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Conserved domains on  [gi|1728080667|ref|WP_147808947|]
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HAD-IA family hydrolase [Bacillus sp. SH7-1]

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 ...
 2-164 5.41e-76

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 cd07523:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 173  Bit Score: 225.33  E-value: 5.41e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667   2 NILWDFDGTLFDTYPVYTKILSEILGDTVDKQEIYKNLKI----SYSHAIQYYNISCEQEEQIKILKGKITAKDMkPFAG 77
Cdd:cd07523     1 NFIWDLDGTLLDSYPAMTKALSETLADFGIPQDLETVYKIikesSVQFAIQYYAEVPDLEEEYKELEAEYLAKPI-LFPG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667  78 VEGILKFA----DKNVIMTHKHKaGVMDILRYYGWEKYFVDMVTIDDGFPRKPNSLAYNHLHKKYN----IDLAIGDREL 149
Cdd:cd07523    80 AKAVLRWIkeqgGKNFLMTHRDH-SALTILKKDGIASYFTEIVTSDNGFPRKPNPEAINYLLNKYQlnpeETVMIGDREL 158

                         170
                  ....*....|....*
gi 1728080667 150 DLLPAKELGISTCMF 164
Cdd:cd07523   159 DIEAGHNAGISTILF 173
 
Name Accession Description Interval E-value
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 2-164 5.41e-76

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the uncharacterized Lactococcus lactis YsbA; The specific function of Lactococcus lactis YsbA is unknown. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases


Pssm-ID: 319825 [Multi-domain]  Cd Length: 173  Bit Score: 225.33  E-value: 5.41e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667   2 NILWDFDGTLFDTYPVYTKILSEILGDTVDKQEIYKNLKI----SYSHAIQYYNISCEQEEQIKILKGKITAKDMkPFAG 77
Cdd:cd07523     1 NFIWDLDGTLLDSYPAMTKALSETLADFGIPQDLETVYKIikesSVQFAIQYYAEVPDLEEEYKELEAEYLAKPI-LFPG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667  78 VEGILKFA----DKNVIMTHKHKaGVMDILRYYGWEKYFVDMVTIDDGFPRKPNSLAYNHLHKKYN----IDLAIGDREL 149
Cdd:cd07523    80 AKAVLRWIkeqgGKNFLMTHRDH-SALTILKKDGIASYFTEIVTSDNGFPRKPNPEAINYLLNKYQlnpeETVMIGDREL 158

                         170
                  ....*....|....*
gi 1728080667 150 DLLPAKELGISTCMF 164
Cdd:cd07523   159 DIEAGHNAGISTILF 173
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
3-185 2.53e-21

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 86.91  E-value: 2.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667   3 ILWDFDGTLFDTYPVYTKILSEIL----GDTVDKQEIYKNLKISYSHAIQYY---NISCEQEEQIKILK---GKITAKDM 72
Cdd:COG0546     4 VLFDLDGTLVDSAPDIAAALNEALaelgLPPLDLEELRALIGLGLRELLRRLlgeDPDEELEELLARFRelyEEELLDET 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667  73 KPFAGVEGILK-FADKNV---IMTHKHKAGVMDILRYYGWEKYFVDMVTIDDGFPRKPNSLAYNHLHKKYNID----LAI 144
Cdd:COG0546    84 RLFPGVRELLEaLKARGIklaVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLDpeevLMV 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1728080667 145 GDRELDLLPAKELGISTCMFQ-GNCDV-------ADYSLAHYSEFFKVV 185
Cdd:COG0546   164 GDSPHDIEAARAAGVPFIGVTwGYGSAeeleaagADYVIDSLAELLALL 212
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
3-163 3.54e-12

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 61.83  E-value: 3.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667   3 ILWDFDGTLFDTYPVYTKILSEIL----GDTVDKQEIYKNLKISYSHAIQYYNISCEQEEQIKILKGK----ITAKDMKP 74
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLeefgYGELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFYLRKyneeLHDKLVKP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667  75 FAGV-EGILKFADKNV---IMTHKHKAGVMDILRYYGWEKYFVDMVTIDDGFPRKPNSLAYNHLHKKYNID----LAIGD 146
Cdd:pfam13419  81 YPGIkELLEELKEQGYklgIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKpeevIYVGD 160

                         170
                  ....*....|....*..
gi 1728080667 147 RELDLLPAKELGISTCM 163
Cdd:pfam13419 161 SPRDIEAAKNAGIKVIA 177
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 3-158 8.61e-10

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; 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/E), (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 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe 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 relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 55.09  E-value: 8.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667   3 ILWDFDGTLFDTYPVYTKILSEILGDTVDKQEIYKNLKISYSHAIQ--YYNISCEQEEQIKILKGKITAKDMKpFAGVEG 80
Cdd:TIGR01549   2 ILFDIDGTLVDIKFAIRRAFPQTFEEFGLDPASFKALKQAGGLAEEewYRIATSALEELQGRFWSEYDAEEAY-IRGAAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667  81 ILKFAD----KNVIMTHKHKAGVMDILRYYGWEKYFVDmVTIDDGFPRKPNSLAYNHLHKKYNID---LAIGDRELDLLP 153
Cdd:TIGR01549  81 LLARLKsagiKLGIISNGSLRAQKLLLRLFGLGDYFEL-ILVSDEPGSKPEPEIFLAALESLGVPpevLHVGDNLNDIEG 159


                  ....*
gi 1728080667 154 AKELG 158
Cdd:TIGR01549 160 ARNAG 164
 
Name Accession Description Interval E-value
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 2-164 5.41e-76

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the uncharacterized Lactococcus lactis YsbA; The specific function of Lactococcus lactis YsbA is unknown. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases


Pssm-ID: 319825 [Multi-domain]  Cd Length: 173  Bit Score: 225.33  E-value: 5.41e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667   2 NILWDFDGTLFDTYPVYTKILSEILGDTVDKQEIYKNLKI----SYSHAIQYYNISCEQEEQIKILKGKITAKDMkPFAG 77
Cdd:cd07523     1 NFIWDLDGTLLDSYPAMTKALSETLADFGIPQDLETVYKIikesSVQFAIQYYAEVPDLEEEYKELEAEYLAKPI-LFPG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667  78 VEGILKFA----DKNVIMTHKHKaGVMDILRYYGWEKYFVDMVTIDDGFPRKPNSLAYNHLHKKYN----IDLAIGDREL 149
Cdd:cd07523    80 AKAVLRWIkeqgGKNFLMTHRDH-SALTILKKDGIASYFTEIVTSDNGFPRKPNPEAINYLLNKYQlnpeETVMIGDREL 158

                         170
                  ....*....|....*
gi 1728080667 150 DLLPAKELGISTCMF 164
Cdd:cd07523   159 DIEAGHNAGISTILF 173
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
3-185 2.53e-21

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 86.91  E-value: 2.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667   3 ILWDFDGTLFDTYPVYTKILSEIL----GDTVDKQEIYKNLKISYSHAIQYY---NISCEQEEQIKILK---GKITAKDM 72
Cdd:COG0546     4 VLFDLDGTLVDSAPDIAAALNEALaelgLPPLDLEELRALIGLGLRELLRRLlgeDPDEELEELLARFRelyEEELLDET 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667  73 KPFAGVEGILK-FADKNV---IMTHKHKAGVMDILRYYGWEKYFVDMVTIDDGFPRKPNSLAYNHLHKKYNID----LAI 144
Cdd:COG0546    84 RLFPGVRELLEaLKARGIklaVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLDpeevLMV 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1728080667 145 GDRELDLLPAKELGISTCMFQ-GNCDV-------ADYSLAHYSEFFKVV 185
Cdd:COG0546   164 GDSPHDIEAARAAGVPFIGVTwGYGSAeeleaagADYVIDSLAELLALL 212
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
3-163 3.54e-12

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 61.83  E-value: 3.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667   3 ILWDFDGTLFDTYPVYTKILSEIL----GDTVDKQEIYKNLKISYSHAIQYYNISCEQEEQIKILKGK----ITAKDMKP 74
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLeefgYGELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFYLRKyneeLHDKLVKP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667  75 FAGV-EGILKFADKNV---IMTHKHKAGVMDILRYYGWEKYFVDMVTIDDGFPRKPNSLAYNHLHKKYNID----LAIGD 146
Cdd:pfam13419  81 YPGIkELLEELKEQGYklgIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKpeevIYVGD 160

                         170
                  ....*....|....*..
gi 1728080667 147 RELDLLPAKELGISTCM 163
Cdd:pfam13419 161 SPRDIEAAKNAGIKVIA 177
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 3-158 6.71e-10

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: 56.06  E-value: 6.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667   3 ILWDFDGTLFDTYPVYTKILSEILGDTVDKQEI---YKNLKIS---YSHAIQYYNISCEQEEQI---------------- 60
Cdd:pfam00702   4 VVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIvaaAEDLPIPvedFTARLLLGKRDWLEELDIlrglvetleaegltvv 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667  61 -KILKGKITAKDM-KPFAGVEGILKFADKN----VIMTHKHKAGVMDILRYYGWEKYFVDMVTIDDGFPRKPNSLAYNHL 134
Cdd:pfam00702  84 lVELLGVIALADElKLYPGAAEALKALKERgikvAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIYLAA 163

                         170       180
                  ....*....|....*....|....*...
gi 1728080667 135 HKKYNID----LAIGDRELDLLPAKELG 158
Cdd:pfam00702 164 LERLGVKpeevLMVGDGVNDIPAAKAAG 191
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 3-158 8.61e-10

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; 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/E), (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 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe 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 relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 55.09  E-value: 8.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667   3 ILWDFDGTLFDTYPVYTKILSEILGDTVDKQEIYKNLKISYSHAIQ--YYNISCEQEEQIKILKGKITAKDMKpFAGVEG 80
Cdd:TIGR01549   2 ILFDIDGTLVDIKFAIRRAFPQTFEEFGLDPASFKALKQAGGLAEEewYRIATSALEELQGRFWSEYDAEEAY-IRGAAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667  81 ILKFAD----KNVIMTHKHKAGVMDILRYYGWEKYFVDmVTIDDGFPRKPNSLAYNHLHKKYNID---LAIGDRELDLLP 153
Cdd:TIGR01549  81 LLARLKsagiKLGIISNGSLRAQKLLLRLFGLGDYFEL-ILVSDEPGSKPEPEIFLAALESLGVPpevLHVGDNLNDIEG 159


                  ....*
gi 1728080667 154 AKELG 158
Cdd:TIGR01549 160 ARNAG 164
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 3-163 1.30e-07

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: 49.34  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667   3 ILWDFDGTLFDTYPVYTK-ILSEILGDTVDKQEI--YKNLK--ISYSHAIQYYNISCEQEEQIK------ILKGKITAKD 71
Cdd:TIGR01509   2 ILFDLDGVLVDTEFAIAKlINREELGLVPDELGVsaVGRLElaLRRFKAQYGRTISPEDAQLLYkqlfyeQIEEEAKLKP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667  72 MKPFAGVEGILKFADKNVIM------THKHKagvmdiLRYYGWEKYFVDMVTIDDGFPRKPNSLAYNHLHKKYNID---- 141
Cdd:TIGR01509  82 LPGVRALLEALRARGKKLALltnsprAHKLV------LALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLEpsec 155

                         170       180
                  ....*....|....*....|..
gi 1728080667 142 LAIGDRELDLLPAKELGISTCM 163
Cdd:TIGR01509 156 VFVDDSPAGIEAAKAAGMHTVG 177
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
3-127 5.28e-07

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 47.90  E-value: 5.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667   3 ILWDFDGTLFDTYPVYTKILSEILGD---TVDKQEIY----KNLKISYSHAIQYYNISCEQEEQIK----ILKGKITAKD 71
Cdd:COG0637     5 VIFDMDGTLVDSEPLHARAWREAFAElgiDLTEEEYRrlmgRSREDILRYLLEEYGLDLPEEELAArkeeLYRELLAEEG 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1728080667  72 MKPFAGVEGILKFADKNVI------MTHKHKAGVmdILRYYGWEKYFVDMVTIDDgFPR-KPN 127
Cdd:COG0637    85 LPLIPGVVELLEALKEAGIkiavatSSPRENAEA--VLEAAGLLDYFDVIVTGDD-VARgKPD 144
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 2-162 3.47e-06

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. 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: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 45.73  E-value: 3.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667   2 NILWDFDGTLFDTYPVYTK----ILSEILGDTVDKQEIYKNLKISYSHAIQYYN-ISCEQ--EEQIKILKgKITAKDMKP 74
Cdd:cd02616     3 TILFDLDGTLIDTNELIIKsfnhTLKEYGLEGYTREEVLPFIGPPLRETFEKIDpDKLEDmvEEFRKYYR-EHNDDLTKE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667  75 FAGV-EGILKFADKNV---IMTHKHKAGVMDILRYYGWEKYFVDMVTIDDGFPRKPNS----LAYNHLHKKYNIDLAIGD 146
Cdd:cd02616    82 YPGVyETLARLKSQGIklgVVTTKLRETALKGLKLLGLDKYFDVIVGGDDVTHHKPDPepvlKALELLGAEPEEALMVGD 161

                         170
                  ....*....|....*.
gi 1728080667 147 RELDLLPAKELGISTC 162
Cdd:cd02616   162 SPHDILAGKNAGVKTV 177
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 89-162 4.01e-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: 43.92  E-value: 4.01e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1728080667  89 VIMTHKHKAGVMDILRYYGWEKYFVDMVTIDDGFPRKPN----SLAYNHLHKKYNIDLAIGDRELDLLPAKELGISTC 162
Cdd:cd01427    27 AIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKpkplLLLLLKLGVDPEEVLFVGDSENDIEAARAAGGRTV 104
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 74-163 1.81e-05

Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGP; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) 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: 319854 [Multi-domain]  Cd Length: 212  Bit Score: 43.76  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728080667  74 PFAGV-EGILKFADKNVIM---THKHKAGVMDILRYYGWEKYFVDMVTIDDgFP-RKPNSLAYNHLHKKYNID----LAI 144
Cdd:cd16417    88 LYPGVkEGLAALKAQGYPLacvTNKPERFVAPLLEALGISDYFSLVLGGDS-LPeKKPDPAPLLHACEKLGIApaqmLMV 166

                          90
                  ....*....|....*....
gi 1728080667 145 GDRELDLLPAKELGISTCM 163
Cdd:cd16417   167 GDSRNDILAARAAGCPSVG 185
 
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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