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Conserved domains on  [gi|2179336972|ref|WP_234787197|]
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HAD family hydrolase [Streptococcus equinus]

Protein Classification

HAD family hydrolase( domain architecture ID 11436852)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 16-221 2.60e-21

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: 88.16  E-value: 2.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  16 VIFLDLDGVIFDSYGLWDKVIEKVLA-LANISYTQTIKKHLWRLNMIESQAY----------LSALFAKENLTYPEKKTQ 84
Cdd:COG1011     3 AVLFDLDGTLLDFDPVIAEALRALAErLGLLDEAEELAEAYRAIEYALWRRYergeitfaelLRRLLEELGLDLAEELAE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  85 QLLEEAYQKVSLMPQAVETLADLAEEDFLIYAVTSNYDDLAKIGLESAGVLQYFSGSYSCIALGF--PDKteDFYQAVLE 162
Cdd:COG1011    83 AFLAALPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVrkPDP--EIFELALE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972 163 TEALFDKTIFYLEDSTRH-LKTAQKFGIQGVYLSNTDNPQDNQEQAFRTIRHLKEFTTIV 221
Cdd:COG1011   161 RLGVPPEEALFVGDSPETdVAGARAAGMRTVWVNRSGEPAPAEPRPDYVISDLAELLELL 220
 
Name Accession Description Interval E-value
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 16-221 2.60e-21

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: 88.16  E-value: 2.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  16 VIFLDLDGVIFDSYGLWDKVIEKVLA-LANISYTQTIKKHLWRLNMIESQAY----------LSALFAKENLTYPEKKTQ 84
Cdd:COG1011     3 AVLFDLDGTLLDFDPVIAEALRALAErLGLLDEAEELAEAYRAIEYALWRRYergeitfaelLRRLLEELGLDLAEELAE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  85 QLLEEAYQKVSLMPQAVETLADLAEEDFLIYAVTSNYDDLAKIGLESAGVLQYFSGSYSCIALGF--PDKteDFYQAVLE 162
Cdd:COG1011    83 AFLAALPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVrkPDP--EIFELALE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972 163 TEALFDKTIFYLEDSTRH-LKTAQKFGIQGVYLSNTDNPQDNQEQAFRTIRHLKEFTTIV 221
Cdd:COG1011   161 RLGVPPEEALFVGDSPETdVAGARAAGMRTVWVNRSGEPAPAEPRPDYVISDLAELLELL 220
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 16-192 3.12e-12

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: 62.82  E-value: 3.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  16 VIFLDLDGVIFDSyglwDKVIEKVLALANISYTQTIKKHLWRLNMIESQAYLSALFAKEN--LTYPEKKTQQLLE--EAY 91
Cdd:TIGR01509   1 AILFDLDGVLVDT----EFAIAKLINREELGLVPDELGVSAVGRLELALRRFKAQYGRTIspEDAQLLYKQLFYEqiEEE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  92 QKVSLMPQAVETLADLAEEDFLIYAVTSNY-DDLAKigLESAGVLQYFSGSYSCIALGFPDKTEDFYQAVLETEAL-FDK 169
Cdd:TIGR01509  77 AKLKPLPGVRALLEALRARGKKLALLTNSPrAHKLV--LALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLePSE 154

                         170       180
                  ....*....|....*....|...
gi 2179336972 170 TIFyLEDSTRHLKTAQKFGIQGV 192
Cdd:TIGR01509 155 CVF-VDDSPAGIEAAKAAGMHTV 176
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 14-198 1.94e-07

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: 49.65  E-value: 1.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  14 KSVIFlDLDGVIFDsYGlWDKVIEKVLALANI---SYTQTIKKHLWRLNM----IESQAYLsALFAKEnltYPEKKTQQL 86
Cdd:cd02603     2 RAVLF-DFGGVLID-PD-PAAAVARFEALTGEpseFVLDTEGLAGAFLELergrITEEEFW-EELREE---LGRPLSAEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  87 LEEAYQK-VSLMPQAVETLADLAEEDFLIYAVTSNYDDLAKIGLE-SAGVLQYFSGSY-SCiALGF--PDKteDFYQAVL 161
Cdd:cd02603    75 FEELVLAaVDPNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLElLPRRGDLFDGVVeSC-RLGVrkPDP--EIYQLAL 151

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2179336972 162 ETEALFDKTIFYLEDSTRHLKTAQKFGIQGVYLSNTD 198
Cdd:cd02603   152 ERLGVKPEEVLFIDDREENVEAARALGIHAILVTDAE 188
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
16-190 5.83e-07

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 47.96  E-value: 5.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  16 VIFlDLDGVIFDS--------------YGLWDKVIEKVLALANISYTQTIKKHLWRLNMIESQAYLSALFAKENLTYpek 81
Cdd:pfam13419   1 IIF-DFDGTLLDTeeliiksfnylleeFGYGELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFYLRKYNEELHDK--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  82 ktqqlleeayqKVSLMPQAVETLADLAEEDFLIYAVTSNYDDLAKIGLESAGVLQYFSGSYSCIALGFPDKTEDFYQAVL 161
Cdd:pfam13419  77 -----------LVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKAL 145

                         170       180       190
                  ....*....|....*....|....*....|
gi 2179336972 162 E-TEALFDKTIfYLEDSTRHLKTAQKFGIQ 190
Cdd:pfam13419 146 EqLGLKPEEVI-YVGDSPRDIEAAKNAGIK 174
 
Name Accession Description Interval E-value
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 16-221 2.60e-21

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: 88.16  E-value: 2.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  16 VIFLDLDGVIFDSYGLWDKVIEKVLA-LANISYTQTIKKHLWRLNMIESQAY----------LSALFAKENLTYPEKKTQ 84
Cdd:COG1011     3 AVLFDLDGTLLDFDPVIAEALRALAErLGLLDEAEELAEAYRAIEYALWRRYergeitfaelLRRLLEELGLDLAEELAE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  85 QLLEEAYQKVSLMPQAVETLADLAEEDFLIYAVTSNYDDLAKIGLESAGVLQYFSGSYSCIALGF--PDKteDFYQAVLE 162
Cdd:COG1011    83 AFLAALPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVrkPDP--EIFELALE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972 163 TEALFDKTIFYLEDSTRH-LKTAQKFGIQGVYLSNTDNPQDNQEQAFRTIRHLKEFTTIV 221
Cdd:COG1011   161 RLGVPPEEALFVGDSPETdVAGARAAGMRTVWVNRSGEPAPAEPRPDYVISDLAELLELL 220
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
14-217 3.48e-14

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 68.70  E-value: 3.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  14 KSVIFlDLDGVIFDSYGLWDKVIEKVLALANISYTQTIKKHLWRLNMIESqayLSALFAKENLTYPEKKTQQLLEEAY-- 91
Cdd:COG0637     3 KAVIF-DMDGTLVDSEPLHARAWREAFAELGIDLTEEEYRRLMGRSREDI---LRYLLEEYGLDLPEEELAARKEELYre 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  92 ----QKVSLMPQAVETLADLAEEDFLIYAVTSNYDDLAKIGLESAGVLQYFSGSYSC--IALGFPDktEDFYQAVLE--- 162
Cdd:COG0637    79 llaeEGLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGddVARGKPD--PDIYLLAAErlg 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2179336972 163 ---TEALFdktifyLEDSTRHLKTAQKFGIQGVYLSNTDNPQDNQEQAFRTIRHLKEF 217
Cdd:COG0637   157 vdpEECVV------FEDSPAGIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 16-192 3.12e-12

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: 62.82  E-value: 3.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  16 VIFLDLDGVIFDSyglwDKVIEKVLALANISYTQTIKKHLWRLNMIESQAYLSALFAKEN--LTYPEKKTQQLLE--EAY 91
Cdd:TIGR01509   1 AILFDLDGVLVDT----EFAIAKLINREELGLVPDELGVSAVGRLELALRRFKAQYGRTIspEDAQLLYKQLFYEqiEEE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  92 QKVSLMPQAVETLADLAEEDFLIYAVTSNY-DDLAKigLESAGVLQYFSGSYSCIALGFPDKTEDFYQAVLETEAL-FDK 169
Cdd:TIGR01509  77 AKLKPLPGVRALLEALRARGKKLALLTNSPrAHKLV--LALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLePSE 154

                         170       180
                  ....*....|....*....|...
gi 2179336972 170 TIFyLEDSTRHLKTAQKFGIQGV 192
Cdd:TIGR01509 155 CVF-VDDSPAGIEAAKAAGMHTV 176
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
14-223 1.11e-11

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 61.87  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  14 KSVIFlDLDGVIFDSYGLWDKVIEKVLA---LANISYTQ-------TIKKHLWRLNMIESQAYLSALFAKENLTYpekkt 83
Cdd:COG0546     2 KLVLF-DLDGTLVDSAPDIAAALNEALAelgLPPLDLEElraliglGLRELLRRLLGEDPDEELEELLARFRELY----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  84 qqlLEEAYQKVSLMPQAVETLADLAEEDFLIYAVTSNYDDLAKIGLESAGVLQYFSGSYSC--IALGFPDktEDFYQAVL 161
Cdd:COG0546    76 ---EEELLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGddVPPAKPK--PEPLLEAL 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2179336972 162 ETEALFDKTIFYLEDSTRHLKTAQKFGIQGVYLSNTDNPQDN--QEQAFRTIRHLKEFTTIVKE 223
Cdd:COG0546   151 ERLGLDPEEVLMVGDSPHDIEAARAAGVPFIGVTWGYGSAEEleAAGADYVIDSLAELLALLAE 214
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 14-198 1.94e-07

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: 49.65  E-value: 1.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  14 KSVIFlDLDGVIFDsYGlWDKVIEKVLALANI---SYTQTIKKHLWRLNM----IESQAYLsALFAKEnltYPEKKTQQL 86
Cdd:cd02603     2 RAVLF-DFGGVLID-PD-PAAAVARFEALTGEpseFVLDTEGLAGAFLELergrITEEEFW-EELREE---LGRPLSAEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  87 LEEAYQK-VSLMPQAVETLADLAEEDFLIYAVTSNYDDLAKIGLE-SAGVLQYFSGSY-SCiALGF--PDKteDFYQAVL 161
Cdd:cd02603    75 FEELVLAaVDPNPEMLDLLEALRAKGYKVYLLSNTWPDHFKFQLElLPRRGDLFDGVVeSC-RLGVrkPDP--EIYQLAL 151

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2179336972 162 ETEALFDKTIFYLEDSTRHLKTAQKFGIQGVYLSNTD 198
Cdd:cd02603   152 ERLGVKPEEVLFIDDREENVEAARALGIHAILVTDAE 188
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
16-190 5.83e-07

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 47.96  E-value: 5.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  16 VIFlDLDGVIFDS--------------YGLWDKVIEKVLALANISYTQTIKKHLWRLNMIESQAYLSALFAKENLTYpek 81
Cdd:pfam13419   1 IIF-DFDGTLLDTeeliiksfnylleeFGYGELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFYLRKYNEELHDK--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  82 ktqqlleeayqKVSLMPQAVETLADLAEEDFLIYAVTSNYDDLAKIGLESAGVLQYFSGSYSCIALGFPDKTEDFYQAVL 161
Cdd:pfam13419  77 -----------LVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKAL 145

                         170       180       190
                  ....*....|....*....|....*....|
gi 2179336972 162 E-TEALFDKTIfYLEDSTRHLKTAQKFGIQ 190
Cdd:pfam13419 146 EqLGLKPEEVI-YVGDSPRDIEAAKNAGIK 174
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 16-188 1.39e-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: 47.20  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  16 VIFLDLDGVIFDSYGLWDKVI-----EKVLALANISYTQTIK---KHLWRLNMIESQAYLSAL--FAKENLTYPEKKTQQ 85
Cdd:pfam00702   3 AVVFDLDGTLTDGEPVVTEAIaelasEHPLAKAIVAAAEDLPipvEDFTARLLLGKRDWLEELdiLRGLVETLEAEGLTV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  86 LLEE------AYQKVSLMPQAVETLADLAEEDFLIYAVTSNYDDLAKIGLESAGVLQYFSGSYSCIALGFPDKTEDFYQA 159
Cdd:pfam00702  83 VLVEllgviaLADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIYLA 162

                         170       180
                  ....*....|....*....|....*....
gi 2179336972 160 VLETEALFDKTIFYLEDSTRHLKTAQKFG 188
Cdd:pfam00702 163 ALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 17-193 4.03e-05

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: 42.75  E-value: 4.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  17 IFLDLDGVIFDSYGLWDKVIEKVLALANIsyTQTIKKhLWRLnMIESQAYLSALFAKEnLTYPEKKTQQLLEEAYQKVSL 96
Cdd:cd07523     2 FIWDLDGTLLDSYPAMTKALSETLADFGI--PQDLET-VYKI-IKESSVQFAIQYYAE-VPDLEEEYKELEAEYLAKPIL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  97 MPQAVETLADLAEEDFLIYAVTSNYDDLAKIgLESAGVLQYFSGSYScIALGFPDKTE-DFYQAVLETEALFDKTIFYLE 175
Cdd:cd07523    77 FPGAKAVLRWIKEQGGKNFLMTHRDHSALTI-LKKDGIASYFTEIVT-SDNGFPRKPNpEAINYLLNKYQLNPEETVMIG 154

                         170
                  ....*....|....*...
gi 2179336972 176 DSTRHLKTAQKFGIQGVY 193
Cdd:cd07523   155 DRELDIEAGHNAGISTIL 172
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 16-188 6.91e-05

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: 42.00  E-value: 6.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  16 VIFLDLDGVIFDSYGLWDKVIEkvlalanisytQTIKKHlwRLNMIESQAYLSALFAKENLT--YPEKKTQQLLEEAYQK 93
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFP-----------QTFEEF--GLDPASFKALKQAGGLAEEEWyrIATSALEELQGRFWSE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  94 V----SLMPQAVETLADLAEEDFLIYAVTSNYDDLAKIGLESAGVLQYFsgSYSCIALGFPDKTE-DFYQAVLETEALFD 168
Cdd:TIGR01549  68 YdaeeAYIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYF--ELILVSDEPGSKPEpEIFLAALESLGVPP 145

                         170       180
                  ....*....|....*....|
gi 2179336972 169 KTIfYLEDSTRHLKTAQKFG 188
Cdd:TIGR01549 146 EVL-HVGDNLNDIEGARNAG 164
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 100-194 1.33e-04

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: 40.07  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972 100 AVETLADLAEEDFLIYAVTSNYDDLAKIGLESAGVLQYFSGSYSCIALGFPDKTEDFYQAVLETEALFDKTIFYLEDSTR 179
Cdd:cd01427    12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSEN 91

                          90
                  ....*....|....*
gi 2179336972 180 HLKTAQKFGIQGVYL 194
Cdd:cd01427    92 DIEAARAAGGRTVAV 106
YqfW COG5663
Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only];
20-226 1.60e-03

Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only];


Pssm-ID: 444382 [Multi-domain]  Cd Length: 187  Bit Score: 38.29  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  20 DLDGVIFDSYGLWDKVIEKVLALaNISYTQtIKKHLWR--LNMIESQAYlsALFAKEnltypekktqqlLEEAYQKVSLM 97
Cdd:COG5663     6 DIDGTITDPYPYFIPLLNKYFGK-NITLED-ITTYDLHevLGLTEEEFD--KFFEEN------------EEEIYTEAPPV 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  98 PQAVETLADLAEEDFLIY--AVTSNYDDLAKIGLESAGVlqyfsGSYSCIALGFPDKTEdfyqAVLETEalFDktiFYLE 175
Cdd:COG5663    70 PGAKEVLNKLKDQHELYYitARPKHLEEVTENWLEKHGI-----PYDELILLGSHDKVE----AAKELG--ID---LFIE 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2179336972 176 DSTRHLKTAQKFGIQgVYLSNTDNPQDNQEQAFRTIRHLKEFTTIVKEEMN 226
Cdd:COG5663   136 DKPDNALQLAEEGIP-VLLFDTPYNRGPLPEGVIRVNNWQEIKQIIEKLFK 185
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 16-139 2.97e-03

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: 37.64  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  16 VIFLDLDGVIFDSYGLWDKVIEKVLA------------LANI--SYTQTIKKHL--WRLNMIEsqaylsaLFAKENLTYP 79
Cdd:cd02616     3 TILFDLDGTLIDTNELIIKSFNHTLKeyglegytreevLPFIgpPLRETFEKIDpdKLEDMVE-------EFRKYYREHN 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2179336972  80 EKKTqqlleEAYqkvslmPQAVETLADLAEEDFLIYAVTSNYDDLAKIGLESAGVLQYFS 139
Cdd:cd02616    76 DDLT-----KEY------PGVYETLARLKSQGIKLGVVTTKLRETALKGLKLLGLDKYFD 124
 
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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