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Conserved domains on  [gi|838967904|gb|KLZ48851|]
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HAD hydrolase, family IB [Klebsiella pneumoniae]

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 ...
 1-219 1.44e-70

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: 214.70  E-value: 1.44e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904   1 MGNTLTIFDLDNTLIQGDSSTVWSQFMVREGLATQKGYLAREARLMADYDRGEMNIADYVALIQAPLAGIPKSDVDALVA 80
Cdd:COG0560    1 RKMRLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVLEEVAAITERAMAGELDFEESLRFRVALLAGLPEEELEELAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904  81 RCVREAilPRVYPQAWELIRRLRAEGEQMLIISASVSLLVQAVAAALEIDQALGIDVAMVDGGYSGEITGIPSYQQGKVA 160
Cdd:COG0560   81 RLFEEV--PRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEVVGPIVDGEGKAE 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904 161 RLAQWREAHPQYDGEVTFYTDSINDLPLCLHADRVRLVNPCPQLQA-AGAGYGWPVLSWR 219
Cdd:COG0560  159 ALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREaADRERGWPVLDLL 218
 
Name Accession Description Interval E-value
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-219 1.44e-70

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: 214.70  E-value: 1.44e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904   1 MGNTLTIFDLDNTLIQGDSSTVWSQFMVREGLATQKGYLAREARLMADYDRGEMNIADYVALIQAPLAGIPKSDVDALVA 80
Cdd:COG0560    1 RKMRLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVLEEVAAITERAMAGELDFEESLRFRVALLAGLPEEELEELAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904  81 RCVREAilPRVYPQAWELIRRLRAEGEQMLIISASVSLLVQAVAAALEIDQALGIDVAMVDGGYSGEITGIPSYQQGKVA 160
Cdd:COG0560   81 RLFEEV--PRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEVVGPIVDGEGKAE 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904 161 RLAQWREAHPQYDGEVTFYTDSINDLPLCLHADRVRLVNPCPQLQA-AGAGYGWPVLSWR 219
Cdd:COG0560  159 ALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREaADRERGWPVLDLL 218
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 5-201 5.48e-69

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: 209.47  E-value: 5.48e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904   5 LTIFDLDNTLIQGDSstvWSQFMVREGLATQKGYL--AREARLMADYDRGEMNIADYVALIQAPLAGIPKsDVDALVARC 82
Cdd:cd02612    1 LAFFDLDGTLIAGDS---FFAFLRFKGIAERRAPLeeLLLLRLMALYALGRLDGAGMEALLGFATAGLAG-ELAALVEEF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904  83 VREAILPRVYPQAWELIRRLRAEGEQMLIISASVSLLVQAVAAALEIDQALGIDVAMVDGGYSGEITGIPSYQQGKVARL 162
Cdd:cd02612   77 VEEYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDNVLGTQLETEDGRYTGRIIGPPCYGEGKVKRL 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 838967904 163 AQWREAHPQYDGEVTFYTDSINDLPLCLHADRVRLVNPC 201
Cdd:cd02612  157 REWLAEEGIDLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 5-204 1.19e-50

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: 163.28  E-value: 1.19e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904    5 LTIFDLDNTLIQGDSSTVWSQFMVREGLAT-QKGYLAREARLMADYDRGEMNIADYVALIQAPLAGIPKSDVDALVARCV 83
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASKNILFeELRLPKVLARFEFFLNRGLDYMAYYRAFALDALAGLLEEDVRAIVEEFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904   84 REAILPRVYPQAWELIRRLRAEGEQMLIISASVSLLVQAVAAALEIDQALGIDVAMV-DGGYSGEITGIPSYQQGKVARL 162
Cdd:TIGR01490  81 NQKIESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTRLEESeDGIYTGNIDGNNCKGEGKVHAL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 838967904  163 AQWrEAHPQYD-GEVTFYTDSINDLPLCLHADRVRLVNPCPQL 204
Cdd:TIGR01490 161 AEL-LAEEQIDlKDSYAYGDSISDLPLLSLVGHPYVVNPDKKL 202
HAD pfam12710
haloacid dehalogenase-like hydrolase;
7-188 7.97e-34

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 119.56  E-value: 7.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904    7 IFDLDNTLIQGDSSTVWSQFMVREGLATQKGYLAREARLMADYDRGEMNIADYVALIQAPLAGIPkSDVDALVARCVREA 86
Cdd:pfam12710   2 LFDLDGTLLDGDSLFLLIRALLRRGGPDLWRALLVLLLLALLRLLGRLSRAGARELLRALLAGLP-EEDAAELERFVAEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904   87 ILPRVYPQAWELIRRLRAEGEQMLIISASVSLLVQAVAAALEIDQALGIDVAMVDGGYSGE--ITGIPSYQQGKVARLAQ 164
Cdd:pfam12710  81 ALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDGRFTGElrLIGPPCAGEGKVRRLRA 160

                         170       180
                  ....*....|....*....|....*.
gi 838967904  165 WREAHPQ--YDGEVTFYTDSINDLPL 188
Cdd:pfam12710 161 WLAARGLglDLADSVAYGDSPSDLPM 186
 
Name Accession Description Interval E-value
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-219 1.44e-70

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: 214.70  E-value: 1.44e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904   1 MGNTLTIFDLDNTLIQGDSSTVWSQFMVREGLATQKGYLAREARLMADYDRGEMNIADYVALIQAPLAGIPKSDVDALVA 80
Cdd:COG0560    1 RKMRLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVLEEVAAITERAMAGELDFEESLRFRVALLAGLPEEELEELAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904  81 RCVREAilPRVYPQAWELIRRLRAEGEQMLIISASVSLLVQAVAAALEIDQALGIDVAMVDGGYSGEITGIPSYQQGKVA 160
Cdd:COG0560   81 RLFEEV--PRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEVVGPIVDGEGKAE 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904 161 RLAQWREAHPQYDGEVTFYTDSINDLPLCLHADRVRLVNPCPQLQA-AGAGYGWPVLSWR 219
Cdd:COG0560  159 ALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREaADRERGWPVLDLL 218
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 5-201 5.48e-69

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: 209.47  E-value: 5.48e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904   5 LTIFDLDNTLIQGDSstvWSQFMVREGLATQKGYL--AREARLMADYDRGEMNIADYVALIQAPLAGIPKsDVDALVARC 82
Cdd:cd02612    1 LAFFDLDGTLIAGDS---FFAFLRFKGIAERRAPLeeLLLLRLMALYALGRLDGAGMEALLGFATAGLAG-ELAALVEEF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904  83 VREAILPRVYPQAWELIRRLRAEGEQMLIISASVSLLVQAVAAALEIDQALGIDVAMVDGGYSGEITGIPSYQQGKVARL 162
Cdd:cd02612   77 VEEYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDNVLGTQLETEDGRYTGRIIGPPCYGEGKVKRL 156

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 838967904 163 AQWREAHPQYDGEVTFYTDSINDLPLCLHADRVRLVNPC 201
Cdd:cd02612  157 REWLAEEGIDLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 5-204 1.19e-50

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: 163.28  E-value: 1.19e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904    5 LTIFDLDNTLIQGDSSTVWSQFMVREGLAT-QKGYLAREARLMADYDRGEMNIADYVALIQAPLAGIPKSDVDALVARCV 83
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASKNILFeELRLPKVLARFEFFLNRGLDYMAYYRAFALDALAGLLEEDVRAIVEEFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904   84 REAILPRVYPQAWELIRRLRAEGEQMLIISASVSLLVQAVAAALEIDQALGIDVAMV-DGGYSGEITGIPSYQQGKVARL 162
Cdd:TIGR01490  81 NQKIESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTRLEESeDGIYTGNIDGNNCKGEGKVHAL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 838967904  163 AQWrEAHPQYD-GEVTFYTDSINDLPLCLHADRVRLVNPCPQL 204
Cdd:TIGR01490 161 AEL-LAEEQIDlKDSYAYGDSISDLPLLSLVGHPYVVNPDKKL 202
HAD pfam12710
haloacid dehalogenase-like hydrolase;
7-188 7.97e-34

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 119.56  E-value: 7.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904    7 IFDLDNTLIQGDSSTVWSQFMVREGLATQKGYLAREARLMADYDRGEMNIADYVALIQAPLAGIPkSDVDALVARCVREA 86
Cdd:pfam12710   2 LFDLDGTLLDGDSLFLLIRALLRRGGPDLWRALLVLLLLALLRLLGRLSRAGARELLRALLAGLP-EEDAAELERFVAEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904   87 ILPRVYPQAWELIRRLRAEGEQMLIISASVSLLVQAVAAALEIDQALGIDVAMVDGGYSGE--ITGIPSYQQGKVARLAQ 164
Cdd:pfam12710  81 ALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDGRFTGElrLIGPPCAGEGKVRRLRA 160

                         170       180
                  ....*....|....*....|....*.
gi 838967904  165 WREAHPQ--YDGEVTFYTDSINDLPL 188
Cdd:pfam12710 161 WLAARGLglDLADSVAYGDSPSDLPM 186
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 5-190 2.57e-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: 81.63  E-value: 2.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904    5 LTIFDLDNTLIQGDSST-VWSQFMVREGLATQKGYLAREARLMadydrgemniadYVALIQAPLAGIPKSDVDALVARCV 83
Cdd:TIGR01488   1 LAIFDFDGTLTRQDSLIdLLAKLLGTNDEVIELTRLAPSGRIS------------FEDALGRRLALLHRSRSEEVAKEFL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904   84 REAILPRVYpqAWELIRRLRAEGEQMLIISASVSLLVQAVAAALEIDQALGIDVAMVDGG-YSGEITGIPS-YQQGKVAR 161
Cdd:TIGR01488  69 ARQVALRPG--ARELISWLKERGIDTVIVSGGFDFFVEPVAEKLGIDDVFANRLEFDDNGlLTGPIEGQVNpEGECKGKV 146

                         170       180
                  ....*....|....*....|....*....
gi 838967904  162 LAQWREAHPQYDGEVTFYTDSINDLPLCL 190
Cdd:TIGR01488 147 LKELLEESKITLKKIIAVGDSVNDLPMLK 175
HAD_PSP_eu cd04309
phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human ...
 7-194 2.69e-10

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: 57.68  E-value: 2.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904   7 IFDLDNTLIQGDSSTVWSQFMvreGLATQKGYLAREArlMadydRGEMNIADyvALiQAPLAGI--PKSDVDALVA-RCv 83
Cdd:cd04309    4 CFDVDSTVIQEEGIDELAKFC---GVGDEVAELTRRA--M----GGSIPFRD--AL-RKRLAIInpTKEQVDEFLEeHP- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904  84 reailPRVYPQAWELIRRLRAEGEQMLIISASVSLLVQAVAAALEIDQALGIDVAMV---DGGYSG-EITGIPSYQQGKV 159
Cdd:cd04309   71 -----PRLTPGVEELVSRLKARGVEVYLISGGFRELIEPVASQLGIPLENVFANRLLfdfNGEYAGfDETQPTSRSGGKA 145

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 838967904 160 ARLAQWREAHPqyDGEVTFYTDSINDLPLCLHADR 194
Cdd:cd04309  146 KVIEQLKEKHH--YKRVIMIGDGATDLEACPPADA 178
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 7-131 5.01e-08

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: 51.57  E-value: 5.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904   7 IFDLDNTLIqgDSSTVWSQFMVR---------EGLATQKGYLAREARLMADYDRGEMNIADYVALIqAPLAGIpksDVDA 77
Cdd:COG1011    5 LFDLDGTLL--DFDPVIAEALRAlaerlglldEAEELAEAYRAIEYALWRRYERGEITFAELLRRL-LEELGL---DLAE 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 838967904  78 LVARCVREAI--LPRVYPQAWELIRRLRAEGEQMLIISASVSLLVQAVAAALEIDQ 131
Cdd:COG1011   79 ELAEAFLAALpeLVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDD 134
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 5-193 2.20e-06

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: 46.97  E-value: 2.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904    5 LTIFDLDNTLIQGdsstvwsqfmvrEGLATqkgyLAREA-----------RLMadydRGEMN----IADYVALIQaplaG 69
Cdd:TIGR00338  16 LVVFDMDSTLINA------------ETIDE----IAKIAgveeevseiteRAM----RGELDfkasLRERVALLK----G 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904   70 IPKSDVDAlvarcVREAilPRVYPQAWELIRRLRAEGEQMLIISASVSLLVQAVAAALEIDQALGIDVAMVDGGYSGEIT 149
Cdd:TIGR00338  72 LPVELLKE-----VREN--LPLTEGAEELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDAAFANRLEVEDGKLTGLVE 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 838967904  150 GIPSYQQGK---VARLAQWREAHPQydgEVTFYTDSINDLPLCLHAD 193
Cdd:TIGR00338 145 GPIVDASYKgktLLILLRKEGISPE---NTVAVGDGANDLSMIKAAG 188
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 5-213 3.56e-06

phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 45.62  E-value: 3.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904   5 LTIFDLDNTLIQGDsstvwsqfmVREGLATQKGYLAREARLMADYDRGEMNIADyvALIQ--APLAGIPKSDVDALVARC 82
Cdd:cd07500    1 LIVFDMDSTLIQQE---------VIDELAAEAGVGEEVAAITERAMRGELDFEE--SLRErvALLKGLPESVLDEVYERL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904  83 vreailpRVYPQAWELIRRLRAEGEQMLIISASVSLLVQAVAAALEIDQALGIDVAMVDGGYSGEITGIPSYQQGKVARL 162
Cdd:cd07500   70 -------TLTPGAEELIQTLKAKGYKTAVVSGGFTYFTDRLAEELGLDYAFANELEIKDGKLTGKVLGPIVDAQRKAETL 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 838967904 163 AQWREAHPQYDGEVTFYTDSINDLPLclhadrvrlvnpcpqLQAAGAGYGW 213
Cdd:cd07500  143 QELAARLGIPLEQTVAVGDGANDLPM---------------LKAAGLGIAF 178
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 7-187 4.29e-06

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: 45.65  E-value: 4.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904    7 IFDLDNTLIQGdsstvwsQFMVREGLATQKGYLAREARLMADYDRGEMNIADYVALIQA-----------------PLAG 69
Cdd:pfam00702   5 VFDLDGTLTDG-------EPVVTEAIAELASEHPLAKAIVAAAEDLPIPVEDFTARLLLgkrdwleeldilrglveTLEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904   70 IPKSDVDALVARCVREAILPRVYPQAWELIRRLRAEGEQMLIISASVSLLVQAVAAALEIDqalgidvAMVDGGYSGEIT 149
Cdd:pfam00702  78 EGLTVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLD-------DYFDVVISGDDV 150

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 838967904  150 GIP-SYQQGKVARLAQWREAHpqydGEVTFYTDSINDLP 187
Cdd:pfam00702 151 GVGkPKPEIYLAALERLGVKP----EEVLMVGDGVNDIP 185
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
7-131 8.24e-04

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 39.14  E-value: 8.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904   7 IFDLDNTLIqgDSSTVWSQFMvreglatqkgylareARLMADYDRGEMNIADYVALIQAPLAGI--------PKSDVDAL 78
Cdd:COG0546    5 LFDLDGTLV--DSAPDIAAAL---------------NEALAELGLPPLDLEELRALIGLGLRELlrrllgedPDEELEEL 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 838967904  79 VARCVRE-----AILPRVYPQAWELIRRLRAEGEQMLIISASVSLLVQAVAAALEIDQ 131
Cdd:COG0546   68 LARFRELyeeelLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDD 125
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 7-126 4.06e-03

subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p); This subfamily includes Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). GPP1p and GPP2p are involved in glycerol biosynthesis, GPP1 is induced in response to both anaerobic and hyperosmotic stress, GPP2 is induced in response to hyperosmotic or oxidative stress, and during diauxic shift; overexpression of DOG1 or DOG2 confers 2-deoxyglucose resistance. These belong to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), and Escherichia coli 6-phosphogluconate phosphatase YieH. 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: 319829 [Multi-domain]  Cd Length: 205  Bit Score: 36.94  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 838967904   7 IFDLDNTLIQGDS--STVWSQFMVREGLATQKGYLAREARLMADYDRGEMNIADYVALIQAPLAGIPKSDVDALVArcvr 84
Cdd:cd07527    3 LFDMDGTLVDSTPavERAWHKWAKEHGVDPEEVLKVSHGRRAIDVIRKLAPDDADIELVLALETEEPESYPEGVIA---- 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 838967904  85 eailprvYPQAWELIRRLRAEGEQ-MLIISASVSLLVQAVAAA 126
Cdd:cd07527   79 -------IPGAVDLLASLPAAGDRwAIVTSGTRALAEARLEAA 114
 
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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