd02603    2 RAVLFDFGGVLIDPDPAAAVARFEALTGEPSEFVLDTEGLAGAFLELERGRITEEEFWE 60
 
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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