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Conserved domains on  [gi|1063708383|ref|NP_001319818|]
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Haloacid dehalogenase-like hydrolase (HAD) superfamily protein [Arabidopsis thaliana]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

HAD (haloacid dehalogenase) family hydrolase; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

EC:  3.6.3.-
Gene Ontology:  GO:0005524|GO:0016887|GO:0005215

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 1-162 3.03e-87

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member TIGR01993:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 183  Bit Score: 254.97  E-value: 3.03e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383   1 MLNQLGIEESEVPKLCLDLYKEYGTTMAGLKVMgYEFDNDEFHEYVHGRLPYEKLKPDPLLRNLLLSMPHRKIIFTNADK 80
Cdd:TIGR01993  30 VAARLKLSPEEARVLRKDYYKEYGTTLAGLMIL-HEIDADEYLRYVHGRLPYDKLKPDPELRNLLLRLPGRKIIFTNGDR 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383  81 AHATRALNRLGLEDCFEGIICFETLNPSsdsntqILCKPSVEAFEAAIRIADiVDPRKTIFFDDSIRNIASAKATGLKTV 160
Cdd:TIGR01993 109 AHARRALRRLGIEDCFDGIFCFDTANPD------LLPKPSPQAYEKALREAG-VDPERAIFFDDSARNIAAGKALGMKTV 181


                  ..
gi 1063708383 161 FV 162
Cdd:TIGR01993 182 LV 183
 
Name Accession Description Interval E-value
Pyr-5-nucltdase TIGR01993
pyrimidine 5'-nucleotidase; This family of proteins includes the SDT1/SSM1 gene from yeast ...
 1-162 3.03e-87

pyrimidine 5'-nucleotidase; This family of proteins includes the SDT1/SSM1 gene from yeast which has been shown to code for a pyrimidine (UMP/CMP) 5'nucleotidase. The family spans plants, fungi and a small number of bacteria. These enzymes are members of the haloacid dehalogenase (HAD) superfamily of hydrolases, specifically the IA subfamily (variant 3, TIGR01509).


Pssm-ID: 273917 [Multi-domain]  Cd Length: 183  Bit Score: 254.97  E-value: 3.03e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383   1 MLNQLGIEESEVPKLCLDLYKEYGTTMAGLKVMgYEFDNDEFHEYVHGRLPYEKLKPDPLLRNLLLSMPHRKIIFTNADK 80
Cdd:TIGR01993  30 VAARLKLSPEEARVLRKDYYKEYGTTLAGLMIL-HEIDADEYLRYVHGRLPYDKLKPDPELRNLLLRLPGRKIIFTNGDR 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383  81 AHATRALNRLGLEDCFEGIICFETLNPSsdsntqILCKPSVEAFEAAIRIADiVDPRKTIFFDDSIRNIASAKATGLKTV 160
Cdd:TIGR01993 109 AHARRALRRLGIEDCFDGIFCFDTANPD------LLPKPSPQAYEKALREAG-VDPERAIFFDDSARNIAAGKALGMKTV 181


                  ..
gi 1063708383 161 FV 162
Cdd:TIGR01993 182 LV 183
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 1-164 5.27e-77

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p; This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and CMP. 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: 319791 [Multi-domain]  Cd Length: 182  Bit Score: 229.06  E-value: 5.27e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383   1 MLNQLGIEESEVPKLCLDLYKEYGTTMAGLkVMGYEFDNDEFHEYVHGRLPYEKLKPDPLLRNLLLSMPHRKIIFTNADK 80
Cdd:cd02604    29 VATKLGLSPEEARRLRKSYYKEYGTTLRGL-MAEHGIDPDEFLDRVVHLILYDHLKPDPKLRNLLLALPGRKIIFTNASK 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383  81 AHATRALNRLGLEDCFEGIICFETLNPSsdsntqilCKPSVEAFEAAIRIADIvDPRKTIFFDDSIRNIASAKATGLKTV 160
Cdd:cd02604   108 NHAIRVLKRLGLADLFDGIFDIEYAGPD--------PKPHPAAFEKAIREAGL-DPKRAAFFDDSIRNLLAAKALGMKTV 178


                  ....
gi 1063708383 161 FVGE 164
Cdd:cd02604   179 LVGP 182
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 30-185 1.95e-20

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: 85.47  E-value: 1.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383  30 LKVMGYEFDNDEFHEYVHGRLPYEKLKPD--PLLRNLLlSMPHRKIIFTNADKAHATRALNRLGLEDCFEGIICfetlnp 107
Cdd:COG1011    69 LEELGLDLAEELAEAFLAALPELVEPYPDalELLEALK-ARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVS------ 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383 108 SSDSNtqiLCKPSVEAFEAAIRIADiVDPRKTIFFDDSIR-NIASAKATGLKTVFV----GESVLVPGADYALSSIHNIK 182
Cdd:COG1011   142 SEEVG---VRKPDPEIFELALERLG-VPPEEALFVGDSPEtDVAGARAAGMRTVWVnrsgEPAPAEPRPDYVISDLAELL 217


                  ...
gi 1063708383 183 EAI 185
Cdd:COG1011   218 ELL 220
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
36-162 8.23e-08

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 50.28  E-value: 8.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383  36 EFDNDEFHEYVHGRLPYEKLKPDPLLRNLLLSMPHRKI---IFTNADKAHATRALNRLGLEDCFEGIICFETLNPSsdsn 112
Cdd:pfam13419  59 EEKIEFYLRKYNEELHDKLVKPYPGIKELLEELKEQGYklgIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGK---- 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063708383 113 tqilcKPSVEAFEAAIRIADIvDPRKTIFFDDSIRNIASAKATGLKTVFV 162
Cdd:pfam13419 135 -----KPDPDPILKALEQLGL-KPEEVIYVGDSPRDIEAAKNAGIKVIAV 178
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
76-178 1.86e-04

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 40.95  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383  76 TNADKAHATRALNRLGLEDCFEGIICfetlnpsSDSNTQIlcKPSVEAFEAAIRIADIvDPRKTIFFDDSIRNIASAKAT 155
Cdd:PRK13222  116 TNKPTPFVAPLLEALGIADYFSVVIG-------GDSLPNK--KPDPAPLLLACEKLGL-DPEEMLFVGDSRNDIQAARAA 185

                          90       100
                  ....*....|....*....|....*....
gi 1063708383 156 GLKTVFV------GESVLVPGADYALSSI 178
Cdd:PRK13222  186 GCPSVGVtygynyGEPIALSEPDVVIDHF 214
 
Name Accession Description Interval E-value
Pyr-5-nucltdase TIGR01993
pyrimidine 5'-nucleotidase; This family of proteins includes the SDT1/SSM1 gene from yeast ...
 1-162 3.03e-87

pyrimidine 5'-nucleotidase; This family of proteins includes the SDT1/SSM1 gene from yeast which has been shown to code for a pyrimidine (UMP/CMP) 5'nucleotidase. The family spans plants, fungi and a small number of bacteria. These enzymes are members of the haloacid dehalogenase (HAD) superfamily of hydrolases, specifically the IA subfamily (variant 3, TIGR01509).


Pssm-ID: 273917 [Multi-domain]  Cd Length: 183  Bit Score: 254.97  E-value: 3.03e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383   1 MLNQLGIEESEVPKLCLDLYKEYGTTMAGLKVMgYEFDNDEFHEYVHGRLPYEKLKPDPLLRNLLLSMPHRKIIFTNADK 80
Cdd:TIGR01993  30 VAARLKLSPEEARVLRKDYYKEYGTTLAGLMIL-HEIDADEYLRYVHGRLPYDKLKPDPELRNLLLRLPGRKIIFTNGDR 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383  81 AHATRALNRLGLEDCFEGIICFETLNPSsdsntqILCKPSVEAFEAAIRIADiVDPRKTIFFDDSIRNIASAKATGLKTV 160
Cdd:TIGR01993 109 AHARRALRRLGIEDCFDGIFCFDTANPD------LLPKPSPQAYEKALREAG-VDPERAIFFDDSARNIAAGKALGMKTV 181


                  ..
gi 1063708383 161 FV 162
Cdd:TIGR01993 182 LV 183
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 1-164 5.27e-77

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p; This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and CMP. 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: 319791 [Multi-domain]  Cd Length: 182  Bit Score: 229.06  E-value: 5.27e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383   1 MLNQLGIEESEVPKLCLDLYKEYGTTMAGLkVMGYEFDNDEFHEYVHGRLPYEKLKPDPLLRNLLLSMPHRKIIFTNADK 80
Cdd:cd02604    29 VATKLGLSPEEARRLRKSYYKEYGTTLRGL-MAEHGIDPDEFLDRVVHLILYDHLKPDPKLRNLLLALPGRKIIFTNASK 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383  81 AHATRALNRLGLEDCFEGIICFETLNPSsdsntqilCKPSVEAFEAAIRIADIvDPRKTIFFDDSIRNIASAKATGLKTV 160
Cdd:cd02604   108 NHAIRVLKRLGLADLFDGIFDIEYAGPD--------PKPHPAAFEKAIREAGL-DPKRAAFFDDSIRNLLAAKALGMKTV 178


                  ....
gi 1063708383 161 FVGE 164
Cdd:cd02604   179 LVGP 182
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 4-162 3.32e-28

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 104.42  E-value: 3.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383   4 QLGIEESEVPKLCLDLYK-EYGTTMAGLKvmGYEFDndeFHEYVHGRLPYEKLKPDPLLRNLLLSMP---HRKIIFTNAD 79
Cdd:TIGR01509  32 ELGVSAVGRLELALRRFKaQYGRTISPED--AQLLY---KQLFYEQIEEEAKLKPLPGVRALLEALRargKKLALLTNSP 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383  80 KAHaTRALNRLGLEDCFEGIICFETLnpssdsntqILCKPSVEAFEAAIRIADiVDPRKTIFFDDSIRNIASAKATGLKT 159
Cdd:TIGR01509 107 RAH-KLVLALLGLRDLFDVVIDSSDV---------GLGKPDPDIYLQALKALG-LEPSECVFVDDSPAGIEAAKAAGMHT 175


                  ...
gi 1063708383 160 VFV 162
Cdd:TIGR01509 176 VGV 178
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 30-185 1.95e-20

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: 85.47  E-value: 1.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383  30 LKVMGYEFDNDEFHEYVHGRLPYEKLKPD--PLLRNLLlSMPHRKIIFTNADKAHATRALNRLGLEDCFEGIICfetlnp 107
Cdd:COG1011    69 LEELGLDLAEELAEAFLAALPELVEPYPDalELLEALK-ARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVS------ 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383 108 SSDSNtqiLCKPSVEAFEAAIRIADiVDPRKTIFFDDSIR-NIASAKATGLKTVFV----GESVLVPGADYALSSIHNIK 182
Cdd:COG1011   142 SEEVG---VRKPDPEIFELALERLG-VPPEEALFVGDSPEtDVAGARAAGMRTVWVnrsgEPAPAEPRPDYVISDLAELL 217


                  ...
gi 1063708383 183 EAI 185
Cdd:COG1011   218 ELL 220
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
40-185 1.67e-13

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 66.49  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383  40 DEFHEYVHGRLpYEKLKPDPLLRNL---LLSMPHRKIIFTNADKAHATRALNRLGLEDCFEGIICFETLNPSsdsntqil 116
Cdd:COG0546    69 ARFRELYEEEL-LDETRLFPGVRELleaLKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPA-------- 139

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063708383 117 cKPSVEAFEAAIRIADiVDPRKTIFFDDSIRNIASAKATGLKTVFV------GESVLVPGADYALSSIHNIKEAI 185
Cdd:COG0546   140 -KPKPEPLLEALERLG-LDPEEVLMVGDSPHDIEAARAAGVPFIGVtwgygsAEELEAAGADYVIDSLAELLALL 212
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
1-181 5.37e-11

Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 59.45  E-value: 5.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383   1 MLNQLGIEESEvpklclDLYKEY--GTTMAGLKVM----GYEFDNDEFH----EYVHGRLPYEKLKPDPLLRNLLLSMPH 70
Cdd:COG0637    27 AFAELGIDLTE------EEYRRLmgRSREDILRYLleeyGLDLPEEELAarkeELYRELLAEEGLPLIPGVVELLEALKE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383  71 RKI---IFTNADKAHATRALNRLGLEDCFEGIICFETLNPSsdsntqilcKPSVEAFEAAIRIADiVDPRKTIFFDDSIR 147
Cdd:COG0637   101 AGIkiaVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARG---------KPDPDIYLLAAERLG-VDPEECVVFEDSPA 170

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1063708383 148 NIASAKATGLKTVFVGESVLV----PGADYALSSIHNI 181
Cdd:COG0637   171 GIRAAKAAGMRVVGVPDGGTAeeelAGADLVVDDLAEL 208
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 31-160 5.58e-10

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: 56.58  E-value: 5.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383  31 KVMGYEFDNDEFHEYVHGRLpyeklKPDPLLRNLLLSMPHRKI---IFTNADKAHATRALNRL-GLEDCFEGII--CFET 104
Cdd:cd02603    64 EELGRPLSAELFEELVLAAV-----DPNPEMLDLLEALRAKGYkvyLLSNTWPDHFKFQLELLpRRGDLFDGVVesCRLG 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063708383 105 LnpssdsntqilCKPSVEAFEAAIRIADiVDPRKTIFFDDSIRNIASAKATGLKTV 160
Cdd:cd02603   139 V-----------RKPDPEIYQLALERLG-VKPEEVLFIDDREENVEAARALGIHAI 182
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
36-162 8.23e-08

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 50.28  E-value: 8.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383  36 EFDNDEFHEYVHGRLPYEKLKPDPLLRNLLLSMPHRKI---IFTNADKAHATRALNRLGLEDCFEGIICFETLNPSsdsn 112
Cdd:pfam13419  59 EEKIEFYLRKYNEELHDKLVKPYPGIKELLEELKEQGYklgIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGK---- 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063708383 113 tqilcKPSVEAFEAAIRIADIvDPRKTIFFDDSIRNIASAKATGLKTVFV 162
Cdd:pfam13419 135 -----KPDPDPILKALEQLGL-KPEEVIYVGDSPRDIEAAKNAGIKVIAV 178
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 73-154 1.87e-07

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: 49.51  E-value: 1.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383  73 IIFTNADKAHATRALNRLGLEDCFEGIICFETLNPSsdsntqilcKPSVEAFEAAIRIADiVDPRKTIFFDDSIRNIASA 152
Cdd:pfam00702 118 AILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVG---------KPKPEIYLAALERLG-VKPEEVLMVGDGVNDIPAA 187


                  ..
gi 1063708383 153 KA 154
Cdd:pfam00702 188 KA 189
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 70-160 1.01e-06

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 45.85  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383  70 HRKIIFTNADKAHATRALNRLGLEDCFEGIICfetlnpssdSNTQILCKPSVEAFEAAIRIADiVDPRKTIFFDDSIRNI 149
Cdd:cd01427    24 IKLAIVTNRSREALRALLEKLGLGDLFDGIIG---------SDGGGTPKPKPKPLLLLLLKLG-VDPEEVLFVGDSENDI 93

                          90
                  ....*....|.
gi 1063708383 150 ASAKATGLKTV 160
Cdd:cd01427    94 EAARAAGGRTV 104
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 35-162 1.17e-06

uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized Bacillus subtilis YhcW; This subfamily includes the uncharacterized Bacillus subtilis YhcW. It belongs 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), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, 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: 319859 [Multi-domain]  Cd Length: 169  Bit Score: 46.86  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383  35 YEFDNDEFHEYVHGRL-----PYEKLKPDPLLRNLLLSMPHRKI---IFTNADKAHATRALNRLGLEDCFEGIICFETLN 106
Cdd:cd16423    18 YEAWQELLNERRNELIkrqfsEKTDLPPIEGVKELLEFLKEKGIklaVASSSPRRWIEPHLERLGLLDYFEVIVTGDDVE 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063708383 107 PSsdsntqilcKPSVEAFEAAIRIADiVDPRKTIFFDDSIRNIASAKATGLKTVFV 162
Cdd:cd16423    98 KS---------KPDPDLYLEAAERLG-VNPEECVVIEDSRNGVLAAKAAGMKCVGV 143
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 30-162 5.07e-05

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. 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: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 42.64  E-value: 5.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383  30 LKVMGYEFDNDEFHEYVHG--RL-PYeklkPD--PLLRNLLLSmPHRKIIFTNADKAHATRALNRLGLEDCFEGIICFET 104
Cdd:cd02588    68 AAELGLELDESDLDELGDAylRLpPF----PDvvAGLRRLREA-GYRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAED 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063708383 105 lnpssdsnTQILcKPSVEAFEAAIRIADiVDPRKTIFFDDSIRNIASAKATGLKTVFV 162
Cdd:cd02588   143 --------VRAY-KPAPAVYELAAERLG-VPPDEILHVASHAWDLAGARALGLRTAWI 190
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
76-178 1.86e-04

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 40.95  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383  76 TNADKAHATRALNRLGLEDCFEGIICfetlnpsSDSNTQIlcKPSVEAFEAAIRIADIvDPRKTIFFDDSIRNIASAKAT 155
Cdd:PRK13222  116 TNKPTPFVAPLLEALGIADYFSVVIG-------GDSLPNK--KPDPAPLLLACEKLGL-DPEEMLFVGDSRNDIQAARAA 185

                          90       100
                  ....*....|....*....|....*....
gi 1063708383 156 GLKTVFV------GESVLVPGADYALSSI 178
Cdd:PRK13222  186 GCPSVGVtygynyGEPIALSEPDVVIDHF 214
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 76-160 5.47e-04

beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; This family represents the beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. Family 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), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. It 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: 319808 [Multi-domain]  Cd Length: 143  Bit Score: 38.75  E-value: 5.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383  76 TNADKAHATRALNRLGL-EDCFEGIICFETLNPSsdsntqilcKPSVEAF-EAAIRIAdiVDPRKTIFFDDSIRNIASAK 153
Cdd:cd07505    64 TSSSRRNVELLLLELGLlRGYFDVIVSGDDVERG---------KPAPDIYlLAAERLG--VDPERCLVFEDSLAGIEAAK 132


                  ....*..
gi 1063708383 154 ATGLKTV 160
Cdd:cd07505   133 AAGMTVV 139
Hydrolase_like pfam13242
HAD-hyrolase-like;
118-190 1.24e-03

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 36.44  E-value: 1.24e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063708383 118 KPSVEAFEAAIRIADIvDPRKTIFFDDSIRN-IASAKATGLKTVFV--GESvlvpGADYALSSIHNIKEAIPDLWE 190
Cdd:pfam13242   4 KPNPGMLERALARLGL-DPERTVMIGDRLDTdILGAREAGARTILVltGVT----RPADLEKAPIRPDYVVDDLAE 74
PLN02811 PLN02811
hydrolase
 118-189 2.62e-03

hydrolase


Pssm-ID: 178407 [Multi-domain]  Cd Length: 220  Bit Score: 37.43  E-value: 2.62e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063708383 118 KPSVEAFEAAIRIADI--VDPRKTIFFDDSIRNIASAKATGLKTVFVGESVL----VPGADYALSSIHNIKeaiPDLW 189
Cdd:PLN02811  137 KPAPDIFLAAARRFEDgpVDPGKVLVFEDAPSGVEAAKNAGMSVVMVPDPRLdksyCKGADQVLSSLLDFK---PEEW 211
PRK09456 PRK09456
?-D-glucose-1-phosphatase; Provisional
 118-169 3.20e-03

?-D-glucose-1-phosphatase; Provisional


Pssm-ID: 181872 [Multi-domain]  Cd Length: 199  Bit Score: 37.33  E-value: 3.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063708383 118 KPSVEAFEAAIRiADIVDPRKTIFFDDSIRNIASAKATGLKTVFVGESVLVP 169
Cdd:PRK09456  141 KPEARIYQHVLQ-AEGFSAADAVFFDDNADNIEAANALGITSILVTDKQTIP 191
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 87-177 3.49e-03

beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); Lactococcus lactis beta-PGM catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate as an intermediate. In the forward G6P-forming direction, this reaction links polysaccharide phosphorolysis to glycolysis, in the reverse direction, the reaction provides G1P for the biosynthesis of exo-polysaccharides. This subfamily belongs to the beta-phosphoglucomutase-like family whose other members include Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, 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: 319788 [Multi-domain]  Cd Length: 174  Bit Score: 36.89  E-value: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383  87 LNRLGLEDCFEGIICFETLNPSsdsntqilcKPSVEAFEAAIRIADiVDPRKTIFFDDSIRNIASAKATGLKTVFVGESV 166
Cdd:cd02598    81 LEKLGLAEYFDAIVDGAVLAKG---------KPDPDIFLAAAEGLG-LNPKDCIGVEDAQAGIRAIKAAGFLVVGVGREE 150

                          90
                  ....*....|.
gi 1063708383 167 LVPGADYALSS 177
Cdd:cd02598   151 DLLGADIVVPD 161
PLN02940 PLN02940
riboflavin kinase
 118-189 3.72e-03

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 37.51  E-value: 3.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063708383 118 KPSVEAF-EAAIRIAdiVDPRKTIFFDDSIRNIASAKATGLKTVFV----GESVLVPGADYALSSIHNIKeaiPDLW 189
Cdd:PLN02940  150 KPSPDIFlEAAKRLN--VEPSNCLVIEDSLPGVMAGKAAGMEVIAVpsipKQTHLYSSADEVINSLLDLQ---PEKW 221
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 65-164 6.90e-03

haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter sphaeroides CbbZ; Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. 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: 319815 [Multi-domain]  Cd Length: 214  Bit Score: 36.14  E-value: 6.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708383  65 LLSMPHRKIIFTNADKAHATRALNRLGLEDCFEGIICFETLnPSSdsntqilcKPSVEAFEAAIRIADIvDPRKTIFFDD 144
Cdd:cd07512    98 LRAAGWRLAICTNKPEAPARALLSALGLADLFAAVVGGDTL-PQR--------KPDPAPLRAAIRRLGG-DVSRALMVGD 167

                          90       100
                  ....*....|....*....|
gi 1063708383 145 SIRNIASAKATGLKTVFVGE 164
Cdd:cd07512   168 SETDAATARAAGVPFVLVTF 187
 
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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